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Database: PDB
Entry: 3NH7
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HEADER    IMMUNE SYSTEM                           14-JUN-10   3NH7              
TITLE     CRYSTAL STRUCTURE OF THE NEUTRALIZING FAB FRAGMENT ABD1556 BOUND TO   
TITLE    2 THE BMP TYPE I RECEPTOR IA                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTIBODY FRAGMENT FAB ABD1556, HEAVY CHAIN;                
COMPND   3 CHAIN: H, I, J, K;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ANTIBODY FRAGMENT FAB ABD1556, LIGHT CHAIN;                
COMPND   7 CHAIN: L, M, N, O;                                                   
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1A;               
COMPND  11 CHAIN: A, B, C, D;                                                   
COMPND  12 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 24-152;                 
COMPND  13 SYNONYM: BMP TYPE I RECEPTOR, BMPR-IA, BMP TYPE-1A RECEPTOR, BMPR-1A,
COMPND  14 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R5, SKR5, ACTIVIN RECEPTOR- 
COMPND  15 LIKE KINASE 3, ALK-3;                                                
COMPND  16 EC: 2.7.11.30;                                                       
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: BMPR1A;                                                        
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PET32A                                    
KEYWDS    ANTIBODY-ANTIGEN COMPLEX, BMP RECEPTOR EXTRACELLULAR DOMAIN, BONE     
KEYWDS   2 MORPHOGENETIC PROTEIN, IMMUNE SYSTEM                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.D.MUELLER,S.HARTH,W.SEBALD                                          
REVDAT   1   27-OCT-10 3NH7    0                                                
JRNL        AUTH   S.HARTH,A.KOTZSCH,J.HU,W.SEBALD,T.D.MUELLER                  
JRNL        TITL   A SELECTION FIT MECHANISM IN BMP RECEPTOR IA AS A POSSIBLE   
JRNL        TITL 2 SOURCE FOR BMP LIGAND-RECEPTOR PROMISCUITY                   
JRNL        REF    PLOS ONE                      V.   5 E1304 2010              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   20927405                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0013049                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 56514                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3020                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4254                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 247                          
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15323                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.25000                                              
REMARK   3    B22 (A**2) : -1.23000                                             
REMARK   3    B33 (A**2) : -1.95000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.99000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.408         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.271         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.456        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15719 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21442 ; 1.624 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2022 ; 7.650 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   611 ;38.169 ;24.566       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2423 ;21.787 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;22.560 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2414 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11892 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10136 ; 0.533 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16401 ; 0.828 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5583 ; 0.624 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5041 ; 0.882 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : K I J                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      2       K     220      1                      
REMARK   3           1     I      2       I     220      1                      
REMARK   3           1     J      2       J     220      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    K    (A):   1607 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   1607 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   1607 ;  0.07 ;  0.05           
REMARK   3   TIGHT THERMAL      1    K (A**2):   1607 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   1607 ;  0.14 ;  0.50           
REMARK   3   TIGHT THERMAL      1    J (A**2):   1607 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : O M N L                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      2       O     213      1                      
REMARK   3           1     M      2       M     213      1                      
REMARK   3           1     N      2       N     213      1                      
REMARK   3           1     L      2       L     213      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    O    (A):   1558 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    M    (A):   1558 ;  0.08 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    N    (A):   1558 ;  0.11 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    L    (A):   1558 ;  0.11 ;  0.05           
REMARK   3   TIGHT THERMAL      2    O (A**2):   1558 ;  0.14 ;  0.50           
REMARK   3   TIGHT THERMAL      2    M (A**2):   1558 ;  0.13 ;  0.50           
REMARK   3   TIGHT THERMAL      2    N (A**2):   1558 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      2    L (A**2):   1558 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D A B C                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     34       D     117      1                      
REMARK   3           1     A     34       A     117      1                      
REMARK   3           1     B     34       B     117      1                      
REMARK   3           1     C     34       C     117      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    D    (A):    647 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    A    (A):    647 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):    647 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):    647 ;  0.09 ;  0.05           
REMARK   3   TIGHT THERMAL      3    D (A**2):    647 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):    647 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):    647 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):    647 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7142  12.0719  11.7351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2877 T22:   0.0192                                     
REMARK   3      T33:   0.0612 T12:  -0.0134                                     
REMARK   3      T13:   0.0524 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9582 L22:   2.0181                                     
REMARK   3      L33:   3.0161 L12:  -1.9450                                     
REMARK   3      L13:  -1.3853 L23:   0.6764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1575 S12:   0.0545 S13:  -0.3080                       
REMARK   3      S21:   0.0023 S22:   0.0983 S23:   0.0500                       
REMARK   3      S31:   0.5116 S32:  -0.1319 S33:   0.0592                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   121        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.0894  12.1356  28.5886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8183 T22:   0.4102                                     
REMARK   3      T33:   0.7688 T12:   0.4228                                     
REMARK   3      T13:   0.2154 T23:   0.0902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6518 L22:   4.3688                                     
REMARK   3      L33:  11.2272 L12:  -3.9644                                     
REMARK   3      L13:  -2.2925 L23:  -4.3497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0849 S12:   0.2838 S13:  -0.3900                       
REMARK   3      S21:  -0.7515 S22:  -0.7328 S23:  -0.5093                       
REMARK   3      S31:   1.4626 S32:   1.0614 S33:   0.8177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1985  23.4730  31.1107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3184 T22:   0.0496                                     
REMARK   3      T33:   0.0785 T12:   0.0375                                     
REMARK   3      T13:   0.0450 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0582 L22:   2.5391                                     
REMARK   3      L33:   1.7146 L12:  -0.7727                                     
REMARK   3      L13:   1.4871 L23:   0.5866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1363 S12:  -0.1191 S13:   0.2061                       
REMARK   3      S21:   0.0100 S22:   0.0762 S23:   0.1442                       
REMARK   3      S31:   0.3451 S32:  -0.0732 S33:   0.0601                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   121        L   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2605  27.2719  28.6114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1618 T22:   0.2630                                     
REMARK   3      T33:   0.3002 T12:   0.1718                                     
REMARK   3      T13:  -0.1156 T23:  -0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5889 L22:   4.4082                                     
REMARK   3      L33:  12.0414 L12:   3.6623                                     
REMARK   3      L13:  -6.3144 L23:  -4.0861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1535 S12:  -0.0695 S13:   0.1126                       
REMARK   3      S21:   0.1098 S22:   0.0585 S23:  -0.5047                       
REMARK   3      S31:  -0.1682 S32:   0.3477 S33:   0.0950                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    34        A   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2895  24.8434  20.7751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2743 T22:   0.3848                                     
REMARK   3      T33:   0.3174 T12:  -0.0094                                     
REMARK   3      T13:   0.1213 T23:   0.0910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6180 L22:  12.3164                                     
REMARK   3      L33:   3.4431 L12:  -1.9701                                     
REMARK   3      L13:  -1.3215 L23:   1.5026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2072 S12:  -0.2744 S13:  -0.1765                       
REMARK   3      S21:   1.3357 S22:  -0.0299 S23:   1.2369                       
REMARK   3      S31:   0.1204 S32:  -0.6274 S33:   0.2371                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2745  -0.0425  40.0704              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0570 T22:   0.2101                                     
REMARK   3      T33:   0.0539 T12:   0.0792                                     
REMARK   3      T13:  -0.0052 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3623 L22:   2.8405                                     
REMARK   3      L33:   2.2302 L12:   1.0436                                     
REMARK   3      L13:  -2.2907 L23:  -0.6284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2459 S12:   0.6113 S13:   0.3765                       
REMARK   3      S21:  -0.2146 S22:  -0.0922 S23:   0.0583                       
REMARK   3      S31:  -0.0467 S32:  -0.4121 S33:  -0.1538                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   121        I   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0932 -12.2583  36.1155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0727 T22:   0.2544                                     
REMARK   3      T33:   0.3263 T12:   0.1233                                     
REMARK   3      T13:   0.0511 T23:   0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9486 L22:  13.6483                                     
REMARK   3      L33:   5.5589 L12:  -2.3689                                     
REMARK   3      L13:  -2.0998 L23:  -2.4810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3677 S12:   0.6438 S13:   0.1721                       
REMARK   3      S21:  -0.3868 S22:  -0.1797 S23:  -0.5349                       
REMARK   3      S31:   0.1007 S32:   0.3728 S33:  -0.1880                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     2        M   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5818 -20.6450  48.0805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1236 T22:   0.1196                                     
REMARK   3      T33:   0.1410 T12:  -0.0753                                     
REMARK   3      T13:  -0.0567 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2127 L22:   1.2917                                     
REMARK   3      L33:   2.4547 L12:  -0.1925                                     
REMARK   3      L13:   0.0854 L23:  -0.8295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.1463 S13:  -0.4384                       
REMARK   3      S21:   0.1387 S22:  -0.1205 S23:   0.0242                       
REMARK   3      S31:   0.1957 S32:  -0.3151 S33:   0.0866                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   121        M   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3121 -15.0704  50.7749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1209 T22:   0.1638                                     
REMARK   3      T33:   0.3275 T12:   0.1133                                     
REMARK   3      T13:  -0.0593 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4446 L22:   9.4330                                     
REMARK   3      L33:   4.7383 L12:   5.7482                                     
REMARK   3      L13:   1.8703 L23:   4.5922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2861 S12:  -0.0859 S13:   0.0024                       
REMARK   3      S21:   0.1377 S22:  -0.0639 S23:  -0.2126                       
REMARK   3      S31:   0.2823 S32:   0.1718 S33:  -0.2222                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    34        B   118                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3269 -14.4180  53.1237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2343 T22:   0.4796                                     
REMARK   3      T33:   0.3342 T12:  -0.1707                                     
REMARK   3      T13:   0.0508 T23:  -0.1285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1630 L22:   7.5604                                     
REMARK   3      L33:  12.4945 L12:   2.7399                                     
REMARK   3      L13:   0.4299 L23:  -2.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1113 S12:   0.4202 S13:  -0.6463                       
REMARK   3      S21:   0.5878 S22:   0.1899 S23:   0.5169                       
REMARK   3      S31:   1.2475 S32:  -1.0145 S33:  -0.3011                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8445  31.4542  91.6261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3466 T22:   0.0677                                     
REMARK   3      T33:   0.1204 T12:  -0.1109                                     
REMARK   3      T13:   0.0459 T23:  -0.0442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7044 L22:   4.4006                                     
REMARK   3      L33:   2.3637 L12:   1.9767                                     
REMARK   3      L13:   1.6423 L23:   1.2911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0560 S12:   0.2569 S13:  -0.2458                       
REMARK   3      S21:  -0.2764 S22:   0.0347 S23:  -0.2812                       
REMARK   3      S31:   0.3386 S32:   0.0116 S33:  -0.0907                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   121        J   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6662  43.6119  86.3455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2589 T22:   0.6442                                     
REMARK   3      T33:   0.1870 T12:  -0.1072                                     
REMARK   3      T13:  -0.0711 T23:   0.1495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0717 L22:  10.5388                                     
REMARK   3      L33:   5.1518 L12:  -1.9794                                     
REMARK   3      L13:   1.2043 L23:   1.3620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0509 S12:   0.7992 S13:   0.2404                       
REMARK   3      S21:  -0.3991 S22:   0.1372 S23:   0.4209                       
REMARK   3      S31:  -0.2095 S32:  -0.6014 S33:  -0.0863                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     2        N   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6341  51.8384 100.1256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3507 T22:   0.1021                                     
REMARK   3      T33:   0.1766 T12:  -0.1011                                     
REMARK   3      T13:   0.0131 T23:  -0.0944                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2151 L22:   0.1516                                     
REMARK   3      L33:   2.3569 L12:   0.5959                                     
REMARK   3      L13:   0.4101 L23:   0.0398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0892 S12:  -0.0511 S13:   0.3045                       
REMARK   3      S21:  -0.1196 S22:   0.1083 S23:  -0.0770                       
REMARK   3      S31:   0.1993 S32:  -0.0090 S33:  -0.0191                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   121        N   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8281  45.5453 100.8181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1318 T22:   0.2467                                     
REMARK   3      T33:   0.1221 T12:   0.0695                                     
REMARK   3      T13:  -0.0741 T23:   0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4106 L22:   8.4982                                     
REMARK   3      L33:   5.1503 L12:   4.3100                                     
REMARK   3      L13:  -1.7346 L23:  -2.5642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1324 S12:   0.2768 S13:   0.1790                       
REMARK   3      S21:   0.1171 S22:   0.2816 S23:   0.1017                       
REMARK   3      S31:  -0.1127 S32:  -0.1620 S33:  -0.1492                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    34        C   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.5627  45.7734 106.6455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3969 T22:   0.2298                                     
REMARK   3      T33:   0.5518 T12:  -0.1216                                     
REMARK   3      T13:  -0.0724 T23:  -0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9400 L22:   4.3356                                     
REMARK   3      L33:  11.4795 L12:   2.0612                                     
REMARK   3      L13:  -0.0578 L23:   2.6324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0617 S12:  -0.1569 S13:   0.1444                       
REMARK   3      S21:   0.3280 S22:   0.0501 S23:  -0.6807                       
REMARK   3      S31:  -1.2140 S32:   0.7685 S33:  -0.1118                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1941  18.9658  61.4381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1202 T22:   0.0730                                     
REMARK   3      T33:   0.0556 T12:   0.0097                                     
REMARK   3      T13:   0.0305 T23:   0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9177 L22:   2.1095                                     
REMARK   3      L33:   2.7318 L12:  -1.3626                                     
REMARK   3      L13:  -0.1332 L23:   0.3013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3122 S12:   0.0526 S13:   0.1330                       
REMARK   3      S21:  -0.0478 S22:  -0.0552 S23:   0.0715                       
REMARK   3      S31:  -0.4374 S32:  -0.1395 S33:  -0.2570                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   121        K   221                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8534  18.0937  76.6165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2724 T22:   0.2004                                     
REMARK   3      T33:   0.3956 T12:   0.0128                                     
REMARK   3      T13:   0.1469 T23:  -0.0531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0469 L22:   4.4784                                     
REMARK   3      L33:   6.3889 L12:  -0.2777                                     
REMARK   3      L13:   0.0452 L23:  -1.6347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3495 S12:  -0.0942 S13:   0.3730                       
REMARK   3      S21:   0.8599 S22:  -0.2190 S23:   0.5876                       
REMARK   3      S31:  -0.2001 S32:  -0.6276 S33:  -0.1305                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     2        O   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0323   7.5787  80.6345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3172 T22:   0.1123                                     
REMARK   3      T33:   0.0919 T12:  -0.1253                                     
REMARK   3      T13:  -0.0927 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6543 L22:   1.6715                                     
REMARK   3      L33:   1.5478 L12:   0.2645                                     
REMARK   3      L13:  -0.9928 L23:  -0.8076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1978 S12:  -0.2130 S13:  -0.2877                       
REMARK   3      S21:   0.2501 S22:  -0.1560 S23:  -0.2317                       
REMARK   3      S31:   0.2812 S32:   0.0912 S33:  -0.0418                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O   121        O   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7697   3.9319  76.1770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2033 T22:   0.1013                                     
REMARK   3      T33:   0.1120 T12:  -0.0745                                     
REMARK   3      T13:   0.0895 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9935 L22:   2.6879                                     
REMARK   3      L33:   7.9973 L12:   1.4186                                     
REMARK   3      L13:   4.6411 L23:   2.3636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4519 S12:  -0.0551 S13:  -0.1543                       
REMARK   3      S21:   0.5318 S22:  -0.3325 S23:   0.2290                       
REMARK   3      S31:   0.2412 S32:  -0.0544 S33:  -0.1194                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    34        D   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5764   5.0289  72.3083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1813 T22:   0.6571                                     
REMARK   3      T33:   0.3086 T12:  -0.0176                                     
REMARK   3      T13:  -0.2000 T23:  -0.1140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7119 L22:  19.7372                                     
REMARK   3      L33:   7.0829 L12:  -3.0908                                     
REMARK   3      L13:  -0.3813 L23:  -2.6050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1678 S12:  -1.0385 S13:  -0.0543                       
REMARK   3      S21:   1.2650 S22:   0.0242 S23:  -1.4256                       
REMARK   3      S31:   0.3164 S32:   0.9904 S33:  -0.1920                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NH7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059824.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : VARIMAX CU HIGHRES                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59539                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AQK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 7.0, 20% (W/V) PEG     
REMARK 280  8000 AND 10% (W/V) GLUCOSE , VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       64.62750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, N, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, O, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS H   136                                                      
REMARK 465     SER H   137                                                      
REMARK 465     THR H   138                                                      
REMARK 465     SER H   139                                                      
REMARK 465     GLY H   140                                                      
REMARK 465     GLY H   141                                                      
REMARK 465     THR H   142                                                      
REMARK 465     SER H   194                                                      
REMARK 465     SER H   195                                                      
REMARK 465     LEU H   196                                                      
REMARK 465     GLY H   197                                                      
REMARK 465     THR H   198                                                      
REMARK 465     GLN H   199                                                      
REMARK 465     LYS H   221                                                      
REMARK 465     SER H   222                                                      
REMARK 465     GLU H   223                                                      
REMARK 465     PHE H   224                                                      
REMARK 465     SER H   225                                                      
REMARK 465     ALA H   226                                                      
REMARK 465     TRP H   227                                                      
REMARK 465     SER H   228                                                      
REMARK 465     HIS H   229                                                      
REMARK 465     PRO H   230                                                      
REMARK 465     GLN H   231                                                      
REMARK 465     PHE H   232                                                      
REMARK 465     GLU H   233                                                      
REMARK 465     LYS H   234                                                      
REMARK 465     ASP L     1                                                      
REMARK 465     GLU L   212                                                      
REMARK 465     ALA L   213                                                      
REMARK 465     GLN A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     LEU A    33                                                      
REMARK 465     VAL A   119                                                      
REMARK 465     ILE A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     PRO A   122                                                      
REMARK 465     PHE A   123                                                      
REMARK 465     PHE A   124                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     GLY A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     ILE A   128                                                      
REMARK 465     ARG A   129                                                      
REMARK 465     LYS I   136                                                      
REMARK 465     SER I   137                                                      
REMARK 465     THR I   138                                                      
REMARK 465     SER I   139                                                      
REMARK 465     GLY I   140                                                      
REMARK 465     LYS I   221                                                      
REMARK 465     SER I   222                                                      
REMARK 465     GLU I   223                                                      
REMARK 465     PHE I   224                                                      
REMARK 465     SER I   225                                                      
REMARK 465     ALA I   226                                                      
REMARK 465     TRP I   227                                                      
REMARK 465     SER I   228                                                      
REMARK 465     HIS I   229                                                      
REMARK 465     PRO I   230                                                      
REMARK 465     GLN I   231                                                      
REMARK 465     PHE I   232                                                      
REMARK 465     GLU I   233                                                      
REMARK 465     LYS I   234                                                      
REMARK 465     ASP M     1                                                      
REMARK 465     GLU M   212                                                      
REMARK 465     ALA M   213                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     MET B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ASP B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     ASN B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     VAL B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     LEU B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     LEU B    33                                                      
REMARK 465     VAL B   119                                                      
REMARK 465     ILE B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     PRO B   122                                                      
REMARK 465     PHE B   123                                                      
REMARK 465     PHE B   124                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     GLY B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     ILE B   128                                                      
REMARK 465     ARG B   129                                                      
REMARK 465     SER J   222                                                      
REMARK 465     GLU J   223                                                      
REMARK 465     PHE J   224                                                      
REMARK 465     SER J   225                                                      
REMARK 465     ALA J   226                                                      
REMARK 465     TRP J   227                                                      
REMARK 465     SER J   228                                                      
REMARK 465     HIS J   229                                                      
REMARK 465     PRO J   230                                                      
REMARK 465     GLN J   231                                                      
REMARK 465     PHE J   232                                                      
REMARK 465     GLU J   233                                                      
REMARK 465     LYS J   234                                                      
REMARK 465     ASP N     1                                                      
REMARK 465     GLU N   212                                                      
REMARK 465     ALA N   213                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     MET C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     THR C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     MET C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     ASP C    15                                                      
REMARK 465     SER C    16                                                      
REMARK 465     ASP C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     LYS C    19                                                      
REMARK 465     LYS C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     ASN C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     VAL C    25                                                      
REMARK 465     THR C    26                                                      
REMARK 465     LEU C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     GLU C    30                                                      
REMARK 465     ASP C    31                                                      
REMARK 465     THR C    32                                                      
REMARK 465     LEU C    33                                                      
REMARK 465     VAL C   119                                                      
REMARK 465     ILE C   120                                                      
REMARK 465     GLY C   121                                                      
REMARK 465     PRO C   122                                                      
REMARK 465     PHE C   123                                                      
REMARK 465     PHE C   124                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     GLY C   126                                                      
REMARK 465     SER C   127                                                      
REMARK 465     ILE C   128                                                      
REMARK 465     ARG C   129                                                      
REMARK 465     LYS K   136                                                      
REMARK 465     SER K   137                                                      
REMARK 465     THR K   138                                                      
REMARK 465     SER K   139                                                      
REMARK 465     GLY K   140                                                      
REMARK 465     GLY K   141                                                      
REMARK 465     SER K   222                                                      
REMARK 465     GLU K   223                                                      
REMARK 465     PHE K   224                                                      
REMARK 465     SER K   225                                                      
REMARK 465     ALA K   226                                                      
REMARK 465     TRP K   227                                                      
REMARK 465     SER K   228                                                      
REMARK 465     HIS K   229                                                      
REMARK 465     PRO K   230                                                      
REMARK 465     GLN K   231                                                      
REMARK 465     PHE K   232                                                      
REMARK 465     GLU K   233                                                      
REMARK 465     LYS K   234                                                      
REMARK 465     ASP O     1                                                      
REMARK 465     GLU O   212                                                      
REMARK 465     ALA O   213                                                      
REMARK 465     GLN D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     MET D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     THR D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     MET D    12                                                      
REMARK 465     LYS D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     ASP D    15                                                      
REMARK 465     SER D    16                                                      
REMARK 465     ASP D    17                                                      
REMARK 465     GLN D    18                                                      
REMARK 465     LYS D    19                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     SER D    21                                                      
REMARK 465     GLU D    22                                                      
REMARK 465     ASN D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     VAL D    25                                                      
REMARK 465     THR D    26                                                      
REMARK 465     LEU D    27                                                      
REMARK 465     ALA D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     GLU D    30                                                      
REMARK 465     ASP D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     LEU D    33                                                      
REMARK 465     VAL D   119                                                      
REMARK 465     ILE D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     PRO D   122                                                      
REMARK 465     PHE D   123                                                      
REMARK 465     PHE D   124                                                      
REMARK 465     ASP D   125                                                      
REMARK 465     GLY D   126                                                      
REMARK 465     SER D   127                                                      
REMARK 465     ILE D   128                                                      
REMARK 465     ARG D   129                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG M    60     OD2  ASP M    81              1.88            
REMARK 500   ND2  ASN O    52     CD2  HIS D    43              1.99            
REMARK 500   NH1  ARG O    60     OD2  ASP O    81              2.02            
REMARK 500   NH1  ARG L    60     OD2  ASP L    81              2.04            
REMARK 500   NH1  ARG N    60     OD2  ASP N    81              2.05            
REMARK 500   ND2  ASN L    52     CD2  HIS A    43              2.07            
REMARK 500   CD2  HIS H   207     OG   SER H   210              2.10            
REMARK 500   OH   TYR M   179     O    HOH M   216              2.11            
REMARK 500   ND2  ASN M    52     CD2  HIS B    43              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG L 191   CZ    ARG L 191   NH2     0.080                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP L  49   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ARG L 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ARG L 191   NE  -  CZ  -  NH2 ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ARG M 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    PRO J 220   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ASP N  49   N   -  CA  -  C   ANGL. DEV. = -19.5 DEGREES          
REMARK 500    ASP N  50   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG N 191   NE  -  CZ  -  NH1 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ARG N 191   NE  -  CZ  -  NH2 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP C  47   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASP C  47   CB  -  CG  -  OD2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG K  98   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG K  98   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP O  49   N   -  CA  -  C   ANGL. DEV. = -20.6 DEGREES          
REMARK 500    ARG O 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR H  28       90.03    -67.94                                   
REMARK 500    SER H  30        7.60    -62.49                                   
REMARK 500    LYS H  43     -157.13   -102.47                                   
REMARK 500    ASP H  62      -38.99    -35.69                                   
REMARK 500    LYS H  65      130.64    -34.43                                   
REMARK 500    LYS H  76     -167.27    -66.43                                   
REMARK 500    HIS H 102      -96.17   -101.07                                   
REMARK 500    SER H 122       95.50   -169.11                                   
REMARK 500    THR H 123      110.46     44.94                                   
REMARK 500    ASP H 151       35.35     71.78                                   
REMARK 500    PHE H 153      143.48    177.90                                   
REMARK 500    ASN H 162       71.09     26.04                                   
REMARK 500    SER H 163       50.99     24.57                                   
REMARK 500    PRO H 209      -17.20    -44.97                                   
REMARK 500    SER H 210       36.13   -144.66                                   
REMARK 500    ASN H 211       46.21     28.35                                   
REMARK 500    SER L  51       28.90   -150.09                                   
REMARK 500    LEU L 108      106.60    -41.82                                   
REMARK 500    PHE A  35       11.86   -156.71                                   
REMARK 500    ASP A  47       44.87   -104.85                                   
REMARK 500    GLN A  86      118.61   -162.17                                   
REMARK 500    CYS A  87      -69.77   -124.99                                   
REMARK 500    TYR A 110       45.75    -73.33                                   
REMARK 500    GLN A 112       51.49   -143.39                                   
REMARK 500    PRO I  41      124.49    -38.20                                   
REMARK 500    LYS I  43     -167.39   -110.49                                   
REMARK 500    LYS I  76     -169.63    -65.12                                   
REMARK 500    HIS I 102      -98.28   -100.48                                   
REMARK 500    SER M  51       27.95   -149.72                                   
REMARK 500    LEU M 108      110.00    -38.98                                   
REMARK 500    PHE B  35       14.93   -160.17                                   
REMARK 500    ASP B  47       44.88   -103.65                                   
REMARK 500    CYS B  87      -67.35   -127.42                                   
REMARK 500    TYR B 110       42.26    -72.16                                   
REMARK 500    GLN B 112       48.76   -148.71                                   
REMARK 500    PRO J  41      122.32    -36.62                                   
REMARK 500    LYS J  76     -175.43    -69.94                                   
REMARK 500    HIS J 102      -96.18   -107.67                                   
REMARK 500    SER J 135       -5.17    -51.03                                   
REMARK 500    SER J 139      -53.55   -132.37                                   
REMARK 500    ASP J 151       63.63     62.85                                   
REMARK 500    SER N  51       31.68   -153.20                                   
REMARK 500    ARG N  60      -38.60    -35.20                                   
REMARK 500    LEU N 108      107.51    -43.54                                   
REMARK 500    PHE C  35       17.21   -157.35                                   
REMARK 500    ASP C  46       27.11    -71.15                                   
REMARK 500    CYS C  87      -68.96   -128.25                                   
REMARK 500    GLN C  94      157.15    -49.34                                   
REMARK 500    TYR C 110       41.16    -71.83                                   
REMARK 500    GLN C 112       53.30   -143.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER L   93     GLY L   94                  -60.82                    
REMARK 500 ALA A   48     ILE A   49                  146.63                    
REMARK 500 ALA B   48     ILE B   49                  145.81                    
REMARK 500 ALA C   48     ILE C   49                  145.85                    
REMARK 500 ALA D   48     ILE D   49                  145.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL H   5        24.2      L          L   OUTSIDE RANGE           
REMARK 500    TYR L  48        21.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR M  48        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP M  50        21.1      L          L   OUTSIDE RANGE           
REMARK 500    TYR N  48        19.8      L          L   OUTSIDE RANGE           
REMARK 500    TYR O  48        20.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP O  49        45.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP O  50        22.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1REW   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF THE BMP TYPE I RECEPTOR BMPR-IA BOUND TO ITS              
REMARK 900 LIGAND BMP-2                                                         
REMARK 900 RELATED ID: 2K3G   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF THE FREE BMP TYPE I RECEPTOR BMPR-IA                
DBREF  3NH7 H    1   234  PDB    3NH7     PDB              1    234             
DBREF  3NH7 L    1   213  PDB    3NH7     PDB              1    213             
DBREF  3NH7 A    1   129  UNP    P36894   BMR1A_HUMAN     24    152             
DBREF  3NH7 I    1   234  PDB    3NH7     PDB              1    234             
DBREF  3NH7 M    1   213  PDB    3NH7     PDB              1    213             
DBREF  3NH7 B    1   129  UNP    P36894   BMR1A_HUMAN     24    152             
DBREF  3NH7 J    1   234  PDB    3NH7     PDB              1    234             
DBREF  3NH7 N    1   213  PDB    3NH7     PDB              1    213             
DBREF  3NH7 C    1   129  UNP    P36894   BMR1A_HUMAN     24    152             
DBREF  3NH7 K    1   234  PDB    3NH7     PDB              1    234             
DBREF  3NH7 O    1   213  PDB    3NH7     PDB              1    213             
DBREF  3NH7 D    1   129  UNP    P36894   BMR1A_HUMAN     24    152             
SEQRES   1 H  234  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  234  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  234  PHE THR PHE SER ASN TYR THR LEU ASN TRP VAL ARG GLN          
SEQRES   4 H  234  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR THR SER          
SEQRES   5 H  234  SER SER GLY SER LEU THR GLY TYR ALA ASP SER VAL LYS          
SEQRES   6 H  234  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 H  234  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  234  ALA VAL TYR TYR CYS ALA ARG GLU ARG TRP HIS VAL ARG          
SEQRES   9 H  234  GLY TYR PHE ASP HIS TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 H  234  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 H  234  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 H  234  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 H  234  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 H  234  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 H  234  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 H  234  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 H  234  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 H  234  SER GLU PHE SER ALA TRP SER HIS PRO GLN PHE GLU LYS          
SEQRES   1 L  213  ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA          
SEQRES   2 L  213  PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER          
SEQRES   3 L  213  LEU GLY SER LYS TYR VAL ILE TRP TYR GLN GLN LYS PRO          
SEQRES   4 L  213  GLY GLN ALA PRO VAL LEU VAL ILE TYR ASP ASP SER ASN          
SEQRES   5 L  213  ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN          
SEQRES   6 L  213  SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN          
SEQRES   7 L  213  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER THR PHE THR          
SEQRES   8 L  213  MET SER GLY ASN GLY THR VAL PHE GLY GLY GLY THR LYS          
SEQRES   9 L  213  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 L  213  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 L  213  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 L  213  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 L  213  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 L  213  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 L  213  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 L  213  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 L  213  ALA PRO THR GLU ALA                                          
SEQRES   1 A  129  GLN ASN LEU ASP SER MET LEU HIS GLY THR GLY MET LYS          
SEQRES   2 A  129  SER ASP SER ASP GLN LYS LYS SER GLU ASN GLY VAL THR          
SEQRES   3 A  129  LEU ALA PRO GLU ASP THR LEU PRO PHE LEU LYS CYS TYR          
SEQRES   4 A  129  CYS SER GLY HIS CYS PRO ASP ASP ALA ILE ASN ASN THR          
SEQRES   5 A  129  CYS ILE THR ASN GLY HIS CYS PHE ALA ILE ILE GLU GLU          
SEQRES   6 A  129  ASP ASP GLN GLY GLU THR THR LEU ALA SER GLY CYS MET          
SEQRES   7 A  129  LYS TYR GLU GLY SER ASP PHE GLN CYS LYS ASP SER PRO          
SEQRES   8 A  129  LYS ALA GLN LEU ARG ARG THR ILE GLU CYS CYS ARG THR          
SEQRES   9 A  129  ASN LEU CYS ASN GLN TYR LEU GLN PRO THR LEU PRO PRO          
SEQRES  10 A  129  VAL VAL ILE GLY PRO PHE PHE ASP GLY SER ILE ARG              
SEQRES   1 I  234  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 I  234  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 I  234  PHE THR PHE SER ASN TYR THR LEU ASN TRP VAL ARG GLN          
SEQRES   4 I  234  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR THR SER          
SEQRES   5 I  234  SER SER GLY SER LEU THR GLY TYR ALA ASP SER VAL LYS          
SEQRES   6 I  234  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 I  234  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 I  234  ALA VAL TYR TYR CYS ALA ARG GLU ARG TRP HIS VAL ARG          
SEQRES   9 I  234  GLY TYR PHE ASP HIS TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 I  234  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 I  234  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 I  234  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 I  234  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 I  234  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 I  234  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 I  234  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 I  234  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 I  234  SER GLU PHE SER ALA TRP SER HIS PRO GLN PHE GLU LYS          
SEQRES   1 M  213  ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA          
SEQRES   2 M  213  PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER          
SEQRES   3 M  213  LEU GLY SER LYS TYR VAL ILE TRP TYR GLN GLN LYS PRO          
SEQRES   4 M  213  GLY GLN ALA PRO VAL LEU VAL ILE TYR ASP ASP SER ASN          
SEQRES   5 M  213  ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN          
SEQRES   6 M  213  SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN          
SEQRES   7 M  213  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER THR PHE THR          
SEQRES   8 M  213  MET SER GLY ASN GLY THR VAL PHE GLY GLY GLY THR LYS          
SEQRES   9 M  213  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 M  213  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 M  213  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 M  213  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 M  213  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 M  213  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 M  213  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 M  213  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 M  213  ALA PRO THR GLU ALA                                          
SEQRES   1 B  129  GLN ASN LEU ASP SER MET LEU HIS GLY THR GLY MET LYS          
SEQRES   2 B  129  SER ASP SER ASP GLN LYS LYS SER GLU ASN GLY VAL THR          
SEQRES   3 B  129  LEU ALA PRO GLU ASP THR LEU PRO PHE LEU LYS CYS TYR          
SEQRES   4 B  129  CYS SER GLY HIS CYS PRO ASP ASP ALA ILE ASN ASN THR          
SEQRES   5 B  129  CYS ILE THR ASN GLY HIS CYS PHE ALA ILE ILE GLU GLU          
SEQRES   6 B  129  ASP ASP GLN GLY GLU THR THR LEU ALA SER GLY CYS MET          
SEQRES   7 B  129  LYS TYR GLU GLY SER ASP PHE GLN CYS LYS ASP SER PRO          
SEQRES   8 B  129  LYS ALA GLN LEU ARG ARG THR ILE GLU CYS CYS ARG THR          
SEQRES   9 B  129  ASN LEU CYS ASN GLN TYR LEU GLN PRO THR LEU PRO PRO          
SEQRES  10 B  129  VAL VAL ILE GLY PRO PHE PHE ASP GLY SER ILE ARG              
SEQRES   1 J  234  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 J  234  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 J  234  PHE THR PHE SER ASN TYR THR LEU ASN TRP VAL ARG GLN          
SEQRES   4 J  234  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR THR SER          
SEQRES   5 J  234  SER SER GLY SER LEU THR GLY TYR ALA ASP SER VAL LYS          
SEQRES   6 J  234  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 J  234  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 J  234  ALA VAL TYR TYR CYS ALA ARG GLU ARG TRP HIS VAL ARG          
SEQRES   9 J  234  GLY TYR PHE ASP HIS TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 J  234  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 J  234  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 J  234  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 J  234  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 J  234  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 J  234  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 J  234  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 J  234  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 J  234  SER GLU PHE SER ALA TRP SER HIS PRO GLN PHE GLU LYS          
SEQRES   1 N  213  ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA          
SEQRES   2 N  213  PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER          
SEQRES   3 N  213  LEU GLY SER LYS TYR VAL ILE TRP TYR GLN GLN LYS PRO          
SEQRES   4 N  213  GLY GLN ALA PRO VAL LEU VAL ILE TYR ASP ASP SER ASN          
SEQRES   5 N  213  ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN          
SEQRES   6 N  213  SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN          
SEQRES   7 N  213  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER THR PHE THR          
SEQRES   8 N  213  MET SER GLY ASN GLY THR VAL PHE GLY GLY GLY THR LYS          
SEQRES   9 N  213  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 N  213  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 N  213  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 N  213  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 N  213  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 N  213  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 N  213  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 N  213  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 N  213  ALA PRO THR GLU ALA                                          
SEQRES   1 C  129  GLN ASN LEU ASP SER MET LEU HIS GLY THR GLY MET LYS          
SEQRES   2 C  129  SER ASP SER ASP GLN LYS LYS SER GLU ASN GLY VAL THR          
SEQRES   3 C  129  LEU ALA PRO GLU ASP THR LEU PRO PHE LEU LYS CYS TYR          
SEQRES   4 C  129  CYS SER GLY HIS CYS PRO ASP ASP ALA ILE ASN ASN THR          
SEQRES   5 C  129  CYS ILE THR ASN GLY HIS CYS PHE ALA ILE ILE GLU GLU          
SEQRES   6 C  129  ASP ASP GLN GLY GLU THR THR LEU ALA SER GLY CYS MET          
SEQRES   7 C  129  LYS TYR GLU GLY SER ASP PHE GLN CYS LYS ASP SER PRO          
SEQRES   8 C  129  LYS ALA GLN LEU ARG ARG THR ILE GLU CYS CYS ARG THR          
SEQRES   9 C  129  ASN LEU CYS ASN GLN TYR LEU GLN PRO THR LEU PRO PRO          
SEQRES  10 C  129  VAL VAL ILE GLY PRO PHE PHE ASP GLY SER ILE ARG              
SEQRES   1 K  234  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 K  234  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 K  234  PHE THR PHE SER ASN TYR THR LEU ASN TRP VAL ARG GLN          
SEQRES   4 K  234  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR THR SER          
SEQRES   5 K  234  SER SER GLY SER LEU THR GLY TYR ALA ASP SER VAL LYS          
SEQRES   6 K  234  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 K  234  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 K  234  ALA VAL TYR TYR CYS ALA ARG GLU ARG TRP HIS VAL ARG          
SEQRES   9 K  234  GLY TYR PHE ASP HIS TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 K  234  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 K  234  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 K  234  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 K  234  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 K  234  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 K  234  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 K  234  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 K  234  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 K  234  SER GLU PHE SER ALA TRP SER HIS PRO GLN PHE GLU LYS          
SEQRES   1 O  213  ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA          
SEQRES   2 O  213  PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER          
SEQRES   3 O  213  LEU GLY SER LYS TYR VAL ILE TRP TYR GLN GLN LYS PRO          
SEQRES   4 O  213  GLY GLN ALA PRO VAL LEU VAL ILE TYR ASP ASP SER ASN          
SEQRES   5 O  213  ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN          
SEQRES   6 O  213  SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN          
SEQRES   7 O  213  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER THR PHE THR          
SEQRES   8 O  213  MET SER GLY ASN GLY THR VAL PHE GLY GLY GLY THR LYS          
SEQRES   9 O  213  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 O  213  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 O  213  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 O  213  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 O  213  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 O  213  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 O  213  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 O  213  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 O  213  ALA PRO THR GLU ALA                                          
SEQRES   1 D  129  GLN ASN LEU ASP SER MET LEU HIS GLY THR GLY MET LYS          
SEQRES   2 D  129  SER ASP SER ASP GLN LYS LYS SER GLU ASN GLY VAL THR          
SEQRES   3 D  129  LEU ALA PRO GLU ASP THR LEU PRO PHE LEU LYS CYS TYR          
SEQRES   4 D  129  CYS SER GLY HIS CYS PRO ASP ASP ALA ILE ASN ASN THR          
SEQRES   5 D  129  CYS ILE THR ASN GLY HIS CYS PHE ALA ILE ILE GLU GLU          
SEQRES   6 D  129  ASP ASP GLN GLY GLU THR THR LEU ALA SER GLY CYS MET          
SEQRES   7 D  129  LYS TYR GLU GLY SER ASP PHE GLN CYS LYS ASP SER PRO          
SEQRES   8 D  129  LYS ALA GLN LEU ARG ARG THR ILE GLU CYS CYS ARG THR          
SEQRES   9 D  129  ASN LEU CYS ASN GLN TYR LEU GLN PRO THR LEU PRO PRO          
SEQRES  10 D  129  VAL VAL ILE GLY PRO PHE PHE ASP GLY SER ILE ARG              
FORMUL  13  HOH   *27(H2 O)                                                     
HELIX    1   1 THR H   28  TYR H   32  5                                   5    
HELIX    2   2 ARG H   87  THR H   91  5                                   5    
HELIX    3   3 SER H  163  ALA H  165  5                                   3    
HELIX    4   4 LYS H  208  ASN H  211  5                                   4    
HELIX    5   5 SER L   26  LYS L   30  5                                   5    
HELIX    6   6 GLN L   78  GLU L   82  5                                   5    
HELIX    7   7 SER L  123  ALA L  129  1                                   7    
HELIX    8   8 THR L  183  HIS L  190  1                                   8    
HELIX    9   9 THR I   28  TYR I   32  5                                   5    
HELIX   10  10 ARG I   87  THR I   91  5                                   5    
HELIX   11  11 SER I  163  ALA I  165  5                                   3    
HELIX   12  12 SER I  194  LEU I  196  5                                   3    
HELIX   13  13 LYS I  208  ASN I  211  5                                   4    
HELIX   14  14 SER M   26  LYS M   30  5                                   5    
HELIX   15  15 GLN M   78  GLU M   82  5                                   5    
HELIX   16  16 SER M  123  GLN M  128  1                                   6    
HELIX   17  17 THR M  183  HIS M  190  1                                   8    
HELIX   18  18 THR J   28  TYR J   32  5                                   5    
HELIX   19  19 ARG J   87  THR J   91  5                                   5    
HELIX   20  20 SER J  163  ALA J  165  5                                   3    
HELIX   21  21 LYS J  208  ASN J  211  5                                   4    
HELIX   22  22 SER N   26  LYS N   30  5                                   5    
HELIX   23  23 GLN N   78  GLU N   82  5                                   5    
HELIX   24  24 SER N  123  ALA N  129  1                                   7    
HELIX   25  25 THR N  183  HIS N  190  1                                   8    
HELIX   26  26 THR K   28  TYR K   32  5                                   5    
HELIX   27  27 ARG K   87  THR K   91  5                                   5    
HELIX   28  28 SER K  163  ALA K  165  5                                   3    
HELIX   29  29 LYS K  208  ASN K  211  5                                   4    
HELIX   30  30 SER O   26  LYS O   30  5                                   5    
HELIX   31  31 GLN O   78  GLU O   82  5                                   5    
HELIX   32  32 SER O  123  ALA O  129  1                                   7    
HELIX   33  33 THR O  183  HIS O  190  1                                   8    
SHEET    1   A 4 GLN H   3  SER H   7  0                                        
SHEET    2   A 4 LEU H  18  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3   A 4 THR H  78  MET H  83 -1  O  MET H  83   N  LEU H  18           
SHEET    4   A 4 PHE H  68  ASP H  73 -1  N  SER H  71   O  TYR H  80           
SHEET    1   B 6 GLY H  10  VAL H  12  0                                        
SHEET    2   B 6 THR H 114  VAL H 118  1  O  THR H 117   N  GLY H  10           
SHEET    3   B 6 ALA H  92  TRP H 101 -1  N  TYR H  94   O  THR H 114           
SHEET    4   B 6 LEU H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5   B 6 LEU H  45  THR H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6   B 6 THR H  58  TYR H  60 -1  O  GLY H  59   N  TYR H  50           
SHEET    1   C 4 GLY H  10  VAL H  12  0                                        
SHEET    2   C 4 THR H 114  VAL H 118  1  O  THR H 117   N  GLY H  10           
SHEET    3   C 4 ALA H  92  TRP H 101 -1  N  TYR H  94   O  THR H 114           
SHEET    4   C 4 GLY H 105  TRP H 110 -1  O  TYR H 106   N  ARG H 100           
SHEET    1   D 4 SER H 127  LEU H 131  0                                        
SHEET    2   D 4 ALA H 144  TYR H 152 -1  O  LEU H 148   N  PHE H 129           
SHEET    3   D 4 TYR H 183  THR H 190 -1  O  TYR H 183   N  TYR H 152           
SHEET    4   D 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  VAL H 188           
SHEET    1   E 4 SER H 127  LEU H 131  0                                        
SHEET    2   E 4 ALA H 144  TYR H 152 -1  O  LEU H 148   N  PHE H 129           
SHEET    3   E 4 TYR H 183  THR H 190 -1  O  TYR H 183   N  TYR H 152           
SHEET    4   E 4 VAL H 176  LEU H 177 -1  N  VAL H 176   O  SER H 184           
SHEET    1   F 3 THR H 158  TRP H 161  0                                        
SHEET    2   F 3 TYR H 201  HIS H 207 -1  O  ASN H 206   N  THR H 158           
SHEET    3   F 3 THR H 212  VAL H 218 -1  O  VAL H 218   N  TYR H 201           
SHEET    1   G 5 SER L   9  VAL L  12  0                                        
SHEET    2   G 5 THR L 103  VAL L 107  1  O  LYS L 104   N  VAL L  10           
SHEET    3   G 5 ALA L  83  PHE L  90 -1  N  TYR L  85   O  THR L 103           
SHEET    4   G 5 ILE L  33  GLN L  37 -1  N  GLN L  37   O  ASP L  84           
SHEET    5   G 5 VAL L  44  ILE L  47 -1  O  ILE L  47   N  TRP L  34           
SHEET    1   H 4 SER L   9  VAL L  12  0                                        
SHEET    2   H 4 THR L 103  VAL L 107  1  O  LYS L 104   N  VAL L  10           
SHEET    3   H 4 ALA L  83  PHE L  90 -1  N  TYR L  85   O  THR L 103           
SHEET    4   H 4 THR L  97  PHE L  99 -1  O  VAL L  98   N  THR L  89           
SHEET    1   I 3 ALA L  18  SER L  23  0                                        
SHEET    2   I 3 THR L  69  ILE L  74 -1  O  LEU L  72   N  ILE L  20           
SHEET    3   I 3 PHE L  61  SER L  66 -1  N  SER L  64   O  THR L  71           
SHEET    1   J 4 SER L 116  PHE L 120  0                                        
SHEET    2   J 4 ALA L 132  PHE L 141 -1  O  LEU L 137   N  THR L 118           
SHEET    3   J 4 TYR L 174  LEU L 182 -1  O  LEU L 182   N  ALA L 132           
SHEET    4   J 4 VAL L 161  THR L 163 -1  N  GLU L 162   O  TYR L 179           
SHEET    1   K 4 SER L 116  PHE L 120  0                                        
SHEET    2   K 4 ALA L 132  PHE L 141 -1  O  LEU L 137   N  THR L 118           
SHEET    3   K 4 TYR L 174  LEU L 182 -1  O  LEU L 182   N  ALA L 132           
SHEET    4   K 4 SER L 167  LYS L 168 -1  N  SER L 167   O  ALA L 175           
SHEET    1   L 4 SER L 155  PRO L 156  0                                        
SHEET    2   L 4 THR L 147  ALA L 152 -1  N  ALA L 152   O  SER L 155           
SHEET    3   L 4 TYR L 193  HIS L 199 -1  O  THR L 198   N  THR L 147           
SHEET    4   L 4 SER L 202  VAL L 208 -1  O  SER L 202   N  HIS L 199           
SHEET    1   M 2 LEU A  36  CYS A  38  0                                        
SHEET    2   M 2 CYS A  53  THR A  55 -1  O  THR A  55   N  LEU A  36           
SHEET    1   N 3 THR A  71  MET A  78  0                                        
SHEET    2   N 3 HIS A  58  GLU A  65 -1  N  ILE A  62   O  ALA A  74           
SHEET    3   N 3 ARG A  97  CYS A 102 -1  O  CYS A 102   N  CYS A  59           
SHEET    1   O 4 GLN I   3  SER I   7  0                                        
SHEET    2   O 4 LEU I  18  SER I  25 -1  O  SER I  21   N  SER I   7           
SHEET    3   O 4 THR I  78  MET I  83 -1  O  MET I  83   N  LEU I  18           
SHEET    4   O 4 PHE I  68  ASP I  73 -1  N  THR I  69   O  GLN I  82           
SHEET    1   P 6 GLY I  10  VAL I  12  0                                        
SHEET    2   P 6 THR I 114  VAL I 118  1  O  THR I 117   N  VAL I  12           
SHEET    3   P 6 ALA I  92  TRP I 101 -1  N  TYR I  94   O  THR I 114           
SHEET    4   P 6 LEU I  34  GLN I  39 -1  N  VAL I  37   O  TYR I  95           
SHEET    5   P 6 GLU I  46  THR I  51 -1  O  GLU I  46   N  ARG I  38           
SHEET    6   P 6 THR I  58  TYR I  60 -1  O  GLY I  59   N  TYR I  50           
SHEET    1   Q 4 GLY I  10  VAL I  12  0                                        
SHEET    2   Q 4 THR I 114  VAL I 118  1  O  THR I 117   N  VAL I  12           
SHEET    3   Q 4 ALA I  92  TRP I 101 -1  N  TYR I  94   O  THR I 114           
SHEET    4   Q 4 GLY I 105  TRP I 110 -1  O  TYR I 106   N  ARG I 100           
SHEET    1   R 4 SER I 127  LEU I 131  0                                        
SHEET    2   R 4 THR I 142  TYR I 152 -1  O  LYS I 150   N  SER I 127           
SHEET    3   R 4 TYR I 183  PRO I 192 -1  O  VAL I 191   N  ALA I 143           
SHEET    4   R 4 VAL I 170  THR I 172 -1  N  HIS I 171   O  VAL I 188           
SHEET    1   S 4 SER I 127  LEU I 131  0                                        
SHEET    2   S 4 THR I 142  TYR I 152 -1  O  LYS I 150   N  SER I 127           
SHEET    3   S 4 TYR I 183  PRO I 192 -1  O  VAL I 191   N  ALA I 143           
SHEET    4   S 4 VAL I 176  LEU I 177 -1  N  VAL I 176   O  SER I 184           
SHEET    1   T 3 THR I 158  TRP I 161  0                                        
SHEET    2   T 3 ILE I 202  HIS I 207 -1  O  ASN I 204   N  SER I 160           
SHEET    3   T 3 THR I 212  LYS I 217 -1  O  THR I 212   N  HIS I 207           
SHEET    1   U 5 SER M   9  VAL M  12  0                                        
SHEET    2   U 5 THR M 103  VAL M 107  1  O  LYS M 104   N  VAL M  10           
SHEET    3   U 5 ALA M  83  PHE M  90 -1  N  TYR M  85   O  THR M 103           
SHEET    4   U 5 VAL M  32  GLN M  37 -1  N  GLN M  37   O  ASP M  84           
SHEET    5   U 5 VAL M  44  ILE M  47 -1  O  ILE M  47   N  TRP M  34           
SHEET    1   V 4 SER M   9  VAL M  12  0                                        
SHEET    2   V 4 THR M 103  VAL M 107  1  O  LYS M 104   N  VAL M  10           
SHEET    3   V 4 ALA M  83  PHE M  90 -1  N  TYR M  85   O  THR M 103           
SHEET    4   V 4 THR M  97  PHE M  99 -1  O  VAL M  98   N  THR M  89           
SHEET    1   W 3 ALA M  18  SER M  23  0                                        
SHEET    2   W 3 THR M  69  ILE M  74 -1  O  ALA M  70   N  CYS M  22           
SHEET    3   W 3 PHE M  61  SER M  66 -1  N  SER M  62   O  THR M  73           
SHEET    1   X 4 SER M 116  PHE M 120  0                                        
SHEET    2   X 4 ALA M 132  PHE M 141 -1  O  LEU M 137   N  THR M 118           
SHEET    3   X 4 TYR M 174  LEU M 182 -1  O  TYR M 174   N  PHE M 141           
SHEET    4   X 4 VAL M 161  THR M 163 -1  N  GLU M 162   O  TYR M 179           
SHEET    1   Y 4 SER M 116  PHE M 120  0                                        
SHEET    2   Y 4 ALA M 132  PHE M 141 -1  O  LEU M 137   N  THR M 118           
SHEET    3   Y 4 TYR M 174  LEU M 182 -1  O  TYR M 174   N  PHE M 141           
SHEET    4   Y 4 SER M 167  LYS M 168 -1  N  SER M 167   O  ALA M 175           
SHEET    1   Z 4 SER M 155  PRO M 156  0                                        
SHEET    2   Z 4 THR M 147  ALA M 152 -1  N  ALA M 152   O  SER M 155           
SHEET    3   Z 4 TYR M 193  HIS M 199 -1  O  THR M 198   N  THR M 147           
SHEET    4   Z 4 SER M 202  VAL M 208 -1  O  SER M 202   N  HIS M 199           
SHEET    1  AA 2 LEU B  36  CYS B  38  0                                        
SHEET    2  AA 2 CYS B  53  THR B  55 -1  O  CYS B  53   N  CYS B  38           
SHEET    1  AB 3 THR B  71  MET B  78  0                                        
SHEET    2  AB 3 HIS B  58  GLU B  65 -1  N  HIS B  58   O  MET B  78           
SHEET    3  AB 3 ARG B  97  CYS B 102 -1  O  CYS B 102   N  CYS B  59           
SHEET    1  AC 4 GLN J   3  SER J   7  0                                        
SHEET    2  AC 4 LEU J  18  SER J  25 -1  O  SER J  21   N  SER J   7           
SHEET    3  AC 4 THR J  78  MET J  83 -1  O  LEU J  81   N  LEU J  20           
SHEET    4  AC 4 PHE J  68  ASP J  73 -1  N  THR J  69   O  GLN J  82           
SHEET    1  AD 6 GLY J  10  VAL J  12  0                                        
SHEET    2  AD 6 THR J 114  VAL J 118  1  O  THR J 117   N  VAL J  12           
SHEET    3  AD 6 ALA J  92  TRP J 101 -1  N  TYR J  94   O  THR J 114           
SHEET    4  AD 6 LEU J  34  GLN J  39 -1  N  VAL J  37   O  TYR J  95           
SHEET    5  AD 6 GLU J  46  THR J  51 -1  O  GLU J  46   N  ARG J  38           
SHEET    6  AD 6 THR J  58  TYR J  60 -1  O  GLY J  59   N  TYR J  50           
SHEET    1  AE 4 GLY J  10  VAL J  12  0                                        
SHEET    2  AE 4 THR J 114  VAL J 118  1  O  THR J 117   N  VAL J  12           
SHEET    3  AE 4 ALA J  92  TRP J 101 -1  N  TYR J  94   O  THR J 114           
SHEET    4  AE 4 GLY J 105  TRP J 110 -1  O  TYR J 106   N  ARG J 100           
SHEET    1  AF 4 SER J 127  LEU J 131  0                                        
SHEET    2  AF 4 THR J 142  TYR J 152 -1  O  LYS J 150   N  SER J 127           
SHEET    3  AF 4 TYR J 183  PRO J 192 -1  O  VAL J 191   N  ALA J 143           
SHEET    4  AF 4 VAL J 170  THR J 172 -1  N  HIS J 171   O  VAL J 188           
SHEET    1  AG 4 SER J 127  LEU J 131  0                                        
SHEET    2  AG 4 THR J 142  TYR J 152 -1  O  LYS J 150   N  SER J 127           
SHEET    3  AG 4 TYR J 183  PRO J 192 -1  O  VAL J 191   N  ALA J 143           
SHEET    4  AG 4 VAL J 176  LEU J 177 -1  N  VAL J 176   O  SER J 184           
SHEET    1  AH 3 THR J 158  TRP J 161  0                                        
SHEET    2  AH 3 ILE J 202  HIS J 207 -1  O  ASN J 204   N  SER J 160           
SHEET    3  AH 3 THR J 212  LYS J 217 -1  O  THR J 212   N  HIS J 207           
SHEET    1  AI 5 SER N   9  VAL N  12  0                                        
SHEET    2  AI 5 THR N 103  VAL N 107  1  O  LYS N 104   N  VAL N  10           
SHEET    3  AI 5 ALA N  83  PHE N  90 -1  N  ALA N  83   O  LEU N 105           
SHEET    4  AI 5 ILE N  33  GLN N  37 -1  N  GLN N  37   O  ASP N  84           
SHEET    5  AI 5 VAL N  44  ILE N  47 -1  O  ILE N  47   N  TRP N  34           
SHEET    1  AJ 4 SER N   9  VAL N  12  0                                        
SHEET    2  AJ 4 THR N 103  VAL N 107  1  O  LYS N 104   N  VAL N  10           
SHEET    3  AJ 4 ALA N  83  PHE N  90 -1  N  ALA N  83   O  LEU N 105           
SHEET    4  AJ 4 THR N  97  PHE N  99 -1  O  VAL N  98   N  THR N  89           
SHEET    1  AK 3 ALA N  18  SER N  23  0                                        
SHEET    2  AK 3 THR N  69  ILE N  74 -1  O  ALA N  70   N  CYS N  22           
SHEET    3  AK 3 PHE N  61  SER N  66 -1  N  SER N  62   O  THR N  73           
SHEET    1  AL 4 SER N 116  PHE N 120  0                                        
SHEET    2  AL 4 ALA N 132  PHE N 141 -1  O  LEU N 137   N  THR N 118           
SHEET    3  AL 4 TYR N 174  LEU N 182 -1  O  LEU N 182   N  ALA N 132           
SHEET    4  AL 4 VAL N 161  THR N 163 -1  N  GLU N 162   O  TYR N 179           
SHEET    1  AM 4 SER N 116  PHE N 120  0                                        
SHEET    2  AM 4 ALA N 132  PHE N 141 -1  O  LEU N 137   N  THR N 118           
SHEET    3  AM 4 TYR N 174  LEU N 182 -1  O  LEU N 182   N  ALA N 132           
SHEET    4  AM 4 SER N 167  LYS N 168 -1  N  SER N 167   O  ALA N 175           
SHEET    1  AN 4 SER N 155  PRO N 156  0                                        
SHEET    2  AN 4 THR N 147  ALA N 152 -1  N  ALA N 152   O  SER N 155           
SHEET    3  AN 4 TYR N 193  HIS N 199 -1  O  GLN N 196   N  ALA N 149           
SHEET    4  AN 4 SER N 202  VAL N 208 -1  O  SER N 202   N  HIS N 199           
SHEET    1  AO 2 LEU C  36  CYS C  38  0                                        
SHEET    2  AO 2 CYS C  53  THR C  55 -1  O  THR C  55   N  LEU C  36           
SHEET    1  AP 3 THR C  71  MET C  78  0                                        
SHEET    2  AP 3 HIS C  58  GLU C  65 -1  N  HIS C  58   O  MET C  78           
SHEET    3  AP 3 ARG C  97  CYS C 102 -1  O  THR C  98   N  ILE C  63           
SHEET    1  AQ 4 GLN K   3  SER K   7  0                                        
SHEET    2  AQ 4 LEU K  18  SER K  25 -1  O  SER K  21   N  SER K   7           
SHEET    3  AQ 4 THR K  78  MET K  83 -1  O  MET K  83   N  LEU K  18           
SHEET    4  AQ 4 PHE K  68  ASP K  73 -1  N  THR K  69   O  GLN K  82           
SHEET    1  AR 6 GLY K  10  VAL K  12  0                                        
SHEET    2  AR 6 THR K 114  VAL K 118  1  O  THR K 117   N  VAL K  12           
SHEET    3  AR 6 ALA K  92  TRP K 101 -1  N  TYR K  94   O  THR K 114           
SHEET    4  AR 6 LEU K  34  GLN K  39 -1  N  VAL K  37   O  TYR K  95           
SHEET    5  AR 6 GLU K  46  THR K  51 -1  O  GLU K  46   N  ARG K  38           
SHEET    6  AR 6 THR K  58  TYR K  60 -1  O  GLY K  59   N  TYR K  50           
SHEET    1  AS 4 GLY K  10  VAL K  12  0                                        
SHEET    2  AS 4 THR K 114  VAL K 118  1  O  THR K 117   N  VAL K  12           
SHEET    3  AS 4 ALA K  92  TRP K 101 -1  N  TYR K  94   O  THR K 114           
SHEET    4  AS 4 GLY K 105  TRP K 110 -1  O  TYR K 106   N  ARG K 100           
SHEET    1  AT 4 SER K 127  LEU K 131  0                                        
SHEET    2  AT 4 ALA K 143  TYR K 152 -1  O  GLY K 146   N  LEU K 131           
SHEET    3  AT 4 TYR K 183  VAL K 191 -1  O  VAL K 191   N  ALA K 143           
SHEET    4  AT 4 VAL K 170  THR K 172 -1  N  HIS K 171   O  VAL K 188           
SHEET    1  AU 4 SER K 127  LEU K 131  0                                        
SHEET    2  AU 4 ALA K 143  TYR K 152 -1  O  GLY K 146   N  LEU K 131           
SHEET    3  AU 4 TYR K 183  VAL K 191 -1  O  VAL K 191   N  ALA K 143           
SHEET    4  AU 4 VAL K 176  LEU K 177 -1  N  VAL K 176   O  SER K 184           
SHEET    1  AV 3 THR K 158  TRP K 161  0                                        
SHEET    2  AV 3 ILE K 202  HIS K 207 -1  O  ASN K 204   N  SER K 160           
SHEET    3  AV 3 THR K 212  LYS K 217 -1  O  THR K 212   N  HIS K 207           
SHEET    1  AW 5 SER O   9  VAL O  12  0                                        
SHEET    2  AW 5 THR O 103  VAL O 107  1  O  THR O 106   N  VAL O  10           
SHEET    3  AW 5 ALA O  83  PHE O  90 -1  N  TYR O  85   O  THR O 103           
SHEET    4  AW 5 ILE O  33  GLN O  37 -1  N  GLN O  37   O  ASP O  84           
SHEET    5  AW 5 VAL O  44  ILE O  47 -1  O  ILE O  47   N  TRP O  34           
SHEET    1  AX 4 SER O   9  VAL O  12  0                                        
SHEET    2  AX 4 THR O 103  VAL O 107  1  O  THR O 106   N  VAL O  10           
SHEET    3  AX 4 ALA O  83  PHE O  90 -1  N  TYR O  85   O  THR O 103           
SHEET    4  AX 4 THR O  97  PHE O  99 -1  O  VAL O  98   N  THR O  89           
SHEET    1  AY 3 ALA O  18  SER O  23  0                                        
SHEET    2  AY 3 THR O  69  ILE O  74 -1  O  ALA O  70   N  CYS O  22           
SHEET    3  AY 3 PHE O  61  SER O  66 -1  N  SER O  62   O  THR O  73           
SHEET    1  AZ 4 SER O 116  PHE O 120  0                                        
SHEET    2  AZ 4 ALA O 132  PHE O 141 -1  O  LEU O 137   N  THR O 118           
SHEET    3  AZ 4 TYR O 174  LEU O 182 -1  O  LEU O 182   N  ALA O 132           
SHEET    4  AZ 4 VAL O 161  THR O 163 -1  N  GLU O 162   O  TYR O 179           
SHEET    1  BA 4 SER O 116  PHE O 120  0                                        
SHEET    2  BA 4 ALA O 132  PHE O 141 -1  O  LEU O 137   N  THR O 118           
SHEET    3  BA 4 TYR O 174  LEU O 182 -1  O  LEU O 182   N  ALA O 132           
SHEET    4  BA 4 SER O 167  LYS O 168 -1  N  SER O 167   O  ALA O 175           
SHEET    1  BB 4 SER O 155  PRO O 156  0                                        
SHEET    2  BB 4 THR O 147  ALA O 152 -1  N  ALA O 152   O  SER O 155           
SHEET    3  BB 4 TYR O 193  HIS O 199 -1  O  THR O 198   N  THR O 147           
SHEET    4  BB 4 SER O 202  VAL O 208 -1  O  SER O 202   N  HIS O 199           
SHEET    1  BC 2 LEU D  36  CYS D  38  0                                        
SHEET    2  BC 2 CYS D  53  THR D  55 -1  O  THR D  55   N  LEU D  36           
SHEET    1  BD 3 THR D  71  MET D  78  0                                        
SHEET    2  BD 3 HIS D  58  GLU D  65 -1  N  ILE D  62   O  ALA D  74           
SHEET    3  BD 3 ARG D  97  CYS D 102 -1  O  CYS D 102   N  CYS D  59           
SSBOND   1 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND   2 CYS H  147    CYS H  203                          1555   1555  2.01  
SSBOND   3 CYS L   22    CYS L   87                          1555   1555  2.08  
SSBOND   4 CYS L  136    CYS L  195                          1555   1555  2.02  
SSBOND   5 CYS A   38    CYS A   59                          1555   1555  2.02  
SSBOND   6 CYS A   40    CYS A   44                          1555   1555  2.05  
SSBOND   7 CYS A   53    CYS A   77                          1555   1555  2.02  
SSBOND   8 CYS A   87    CYS A  101                          1555   1555  2.05  
SSBOND   9 CYS A  102    CYS A  107                          1555   1555  2.04  
SSBOND  10 CYS I   22    CYS I   96                          1555   1555  2.06  
SSBOND  11 CYS I  147    CYS I  203                          1555   1555  2.03  
SSBOND  12 CYS M   22    CYS M   87                          1555   1555  2.04  
SSBOND  13 CYS M  136    CYS M  195                          1555   1555  2.03  
SSBOND  14 CYS B   38    CYS B   59                          1555   1555  2.02  
SSBOND  15 CYS B   40    CYS B   44                          1555   1555  2.07  
SSBOND  16 CYS B   53    CYS B   77                          1555   1555  2.04  
SSBOND  17 CYS B   87    CYS B  101                          1555   1555  2.03  
SSBOND  18 CYS B  102    CYS B  107                          1555   1555  2.05  
SSBOND  19 CYS J   22    CYS J   96                          1555   1555  2.02  
SSBOND  20 CYS J  147    CYS J  203                          1555   1555  2.02  
SSBOND  21 CYS N   22    CYS N   87                          1555   1555  2.07  
SSBOND  22 CYS N  136    CYS N  195                          1555   1555  2.02  
SSBOND  23 CYS C   38    CYS C   59                          1555   1555  2.03  
SSBOND  24 CYS C   40    CYS C   44                          1555   1555  2.04  
SSBOND  25 CYS C   53    CYS C   77                          1555   1555  2.03  
SSBOND  26 CYS C   87    CYS C  101                          1555   1555  2.03  
SSBOND  27 CYS C  102    CYS C  107                          1555   1555  2.02  
SSBOND  28 CYS K   22    CYS K   96                          1555   1555  2.07  
SSBOND  29 CYS K  147    CYS K  203                          1555   1555  2.02  
SSBOND  30 CYS O   22    CYS O   87                          1555   1555  2.03  
SSBOND  31 CYS O  136    CYS O  195                          1555   1555  2.02  
SSBOND  32 CYS D   38    CYS D   59                          1555   1555  2.02  
SSBOND  33 CYS D   40    CYS D   44                          1555   1555  2.03  
SSBOND  34 CYS D   53    CYS D   77                          1555   1555  2.05  
SSBOND  35 CYS D   87    CYS D  101                          1555   1555  2.04  
SSBOND  36 CYS D  102    CYS D  107                          1555   1555  2.03  
CISPEP   1 PHE H  153    PRO H  154          0       -12.28                     
CISPEP   2 GLU H  155    PRO H  156          0         1.43                     
CISPEP   3 TYR L  142    PRO L  143          0        -1.32                     
CISPEP   4 PHE I  153    PRO I  154          0        -1.08                     
CISPEP   5 GLU I  155    PRO I  156          0         1.79                     
CISPEP   6 TYR M  142    PRO M  143          0        -3.78                     
CISPEP   7 PHE J  153    PRO J  154          0        -0.31                     
CISPEP   8 GLU J  155    PRO J  156          0         1.26                     
CISPEP   9 TYR N  142    PRO N  143          0        -1.36                     
CISPEP  10 PHE K  153    PRO K  154          0        -1.93                     
CISPEP  11 GLU K  155    PRO K  156          0         6.70                     
CISPEP  12 TYR O  142    PRO O  143          0         0.17                     
CRYST1   89.320  129.255  100.239  90.00  92.27  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011196  0.000000  0.000444        0.00000                         
SCALE2      0.000000  0.007737  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009984        0.00000                         
ATOM      1  N   GLN H   1      16.028   1.577  22.330  1.00 81.65           N  
ANISOU    1  N   GLN H   1    11211   8041  11770  -1265   3138   2449       N  
ATOM      2  CA  GLN H   1      17.335   1.807  23.020  1.00 80.50           C  
ANISOU    2  CA  GLN H   1    11266   8049  11272   -872   3087   2662       C  
ATOM      3  C   GLN H   1      18.446   2.123  22.020  1.00 76.48           C  
ANISOU    3  C   GLN H   1    10884   7512  10662   -842   2796   2338       C  
ATOM      4  O   GLN H   1      19.247   1.262  21.659  1.00 76.94           O  
ANISOU    4  O   GLN H   1    11082   7253  10898   -820   2867   2354       O  
ATOM      5  CB  GLN H   1      17.696   0.602  23.896  1.00 85.61           C  
ANISOU    5  CB  GLN H   1    12026   8416  12084   -704   3453   3124       C  
ATOM      6  CG  GLN H   1      17.480  -0.766  23.244  1.00 89.67           C  
ANISOU    6  CG  GLN H   1    12556   8344  13171   -980   3693   3107       C  
ATOM      7  CD  GLN H   1      18.757  -1.317  22.632  1.00 89.46           C  
ANISOU    7  CD  GLN H   1    12729   8050  13210   -882   3620   3004       C  
ATOM      8  OE1 GLN H   1      19.452  -0.619  21.888  1.00 86.10           O  
ANISOU    8  OE1 GLN H   1    12358   7800  12557   -850   3291   2672       O  
ATOM      9  NE2 GLN H   1      19.081  -2.572  22.953  1.00 93.04           N  
ANISOU    9  NE2 GLN H   1    13291   8073  13987   -820   3948   3309       N  
ATOM     10  N   VAL H   2      18.467   3.368  21.561  1.00 71.75           N  
ANISOU   10  N   VAL H   2    10229   7238   9794   -837   2488   2054       N  
ATOM     11  CA  VAL H   2      19.373   3.786  20.498  1.00 67.75           C  
ANISOU   11  CA  VAL H   2     9806   6730   9204   -840   2221   1738       C  
ATOM     12  C   VAL H   2      20.776   3.199  20.626  1.00 66.58           C  
ANISOU   12  C   VAL H   2     9853   6426   9020   -622   2254   1855       C  
ATOM     13  O   VAL H   2      21.316   3.117  21.719  1.00 67.53           O  
ANISOU   13  O   VAL H   2    10042   6659   8956   -340   2356   2154       O  
ATOM     14  CB  VAL H   2      19.488   5.338  20.443  1.00 64.36           C  
ANISOU   14  CB  VAL H   2     9321   6711   8423   -728   1940   1562       C  
ATOM     15  CG1 VAL H   2      20.439   5.784  19.310  1.00 60.13           C  
ANISOU   15  CG1 VAL H   2     8862   6165   7820   -730   1698   1274       C  
ATOM     16  CG2 VAL H   2      18.111   5.952  20.266  1.00 64.34           C  
ANISOU   16  CG2 VAL H   2     9123   6875   8447   -915   1898   1445       C  
ATOM     17  N   GLN H   3      21.353   2.789  19.502  1.00 65.14           N  
ANISOU   17  N   GLN H   3     9742   6014   8992   -732   2166   1612       N  
ATOM     18  CA  GLN H   3      22.788   2.535  19.438  1.00 64.93           C  
ANISOU   18  CA  GLN H   3     9880   5921   8870   -511   2121   1644       C  
ATOM     19  C   GLN H   3      23.476   3.147  18.219  1.00 61.48           C  
ANISOU   19  C   GLN H   3     9463   5556   8339   -558   1856   1291       C  
ATOM     20  O   GLN H   3      22.905   3.251  17.137  1.00 61.46           O  
ANISOU   20  O   GLN H   3     9386   5509   8457   -796   1758   1004       O  
ATOM     21  CB  GLN H   3      23.084   1.054  19.477  1.00 69.75           C  
ANISOU   21  CB  GLN H   3    10602   6096   9804   -513   2380   1812       C  
ATOM     22  CG  GLN H   3      23.558   0.527  20.798  1.00 72.84           C  
ANISOU   22  CG  GLN H   3    11083   6482  10112   -207   2602   2260       C  
ATOM     23  CD  GLN H   3      23.943  -0.930  20.660  1.00 78.09           C  
ANISOU   23  CD  GLN H   3    11871   6660  11139   -201   2860   2411       C  
ATOM     24  OE1 GLN H   3      24.780  -1.289  19.817  1.00 77.63           O  
ANISOU   24  OE1 GLN H   3    11906   6416  11173   -202   2778   2206       O  
ATOM     25  NE2 GLN H   3      23.308  -1.794  21.458  1.00 82.74           N  
ANISOU   25  NE2 GLN H   3    12454   7018  11964   -197   3197   2772       N  
ATOM     26  N   LEU H   4      24.728   3.523  18.401  1.00 58.48           N  
ANISOU   26  N   LEU H   4     9171   5308   7739   -313   1750   1318       N  
ATOM     27  CA  LEU H   4      25.476   4.141  17.343  1.00 56.12           C  
ANISOU   27  CA  LEU H   4     8887   5092   7345   -327   1533   1038       C  
ATOM     28  C   LEU H   4      26.938   3.679  17.396  1.00 56.67           C  
ANISOU   28  C   LEU H   4     9085   5080   7368   -102   1542   1100       C  
ATOM     29  O   LEU H   4      27.634   3.965  18.354  1.00 57.75           O  
ANISOU   29  O   LEU H   4     9239   5397   7305    151   1536   1277       O  
ATOM     30  CB  LEU H   4      25.396   5.656  17.514  1.00 53.25           C  
ANISOU   30  CB  LEU H   4     8424   5095   6714   -271   1336    955       C  
ATOM     31  CG  LEU H   4      24.055   6.337  17.226  1.00 52.12           C  
ANISOU   31  CG  LEU H   4     8141   5078   6583   -469   1278    842       C  
ATOM     32  CD1 LEU H   4      24.124   7.829  17.511  1.00 49.08           C  
ANISOU   32  CD1 LEU H   4     7675   5014   5958   -365   1110    786       C  
ATOM     33  CD2 LEU H   4      23.654   6.109  15.782  1.00 52.03           C  
ANISOU   33  CD2 LEU H   4     8098   4949   6722   -697   1209    576       C  
ATOM     34  N   VAL H   5      27.435   2.976  16.386  1.00 56.29           N  
ANISOU   34  N   VAL H   5     9109   4792   7485   -172   1550    937       N  
ATOM     35  CA  VAL H   5      28.825   2.521  16.498  1.00 56.22           C  
ANISOU   35  CA  VAL H   5     9212   4719   7431     65   1570   1013       C  
ATOM     36  C   VAL H   5      29.776   2.826  15.327  1.00 55.01           C  
ANISOU   36  C   VAL H   5     9076   4602   7222     69   1415    749       C  
ATOM     37  O   VAL H   5      29.638   2.315  14.205  1.00 55.51           O  
ANISOU   37  O   VAL H   5     9163   4480   7449    -89   1416    527       O  
ATOM     38  CB  VAL H   5      28.950   1.050  17.069  1.00 59.49           C  
ANISOU   38  CB  VAL H   5     9740   4783   8079    163   1837   1268       C  
ATOM     39  CG1 VAL H   5      27.601   0.301  17.080  1.00 60.55           C  
ANISOU   39  CG1 VAL H   5     9844   4637   8525    -87   2028   1310       C  
ATOM     40  CG2 VAL H   5      30.052   0.271  16.379  1.00 59.02           C  
ANISOU   40  CG2 VAL H   5     9793   4501   8132    260   1862   1175       C  
ATOM     41  N   GLU H   6      30.741   3.692  15.614  1.00 53.89           N  
ANISOU   41  N   GLU H   6     8905   4724   6846    256   1284    760       N  
ATOM     42  CA  GLU H   6      31.718   4.133  14.625  1.00 52.95           C  
ANISOU   42  CA  GLU H   6     8779   4683   6658    283   1154    554       C  
ATOM     43  C   GLU H   6      32.757   3.058  14.401  1.00 55.09           C  
ANISOU   43  C   GLU H   6     9159   4748   7026    431   1247    579       C  
ATOM     44  O   GLU H   6      33.078   2.295  15.310  1.00 57.63           O  
ANISOU   44  O   GLU H   6     9547   4966   7384    612   1377    808       O  
ATOM     45  CB  GLU H   6      32.418   5.408  15.077  1.00 51.71           C  
ANISOU   45  CB  GLU H   6     8524   4847   6277    419   1008    551       C  
ATOM     46  CG  GLU H   6      31.489   6.510  15.567  1.00 53.97           C  
ANISOU   46  CG  GLU H   6     8702   5338   6466    333    930    554       C  
ATOM     47  CD  GLU H   6      31.148   6.399  17.055  1.00 58.39           C  
ANISOU   47  CD  GLU H   6     9248   5997   6939    472    999    775       C  
ATOM     48  OE1 GLU H   6      31.314   5.298  17.631  1.00 62.02           O  
ANISOU   48  OE1 GLU H   6     9797   6314   7455    594   1146    970       O  
ATOM     49  OE2 GLU H   6      30.684   7.403  17.658  1.00 59.54           O  
ANISOU   49  OE2 GLU H   6     9292   6367   6961    477    922    766       O  
ATOM     50  N   SER H   7      33.278   2.994  13.183  1.00 54.57           N  
ANISOU   50  N   SER H   7     9106   4636   6990    380   1192    357       N  
ATOM     51  CA  SER H   7      34.355   2.079  12.845  1.00 53.89           C  
ANISOU   51  CA  SER H   7     9111   4381   6984    535   1266    340       C  
ATOM     52  C   SER H   7      35.095   2.648  11.666  1.00 52.27           C  
ANISOU   52  C   SER H   7     8860   4319   6681    525   1149    113       C  
ATOM     53  O   SER H   7      34.630   3.581  11.009  1.00 50.93           O  
ANISOU   53  O   SER H   7     8607   4325   6420    380   1039    -22       O  
ATOM     54  CB  SER H   7      33.787   0.739  12.431  1.00 56.04           C  
ANISOU   54  CB  SER H   7     9483   4270   7538    424   1425    283       C  
ATOM     55  OG  SER H   7      33.189   0.865  11.168  1.00 55.91           O  
ANISOU   55  OG  SER H   7     9427   4247   7569    199   1352    -21       O  
ATOM     56  N   GLY H   8      36.242   2.071  11.361  1.00 53.26           N  
ANISOU   56  N   GLY H   8     9036   4374   6825    695   1189     86       N  
ATOM     57  CA  GLY H   8      36.921   2.427  10.123  1.00 50.93           C  
ANISOU   57  CA  GLY H   8     8702   4192   6456    689   1118   -127       C  
ATOM     58  C   GLY H   8      37.985   3.472  10.298  1.00 49.13           C  
ANISOU   58  C   GLY H   8     8362   4248   6056    823   1024    -85       C  
ATOM     59  O   GLY H   8      38.660   3.813   9.339  1.00 50.81           O  
ANISOU   59  O   GLY H   8     8528   4568   6210    840    992   -216       O  
ATOM     60  N   GLY H   9      38.168   3.958  11.521  1.00 48.40           N  
ANISOU   60  N   GLY H   9     8211   4287   5892    926    990     87       N  
ATOM     61  CA  GLY H   9      39.251   4.905  11.814  1.00 48.00           C  
ANISOU   61  CA  GLY H   9     8020   4496   5721   1054    901     89       C  
ATOM     62  C   GLY H   9      40.648   4.306  11.702  1.00 49.31           C  
ANISOU   62  C   GLY H   9     8184   4665   5887   1278    940     86       C  
ATOM     63  O   GLY H   9      40.865   3.371  10.944  1.00 49.13           O  
ANISOU   63  O   GLY H   9     8262   4457   5946   1306   1024     22       O  
ATOM     64  N   GLY H  10      41.605   4.860  12.438  1.00 50.31           N  
ANISOU   64  N   GLY H  10     8174   5016   5926   1443    873    125       N  
ATOM     65  CA  GLY H  10      42.955   4.283  12.488  1.00 54.00           C  
ANISOU   65  CA  GLY H  10     8610   5528   6382   1689    903    136       C  
ATOM     66  C   GLY H  10      44.062   5.167  11.945  1.00 54.03           C  
ANISOU   66  C   GLY H  10     8426   5745   6358   1704    841      0       C  
ATOM     67  O   GLY H  10      43.934   6.365  11.938  1.00 54.09           O  
ANISOU   67  O   GLY H  10     8295   5903   6355   1568    764    -69       O  
ATOM     68  N   LEU H  11      45.144   4.576  11.459  1.00 56.34           N  
ANISOU   68  N   LEU H  11     8706   6034   6668   1866    893    -37       N  
ATOM     69  CA  LEU H  11      46.256   5.370  10.931  1.00 55.95           C  
ANISOU   69  CA  LEU H  11     8454   6187   6617   1881    862   -153       C  
ATOM     70  C   LEU H  11      46.198   5.721   9.435  1.00 54.78           C  
ANISOU   70  C   LEU H  11     8312   5996   6505   1717    923   -261       C  
ATOM     71  O   LEU H  11      45.704   4.946   8.613  1.00 56.71           O  
ANISOU   71  O   LEU H  11     8726   6063   6761   1679    996   -295       O  
ATOM     72  CB  LEU H  11      47.573   4.689  11.270  1.00 59.10           C  
ANISOU   72  CB  LEU H  11     8781   6680   6993   2173    881   -134       C  
ATOM     73  CG  LEU H  11      48.207   5.256  12.536  1.00 61.02           C  
ANISOU   73  CG  LEU H  11     8814   7207   7164   2320    764   -123       C  
ATOM     74  CD1 LEU H  11      48.543   4.192  13.614  1.00 62.36           C  
ANISOU   74  CD1 LEU H  11     9046   7410   7240   2647    771     36       C  
ATOM     75  CD2 LEU H  11      49.415   6.133  12.140  1.00 62.22           C  
ANISOU   75  CD2 LEU H  11     8688   7587   7364   2314    728   -279       C  
ATOM     76  N   VAL H  12      46.701   6.901   9.085  1.00 52.41           N  
ANISOU   76  N   VAL H  12     7814   5868   6230   1629    902   -320       N  
ATOM     77  CA  VAL H  12      46.763   7.335   7.694  1.00 50.23           C  
ANISOU   77  CA  VAL H  12     7515   5606   5962   1519    983   -373       C  
ATOM     78  C   VAL H  12      47.874   8.351   7.545  1.00 51.11           C  
ANISOU   78  C   VAL H  12     7366   5904   6150   1522   1004   -402       C  
ATOM     79  O   VAL H  12      48.141   9.103   8.468  1.00 51.87           O  
ANISOU   79  O   VAL H  12     7293   6100   6316   1501    927   -420       O  
ATOM     80  CB  VAL H  12      45.531   8.113   7.284  1.00 48.20           C  
ANISOU   80  CB  VAL H  12     7306   5311   5697   1296    967   -353       C  
ATOM     81  CG1 VAL H  12      45.075   7.657   5.950  1.00 47.38           C  
ANISOU   81  CG1 VAL H  12     7330   5155   5519   1257   1042   -399       C  
ATOM     82  CG2 VAL H  12      44.425   8.009   8.324  1.00 47.93           C  
ANISOU   82  CG2 VAL H  12     7369   5186   5655   1228    882   -305       C  
ATOM     83  N   GLN H  13      48.500   8.407   6.374  1.00 51.98           N  
ANISOU   83  N   GLN H  13     7425   6069   6258   1542   1117   -421       N  
ATOM     84  CA  GLN H  13      49.468   9.463   6.095  1.00 50.51           C  
ANISOU   84  CA  GLN H  13     6974   6031   6188   1506   1180   -426       C  
ATOM     85  C   GLN H  13      48.747  10.739   5.723  1.00 47.73           C  
ANISOU   85  C   GLN H  13     6564   5661   5909   1294   1213   -362       C  
ATOM     86  O   GLN H  13      47.548  10.727   5.462  1.00 45.43           O  
ANISOU   86  O   GLN H  13     6444   5282   5534   1200   1190   -319       O  
ATOM     87  CB  GLN H  13      50.434   9.014   5.015  1.00 52.72           C  
ANISOU   87  CB  GLN H  13     7210   6392   6429   1633   1316   -439       C  
ATOM     88  CG  GLN H  13      51.225   7.828   5.528  1.00 57.45           C  
ANISOU   88  CG  GLN H  13     7840   7002   6989   1867   1283   -499       C  
ATOM     89  CD  GLN H  13      52.233   7.293   4.547  1.00 60.52           C  
ANISOU   89  CD  GLN H  13     8180   7477   7337   2025   1413   -533       C  
ATOM     90  OE1 GLN H  13      53.341   6.912   4.927  1.00 62.28           O  
ANISOU   90  OE1 GLN H  13     8268   7801   7595   2203   1415   -572       O  
ATOM     91  NE2 GLN H  13      51.856   7.254   3.272  1.00 61.66           N  
ANISOU   91  NE2 GLN H  13     8423   7617   7386   1984   1522   -526       N  
ATOM     92  N   PRO H  14      49.460  11.861   5.761  1.00 48.58           N  
ANISOU   92  N   PRO H  14     6414   5842   6201   1219   1270   -360       N  
ATOM     93  CA  PRO H  14      48.872  13.124   5.311  1.00 46.99           C  
ANISOU   93  CA  PRO H  14     6148   5592   6115   1039   1347   -267       C  
ATOM     94  C   PRO H  14      48.594  12.993   3.837  1.00 46.09           C  
ANISOU   94  C   PRO H  14     6145   5506   5863   1062   1494   -142       C  
ATOM     95  O   PRO H  14      49.432  12.468   3.120  1.00 47.53           O  
ANISOU   95  O   PRO H  14     6296   5783   5980   1186   1594   -143       O  
ATOM     96  CB  PRO H  14      50.007  14.129   5.535  1.00 47.99           C  
ANISOU   96  CB  PRO H  14     5947   5770   6516    984   1424   -308       C  
ATOM     97  CG  PRO H  14      50.835  13.517   6.660  1.00 48.84           C  
ANISOU   97  CG  PRO H  14     5948   5978   6629   1108   1284   -480       C  
ATOM     98  CD  PRO H  14      50.797  12.049   6.362  1.00 50.18           C  
ANISOU   98  CD  PRO H  14     6352   6165   6548   1295   1261   -458       C  
ATOM     99  N   GLY H  15      47.424  13.427   3.397  1.00 43.99           N  
ANISOU   99  N   GLY H  15     5998   5192   5524    969   1501    -47       N  
ATOM    100  CA  GLY H  15      47.090  13.409   1.989  1.00 45.45           C  
ANISOU  100  CA  GLY H  15     6264   5467   5538   1016   1630     69       C  
ATOM    101  C   GLY H  15      46.291  12.167   1.697  1.00 47.84           C  
ANISOU  101  C   GLY H  15     6812   5776   5589   1084   1530    -34       C  
ATOM    102  O   GLY H  15      45.770  11.978   0.589  1.00 49.78           O  
ANISOU  102  O   GLY H  15     7149   6129   5636   1132   1585     -4       O  
ATOM    103  N   GLY H  16      46.206  11.298   2.702  1.00 47.94           N  
ANISOU  103  N   GLY H  16     6918   5682   5616   1099   1391   -165       N  
ATOM    104  CA  GLY H  16      45.521  10.028   2.542  1.00 46.29           C  
ANISOU  104  CA  GLY H  16     6926   5413   5248   1148   1317   -279       C  
ATOM    105  C   GLY H  16      44.038  10.266   2.640  1.00 44.40           C  
ANISOU  105  C   GLY H  16     6797   5119   4955   1013   1233   -265       C  
ATOM    106  O   GLY H  16      43.591  11.396   2.805  1.00 42.64           O  
ANISOU  106  O   GLY H  16     6491   4911   4799    909   1234   -155       O  
ATOM    107  N   SER H  17      43.272   9.201   2.470  1.00 45.36           N  
ANISOU  107  N   SER H  17     7091   5170   4974   1017   1173   -386       N  
ATOM    108  CA  SER H  17      41.865   9.232   2.833  1.00 43.21           C  
ANISOU  108  CA  SER H  17     6909   4822   4685    882   1077   -398       C  
ATOM    109  C   SER H  17      41.486   7.992   3.612  1.00 42.18           C  
ANISOU  109  C   SER H  17     6921   4495   4610    878   1013   -501       C  
ATOM    110  O   SER H  17      42.073   6.930   3.426  1.00 43.10           O  
ANISOU  110  O   SER H  17     7107   4537   4731    989   1051   -600       O  
ATOM    111  CB  SER H  17      40.948   9.450   1.616  1.00 42.85           C  
ANISOU  111  CB  SER H  17     6891   4926   4465    850   1086   -427       C  
ATOM    112  OG  SER H  17      41.531   9.066   0.399  1.00 43.06           O  
ANISOU  112  OG  SER H  17     6914   5106   4342    980   1169   -499       O  
ATOM    113  N   LEU H  18      40.549   8.162   4.529  1.00 40.91           N  
ANISOU  113  N   LEU H  18     6792   4241   4509    765    937   -456       N  
ATOM    114  CA  LEU H  18      39.871   7.044   5.180  1.00 42.25           C  
ANISOU  114  CA  LEU H  18     7099   4214   4741    733    906   -515       C  
ATOM    115  C   LEU H  18      38.374   7.215   4.979  1.00 44.34           C  
ANISOU  115  C   LEU H  18     7397   4478   4974    568    851   -553       C  
ATOM    116  O   LEU H  18      37.880   8.329   4.746  1.00 44.50           O  
ANISOU  116  O   LEU H  18     7332   4642   4932    498    819   -485       O  
ATOM    117  CB  LEU H  18      40.112   7.075   6.676  1.00 39.98           C  
ANISOU  117  CB  LEU H  18     6796   3849   4547    772    875   -396       C  
ATOM    118  CG  LEU H  18      41.448   6.659   7.279  1.00 41.36           C  
ANISOU  118  CG  LEU H  18     6938   4016   4762    959    904   -358       C  
ATOM    119  CD1 LEU H  18      41.349   6.782   8.817  1.00 39.00           C  
ANISOU  119  CD1 LEU H  18     6613   3707   4497   1000    850   -243       C  
ATOM    120  CD2 LEU H  18      41.863   5.217   6.831  1.00 41.48           C  
ANISOU  120  CD2 LEU H  18     7082   3871   4806   1080    981   -443       C  
ATOM    121  N   ARG H  19      37.632   6.130   5.124  1.00 47.30           N  
ANISOU  121  N   ARG H  19     7879   4675   5416    508    852   -653       N  
ATOM    122  CA  ARG H  19      36.185   6.240   5.192  1.00 47.04           C  
ANISOU  122  CA  ARG H  19     7852   4632   5391    340    798   -687       C  
ATOM    123  C   ARG H  19      35.708   5.719   6.520  1.00 46.23           C  
ANISOU  123  C   ARG H  19     7807   4325   5433    294    813   -587       C  
ATOM    124  O   ARG H  19      35.941   4.561   6.826  1.00 49.26           O  
ANISOU  124  O   ARG H  19     8287   4491   5941    340    884   -614       O  
ATOM    125  CB  ARG H  19      35.561   5.396   4.103  1.00 50.90           C  
ANISOU  125  CB  ARG H  19     8381   5101   5858    277    796   -934       C  
ATOM    126  CG  ARG H  19      34.087   5.224   4.326  1.00 53.36           C  
ANISOU  126  CG  ARG H  19     8684   5356   6234     95    750  -1000       C  
ATOM    127  CD  ARG H  19      33.352   5.383   3.042  1.00 56.35           C  
ANISOU  127  CD  ARG H  19     8993   5953   6463     39    683  -1209       C  
ATOM    128  NE  ARG H  19      32.824   4.127   2.550  1.00 60.24           N  
ANISOU  128  NE  ARG H  19     9521   6301   7068    -47    691  -1506       N  
ATOM    129  CZ  ARG H  19      31.694   4.057   1.855  1.00 63.19           C  
ANISOU  129  CZ  ARG H  19     9810   6813   7386   -166    612  -1729       C  
ATOM    130  NH1 ARG H  19      31.009   5.173   1.576  1.00 60.78           N  
ANISOU  130  NH1 ARG H  19     9398   6805   6891   -182    525  -1643       N  
ATOM    131  NH2 ARG H  19      31.256   2.878   1.430  1.00 67.17           N  
ANISOU  131  NH2 ARG H  19    10322   7162   8039   -260    622  -2052       N  
ATOM    132  N   LEU H  20      35.061   6.563   7.309  1.00 44.81           N  
ANISOU  132  N   LEU H  20     7569   4216   5241    224    764   -458       N  
ATOM    133  CA  LEU H  20      34.418   6.146   8.566  1.00 45.57           C  
ANISOU  133  CA  LEU H  20     7706   4170   5439    185    788   -343       C  
ATOM    134  C   LEU H  20      32.944   5.692   8.365  1.00 47.38           C  
ANISOU  134  C   LEU H  20     7947   4312   5742     -4    791   -432       C  
ATOM    135  O   LEU H  20      32.171   6.309   7.625  1.00 47.51           O  
ANISOU  135  O   LEU H  20     7890   4482   5678   -110    722   -527       O  
ATOM    136  CB  LEU H  20      34.465   7.291   9.605  1.00 43.58           C  
ANISOU  136  CB  LEU H  20     7367   4065   5128    221    734   -188       C  
ATOM    137  CG  LEU H  20      35.686   8.218   9.813  1.00 42.34           C  
ANISOU  137  CG  LEU H  20     7117   4057   4913    350    700   -145       C  
ATOM    138  CD1 LEU H  20      35.582   9.033  11.073  1.00 39.82           C  
ANISOU  138  CD1 LEU H  20     6716   3838   4577    383    650    -49       C  
ATOM    139  CD2 LEU H  20      36.972   7.430   9.893  1.00 43.97           C  
ANISOU  139  CD2 LEU H  20     7364   4200   5141    517    750   -142       C  
ATOM    140  N   SER H  21      32.536   4.646   9.062  1.00 49.32           N  
ANISOU  140  N   SER H  21     8266   4321   6151    -38    882   -384       N  
ATOM    141  CA  SER H  21      31.138   4.241   9.042  1.00 50.37           C  
ANISOU  141  CA  SER H  21     8377   4359   6402   -235    903   -456       C  
ATOM    142  C   SER H  21      30.612   4.369  10.451  1.00 49.81           C  
ANISOU  142  C   SER H  21     8300   4252   6373   -234    956   -218       C  
ATOM    143  O   SER H  21      31.395   4.245  11.383  1.00 49.17           O  
ANISOU  143  O   SER H  21     8269   4138   6274    -64   1007    -29       O  
ATOM    144  CB  SER H  21      31.060   2.777   8.650  1.00 54.99           C  
ANISOU  144  CB  SER H  21     9043   4639   7212   -293   1013   -605       C  
ATOM    145  OG  SER H  21      32.048   2.486   7.673  1.00 58.07           O  
ANISOU  145  OG  SER H  21     9474   5039   7551   -189    998   -771       O  
ATOM    146  N   CYS H  22      29.304   4.596  10.625  1.00 49.40           N  
ANISOU  146  N   CYS H  22     8172   4237   6359   -401    944   -227       N  
ATOM    147  CA  CYS H  22      28.695   4.334  11.937  1.00 49.56           C  
ANISOU  147  CA  CYS H  22     8197   4169   6464   -407   1048     -4       C  
ATOM    148  C   CYS H  22      27.321   3.678  11.859  1.00 49.91           C  
ANISOU  148  C   CYS H  22     8189   4062   6714   -634   1128    -74       C  
ATOM    149  O   CYS H  22      26.414   4.174  11.207  1.00 49.22           O  
ANISOU  149  O   CYS H  22     7989   4119   6591   -788   1034   -241       O  
ATOM    150  CB  CYS H  22      28.733   5.558  12.866  1.00 49.68           C  
ANISOU  150  CB  CYS H  22     8148   4444   6284   -301    973    161       C  
ATOM    151  SG  CYS H  22      27.183   6.386  13.141  1.00 51.27           S  
ANISOU  151  SG  CYS H  22     8216   4815   6450   -460    926    166       S  
ATOM    152  N   ALA H  23      27.211   2.515  12.499  1.00 51.83           N  
ANISOU  152  N   ALA H  23     8502   4001   7188   -643   1318     57       N  
ATOM    153  CA  ALA H  23      26.042   1.646  12.367  1.00 52.57           C  
ANISOU  153  CA  ALA H  23     8540   3860   7575   -879   1440    -33       C  
ATOM    154  C   ALA H  23      24.976   2.024  13.387  1.00 52.28           C  
ANISOU  154  C   ALA H  23     8411   3916   7537   -945   1505    177       C  
ATOM    155  O   ALA H  23      25.252   2.046  14.579  1.00 53.73           O  
ANISOU  155  O   ALA H  23     8648   4111   7656   -777   1608    492       O  
ATOM    156  CB  ALA H  23      26.447   0.208  12.531  1.00 52.95           C  
ANISOU  156  CB  ALA H  23     8703   3486   7930   -859   1652     24       C  
ATOM    157  N   ALA H  24      23.774   2.356  12.926  1.00 50.65           N  
ANISOU  157  N   ALA H  24     8052   3821   7372  -1163   1438      0       N  
ATOM    158  CA  ALA H  24      22.728   2.757  13.840  1.00 50.04           C  
ANISOU  158  CA  ALA H  24     7868   3858   7286  -1223   1499    183       C  
ATOM    159  C   ALA H  24      21.821   1.581  14.102  1.00 54.37           C  
ANISOU  159  C   ALA H  24     8361   4081   8216  -1429   1725    211       C  
ATOM    160  O   ALA H  24      21.774   0.646  13.310  1.00 56.31           O  
ANISOU  160  O   ALA H  24     8606   4056   8735  -1584   1777    -25       O  
ATOM    161  CB  ALA H  24      21.941   3.919  13.275  1.00 46.87           C  
ANISOU  161  CB  ALA H  24     7314   3800   6696  -1309   1299      7       C  
ATOM    162  N   SER H  25      21.095   1.640  15.215  1.00 56.29           N  
ANISOU  162  N   SER H  25     8545   4352   8491  -1431   1871    489       N  
ATOM    163  CA  SER H  25      20.103   0.635  15.539  1.00 61.06           C  
ANISOU  163  CA  SER H  25     9059   4658   9482  -1646   2118    553       C  
ATOM    164  C   SER H  25      19.259   1.087  16.726  1.00 61.75           C  
ANISOU  164  C   SER H  25     9050   4925   9486  -1613   2232    860       C  
ATOM    165  O   SER H  25      19.661   1.992  17.462  1.00 59.37           O  
ANISOU  165  O   SER H  25     8797   4926   8836  -1373   2150   1056       O  
ATOM    166  CB  SER H  25      20.776  -0.704  15.840  1.00 64.28           C  
ANISOU  166  CB  SER H  25     9619   4609  10195  -1589   2373    723       C  
ATOM    167  OG  SER H  25      21.807  -0.534  16.786  1.00 63.75           O  
ANISOU  167  OG  SER H  25     9715   4621   9884  -1252   2422   1078       O  
ATOM    168  N   GLY H  26      18.102   0.449  16.912  1.00 64.38           N  
ANISOU  168  N   GLY H  26     9233   5077  10152  -1854   2428    881       N  
ATOM    169  CA  GLY H  26      17.204   0.797  18.007  1.00 65.29           C  
ANISOU  169  CA  GLY H  26     9233   5363  10211  -1836   2568   1173       C  
ATOM    170  C   GLY H  26      16.390   2.047  17.713  1.00 62.68           C  
ANISOU  170  C   GLY H  26     8727   5462   9628  -1898   2330    978       C  
ATOM    171  O   GLY H  26      15.737   2.597  18.595  1.00 63.12           O  
ANISOU  171  O   GLY H  26     8689   5746   9546  -1833   2392   1187       O  
ATOM    172  N   PHE H  27      16.468   2.530  16.482  1.00 59.81           N  
ANISOU  172  N   PHE H  27     8320   5227   9177  -1985   2062    592       N  
ATOM    173  CA  PHE H  27      15.576   3.590  16.042  1.00 58.35           C  
ANISOU  173  CA  PHE H  27     7946   5412   8813  -2059   1857    393       C  
ATOM    174  C   PHE H  27      15.340   3.521  14.539  1.00 58.73           C  
ANISOU  174  C   PHE H  27     7890   5490   8936  -2245   1660    -54       C  
ATOM    175  O   PHE H  27      16.167   3.018  13.797  1.00 56.77           O  
ANISOU  175  O   PHE H  27     7760   5068   8741  -2238   1609   -222       O  
ATOM    176  CB  PHE H  27      16.071   4.972  16.470  1.00 54.30           C  
ANISOU  176  CB  PHE H  27     7503   5258   7868  -1783   1682    514       C  
ATOM    177  CG  PHE H  27      17.333   5.396  15.815  1.00 51.56           C  
ANISOU  177  CG  PHE H  27     7322   4949   7320  -1622   1496    400       C  
ATOM    178  CD1 PHE H  27      18.536   4.767  16.111  1.00 52.39           C  
ANISOU  178  CD1 PHE H  27     7627   4832   7448  -1481   1583    537       C  
ATOM    179  CD2 PHE H  27      17.335   6.431  14.910  1.00 50.28           C  
ANISOU  179  CD2 PHE H  27     7105   5049   6948  -1593   1251    180       C  
ATOM    180  CE1 PHE H  27      19.732   5.165  15.513  1.00 49.66           C  
ANISOU  180  CE1 PHE H  27     7412   4532   6924  -1333   1422    433       C  
ATOM    181  CE2 PHE H  27      18.528   6.847  14.314  1.00 48.59           C  
ANISOU  181  CE2 PHE H  27     7032   4867   6564  -1443   1109    105       C  
ATOM    182  CZ  PHE H  27      19.734   6.207  14.629  1.00 47.79           C  
ANISOU  182  CZ  PHE H  27     7117   4547   6494  -1322   1194    222       C  
ATOM    183  N   THR H  28      14.174   3.968  14.096  1.00 61.21           N  
ANISOU  183  N   THR H  28     7962   6043   9250  -2399   1556   -254       N  
ATOM    184  CA  THR H  28      13.917   3.979  12.679  1.00 62.95           C  
ANISOU  184  CA  THR H  28     8059   6385   9473  -2529   1348   -683       C  
ATOM    185  C   THR H  28      14.845   5.021  12.068  1.00 58.72           C  
ANISOU  185  C   THR H  28     7662   6106   8541  -2281   1110   -718       C  
ATOM    186  O   THR H  28      14.512   6.196  12.007  1.00 58.37           O  
ANISOU  186  O   THR H  28     7548   6405   8226  -2163    963   -687       O  
ATOM    187  CB  THR H  28      12.450   4.266  12.388  1.00 65.47           C  
ANISOU  187  CB  THR H  28     8064   6958   9853  -2715   1283   -877       C  
ATOM    188  OG1 THR H  28      12.370   5.040  11.191  1.00 65.03           O  
ANISOU  188  OG1 THR H  28     7922   7259   9527  -2651    996  -1169       O  
ATOM    189  CG2 THR H  28      11.829   5.050  13.538  1.00 64.78           C  
ANISOU  189  CG2 THR H  28     7916   7063   9635  -2617   1363   -554       C  
ATOM    190  N   PHE H  29      16.037   4.569  11.678  1.00 58.14           N  
ANISOU  190  N   PHE H  29     7788   5839   8464  -2195   1104   -756       N  
ATOM    191  CA  PHE H  29      17.180   5.391  11.193  1.00 53.88           C  
ANISOU  191  CA  PHE H  29     7409   5461   7602  -1955    938   -739       C  
ATOM    192  C   PHE H  29      16.843   6.558  10.266  1.00 52.56           C  
ANISOU  192  C   PHE H  29     7126   5698   7145  -1878    704   -896       C  
ATOM    193  O   PHE H  29      17.157   7.684  10.562  1.00 50.64           O  
ANISOU  193  O   PHE H  29     6934   5645   6663  -1690    633   -719       O  
ATOM    194  CB  PHE H  29      18.165   4.459  10.487  1.00 54.46           C  
ANISOU  194  CB  PHE H  29     7620   5283   7789  -1961    957   -906       C  
ATOM    195  CG  PHE H  29      19.423   5.121  10.006  1.00 52.16           C  
ANISOU  195  CG  PHE H  29     7487   5113   7218  -1730    830   -878       C  
ATOM    196  CD1 PHE H  29      20.346   5.644  10.901  1.00 49.51           C  
ANISOU  196  CD1 PHE H  29     7308   4760   6744  -1523    872   -574       C  
ATOM    197  CD2 PHE H  29      19.741   5.138   8.658  1.00 51.72           C  
ANISOU  197  CD2 PHE H  29     7412   5189   7049  -1715    684  -1168       C  
ATOM    198  CE1 PHE H  29      21.550   6.224  10.433  1.00 46.59           C  
ANISOU  198  CE1 PHE H  29     7057   4482   6163  -1332    771   -565       C  
ATOM    199  CE2 PHE H  29      20.942   5.737   8.201  1.00 49.20           C  
ANISOU  199  CE2 PHE H  29     7228   4975   6490  -1502    599  -1115       C  
ATOM    200  CZ  PHE H  29      21.841   6.249   9.083  1.00 45.40           C  
ANISOU  200  CZ  PHE H  29     6889   4442   5919  -1328    650   -819       C  
ATOM    201  N   SER H  30      16.217   6.276   9.131  1.00 55.04           N  
ANISOU  201  N   SER H  30     7277   6148   7489  -2009    591  -1236       N  
ATOM    202  CA  SER H  30      15.871   7.301   8.153  1.00 54.71           C  
ANISOU  202  CA  SER H  30     7113   6520   7153  -1902    379  -1371       C  
ATOM    203  C   SER H  30      14.888   8.399   8.615  1.00 53.49           C  
ANISOU  203  C   SER H  30     6809   6650   6864  -1847    329  -1223       C  
ATOM    204  O   SER H  30      14.455   9.221   7.804  1.00 53.70           O  
ANISOU  204  O   SER H  30     6711   7026   6666  -1747    168  -1318       O  
ATOM    205  CB  SER H  30      15.328   6.629   6.908  1.00 58.51           C  
ANISOU  205  CB  SER H  30     7418   7124   7689  -2046    269  -1797       C  
ATOM    206  OG  SER H  30      14.127   5.963   7.232  1.00 63.48           O  
ANISOU  206  OG  SER H  30     7832   7687   8601  -2301    340  -1943       O  
ATOM    207  N   ASN H  31      14.553   8.422   9.898  1.00 52.34           N  
ANISOU  207  N   ASN H  31     6674   6375   6840  -1881    474   -982       N  
ATOM    208  CA  ASN H  31      13.671   9.439  10.443  1.00 52.42           C  
ANISOU  208  CA  ASN H  31     6551   6634   6733  -1812    446   -841       C  
ATOM    209  C   ASN H  31      14.432  10.575  11.126  1.00 50.67           C  
ANISOU  209  C   ASN H  31     6491   6451   6309  -1563    441   -565       C  
ATOM    210  O   ASN H  31      13.801  11.485  11.686  1.00 51.93           O  
ANISOU  210  O   ASN H  31     6563   6790   6378  -1477    431   -442       O  
ATOM    211  CB  ASN H  31      12.768   8.824  11.500  1.00 54.77           C  
ANISOU  211  CB  ASN H  31     6734   6802   7273  -1987    625   -746       C  
ATOM    212  CG  ASN H  31      11.485   8.278  10.935  1.00 59.06           C  
ANISOU  212  CG  ASN H  31     6989   7459   7991  -2224    599  -1020       C  
ATOM    213  OD1 ASN H  31      10.555   7.967  11.684  1.00 61.67           O  
ANISOU  213  OD1 ASN H  31     7165   7755   8510  -2367    736   -950       O  
ATOM    214  ND2 ASN H  31      11.415   8.161   9.620  1.00 60.49           N  
ANISOU  214  ND2 ASN H  31     7075   7804   8105  -2258    427  -1342       N  
ATOM    215  N   TYR H  32      15.768  10.507  11.125  1.00 47.34           N  
ANISOU  215  N   TYR H  32     6287   5858   5841  -1452    455   -490       N  
ATOM    216  CA  TYR H  32      16.598  11.405  11.929  1.00 43.59           C  
ANISOU  216  CA  TYR H  32     5952   5369   5240  -1248    472   -265       C  
ATOM    217  C   TYR H  32      17.812  11.973  11.187  1.00 43.33           C  
ANISOU  217  C   TYR H  32     6051   5345   5067  -1092    383   -276       C  
ATOM    218  O   TYR H  32      18.395  11.325  10.326  1.00 42.09           O  
ANISOU  218  O   TYR H  32     5957   5109   4927  -1129    358   -406       O  
ATOM    219  CB  TYR H  32      17.109  10.682  13.163  1.00 41.48           C  
ANISOU  219  CB  TYR H  32     5808   4863   5089  -1252    635    -91       C  
ATOM    220  CG  TYR H  32      16.063  10.388  14.185  1.00 41.52           C  
ANISOU  220  CG  TYR H  32     5701   4877   5198  -1338    765     22       C  
ATOM    221  CD1 TYR H  32      15.357   9.190  14.170  1.00 43.69           C  
ANISOU  221  CD1 TYR H  32     5891   4997   5714  -1559    889    -35       C  
ATOM    222  CD2 TYR H  32      15.790  11.289  15.179  1.00 40.68           C  
ANISOU  222  CD2 TYR H  32     5562   4925   4970  -1201    783    179       C  
ATOM    223  CE1 TYR H  32      14.391   8.921  15.110  1.00 45.27           C  
ANISOU  223  CE1 TYR H  32     5970   5202   6027  -1641   1041    100       C  
ATOM    224  CE2 TYR H  32      14.807  11.031  16.132  1.00 42.88           C  
ANISOU  224  CE2 TYR H  32     5725   5246   5321  -1262    920    300       C  
ATOM    225  CZ  TYR H  32      14.104   9.849  16.099  1.00 44.55           C  
ANISOU  225  CZ  TYR H  32     5849   5309   5769  -1482   1057    281       C  
ATOM    226  OH  TYR H  32      13.122   9.615  17.057  1.00 45.71           O  
ANISOU  226  OH  TYR H  32     5865   5502   6002  -1541   1223    432       O  
ATOM    227  N   THR H  33      18.206  13.184  11.562  1.00 42.99           N  
ANISOU  227  N   THR H  33     6040   5385   4909   -917    351   -146       N  
ATOM    228  CA  THR H  33      19.417  13.781  11.053  1.00 42.30           C  
ANISOU  228  CA  THR H  33     6064   5269   4738   -775    308   -119       C  
ATOM    229  C   THR H  33      20.604  13.205  11.831  1.00 41.71           C  
ANISOU  229  C   THR H  33     6146   4976   4726   -743    386    -48       C  
ATOM    230  O   THR H  33      20.515  12.974  13.035  1.00 41.28           O  
ANISOU  230  O   THR H  33     6109   4859   4717   -737    463     52       O  
ATOM    231  CB  THR H  33      19.407  15.305  11.234  1.00 42.78           C  
ANISOU  231  CB  THR H  33     6083   5451   4720   -614    270    -19       C  
ATOM    232  OG1 THR H  33      18.345  15.886  10.460  1.00 44.83           O  
ANISOU  232  OG1 THR H  33     6198   5932   4903   -597    201    -54       O  
ATOM    233  CG2 THR H  33      20.766  15.909  10.797  1.00 42.87           C  
ANISOU  233  CG2 THR H  33     6197   5385   4706   -487    262     23       C  
ATOM    234  N   LEU H  34      21.707  12.962  11.131  1.00 40.08           N  
ANISOU  234  N   LEU H  34     6040   4686   4503   -699    371    -91       N  
ATOM    235  CA  LEU H  34      22.899  12.442  11.754  1.00 39.60           C  
ANISOU  235  CA  LEU H  34     6110   4449   4487   -641    433    -31       C  
ATOM    236  C   LEU H  34      24.036  13.444  11.622  1.00 39.05           C  
ANISOU  236  C   LEU H  34     6074   4404   4357   -492    397      8       C  
ATOM    237  O   LEU H  34      24.086  14.235  10.665  1.00 38.98           O  
ANISOU  237  O   LEU H  34     6023   4495   4292   -450    347    -15       O  
ATOM    238  CB  LEU H  34      23.284  11.118  11.122  1.00 41.58           C  
ANISOU  238  CB  LEU H  34     6440   4545   4814   -725    472   -132       C  
ATOM    239  CG  LEU H  34      22.400   9.987  11.647  1.00 45.94           C  
ANISOU  239  CG  LEU H  34     6969   4969   5515   -876    564   -140       C  
ATOM    240  CD1 LEU H  34      22.533   9.805  13.184  1.00 45.32           C  
ANISOU  240  CD1 LEU H  34     6938   4806   5474   -808    674     66       C  
ATOM    241  CD2 LEU H  34      20.954  10.241  11.262  1.00 46.97           C  
ANISOU  241  CD2 LEU H  34     6936   5261   5649  -1003    516   -233       C  
ATOM    242  N   ASN H  35      24.930  13.446  12.600  1.00 37.66           N  
ANISOU  242  N   ASN H  35     5956   4153   4199   -402    430     73       N  
ATOM    243  CA  ASN H  35      26.048  14.375  12.579  1.00 36.76           C  
ANISOU  243  CA  ASN H  35     5841   4049   4078   -283    403     77       C  
ATOM    244  C   ASN H  35      27.403  13.662  12.705  1.00 36.92           C  
ANISOU  244  C   ASN H  35     5952   3961   4116   -218    432     73       C  
ATOM    245  O   ASN H  35      27.516  12.564  13.280  1.00 36.21           O  
ANISOU  245  O   ASN H  35     5933   3785   4039   -218    483    109       O  
ATOM    246  CB  ASN H  35      25.919  15.411  13.708  1.00 36.44           C  
ANISOU  246  CB  ASN H  35     5724   4082   4039   -202    385    101       C  
ATOM    247  CG  ASN H  35      24.777  16.375  13.497  1.00 36.03           C  
ANISOU  247  CG  ASN H  35     5574   4132   3984   -224    359    106       C  
ATOM    248  OD1 ASN H  35      24.992  17.530  13.168  1.00 35.49           O  
ANISOU  248  OD1 ASN H  35     5448   4076   3959   -165    342     99       O  
ATOM    249  ND2 ASN H  35      23.548  15.900  13.669  1.00 38.42           N  
ANISOU  249  ND2 ASN H  35     5844   4497   4257   -305    370    126       N  
ATOM    250  N   TRP H  36      28.439  14.286  12.176  1.00 34.69           N  
ANISOU  250  N   TRP H  36     5656   3676   3849   -152    417     47       N  
ATOM    251  CA  TRP H  36      29.756  13.913  12.629  1.00 35.81           C  
ANISOU  251  CA  TRP H  36     5835   3762   4008    -58    433     39       C  
ATOM    252  C   TRP H  36      30.266  15.011  13.536  1.00 36.18           C  
ANISOU  252  C   TRP H  36     5782   3876   4089     28    398     11       C  
ATOM    253  O   TRP H  36      30.146  16.197  13.214  1.00 38.00           O  
ANISOU  253  O   TRP H  36     5926   4129   4384     16    384    -13       O  
ATOM    254  CB  TRP H  36      30.706  13.706  11.458  1.00 36.35           C  
ANISOU  254  CB  TRP H  36     5938   3785   4089    -43    453      5       C  
ATOM    255  CG  TRP H  36      30.469  12.440  10.789  1.00 37.07           C  
ANISOU  255  CG  TRP H  36     6126   3802   4155    -98    483    -26       C  
ATOM    256  CD1 TRP H  36      29.798  12.247   9.629  1.00 37.76           C  
ANISOU  256  CD1 TRP H  36     6219   3925   4203   -176    475    -85       C  
ATOM    257  CD2 TRP H  36      30.839  11.145  11.270  1.00 37.58           C  
ANISOU  257  CD2 TRP H  36     6288   3743   4248    -70    530    -17       C  
ATOM    258  NE1 TRP H  36      29.742  10.906   9.341  1.00 39.13           N  
ANISOU  258  NE1 TRP H  36     6478   3989   4401   -223    508   -160       N  
ATOM    259  CE2 TRP H  36      30.375  10.211  10.341  1.00 38.71           C  
ANISOU  259  CE2 TRP H  36     6490   3808   4409   -160    556   -100       C  
ATOM    260  CE3 TRP H  36      31.527  10.690  12.399  1.00 37.90           C  
ANISOU  260  CE3 TRP H  36     6360   3743   4298     43    558     52       C  
ATOM    261  CZ2 TRP H  36      30.597   8.849  10.487  1.00 39.86           C  
ANISOU  261  CZ2 TRP H  36     6737   3776   4633   -158    627   -116       C  
ATOM    262  CZ3 TRP H  36      31.755   9.352  12.537  1.00 38.14           C  
ANISOU  262  CZ3 TRP H  36     6496   3624   4373     74    632     84       C  
ATOM    263  CH2 TRP H  36      31.279   8.438  11.590  1.00 39.48           C  
ANISOU  263  CH2 TRP H  36     6734   3656   4610    -37    676      2       C  
ATOM    264  N   VAL H  37      30.800  14.635  14.685  1.00 35.47           N  
ANISOU  264  N   VAL H  37     5691   3825   3960    128    388      8       N  
ATOM    265  CA  VAL H  37      31.439  15.601  15.544  1.00 35.50           C  
ANISOU  265  CA  VAL H  37     5574   3924   3992    221    336    -87       C  
ATOM    266  C   VAL H  37      32.760  14.991  15.960  1.00 37.61           C  
ANISOU  266  C   VAL H  37     5843   4219   4228    345    326   -116       C  
ATOM    267  O   VAL H  37      32.827  13.780  16.174  1.00 40.14           O  
ANISOU  267  O   VAL H  37     6270   4514   4469    398    365    -18       O  
ATOM    268  CB  VAL H  37      30.607  15.824  16.765  1.00 35.12           C  
ANISOU  268  CB  VAL H  37     5483   4001   3862    271    311    -87       C  
ATOM    269  CG1 VAL H  37      31.305  16.790  17.739  1.00 36.19           C  
ANISOU  269  CG1 VAL H  37     5471   4267   4014    385    239   -252       C  
ATOM    270  CG2 VAL H  37      29.264  16.308  16.361  1.00 35.64           C  
ANISOU  270  CG2 VAL H  37     5541   4050   3951    161    324    -50       C  
ATOM    271  N   ARG H  38      33.813  15.794  16.076  1.00 38.22           N  
ANISOU  271  N   ARG H  38     5791   4340   4390    395    285   -248       N  
ATOM    272  CA  ARG H  38      35.118  15.239  16.495  1.00 39.20           C  
ANISOU  272  CA  ARG H  38     5882   4535   4475    532    262   -294       C  
ATOM    273  C   ARG H  38      35.791  15.953  17.672  1.00 38.71           C  
ANISOU  273  C   ARG H  38     5637   4667   4402    656    169   -477       C  
ATOM    274  O   ARG H  38      35.307  16.976  18.157  1.00 41.80           O  
ANISOU  274  O   ARG H  38     5923   5113   4847    626    126   -599       O  
ATOM    275  CB  ARG H  38      36.063  15.163  15.299  1.00 39.27           C  
ANISOU  275  CB  ARG H  38     5894   4433   4595    487    309   -300       C  
ATOM    276  CG  ARG H  38      36.793  16.451  15.036  1.00 39.08           C  
ANISOU  276  CG  ARG H  38     5688   4401   4759    442    301   -443       C  
ATOM    277  CD  ARG H  38      37.402  16.536  13.631  1.00 37.77           C  
ANISOU  277  CD  ARG H  38     5531   4115   4707    372    392   -389       C  
ATOM    278  NE  ARG H  38      37.699  17.932  13.331  1.00 37.48           N  
ANISOU  278  NE  ARG H  38     5328   4016   4898    295    430   -466       N  
ATOM    279  CZ  ARG H  38      38.303  18.375  12.239  1.00 38.72           C  
ANISOU  279  CZ  ARG H  38     5433   4080   5198    244    536   -414       C  
ATOM    280  NH1 ARG H  38      38.718  17.537  11.299  1.00 39.84           N  
ANISOU  280  NH1 ARG H  38     5673   4217   5248    271    596   -311       N  
ATOM    281  NH2 ARG H  38      38.504  19.675  12.098  1.00 40.03           N  
ANISOU  281  NH2 ARG H  38     5440   4154   5617    174    598   -463       N  
ATOM    282  N   GLN H  39      36.885  15.397  18.157  1.00 38.02           N  
ANISOU  282  N   GLN H  39     5502   4702   4240    812    133   -517       N  
ATOM    283  CA  GLN H  39      37.583  15.965  19.312  1.00 39.42           C  
ANISOU  283  CA  GLN H  39     5479   5130   4371    959     21   -732       C  
ATOM    284  C   GLN H  39      39.064  15.536  19.333  1.00 43.00           C  
ANISOU  284  C   GLN H  39     5836   5686   4818   1091    -13   -806       C  
ATOM    285  O   GLN H  39      39.385  14.342  19.453  1.00 44.27           O  
ANISOU  285  O   GLN H  39     6111   5885   4826   1238     18   -641       O  
ATOM    286  CB  GLN H  39      36.882  15.510  20.592  1.00 39.39           C  
ANISOU  286  CB  GLN H  39     5512   5342   4112   1127    -13   -660       C  
ATOM    287  CG  GLN H  39      37.342  16.169  21.866  1.00 40.33           C  
ANISOU  287  CG  GLN H  39     5414   5787   4124   1300   -144   -912       C  
ATOM    288  CD  GLN H  39      36.818  15.482  23.085  1.00 41.59           C  
ANISOU  288  CD  GLN H  39     5623   6210   3969   1531   -152   -777       C  
ATOM    289  OE1 GLN H  39      36.710  16.082  24.119  1.00 43.52           O  
ANISOU  289  OE1 GLN H  39     5719   6733   4083   1659   -246   -963       O  
ATOM    290  NE2 GLN H  39      36.499  14.203  22.972  1.00 43.93           N  
ANISOU  290  NE2 GLN H  39     6122   6419   4148   1595    -39   -453       N  
ATOM    291  N   ALA H  40      39.968  16.496  19.165  1.00 45.41           N  
ANISOU  291  N   ALA H  40     5922   6011   5320   1034    -59  -1048       N  
ATOM    292  CA  ALA H  40      41.414  16.188  19.147  1.00 49.32           C  
ANISOU  292  CA  ALA H  40     6280   6623   5836   1147    -94  -1149       C  
ATOM    293  C   ALA H  40      41.860  15.823  20.562  1.00 51.60           C  
ANISOU  293  C   ALA H  40     6450   7281   5874   1421   -225  -1259       C  
ATOM    294  O   ALA H  40      41.379  16.422  21.527  1.00 53.43           O  
ANISOU  294  O   ALA H  40     6581   7697   6023   1474   -314  -1414       O  
ATOM    295  CB  ALA H  40      42.224  17.390  18.611  1.00 49.81           C  
ANISOU  295  CB  ALA H  40     6103   6599   6225    988    -87  -1391       C  
ATOM    296  N   PRO H  41      42.769  14.851  20.701  1.00 51.51           N  
ANISOU  296  N   PRO H  41     6442   7406   5723   1624   -236  -1179       N  
ATOM    297  CA  PRO H  41      42.998  14.298  22.029  1.00 54.11           C  
ANISOU  297  CA  PRO H  41     6710   8108   5741   1941   -336  -1181       C  
ATOM    298  C   PRO H  41      43.075  15.399  23.081  1.00 56.53           C  
ANISOU  298  C   PRO H  41     6741   8724   6014   1993   -496  -1540       C  
ATOM    299  O   PRO H  41      43.909  16.304  22.978  1.00 59.58           O  
ANISOU  299  O   PRO H  41     6860   9164   6615   1903   -576  -1874       O  
ATOM    300  CB  PRO H  41      44.351  13.591  21.897  1.00 55.70           C  
ANISOU  300  CB  PRO H  41     6827   8435   5902   2127   -353  -1177       C  
ATOM    301  CG  PRO H  41      44.500  13.319  20.472  1.00 54.68           C  
ANISOU  301  CG  PRO H  41     6837   7941   5996   1925   -216  -1045       C  
ATOM    302  CD  PRO H  41      43.844  14.504  19.777  1.00 52.57           C  
ANISOU  302  CD  PRO H  41     6546   7435   5994   1601   -180  -1162       C  
ATOM    303  N   GLY H  42      42.198  15.352  24.075  1.00 56.46           N  
ANISOU  303  N   GLY H  42     6780   8911   5760   2129   -533  -1492       N  
ATOM    304  CA  GLY H  42      42.268  16.326  25.163  1.00 58.58           C  
ANISOU  304  CA  GLY H  42     6779   9527   5950   2223   -697  -1868       C  
ATOM    305  C   GLY H  42      41.989  17.784  24.832  1.00 56.79           C  
ANISOU  305  C   GLY H  42     6400   9111   6067   1936   -724  -2198       C  
ATOM    306  O   GLY H  42      42.243  18.654  25.642  1.00 57.03           O  
ANISOU  306  O   GLY H  42     6165   9399   6106   1992   -864  -2592       O  
ATOM    307  N   LYS H  43      41.504  18.058  23.628  1.00 55.07           N  
ANISOU  307  N   LYS H  43     6334   8448   6140   1643   -584  -2048       N  
ATOM    308  CA  LYS H  43      40.982  19.381  23.313  1.00 55.40           C  
ANISOU  308  CA  LYS H  43     6286   8268   6497   1398   -565  -2260       C  
ATOM    309  C   LYS H  43      39.468  19.317  23.344  1.00 52.62           C  
ANISOU  309  C   LYS H  43     6160   7797   6037   1349   -491  -2031       C  
ATOM    310  O   LYS H  43      38.911  18.432  23.982  1.00 52.44           O  
ANISOU  310  O   LYS H  43     6281   7960   5684   1531   -490  -1816       O  
ATOM    311  CB  LYS H  43      41.471  19.880  21.954  1.00 55.67           C  
ANISOU  311  CB  LYS H  43     6300   7921   6929   1134   -448  -2243       C  
ATOM    312  CG  LYS H  43      42.961  19.781  21.775  1.00 59.26           C  
ANISOU  312  CG  LYS H  43     6547   8471   7499   1170   -486  -2408       C  
ATOM    313  CD  LYS H  43      43.712  20.761  22.669  1.00 65.53           C  
ANISOU  313  CD  LYS H  43     6963   9503   8434   1202   -637  -2911       C  
ATOM    314  CE  LYS H  43      45.239  20.485  22.678  1.00 68.69           C  
ANISOU  314  CE  LYS H  43     7119  10098   8882   1290   -704  -3090       C  
ATOM    315  NZ  LYS H  43      45.811  20.391  21.293  1.00 68.68           N  
ANISOU  315  NZ  LYS H  43     7171   9760   9163   1100   -532  -2894       N  
ATOM    316  N   GLY H  44      38.813  20.247  22.650  1.00 50.70           N  
ANISOU  316  N   GLY H  44     5936   7246   6080   1113   -413  -2058       N  
ATOM    317  CA  GLY H  44      37.356  20.379  22.707  1.00 48.06           C  
ANISOU  317  CA  GLY H  44     5764   6824   5674   1062   -356  -1897       C  
ATOM    318  C   GLY H  44      36.533  19.807  21.556  1.00 43.73           C  
ANISOU  318  C   GLY H  44     5481   5980   5154    914   -212  -1519       C  
ATOM    319  O   GLY H  44      37.060  19.286  20.594  1.00 42.50           O  
ANISOU  319  O   GLY H  44     5411   5662   5076    843   -142  -1366       O  
ATOM    320  N   LEU H  45      35.215  19.901  21.654  1.00 43.37           N  
ANISOU  320  N   LEU H  45     5549   5893   5036    877   -170  -1392       N  
ATOM    321  CA  LEU H  45      34.381  19.338  20.611  1.00 42.45           C  
ANISOU  321  CA  LEU H  45     5650   5547   4931    744    -54  -1080       C  
ATOM    322  C   LEU H  45      34.386  20.254  19.383  1.00 41.44           C  
ANISOU  322  C   LEU H  45     5499   5133   5115    550     19  -1090       C  
ATOM    323  O   LEU H  45      34.255  21.456  19.509  1.00 41.06           O  
ANISOU  323  O   LEU H  45     5314   5018   5268    499     12  -1273       O  
ATOM    324  CB  LEU H  45      32.949  19.159  21.126  1.00 41.65           C  
ANISOU  324  CB  LEU H  45     5643   5519   4662    766    -30   -950       C  
ATOM    325  CG  LEU H  45      32.723  18.246  22.327  1.00 41.87           C  
ANISOU  325  CG  LEU H  45     5710   5826   4373    970    -52   -858       C  
ATOM    326  CD1 LEU H  45      31.241  18.154  22.619  1.00 40.07           C  
ANISOU  326  CD1 LEU H  45     5563   5622   4042    946      9   -707       C  
ATOM    327  CD2 LEU H  45      33.302  16.853  21.996  1.00 42.60           C  
ANISOU  327  CD2 LEU H  45     5945   5876   4366   1024      4   -629       C  
ATOM    328  N   GLU H  46      34.572  19.675  18.207  1.00 40.92           N  
ANISOU  328  N   GLU H  46     5560   4902   5087    464    101   -892       N  
ATOM    329  CA  GLU H  46      34.350  20.390  16.948  1.00 41.32           C  
ANISOU  329  CA  GLU H  46     5624   4720   5358    317    197   -810       C  
ATOM    330  C   GLU H  46      33.365  19.639  16.036  1.00 38.59           C  
ANISOU  330  C   GLU H  46     5474   4304   4886    255    260   -554       C  
ATOM    331  O   GLU H  46      33.619  18.492  15.694  1.00 37.87           O  
ANISOU  331  O   GLU H  46     5501   4224   4665    273    274   -444       O  
ATOM    332  CB  GLU H  46      35.680  20.619  16.206  1.00 42.81           C  
ANISOU  332  CB  GLU H  46     5721   4803   5740    278    248   -856       C  
ATOM    333  CG  GLU H  46      35.571  21.298  14.826  1.00 42.55           C  
ANISOU  333  CG  GLU H  46     5702   4552   5912    163    382   -714       C  
ATOM    334  CD  GLU H  46      36.926  21.383  14.141  1.00 45.80           C  
ANISOU  334  CD  GLU H  46     6021   4889   6493    139    455   -730       C  
ATOM    335  OE1 GLU H  46      37.821  20.573  14.494  1.00 47.33           O  
ANISOU  335  OE1 GLU H  46     6198   5203   6582    210    398   -800       O  
ATOM    336  OE2 GLU H  46      37.121  22.256  13.273  1.00 46.83           O  
ANISOU  336  OE2 GLU H  46     6083   4848   6863     65    584   -659       O  
ATOM    337  N   TRP H  47      32.254  20.289  15.676  1.00 37.59           N  
ANISOU  337  N   TRP H  47     5362   4113   4807    192    293   -487       N  
ATOM    338  CA  TRP H  47      31.280  19.771  14.724  1.00 38.37           C  
ANISOU  338  CA  TRP H  47     5595   4175   4807    128    339   -294       C  
ATOM    339  C   TRP H  47      31.859  19.791  13.323  1.00 40.55           C  
ANISOU  339  C   TRP H  47     5900   4347   5161     85    417   -196       C  
ATOM    340  O   TRP H  47      32.422  20.818  12.884  1.00 42.76           O  
ANISOU  340  O   TRP H  47     6078   4524   5643     75    480   -212       O  
ATOM    341  CB  TRP H  47      30.043  20.643  14.686  1.00 37.68           C  
ANISOU  341  CB  TRP H  47     5474   4079   4763    103    351   -262       C  
ATOM    342  CG  TRP H  47      28.996  20.245  13.660  1.00 38.36           C  
ANISOU  342  CG  TRP H  47     5652   4174   4748     47    382    -95       C  
ATOM    343  CD1 TRP H  47      27.991  19.320  13.830  1.00 39.30           C  
ANISOU  343  CD1 TRP H  47     5847   4385   4701     14    355    -39       C  
ATOM    344  CD2 TRP H  47      28.775  20.831  12.372  1.00 38.96           C  
ANISOU  344  CD2 TRP H  47     5723   4193   4886     33    447     23       C  
ATOM    345  NE1 TRP H  47      27.169  19.289  12.719  1.00 39.29           N  
ANISOU  345  NE1 TRP H  47     5871   4403   4655    -33    375     59       N  
ATOM    346  CE2 TRP H  47      27.627  20.199  11.809  1.00 39.97           C  
ANISOU  346  CE2 TRP H  47     5915   4423   4849     -2    427    110       C  
ATOM    347  CE3 TRP H  47      29.408  21.842  11.649  1.00 39.07           C  
ANISOU  347  CE3 TRP H  47     5669   4090   5085     56    534     74       C  
ATOM    348  CZ2 TRP H  47      27.136  20.521  10.544  1.00 39.94           C  
ANISOU  348  CZ2 TRP H  47     5908   4459   4807     13    464    230       C  
ATOM    349  CZ3 TRP H  47      28.928  22.162  10.401  1.00 40.38           C  
ANISOU  349  CZ3 TRP H  47     5851   4270   5219     81    601    246       C  
ATOM    350  CH2 TRP H  47      27.790  21.517   9.861  1.00 41.21           C  
ANISOU  350  CH2 TRP H  47     6020   4531   5109     73    554    316       C  
ATOM    351  N   VAL H  48      31.636  18.687  12.611  1.00 38.83           N  
ANISOU  351  N   VAL H  48     5811   4151   4792     63    428    -94       N  
ATOM    352  CA  VAL H  48      32.193  18.483  11.304  1.00 38.46           C  
ANISOU  352  CA  VAL H  48     5801   4062   4750     52    494    -16       C  
ATOM    353  C   VAL H  48      31.153  18.559  10.199  1.00 39.41           C  
ANISOU  353  C   VAL H  48     5968   4222   4785     22    522     98       C  
ATOM    354  O   VAL H  48      31.386  19.250   9.198  1.00 39.35           O  
ANISOU  354  O   VAL H  48     5921   4199   4831     48    600    192       O  
ATOM    355  CB  VAL H  48      32.862  17.126  11.216  1.00 38.40           C  
ANISOU  355  CB  VAL H  48     5891   4066   4635     74    484    -34       C  
ATOM    356  CG1 VAL H  48      33.182  16.848   9.787  1.00 38.19           C  
ANISOU  356  CG1 VAL H  48     5910   4033   4567     72    549     31       C  
ATOM    357  CG2 VAL H  48      34.149  17.124  12.078  1.00 38.37           C  
ANISOU  357  CG2 VAL H  48     5811   4061   4705    144    463   -135       C  
ATOM    358  N   SER H  49      30.011  17.877  10.387  1.00 38.68           N  
ANISOU  358  N   SER H  49     5938   4198   4561    -21    468     97       N  
ATOM    359  CA  SER H  49      29.049  17.659   9.299  1.00 39.77           C  
ANISOU  359  CA  SER H  49     6104   4426   4579    -47    467    155       C  
ATOM    360  C   SER H  49      27.678  17.067   9.709  1.00 42.24           C  
ANISOU  360  C   SER H  49     6433   4810   4806   -119    408    123       C  
ATOM    361  O   SER H  49      27.583  16.290  10.694  1.00 44.27           O  
ANISOU  361  O   SER H  49     6732   5026   5064   -158    390     78       O  
ATOM    362  CB  SER H  49      29.689  16.768   8.223  1.00 39.27           C  
ANISOU  362  CB  SER H  49     6111   4384   4425    -37    491    139       C  
ATOM    363  OG  SER H  49      28.789  16.500   7.165  1.00 39.69           O  
ANISOU  363  OG  SER H  49     6169   4575   4335    -48    470    142       O  
ATOM    364  N   TYR H  50      26.634  17.410   8.932  1.00 41.92           N  
ANISOU  364  N   TYR H  50     6347   4893   4689   -123    391    161       N  
ATOM    365  CA  TYR H  50      25.282  16.834   9.068  1.00 41.29           C  
ANISOU  365  CA  TYR H  50     6244   4908   4535   -206    338    113       C  
ATOM    366  C   TYR H  50      24.747  16.372   7.709  1.00 43.14           C  
ANISOU  366  C   TYR H  50     6461   5297   4633   -219    305     66       C  
ATOM    367  O   TYR H  50      25.161  16.902   6.676  1.00 45.10           O  
ANISOU  367  O   TYR H  50     6696   5631   4811   -119    327    128       O  
ATOM    368  CB  TYR H  50      24.304  17.855   9.695  1.00 40.58           C  
ANISOU  368  CB  TYR H  50     6060   4879   4479   -179    325    167       C  
ATOM    369  CG  TYR H  50      23.567  18.744   8.708  1.00 40.56           C  
ANISOU  369  CG  TYR H  50     5973   5026   4412   -101    318    248       C  
ATOM    370  CD1 TYR H  50      22.366  18.352   8.152  1.00 40.99           C  
ANISOU  370  CD1 TYR H  50     5962   5269   4343   -137    259    207       C  
ATOM    371  CD2 TYR H  50      24.088  19.993   8.335  1.00 40.95           C  
ANISOU  371  CD2 TYR H  50     5992   5029   4538     23    382    372       C  
ATOM    372  CE1 TYR H  50      21.701  19.184   7.239  1.00 44.28           C  
ANISOU  372  CE1 TYR H  50     6289   5872   4665    -19    246    298       C  
ATOM    373  CE2 TYR H  50      23.443  20.828   7.417  1.00 41.75           C  
ANISOU  373  CE2 TYR H  50     6020   5267   4575    139    401    500       C  
ATOM    374  CZ  TYR H  50      22.243  20.429   6.877  1.00 44.10           C  
ANISOU  374  CZ  TYR H  50     6257   5799   4701    135    325    469       C  
ATOM    375  OH  TYR H  50      21.592  21.256   5.975  1.00 45.81           O  
ANISOU  375  OH  TYR H  50     6388   6199   4818    293    337    611       O  
ATOM    376  N   THR H  51      23.870  15.362   7.707  1.00 43.82           N  
ANISOU  376  N   THR H  51     6534   5429   4687   -336    262    -54       N  
ATOM    377  CA  THR H  51      22.957  15.084   6.570  1.00 44.18           C  
ANISOU  377  CA  THR H  51     6496   5692   4599   -355    197   -156       C  
ATOM    378  C   THR H  51      21.531  15.048   7.083  1.00 44.39           C  
ANISOU  378  C   THR H  51     6411   5809   4648   -448    155   -196       C  
ATOM    379  O   THR H  51      21.249  14.425   8.128  1.00 42.75           O  
ANISOU  379  O   THR H  51     6222   5459   4563   -566    189   -218       O  
ATOM    380  CB  THR H  51      23.049  13.670   6.062  1.00 45.11           C  
ANISOU  380  CB  THR H  51     6653   5774   4713   -463    180   -358       C  
ATOM    381  OG1 THR H  51      24.111  12.981   6.706  1.00 45.70           O  
ANISOU  381  OG1 THR H  51     6859   5597   4908   -490    248   -349       O  
ATOM    382  CG2 THR H  51      23.147  13.611   4.566  1.00 47.59           C  
ANISOU  382  CG2 THR H  51     6929   6312   4842   -378    130   -458       C  
ATOM    383  N   SER H  52      20.608  15.617   6.311  1.00 45.50           N  
ANISOU  383  N   SER H  52     6423   6208   4659   -385     91   -202       N  
ATOM    384  CA  SER H  52      19.208  15.584   6.725  1.00 45.58           C  
ANISOU  384  CA  SER H  52     6293   6338   4686   -470     47   -255       C  
ATOM    385  C   SER H  52      18.784  14.132   6.783  1.00 46.64           C  
ANISOU  385  C   SER H  52     6404   6409   4909   -678     36   -471       C  
ATOM    386  O   SER H  52      19.536  13.240   6.379  1.00 46.78           O  
ANISOU  386  O   SER H  52     6514   6307   4955   -729     52   -585       O  
ATOM    387  CB  SER H  52      18.316  16.451   5.811  1.00 45.82           C  
ANISOU  387  CB  SER H  52     6171   6696   4542   -330    -28   -223       C  
ATOM    388  OG  SER H  52      17.832  15.764   4.676  1.00 47.03           O  
ANISOU  388  OG  SER H  52     6223   7096   4549   -355   -122   -426       O  
ATOM    389  N   SER H  53      17.603  13.886   7.332  1.00 48.14           N  
ANISOU  389  N   SER H  53     6465   6650   5176   -801     30   -526       N  
ATOM    390  CA  SER H  53      17.052  12.538   7.385  1.00 48.20           C  
ANISOU  390  CA  SER H  53     6411   6573   5330  -1024     46   -734       C  
ATOM    391  C   SER H  53      17.036  11.875   6.020  1.00 50.66           C  
ANISOU  391  C   SER H  53     6658   7030   5558  -1058    -47  -1004       C  
ATOM    392  O   SER H  53      17.449  10.725   5.900  1.00 51.19           O  
ANISOU  392  O   SER H  53     6789   6897   5763  -1189     -6  -1169       O  
ATOM    393  CB  SER H  53      15.655  12.589   7.960  1.00 47.63           C  
ANISOU  393  CB  SER H  53     6152   6611   5332  -1132     48   -751       C  
ATOM    394  OG  SER H  53      14.878  13.476   7.211  1.00 46.62           O  
ANISOU  394  OG  SER H  53     5861   6830   5021  -1013    -68   -777       O  
ATOM    395  N   SER H  54      16.575  12.601   4.995  1.00 52.53           N  
ANISOU  395  N   SER H  54     6768   7628   5565   -917   -166  -1052       N  
ATOM    396  CA  SER H  54      16.368  12.013   3.663  1.00 55.43           C  
ANISOU  396  CA  SER H  54     7023   8242   5796   -922   -280  -1353       C  
ATOM    397  C   SER H  54      17.665  11.969   2.884  1.00 55.04           C  
ANISOU  397  C   SER H  54     7134   8167   5612   -779   -271  -1340       C  
ATOM    398  O   SER H  54      17.685  11.553   1.737  1.00 57.17           O  
ANISOU  398  O   SER H  54     7333   8667   5721   -732   -360  -1579       O  
ATOM    399  CB  SER H  54      15.406  12.852   2.845  1.00 57.72           C  
ANISOU  399  CB  SER H  54     7103   8996   5832   -766   -412  -1377       C  
ATOM    400  OG  SER H  54      16.157  13.660   1.939  1.00 58.21           O  
ANISOU  400  OG  SER H  54     7240   9252   5627   -492   -434  -1225       O  
ATOM    401  N   GLY H  55      18.736  12.454   3.500  1.00 53.64           N  
ANISOU  401  N   GLY H  55     7150   7747   5484   -693   -166  -1072       N  
ATOM    402  CA  GLY H  55      20.066  12.515   2.880  1.00 51.88           C  
ANISOU  402  CA  GLY H  55     7074   7479   5158   -551   -129  -1013       C  
ATOM    403  C   GLY H  55      20.272  13.662   1.912  1.00 51.94           C  
ANISOU  403  C   GLY H  55     7046   7795   4894   -291   -158   -848       C  
ATOM    404  O   GLY H  55      21.345  13.788   1.352  1.00 52.10           O  
ANISOU  404  O   GLY H  55     7167   7804   4824   -163   -108   -774       O  
ATOM    405  N   SER H  56      19.260  14.504   1.716  1.00 52.27           N  
ANISOU  405  N   SER H  56     6939   8109   4812   -195   -218   -766       N  
ATOM    406  CA  SER H  56      19.307  15.482   0.643  1.00 53.58           C  
ANISOU  406  CA  SER H  56     7047   8611   4699     82   -236   -604       C  
ATOM    407  C   SER H  56      19.911  16.822   1.055  1.00 52.09           C  
ANISOU  407  C   SER H  56     6948   8273   4570    243   -110   -220       C  
ATOM    408  O   SER H  56      20.399  17.578   0.226  1.00 53.00           O  
ANISOU  408  O   SER H  56     7073   8541   4523    472    -53    -20       O  
ATOM    409  CB  SER H  56      17.913  15.670   0.012  1.00 56.76           C  
ANISOU  409  CB  SER H  56     7219   9448   4900    156   -372   -723       C  
ATOM    410  OG  SER H  56      17.083  16.580   0.707  1.00 56.28           O  
ANISOU  410  OG  SER H  56     7082   9394   4910    191   -361   -532       O  
ATOM    411  N   LEU H  57      19.826  17.150   2.329  1.00 50.16           N  
ANISOU  411  N   LEU H  57     6751   7743   4566    132    -56   -121       N  
ATOM    412  CA  LEU H  57      20.420  18.375   2.794  1.00 48.95           C  
ANISOU  412  CA  LEU H  57     6664   7410   4524    255     61    173       C  
ATOM    413  C   LEU H  57      21.696  17.957   3.470  1.00 47.36           C  
ANISOU  413  C   LEU H  57     6620   6868   4508    147    141    162       C  
ATOM    414  O   LEU H  57      21.747  16.942   4.127  1.00 47.43           O  
ANISOU  414  O   LEU H  57     6677   6724   4618    -33    114     -9       O  
ATOM    415  CB  LEU H  57      19.494  19.063   3.791  1.00 48.60           C  
ANISOU  415  CB  LEU H  57     6549   7311   4608    230     58    248       C  
ATOM    416  CG  LEU H  57      18.545  20.155   3.289  1.00 49.75           C  
ANISOU  416  CG  LEU H  57     6558   7716   4629    438     44    414       C  
ATOM    417  CD1 LEU H  57      18.541  20.295   1.771  1.00 52.02           C  
ANISOU  417  CD1 LEU H  57     6784   8353   4629    653     19    476       C  
ATOM    418  CD2 LEU H  57      17.129  19.959   3.842  1.00 49.42           C  
ANISOU  418  CD2 LEU H  57     6370   7815   4592    346    -51    287       C  
ATOM    419  N   THR H  58      22.724  18.764   3.343  1.00 47.91           N  
ANISOU  419  N   THR H  58     6752   6812   4638    266    252    360       N  
ATOM    420  CA  THR H  58      24.036  18.354   3.761  1.00 47.41           C  
ANISOU  420  CA  THR H  58     6808   6493   4711    196    318    335       C  
ATOM    421  C   THR H  58      24.773  19.616   4.200  1.00 47.03           C  
ANISOU  421  C   THR H  58     6769   6251   4849    281    439    547       C  
ATOM    422  O   THR H  58      24.435  20.715   3.747  1.00 48.34           O  
ANISOU  422  O   THR H  58     6868   6495   5004    429    500    741       O  
ATOM    423  CB  THR H  58      24.699  17.634   2.578  1.00 50.19           C  
ANISOU  423  CB  THR H  58     7197   6984   4888    253    321    260       C  
ATOM    424  OG1 THR H  58      25.245  16.401   3.029  1.00 51.37           O  
ANISOU  424  OG1 THR H  58     7438   6965   5117    103    296     62       O  
ATOM    425  CG2 THR H  58      25.756  18.473   1.856  1.00 50.63           C  
ANISOU  425  CG2 THR H  58     7270   7040   4926    427    455    485       C  
ATOM    426  N   GLY H  59      25.722  19.495   5.124  1.00 45.08           N  
ANISOU  426  N   GLY H  59     6586   5749   4793    196    478    506       N  
ATOM    427  CA  GLY H  59      26.406  20.688   5.649  1.00 42.43           C  
ANISOU  427  CA  GLY H  59     6224   5215   4684    246    583    636       C  
ATOM    428  C   GLY H  59      27.734  20.433   6.340  1.00 41.33           C  
ANISOU  428  C   GLY H  59     6130   4867   4707    180    619    558       C  
ATOM    429  O   GLY H  59      27.941  19.394   6.979  1.00 38.10           O  
ANISOU  429  O   GLY H  59     5783   4421   4272     85    550    408       O  
ATOM    430  N   TYR H  60      28.649  21.389   6.223  1.00 42.51           N  
ANISOU  430  N   TYR H  60     6234   4877   5042    237    740    668       N  
ATOM    431  CA  TYR H  60      30.006  21.131   6.661  1.00 42.78           C  
ANISOU  431  CA  TYR H  60     6277   4764   5212    190    774    584       C  
ATOM    432  C   TYR H  60      30.653  22.254   7.434  1.00 43.00           C  
ANISOU  432  C   TYR H  60     6208   4585   5547    179    847    573       C  
ATOM    433  O   TYR H  60      30.239  23.386   7.333  1.00 45.00           O  
ANISOU  433  O   TYR H  60     6390   4761   5946    227    926    684       O  
ATOM    434  CB  TYR H  60      30.857  20.821   5.453  1.00 43.26           C  
ANISOU  434  CB  TYR H  60     6361   4892   5186    254    863    676       C  
ATOM    435  CG  TYR H  60      30.433  19.573   4.696  1.00 43.70           C  
ANISOU  435  CG  TYR H  60     6503   5149   4953    261    781    605       C  
ATOM    436  CD1 TYR H  60      30.861  18.301   5.102  1.00 41.47           C  
ANISOU  436  CD1 TYR H  60     6300   4836   4620    185    707    426       C  
ATOM    437  CD2 TYR H  60      29.656  19.665   3.537  1.00 43.76           C  
ANISOU  437  CD2 TYR H  60     6498   5381   4746    361    786    705       C  
ATOM    438  CE1 TYR H  60      30.516  17.156   4.366  1.00 41.55           C  
ANISOU  438  CE1 TYR H  60     6377   4989   4420    182    648    322       C  
ATOM    439  CE2 TYR H  60      29.318  18.530   2.813  1.00 44.12           C  
ANISOU  439  CE2 TYR H  60     6594   5623   4545    363    703    574       C  
ATOM    440  CZ  TYR H  60      29.744  17.272   3.235  1.00 43.09           C  
ANISOU  440  CZ  TYR H  60     6545   5412   4416    258    638    368       C  
ATOM    441  OH  TYR H  60      29.398  16.135   2.513  1.00 44.53           O  
ANISOU  441  OH  TYR H  60     6766   5748   4404    248    565    197       O  
ATOM    442  N   ALA H  61      31.689  21.934   8.195  1.00 42.92           N  
ANISOU  442  N   ALA H  61     6178   4485   5646    124    824    423       N  
ATOM    443  CA  ALA H  61      32.512  22.959   8.831  1.00 42.96           C  
ANISOU  443  CA  ALA H  61     6051   4307   5966    104    892    352       C  
ATOM    444  C   ALA H  61      33.578  23.451   7.860  1.00 44.58           C  
ANISOU  444  C   ALA H  61     6190   4418   6332    129   1063    489       C  
ATOM    445  O   ALA H  61      34.273  22.649   7.239  1.00 46.06           O  
ANISOU  445  O   ALA H  61     6425   4688   6387    145   1081    517       O  
ATOM    446  CB  ALA H  61      33.165  22.402  10.072  1.00 41.81           C  
ANISOU  446  CB  ALA H  61     5881   4167   5837     61    780    116       C  
ATOM    447  N   ASP H  62      33.714  24.759   7.730  1.00 45.85           N  
ANISOU  447  N   ASP H  62     6233   4392   6795    137   1209    580       N  
ATOM    448  CA  ASP H  62      34.771  25.326   6.920  1.00 48.99           C  
ANISOU  448  CA  ASP H  62     6538   4665   7412    149   1411    727       C  
ATOM    449  C   ASP H  62      36.087  24.524   6.977  1.00 49.04           C  
ANISOU  449  C   ASP H  62     6516   4716   7401    106   1392    600       C  
ATOM    450  O   ASP H  62      36.796  24.372   5.984  1.00 49.44           O  
ANISOU  450  O   ASP H  62     6558   4801   7427    150   1527    759       O  
ATOM    451  CB  ASP H  62      35.050  26.740   7.396  1.00 52.23           C  
ANISOU  451  CB  ASP H  62     6779   4783   8282    100   1544    692       C  
ATOM    452  CG  ASP H  62      34.104  27.757   6.810  1.00 54.42           C  
ANISOU  452  CG  ASP H  62     7062   4959   8658    192   1685    954       C  
ATOM    453  OD1 ASP H  62      33.368  27.440   5.851  1.00 55.21           O  
ANISOU  453  OD1 ASP H  62     7274   5247   8457    312   1702   1200       O  
ATOM    454  OD2 ASP H  62      34.127  28.899   7.302  1.00 57.15           O  
ANISOU  454  OD2 ASP H  62     7283   5035   9397    155   1785    901       O  
ATOM    455  N   SER H  63      36.430  24.024   8.148  1.00 48.19           N  
ANISOU  455  N   SER H  63     6383   4634   7294     46   1231    321       N  
ATOM    456  CA  SER H  63      37.685  23.323   8.275  1.00 49.13           C  
ANISOU  456  CA  SER H  63     6454   4805   7407     31   1210    200       C  
ATOM    457  C   SER H  63      37.676  21.999   7.539  1.00 49.61           C  
ANISOU  457  C   SER H  63     6681   5052   7118     98   1168    286       C  
ATOM    458  O   SER H  63      38.725  21.331   7.457  1.00 50.86           O  
ANISOU  458  O   SER H  63     6815   5262   7247    115   1170    220       O  
ATOM    459  CB  SER H  63      38.051  23.089   9.740  1.00 47.91           C  
ANISOU  459  CB  SER H  63     6221   4683   7299     -4   1042   -110       C  
ATOM    460  OG  SER H  63      36.982  22.474  10.434  1.00 47.06           O  
ANISOU  460  OG  SER H  63     6249   4695   6937     24    882   -164       O  
ATOM    461  N   VAL H  64      36.520  21.583   7.018  1.00 47.55           N  
ANISOU  461  N   VAL H  64     6570   4896   6599    139   1124    402       N  
ATOM    462  CA  VAL H  64      36.514  20.300   6.290  1.00 46.57           C  
ANISOU  462  CA  VAL H  64     6587   4935   6174    193   1083    426       C  
ATOM    463  C   VAL H  64      35.878  20.344   4.903  1.00 47.56           C  
ANISOU  463  C   VAL H  64     6777   5185   6108    273   1166    629       C  
ATOM    464  O   VAL H  64      36.202  19.496   4.069  1.00 47.77           O  
ANISOU  464  O   VAL H  64     6872   5344   5936    334   1181    640       O  
ATOM    465  CB  VAL H  64      35.970  19.111   7.130  1.00 44.09           C  
ANISOU  465  CB  VAL H  64     6394   4688   5671    169    905    264       C  
ATOM    466  CG1 VAL H  64      36.654  19.058   8.516  1.00 42.44           C  
ANISOU  466  CG1 VAL H  64     6109   4422   5594    145    824     85       C  
ATOM    467  CG2 VAL H  64      34.478  19.183   7.263  1.00 42.18           C  
ANISOU  467  CG2 VAL H  64     6219   4491   5315    144    831    293       C  
ATOM    468  N   LYS H  65      35.011  21.342   4.663  1.00 48.11           N  
ANISOU  468  N   LYS H  65     6814   5232   6234    296   1221    778       N  
ATOM    469  CA  LYS H  65      34.334  21.574   3.362  1.00 48.35           C  
ANISOU  469  CA  LYS H  65     6876   5428   6066    418   1303   1000       C  
ATOM    470  C   LYS H  65      35.262  21.193   2.192  1.00 47.60           C  
ANISOU  470  C   LYS H  65     6781   5459   5846    516   1429   1108       C  
ATOM    471  O   LYS H  65      36.431  21.605   2.168  1.00 47.34           O  
ANISOU  471  O   LYS H  65     6654   5301   6031    505   1572   1162       O  
ATOM    472  CB  LYS H  65      33.980  23.064   3.234  1.00 51.43           C  
ANISOU  472  CB  LYS H  65     7170   5690   6682    465   1452   1221       C  
ATOM    473  CG  LYS H  65      32.538  23.421   2.845  1.00 54.19           C  
ANISOU  473  CG  LYS H  65     7552   6178   6859    557   1413   1350       C  
ATOM    474  CD  LYS H  65      32.457  24.830   2.145  1.00 60.10           C  
ANISOU  474  CD  LYS H  65     8213   6840   7783    693   1645   1689       C  
ATOM    475  CE  LYS H  65      32.163  26.069   3.066  1.00 61.83           C  
ANISOU  475  CE  LYS H  65     8346   6755   8392    638   1706   1699       C  
ATOM    476  NZ  LYS H  65      30.927  25.967   3.945  1.00 61.16           N  
ANISOU  476  NZ  LYS H  65     8298   6711   8230    593   1513   1530       N  
ATOM    477  N   GLY H  66      34.759  20.402   1.241  1.00 45.02           N  
ANISOU  477  N   GLY H  66     6539   5392   5174    612   1378   1110       N  
ATOM    478  CA  GLY H  66      35.546  20.053   0.061  1.00 45.08           C  
ANISOU  478  CA  GLY H  66     6543   5572   5012    740   1499   1204       C  
ATOM    479  C   GLY H  66      36.447  18.838   0.214  1.00 45.03           C  
ANISOU  479  C   GLY H  66     6591   5568   4951    699   1435    981       C  
ATOM    480  O   GLY H  66      36.849  18.237  -0.761  1.00 46.68           O  
ANISOU  480  O   GLY H  66     6826   5969   4941    811   1481    978       O  
ATOM    481  N   ARG H  67      36.744  18.440   1.441  1.00 43.80           N  
ANISOU  481  N   ARG H  67     6451   5218   4972    563   1328    789       N  
ATOM    482  CA  ARG H  67      37.660  17.340   1.659  1.00 43.50           C  
ANISOU  482  CA  ARG H  67     6457   5163   4909    553   1284    610       C  
ATOM    483  C   ARG H  67      36.899  16.133   2.228  1.00 43.47           C  
ANISOU  483  C   ARG H  67     6585   5155   4777    488   1097    388       C  
ATOM    484  O   ARG H  67      37.268  14.970   1.987  1.00 44.26           O  
ANISOU  484  O   ARG H  67     6764   5291   4763    520   1061    244       O  
ATOM    485  CB  ARG H  67      38.807  17.777   2.594  1.00 42.30           C  
ANISOU  485  CB  ARG H  67     6192   4820   5061    488   1332    580       C  
ATOM    486  CG  ARG H  67      39.527  19.040   2.138  1.00 43.05           C  
ANISOU  486  CG  ARG H  67     6126   4855   5378    511   1542    788       C  
ATOM    487  CD  ARG H  67      40.785  19.371   2.949  1.00 43.08           C  
ANISOU  487  CD  ARG H  67     5974   4700   5692    439   1587    696       C  
ATOM    488  NE  ARG H  67      40.509  19.692   4.342  1.00 41.29           N  
ANISOU  488  NE  ARG H  67     5706   4331   5652    328   1452    532       N  
ATOM    489  CZ  ARG H  67      40.778  18.875   5.347  1.00 39.93           C  
ANISOU  489  CZ  ARG H  67     5565   4165   5444    308   1293    318       C  
ATOM    490  NH1 ARG H  67      41.341  17.702   5.100  1.00 40.91           N  
ANISOU  490  NH1 ARG H  67     5765   4385   5394    383   1259    251       N  
ATOM    491  NH2 ARG H  67      40.500  19.222   6.591  1.00 39.27           N  
ANISOU  491  NH2 ARG H  67     5430   4002   5488    239   1178    178       N  
ATOM    492  N   PHE H  68      35.821  16.414   2.957  1.00 41.54           N  
ANISOU  492  N   PHE H  68     6357   4853   4571    402    999    370       N  
ATOM    493  CA  PHE H  68      35.029  15.361   3.575  1.00 40.73           C  
ANISOU  493  CA  PHE H  68     6358   4721   4395    325    855    196       C  
ATOM    494  C   PHE H  68      33.678  15.329   2.909  1.00 41.34           C  
ANISOU  494  C   PHE H  68     6458   4957   4294    321    797    191       C  
ATOM    495  O   PHE H  68      33.140  16.372   2.593  1.00 42.96           O  
ANISOU  495  O   PHE H  68     6595   5238   4489    357    833    341       O  
ATOM    496  CB  PHE H  68      34.825  15.670   5.047  1.00 37.79           C  
ANISOU  496  CB  PHE H  68     5966   4195   4199    238    790    169       C  
ATOM    497  CG  PHE H  68      36.054  15.566   5.855  1.00 36.06           C  
ANISOU  497  CG  PHE H  68     5707   3868   4126    252    807    122       C  
ATOM    498  CD1 PHE H  68      37.293  15.500   5.247  1.00 37.44           C  
ANISOU  498  CD1 PHE H  68     5838   4062   4327    324    900    140       C  
ATOM    499  CD2 PHE H  68      35.972  15.530   7.237  1.00 36.05           C  
ANISOU  499  CD2 PHE H  68     5694   3784   4218    212    729     54       C  
ATOM    500  CE1 PHE H  68      38.467  15.399   6.023  1.00 39.60           C  
ANISOU  500  CE1 PHE H  68     6041   4268   4736    347    903     76       C  
ATOM    501  CE2 PHE H  68      37.116  15.436   8.039  1.00 37.70           C  
ANISOU  501  CE2 PHE H  68     5839   3951   4533    254    723    -11       C  
ATOM    502  CZ  PHE H  68      38.381  15.373   7.440  1.00 39.09           C  
ANISOU  502  CZ  PHE H  68     5956   4141   4753    317    804     -8       C  
ATOM    503  N   THR H  69      33.143  14.145   2.659  1.00 42.21           N  
ANISOU  503  N   THR H  69     6646   5115   4275    286    714     10       N  
ATOM    504  CA  THR H  69      31.793  14.038   2.119  1.00 44.03           C  
ANISOU  504  CA  THR H  69     6863   5517   4350    263    634    -53       C  
ATOM    505  C   THR H  69      30.987  13.152   3.027  1.00 44.65           C  
ANISOU  505  C   THR H  69     6993   5462   4511    115    539   -210       C  
ATOM    506  O   THR H  69      31.314  11.976   3.199  1.00 46.40           O  
ANISOU  506  O   THR H  69     7292   5562   4775     71    530   -365       O  
ATOM    507  CB  THR H  69      31.733  13.400   0.744  1.00 45.77           C  
ANISOU  507  CB  THR H  69     7086   5972   4331    354    624   -181       C  
ATOM    508  OG1 THR H  69      32.704  14.004  -0.123  1.00 47.21           O  
ANISOU  508  OG1 THR H  69     7232   6280   4424    514    747    -23       O  
ATOM    509  CG2 THR H  69      30.319  13.571   0.161  1.00 46.79           C  
ANISOU  509  CG2 THR H  69     7148   6346   4283    356    530   -237       C  
ATOM    510  N   ILE H  70      29.945  13.719   3.625  1.00 43.37           N  
ANISOU  510  N   ILE H  70     6782   5306   4389     47    489   -154       N  
ATOM    511  CA  ILE H  70      29.105  12.960   4.519  1.00 41.63           C  
ANISOU  511  CA  ILE H  70     6591   4971   4257    -92    427   -264       C  
ATOM    512  C   ILE H  70      28.126  12.211   3.647  1.00 42.75           C  
ANISOU  512  C   ILE H  70     6702   5264   4277   -147    358   -458       C  
ATOM    513  O   ILE H  70      27.855  12.637   2.535  1.00 42.51           O  
ANISOU  513  O   ILE H  70     6604   5485   4061    -55    334   -466       O  
ATOM    514  CB  ILE H  70      28.287  13.882   5.433  1.00 40.11           C  
ANISOU  514  CB  ILE H  70     6334   4768   4135   -132    404   -146       C  
ATOM    515  CG1 ILE H  70      27.731  13.068   6.614  1.00 38.39           C  
ANISOU  515  CG1 ILE H  70     6154   4399   4033   -257    383   -210       C  
ATOM    516  CG2 ILE H  70      27.180  14.543   4.613  1.00 39.46           C  
ANISOU  516  CG2 ILE H  70     6155   4924   3914   -100    357   -123       C  
ATOM    517  CD1 ILE H  70      27.089  13.869   7.674  1.00 35.22           C  
ANISOU  517  CD1 ILE H  70     5698   3990   3696   -277    371   -108       C  
ATOM    518  N   SER H  71      27.597  11.100   4.146  1.00 43.05           N  
ANISOU  518  N   SER H  71     6772   5158   4425   -286    335   -615       N  
ATOM    519  CA  SER H  71      26.489  10.448   3.464  1.00 45.72           C  
ANISOU  519  CA  SER H  71     7037   5630   4706   -379    261   -844       C  
ATOM    520  C   SER H  71      25.847   9.361   4.299  1.00 46.36           C  
ANISOU  520  C   SER H  71     7137   5477   5002   -565    278   -963       C  
ATOM    521  O   SER H  71      26.338   8.997   5.366  1.00 45.58           O  
ANISOU  521  O   SER H  71     7131   5121   5066   -591    356   -849       O  
ATOM    522  CB  SER H  71      26.877   9.907   2.080  1.00 46.03           C  
ANISOU  522  CB  SER H  71     7069   5836   4583   -300    235  -1053       C  
ATOM    523  OG  SER H  71      27.765   8.816   2.192  1.00 46.15           O  
ANISOU  523  OG  SER H  71     7197   5613   4723   -320    297  -1170       O  
ATOM    524  N   ARG H  72      24.738   8.841   3.793  1.00 47.64           N  
ANISOU  524  N   ARG H  72     7192   5745   5165   -685    212  -1191       N  
ATOM    525  CA  ARG H  72      24.022   7.853   4.513  1.00 47.71           C  
ANISOU  525  CA  ARG H  72     7188   5523   5418   -881    255  -1296       C  
ATOM    526  C   ARG H  72      23.431   6.875   3.546  1.00 53.11           C  
ANISOU  526  C   ARG H  72     7778   6262   6139   -996    201  -1671       C  
ATOM    527  O   ARG H  72      23.260   7.173   2.363  1.00 57.00           O  
ANISOU  527  O   ARG H  72     8177   7078   6402   -913     93  -1844       O  
ATOM    528  CB  ARG H  72      22.935   8.515   5.329  1.00 46.04           C  
ANISOU  528  CB  ARG H  72     6877   5379   5239   -953    241  -1153       C  
ATOM    529  CG  ARG H  72      21.885   9.233   4.551  1.00 44.26           C  
ANISOU  529  CG  ARG H  72     6474   5509   4832   -940    119  -1244       C  
ATOM    530  CD  ARG H  72      20.611   9.207   5.353  1.00 45.53           C  
ANISOU  530  CD  ARG H  72     6514   5655   5130  -1095    127  -1229       C  
ATOM    531  NE  ARG H  72      20.608  10.181   6.447  1.00 43.15           N  
ANISOU  531  NE  ARG H  72     6246   5325   4824  -1022    172   -926       N  
ATOM    532  CZ  ARG H  72      19.998  10.011   7.621  1.00 42.62           C  
ANISOU  532  CZ  ARG H  72     6156   5123   4916  -1126    248   -820       C  
ATOM    533  NH1 ARG H  72      19.370   8.870   7.929  1.00 43.13           N  
ANISOU  533  NH1 ARG H  72     6171   5018   5199  -1323    318   -946       N  
ATOM    534  NH2 ARG H  72      20.061  10.986   8.511  1.00 40.50           N  
ANISOU  534  NH2 ARG H  72     5909   4879   4600  -1024    271   -587       N  
ATOM    535  N   ASP H  73      23.142   5.682   4.032  1.00 55.75           N  
ANISOU  535  N   ASP H  73     8130   6285   6770  -1176    286  -1806       N  
ATOM    536  CA  ASP H  73      22.402   4.746   3.224  1.00 59.53           C  
ANISOU  536  CA  ASP H  73     8477   6783   7357  -1333    237  -2217       C  
ATOM    537  C   ASP H  73      21.240   4.220   4.023  1.00 61.02           C  
ANISOU  537  C   ASP H  73     8556   6784   7844  -1575    304  -2250       C  
ATOM    538  O   ASP H  73      21.407   3.309   4.821  1.00 62.42           O  
ANISOU  538  O   ASP H  73     8823   6557   8338  -1684    466  -2186       O  
ATOM    539  CB  ASP H  73      23.279   3.584   2.816  1.00 61.62           C  
ANISOU  539  CB  ASP H  73     8855   6783   7773  -1332    309  -2430       C  
ATOM    540  CG  ASP H  73      22.550   2.628   1.930  1.00 66.36           C  
ANISOU  540  CG  ASP H  73     9303   7405   8507  -1496    250  -2924       C  
ATOM    541  OD1 ASP H  73      21.296   2.676   1.918  1.00 68.03           O  
ANISOU  541  OD1 ASP H  73     9316   7747   8784  -1663    186  -3074       O  
ATOM    542  OD2 ASP H  73      23.226   1.860   1.221  1.00 68.99           O  
ANISOU  542  OD2 ASP H  73     9692   7647   8873  -1452    261  -3188       O  
ATOM    543  N   ASN H  74      20.058   4.779   3.818  1.00 61.41           N  
ANISOU  543  N   ASN H  74     8404   7128   7802  -1646    197  -2329       N  
ATOM    544  CA  ASN H  74      18.931   4.369   4.639  1.00 62.09           C  
ANISOU  544  CA  ASN H  74     8364   7055   8174  -1875    278  -2327       C  
ATOM    545  C   ASN H  74      18.486   2.912   4.495  1.00 66.57           C  
ANISOU  545  C   ASN H  74     8846   7310   9139  -2133    368  -2672       C  
ATOM    546  O   ASN H  74      17.729   2.430   5.326  1.00 68.41           O  
ANISOU  546  O   ASN H  74     9002   7307   9684  -2331    503  -2608       O  
ATOM    547  CB  ASN H  74      17.806   5.382   4.527  1.00 61.49           C  
ANISOU  547  CB  ASN H  74     8082   7378   7903  -1867    149  -2303       C  
ATOM    548  CG  ASN H  74      18.158   6.673   5.242  1.00 58.26           C  
ANISOU  548  CG  ASN H  74     7780   7077   7280  -1669    156  -1878       C  
ATOM    549  OD1 ASN H  74      18.947   6.672   6.175  1.00 56.42           O  
ANISOU  549  OD1 ASN H  74     7730   6583   7124  -1610    280  -1602       O  
ATOM    550  ND2 ASN H  74      17.613   7.775   4.794  1.00 59.02           N  
ANISOU  550  ND2 ASN H  74     7752   7561   7110  -1549     24  -1839       N  
ATOM    551  N   SER H  75      19.018   2.224   3.476  1.00 68.66           N  
ANISOU  551  N   SER H  75     9128   7552   9408  -2119    317  -3023       N  
ATOM    552  CA  SER H  75      18.863   0.786   3.237  1.00 73.64           C  
ANISOU  552  CA  SER H  75     9709   7821  10450  -2338    415  -3397       C  
ATOM    553  C   SER H  75      19.496  -0.042   4.323  1.00 74.17           C  
ANISOU  553  C   SER H  75     9983   7318  10880  -2382    676  -3119       C  
ATOM    554  O   SER H  75      18.836  -0.814   5.004  1.00 77.04           O  
ANISOU  554  O   SER H  75    10279   7333  11660  -2606    850  -3111       O  
ATOM    555  CB  SER H  75      19.609   0.398   1.966  1.00 75.76           C  
ANISOU  555  CB  SER H  75    10009   8212  10566  -2224    305  -3775       C  
ATOM    556  OG  SER H  75      18.739   0.313   0.871  1.00 81.33           O  
ANISOU  556  OG  SER H  75    10446   9281  11176  -2310    119  -4274       O  
ATOM    557  N   LYS H  76      20.820   0.020   4.374  1.00 73.05           N  
ANISOU  557  N   LYS H  76    10078   7079  10596  -2157    713  -2922       N  
ATOM    558  CA  LYS H  76      21.558  -0.452   5.526  1.00 72.53           C  
ANISOU  558  CA  LYS H  76    10225   6587  10746  -2097    937  -2541       C  
ATOM    559  C   LYS H  76      21.106   0.549   6.567  1.00 69.88           C  
ANISOU  559  C   LYS H  76     9874   6420  10257  -2054    945  -2128       C  
ATOM    560  O   LYS H  76      20.116   1.245   6.336  1.00 71.74           O  
ANISOU  560  O   LYS H  76     9925   6977  10358  -2134    818  -2213       O  
ATOM    561  CB  LYS H  76      23.055  -0.365   5.240  1.00 71.47           C  
ANISOU  561  CB  LYS H  76    10303   6446  10406  -1835    922  -2445       C  
ATOM    562  CG  LYS H  76      23.443  -1.084   3.917  1.00 74.96           C  
ANISOU  562  CG  LYS H  76    10724   6888  10872  -1835    850  -2927       C  
ATOM    563  CD  LYS H  76      24.642  -0.441   3.206  1.00 73.48           C  
ANISOU  563  CD  LYS H  76    10647   6987  10285  -1557    736  -2892       C  
ATOM    564  CE  LYS H  76      25.890  -1.335   3.195  1.00 75.27           C  
ANISOU  564  CE  LYS H  76    11063   6875  10663  -1427    867  -2899       C  
ATOM    565  NZ  LYS H  76      25.990  -2.251   2.009  1.00 77.62           N  
ANISOU  565  NZ  LYS H  76    11310   7123  11061  -1467    832  -3425       N  
ATOM    566  N   ASN H  77      21.746   0.625   7.719  1.00 66.60           N  
ANISOU  566  N   ASN H  77     9629   5818   9858  -1921   1089  -1704       N  
ATOM    567  CA  ASN H  77      21.351   1.670   8.646  1.00 63.34           C  
ANISOU  567  CA  ASN H  77     9189   5623   9255  -1854   1071  -1366       C  
ATOM    568  C   ASN H  77      22.641   2.279   9.016  1.00 60.64           C  
ANISOU  568  C   ASN H  77     9029   5350   8660  -1583   1047  -1101       C  
ATOM    569  O   ASN H  77      23.119   2.115  10.124  1.00 61.36           O  
ANISOU  569  O   ASN H  77     9238   5274   8804  -1474   1186   -782       O  
ATOM    570  CB  ASN H  77      20.646   1.118   9.879  1.00 65.71           C  
ANISOU  570  CB  ASN H  77     9462   5657   9848  -1975   1293  -1116       C  
ATOM    571  CG  ASN H  77      19.160   0.894   9.653  1.00 68.92           C  
ANISOU  571  CG  ASN H  77     9623   6099  10466  -2256   1298  -1338       C  
ATOM    572  OD1 ASN H  77      18.450   1.779   9.185  1.00 69.80           O  
ANISOU  572  OD1 ASN H  77     9573   6589  10357  -2284   1115  -1470       O  
ATOM    573  ND2 ASN H  77      18.686  -0.286   9.993  1.00 72.27           N  
ANISOU  573  ND2 ASN H  77    10002   6123  11334  -2457   1519  -1372       N  
ATOM    574  N   THR H  78      23.225   2.970   8.051  1.00 58.41           N  
ANISOU  574  N   THR H  78     8755   5336   8100  -1462    875  -1242       N  
ATOM    575  CA  THR H  78      24.632   3.265   8.096  1.00 55.40           C  
ANISOU  575  CA  THR H  78     8533   4963   7553  -1232    866  -1094       C  
ATOM    576  C   THR H  78      24.927   4.694   7.656  1.00 53.58           C  
ANISOU  576  C   THR H  78     8264   5113   6979  -1091    703  -1040       C  
ATOM    577  O   THR H  78      24.496   5.161   6.601  1.00 54.13           O  
ANISOU  577  O   THR H  78     8227   5443   6895  -1114    573  -1240       O  
ATOM    578  CB  THR H  78      25.405   2.250   7.215  1.00 55.87           C  
ANISOU  578  CB  THR H  78     8673   4831   7722  -1212    896  -1343       C  
ATOM    579  OG1 THR H  78      24.973   0.917   7.536  1.00 58.62           O  
ANISOU  579  OG1 THR H  78     9034   4783   8456  -1371   1065  -1427       O  
ATOM    580  CG2 THR H  78      26.921   2.375   7.416  1.00 52.65           C  
ANISOU  580  CG2 THR H  78     8426   4387   7193   -971    923  -1164       C  
ATOM    581  N   LEU H  79      25.695   5.384   8.468  1.00 51.27           N  
ANISOU  581  N   LEU H  79     8051   4854   6576   -929    719   -767       N  
ATOM    582  CA  LEU H  79      26.067   6.712   8.119  1.00 50.95           C  
ANISOU  582  CA  LEU H  79     7974   5098   6285   -803    604   -702       C  
ATOM    583  C   LEU H  79      27.565   6.692   7.820  1.00 50.43           C  
ANISOU  583  C   LEU H  79     8015   4997   6149   -634    616   -673       C  
ATOM    584  O   LEU H  79      28.326   6.003   8.509  1.00 49.28           O  
ANISOU  584  O   LEU H  79     7974   4640   6111   -564    710   -575       O  
ATOM    585  CB  LEU H  79      25.755   7.622   9.302  1.00 50.38           C  
ANISOU  585  CB  LEU H  79     7870   5104   6168   -761    608   -462       C  
ATOM    586  CG  LEU H  79      26.442   8.977   9.335  1.00 49.59           C  
ANISOU  586  CG  LEU H  79     7757   5193   5894   -609    537   -347       C  
ATOM    587  CD1 LEU H  79      25.769   9.925   8.375  1.00 49.67           C  
ANISOU  587  CD1 LEU H  79     7654   5450   5769   -624    437   -422       C  
ATOM    588  CD2 LEU H  79      26.396   9.505  10.751  1.00 49.08           C  
ANISOU  588  CD2 LEU H  79     7685   5128   5833   -549    568   -152       C  
ATOM    589  N   TYR H  80      27.971   7.452   6.801  1.00 49.91           N  
ANISOU  589  N   TYR H  80     7912   5153   5900   -551    534   -738       N  
ATOM    590  CA  TYR H  80      29.369   7.518   6.357  1.00 50.21           C  
ANISOU  590  CA  TYR H  80     8018   5197   5864   -396    553   -721       C  
ATOM    591  C   TYR H  80      30.001   8.914   6.404  1.00 49.19           C  
ANISOU  591  C   TYR H  80     7842   5244   5603   -274    523   -551       C  
ATOM    592  O   TYR H  80      29.308   9.955   6.366  1.00 48.32           O  
ANISOU  592  O   TYR H  80     7643   5297   5418   -292    472   -482       O  
ATOM    593  CB  TYR H  80      29.514   7.035   4.918  1.00 50.15           C  
ANISOU  593  CB  TYR H  80     8001   5286   5769   -382    524   -964       C  
ATOM    594  CG  TYR H  80      29.030   5.657   4.680  1.00 52.65           C  
ANISOU  594  CG  TYR H  80     8345   5411   6250   -503    556  -1206       C  
ATOM    595  CD1 TYR H  80      27.787   5.439   4.124  1.00 54.44           C  
ANISOU  595  CD1 TYR H  80     8463   5738   6483   -650    490  -1424       C  
ATOM    596  CD2 TYR H  80      29.806   4.566   4.992  1.00 53.83           C  
ANISOU  596  CD2 TYR H  80     8610   5272   6570   -467    657  -1234       C  
ATOM    597  CE1 TYR H  80      27.322   4.167   3.884  1.00 57.82           C  
ANISOU  597  CE1 TYR H  80     8887   5963   7119   -790    526  -1696       C  
ATOM    598  CE2 TYR H  80      29.349   3.276   4.751  1.00 57.39           C  
ANISOU  598  CE2 TYR H  80     9081   5489   7237   -589    711  -1474       C  
ATOM    599  CZ  TYR H  80      28.100   3.081   4.193  1.00 59.43           C  
ANISOU  599  CZ  TYR H  80     9219   5831   7532   -766    646  -1722       C  
ATOM    600  OH  TYR H  80      27.617   1.801   3.925  1.00 63.98           O  
ANISOU  600  OH  TYR H  80     9784   6151   8375   -917    705  -2014       O  
ATOM    601  N   LEU H  81      31.334   8.917   6.434  1.00 48.50           N  
ANISOU  601  N   LEU H  81     7803   5112   5514   -147    566   -496       N  
ATOM    602  CA  LEU H  81      32.101  10.149   6.259  1.00 46.99           C  
ANISOU  602  CA  LEU H  81     7548   5058   5248    -45    564   -376       C  
ATOM    603  C   LEU H  81      33.378   9.869   5.465  1.00 47.21           C  
ANISOU  603  C   LEU H  81     7601   5104   5232     72    614   -418       C  
ATOM    604  O   LEU H  81      34.324   9.289   6.006  1.00 48.70           O  
ANISOU  604  O   LEU H  81     7842   5164   5498    142    655   -406       O  
ATOM    605  CB  LEU H  81      32.444  10.778   7.606  1.00 43.02           C  
ANISOU  605  CB  LEU H  81     7018   4500   4828    -14    565   -234       C  
ATOM    606  CG  LEU H  81      33.340  11.972   7.351  1.00 42.10           C  
ANISOU  606  CG  LEU H  81     6815   4479   4704     69    581   -156       C  
ATOM    607  CD1 LEU H  81      32.475  13.159   7.027  1.00 42.18           C  
ANISOU  607  CD1 LEU H  81     6739   4606   4681     29    559    -90       C  
ATOM    608  CD2 LEU H  81      34.268  12.304   8.523  1.00 42.46           C  
ANISOU  608  CD2 LEU H  81     6819   4472   4841    137    584   -105       C  
ATOM    609  N   GLN H  82      33.407  10.271   4.192  1.00 46.47           N  
ANISOU  609  N   GLN H  82     7463   5196   4998    119    619   -455       N  
ATOM    610  CA  GLN H  82      34.594  10.070   3.346  1.00 45.43           C  
ANISOU  610  CA  GLN H  82     7338   5122   4799    246    684   -485       C  
ATOM    611  C   GLN H  82      35.625  11.172   3.554  1.00 44.95           C  
ANISOU  611  C   GLN H  82     7196   5096   4786    326    748   -303       C  
ATOM    612  O   GLN H  82      35.429  12.311   3.127  1.00 46.13           O  
ANISOU  612  O   GLN H  82     7260   5373   4893    343    775   -175       O  
ATOM    613  CB  GLN H  82      34.190   9.987   1.875  1.00 47.07           C  
ANISOU  613  CB  GLN H  82     7521   5561   4804    293    674   -600       C  
ATOM    614  CG  GLN H  82      35.348   9.732   0.938  1.00 48.42           C  
ANISOU  614  CG  GLN H  82     7694   5829   4873    441    754   -638       C  
ATOM    615  CD  GLN H  82      35.970   8.388   1.199  1.00 50.22           C  
ANISOU  615  CD  GLN H  82     8021   5858   5203    455    772   -809       C  
ATOM    616  OE1 GLN H  82      37.192   8.214   1.077  1.00 50.97           O  
ANISOU  616  OE1 GLN H  82     8122   5932   5313    572    848   -782       O  
ATOM    617  NE2 GLN H  82      35.134   7.417   1.581  1.00 49.58           N  
ANISOU  617  NE2 GLN H  82     8008   5612   5219    339    718   -976       N  
ATOM    618  N   MET H  83      36.725  10.849   4.217  1.00 44.90           N  
ANISOU  618  N   MET H  83     7200   4972   4887    380    782   -292       N  
ATOM    619  CA  MET H  83      37.707  11.869   4.577  1.00 44.93           C  
ANISOU  619  CA  MET H  83     7090   4993   4990    427    834   -167       C  
ATOM    620  C   MET H  83      38.872  11.877   3.650  1.00 47.25           C  
ANISOU  620  C   MET H  83     7336   5374   5245    539    934   -154       C  
ATOM    621  O   MET H  83      39.755  11.063   3.831  1.00 50.89           O  
ANISOU  621  O   MET H  83     7826   5778   5731    614    952   -225       O  
ATOM    622  CB  MET H  83      38.278  11.573   5.947  1.00 44.01           C  
ANISOU  622  CB  MET H  83     6969   4752   4999    443    797   -177       C  
ATOM    623  CG  MET H  83      37.359  11.937   7.080  1.00 44.45           C  
ANISOU  623  CG  MET H  83     7023   4759   5108    359    720   -147       C  
ATOM    624  SD  MET H  83      37.725  10.938   8.523  1.00 44.30           S  
ANISOU  624  SD  MET H  83     7063   4636   5133    428    681   -167       S  
ATOM    625  CE  MET H  83      38.689  12.130   9.434  1.00 40.16           C  
ANISOU  625  CE  MET H  83     6354   4198   4708    480    653   -156       C  
ATOM    626  N   ASN H  84      38.927  12.800   2.699  1.00 49.05           N  
ANISOU  626  N   ASN H  84     7481   5741   5416    571   1018    -39       N  
ATOM    627  CA  ASN H  84      40.099  12.908   1.810  1.00 50.54           C  
ANISOU  627  CA  ASN H  84     7599   6032   5572    688   1149     12       C  
ATOM    628  C   ASN H  84      41.057  14.068   2.119  1.00 49.91           C  
ANISOU  628  C   ASN H  84     7349   5914   5701    683   1257    158       C  
ATOM    629  O   ASN H  84      40.735  14.972   2.872  1.00 46.02           O  
ANISOU  629  O   ASN H  84     6786   5328   5372    592   1234    219       O  
ATOM    630  CB  ASN H  84      39.666  13.003   0.348  1.00 52.70           C  
ANISOU  630  CB  ASN H  84     7884   6529   5611    774   1212     56       C  
ATOM    631  CG  ASN H  84      38.868  11.818  -0.092  1.00 54.13           C  
ANISOU  631  CG  ASN H  84     8191   6770   5605    780   1110   -159       C  
ATOM    632  OD1 ASN H  84      38.179  11.865  -1.096  1.00 55.48           O  
ANISOU  632  OD1 ASN H  84     8365   7153   5563    834   1103   -180       O  
ATOM    633  ND2 ASN H  84      38.929  10.751   0.674  1.00 55.34           N  
ANISOU  633  ND2 ASN H  84     8438   6739   5850    730   1034   -325       N  
ATOM    634  N   SER H  85      42.232  14.038   1.482  1.00 51.78           N  
ANISOU  634  N   SER H  85     7504   6224   5944    780   1385    197       N  
ATOM    635  CA  SER H  85      43.259  15.069   1.681  1.00 50.09           C  
ANISOU  635  CA  SER H  85     7094   5966   5973    761   1514    312       C  
ATOM    636  C   SER H  85      43.475  15.348   3.159  1.00 47.48           C  
ANISOU  636  C   SER H  85     6686   5481   5874    662   1408    211       C  
ATOM    637  O   SER H  85      43.418  16.504   3.611  1.00 46.41           O  
ANISOU  637  O   SER H  85     6419   5257   5958    569   1443    272       O  
ATOM    638  CB  SER H  85      42.901  16.336   0.911  1.00 51.20           C  
ANISOU  638  CB  SER H  85     7148   6147   6157    753   1666    549       C  
ATOM    639  OG  SER H  85      42.899  16.085  -0.494  1.00 52.46           O  
ANISOU  639  OG  SER H  85     7349   6522   6062    896   1781    654       O  
ATOM    640  N   LEU H  86      43.711  14.265   3.901  1.00 45.18           N  
ANISOU  640  N   LEU H  86     6473   5165   5528    702   1285     52       N  
ATOM    641  CA  LEU H  86      43.801  14.331   5.353  1.00 44.84           C  
ANISOU  641  CA  LEU H  86     6377   5043   5617    657   1160    -52       C  
ATOM    642  C   LEU H  86      45.013  15.147   5.801  1.00 46.81           C  
ANISOU  642  C   LEU H  86     6376   5298   6111    643   1215    -88       C  
ATOM    643  O   LEU H  86      46.017  15.224   5.086  1.00 48.74           O  
ANISOU  643  O   LEU H  86     6508   5599   6412    694   1346    -50       O  
ATOM    644  CB  LEU H  86      43.809  12.922   5.977  1.00 42.28           C  
ANISOU  644  CB  LEU H  86     6197   4702   5164    747   1049   -161       C  
ATOM    645  CG  LEU H  86      42.401  12.382   6.297  1.00 39.84           C  
ANISOU  645  CG  LEU H  86     6077   4323   4738    691    953   -168       C  
ATOM    646  CD1 LEU H  86      42.412  10.923   6.442  1.00 39.10           C  
ANISOU  646  CD1 LEU H  86     6139   4173   4544    782    920   -234       C  
ATOM    647  CD2 LEU H  86      41.748  13.010   7.510  1.00 37.20           C  
ANISOU  647  CD2 LEU H  86     5701   3951   4481    611    855   -174       C  
ATOM    648  N   ARG H  87      44.903  15.785   6.961  1.00 47.42           N  
ANISOU  648  N   ARG H  87     6346   5330   6343    572   1121   -180       N  
ATOM    649  CA  ARG H  87      46.008  16.565   7.525  1.00 49.82           C  
ANISOU  649  CA  ARG H  87     6375   5646   6908    541   1144   -291       C  
ATOM    650  C   ARG H  87      46.160  16.262   8.981  1.00 49.88           C  
ANISOU  650  C   ARG H  87     6328   5723   6901    590    961   -480       C  
ATOM    651  O   ARG H  87      45.255  15.722   9.604  1.00 49.50           O  
ANISOU  651  O   ARG H  87     6450   5677   6680    621    843   -482       O  
ATOM    652  CB  ARG H  87      45.720  18.041   7.453  1.00 51.39           C  
ANISOU  652  CB  ARG H  87     6427   5723   7378    393   1235   -251       C  
ATOM    653  CG  ARG H  87      45.055  18.473   6.195  1.00 52.37           C  
ANISOU  653  CG  ARG H  87     6649   5784   7464    364   1394    -11       C  
ATOM    654  CD  ARG H  87      45.149  19.972   6.082  1.00 52.00           C  
ANISOU  654  CD  ARG H  87     6406   5585   7767    244   1544     57       C  
ATOM    655  NE  ARG H  87      44.246  20.665   6.979  1.00 49.44           N  
ANISOU  655  NE  ARG H  87     6080   5154   7551    158   1440    -32       N  
ATOM    656  CZ  ARG H  87      43.286  21.461   6.540  1.00 48.85           C  
ANISOU  656  CZ  ARG H  87     6062   4968   7530    116   1525    137       C  
ATOM    657  NH1 ARG H  87      43.117  21.596   5.247  1.00 49.52           N  
ANISOU  657  NH1 ARG H  87     6212   5068   7535    169   1701    407       N  
ATOM    658  NH2 ARG H  87      42.521  22.137   7.379  1.00 49.06           N  
ANISOU  658  NH2 ARG H  87     6069   4894   7678     47   1441     40       N  
ATOM    659  N   ALA H  88      47.278  16.689   9.546  1.00 52.02           N  
ANISOU  659  N   ALA H  88     6336   6070   7359    599    944   -642       N  
ATOM    660  CA  ALA H  88      47.529  16.482  10.976  1.00 52.24           C  
ANISOU  660  CA  ALA H  88     6265   6239   7346    685    758   -846       C  
ATOM    661  C   ALA H  88      46.383  17.042  11.821  1.00 51.18           C  
ANISOU  661  C   ALA H  88     6183   6062   7200    612    653   -900       C  
ATOM    662  O   ALA H  88      45.945  16.407  12.767  1.00 51.75           O  
ANISOU  662  O   ALA H  88     6354   6241   7067    723    515   -937       O  
ATOM    663  CB  ALA H  88      48.885  17.078  11.392  1.00 52.45           C  
ANISOU  663  CB  ALA H  88     5937   6379   7614    681    751  -1065       C  
ATOM    664  N   GLU H  89      45.887  18.215  11.444  1.00 51.38           N  
ANISOU  664  N   GLU H  89     6146   5929   7447    443    741   -877       N  
ATOM    665  CA  GLU H  89      44.733  18.855  12.087  1.00 50.47           C  
ANISOU  665  CA  GLU H  89     6081   5751   7345    370    669   -916       C  
ATOM    666  C   GLU H  89      43.496  17.950  12.102  1.00 48.67           C  
ANISOU  666  C   GLU H  89     6155   5529   6808    427    610   -755       C  
ATOM    667  O   GLU H  89      42.577  18.152  12.904  1.00 48.52           O  
ANISOU  667  O   GLU H  89     6186   5528   6723    418    517   -800       O  
ATOM    668  CB  GLU H  89      44.389  20.173  11.375  1.00 51.63           C  
ANISOU  668  CB  GLU H  89     6146   5682   7789    204    824   -843       C  
ATOM    669  CG  GLU H  89      45.469  21.252  11.474  1.00 56.86           C  
ANISOU  669  CG  GLU H  89     6478   6271   8856    103    908  -1024       C  
ATOM    670  CD  GLU H  89      46.680  21.059  10.521  1.00 60.07           C  
ANISOU  670  CD  GLU H  89     6770   6679   9374    107   1067   -934       C  
ATOM    671  OE1 GLU H  89      46.922  19.954   9.962  1.00 59.47           O  
ANISOU  671  OE1 GLU H  89     6850   6716   9032    226   1074   -798       O  
ATOM    672  OE2 GLU H  89      47.413  22.051  10.334  1.00 63.86           O  
ANISOU  672  OE2 GLU H  89     6986   7036  10242    -12   1202  -1013       O  
ATOM    673  N   ASP H  90      43.437  16.948  11.232  1.00 46.30           N  
ANISOU  673  N   ASP H  90     6045   5216   6333    482    670   -586       N  
ATOM    674  CA  ASP H  90      42.233  16.136  11.269  1.00 44.22           C  
ANISOU  674  CA  ASP H  90     6032   4932   5838    503    623   -473       C  
ATOM    675  C   ASP H  90      42.270  15.056  12.338  1.00 43.60           C  
ANISOU  675  C   ASP H  90     6030   4962   5572    647    509   -514       C  
ATOM    676  O   ASP H  90      41.192  14.463  12.631  1.00 43.00           O  
ANISOU  676  O   ASP H  90     6133   4857   5349    651    476   -429       O  
ATOM    677  CB  ASP H  90      41.874  15.536   9.919  1.00 43.63           C  
ANISOU  677  CB  ASP H  90     6131   4790   5656    488    724   -314       C  
ATOM    678  CG  ASP H  90      41.744  16.565   8.865  1.00 44.72           C  
ANISOU  678  CG  ASP H  90     6205   4861   5926    393    851   -218       C  
ATOM    679  OD1 ASP H  90      40.914  17.485   9.013  1.00 43.91           O  
ANISOU  679  OD1 ASP H  90     6077   4697   5908    307    851   -189       O  
ATOM    680  OD2 ASP H  90      42.495  16.454   7.881  1.00 47.18           O  
ANISOU  680  OD2 ASP H  90     6486   5187   6252    425    965   -154       O  
ATOM    681  N   THR H  91      43.455  14.790  12.920  1.00 39.92           N  
ANISOU  681  N   THR H  91     5423   4629   5114    777    462   -624       N  
ATOM    682  CA  THR H  91      43.508  13.745  13.945  1.00 39.47           C  
ANISOU  682  CA  THR H  91     5442   4696   4858    964    373   -613       C  
ATOM    683  C   THR H  91      42.656  14.099  15.132  1.00 37.24           C  
ANISOU  683  C   THR H  91     5149   4504   4496    978    273   -657       C  
ATOM    684  O   THR H  91      42.790  15.165  15.684  1.00 38.64           O  
ANISOU  684  O   THR H  91     5131   4766   4782    931    208   -832       O  
ATOM    685  CB  THR H  91      44.936  13.244  14.393  1.00 42.89           C  
ANISOU  685  CB  THR H  91     5728   5309   5261   1163    330   -701       C  
ATOM    686  OG1 THR H  91      45.029  13.311  15.821  1.00 43.46           O  
ANISOU  686  OG1 THR H  91     5685   5606   5219   1311    195   -808       O  
ATOM    687  CG2 THR H  91      46.097  14.037  13.771  1.00 44.38           C  
ANISOU  687  CG2 THR H  91     5673   5521   5668   1093    379   -835       C  
ATOM    688  N   ALA H  92      41.742  13.215  15.484  1.00 36.77           N  
ANISOU  688  N   ALA H  92     5295   4411   4267   1033    276   -505       N  
ATOM    689  CA  ALA H  92      40.720  13.495  16.479  1.00 38.58           C  
ANISOU  689  CA  ALA H  92     5543   4715   4402   1037    215   -501       C  
ATOM    690  C   ALA H  92      39.961  12.212  16.606  1.00 40.42           C  
ANISOU  690  C   ALA H  92     6007   4863   4487   1103    274   -286       C  
ATOM    691  O   ALA H  92      40.042  11.372  15.713  1.00 42.52           O  
ANISOU  691  O   ALA H  92     6415   4962   4779   1078    360   -187       O  
ATOM    692  CB  ALA H  92      39.784  14.557  15.990  1.00 34.45           C  
ANISOU  692  CB  ALA H  92     5009   4072   4008    826    235   -532       C  
ATOM    693  N   VAL H  93      39.235  12.058  17.708  1.00 42.39           N  
ANISOU  693  N   VAL H  93     6284   5224   4597   1189    242   -224       N  
ATOM    694  CA  VAL H  93      38.286  10.972  17.869  1.00 42.31           C  
ANISOU  694  CA  VAL H  93     6479   5095   4503   1208    332     -2       C  
ATOM    695  C   VAL H  93      37.045  11.459  17.186  1.00 41.46           C  
ANISOU  695  C   VAL H  93     6434   4832   4486    965    363      2       C  
ATOM    696  O   VAL H  93      36.616  12.579  17.442  1.00 42.52           O  
ANISOU  696  O   VAL H  93     6457   5051   4645    887    300   -107       O  
ATOM    697  CB  VAL H  93      37.955  10.742  19.343  1.00 44.11           C  
ANISOU  697  CB  VAL H  93     6684   5538   4536   1406    307     87       C  
ATOM    698  CG1 VAL H  93      36.583  10.090  19.508  1.00 43.02           C  
ANISOU  698  CG1 VAL H  93     6712   5260   4375   1334    416    297       C  
ATOM    699  CG2 VAL H  93      39.065   9.937  20.016  1.00 45.50           C  
ANISOU  699  CG2 VAL H  93     6833   5877   4576   1704    300    159       C  
ATOM    700  N   TYR H  94      36.506  10.647  16.279  1.00 41.02           N  
ANISOU  700  N   TYR H  94     6539   4556   4491    853    455    101       N  
ATOM    701  CA  TYR H  94      35.275  10.958  15.562  1.00 37.64           C  
ANISOU  701  CA  TYR H  94     6163   4013   4126    641    479    103       C  
ATOM    702  C   TYR H  94      34.057  10.298  16.181  1.00 37.71           C  
ANISOU  702  C   TYR H  94     6262   3972   4094    612    539    240       C  
ATOM    703  O   TYR H  94      34.081   9.111  16.489  1.00 36.83           O  
ANISOU  703  O   TYR H  94     6259   3759   3978    693    628    373       O  
ATOM    704  CB  TYR H  94      35.423  10.550  14.108  1.00 37.94           C  
ANISOU  704  CB  TYR H  94     6279   3891   4247    534    529     69       C  
ATOM    705  CG  TYR H  94      36.270  11.538  13.364  1.00 38.71           C  
ANISOU  705  CG  TYR H  94     6262   4047   4400    513    494    -40       C  
ATOM    706  CD1 TYR H  94      37.647  11.578  13.557  1.00 39.79           C  
ANISOU  706  CD1 TYR H  94     6313   4256   4549    645    479    -92       C  
ATOM    707  CD2 TYR H  94      35.700  12.489  12.540  1.00 37.26           C  
ANISOU  707  CD2 TYR H  94     6032   3859   4266    375    490    -74       C  
ATOM    708  CE1 TYR H  94      38.430  12.511  12.934  1.00 39.72           C  
ANISOU  708  CE1 TYR H  94     6172   4286   4633    611    475   -181       C  
ATOM    709  CE2 TYR H  94      36.484  13.457  11.940  1.00 37.66           C  
ANISOU  709  CE2 TYR H  94     5965   3944   4400    366    496   -130       C  
ATOM    710  CZ  TYR H  94      37.844  13.464  12.123  1.00 38.30           C  
ANISOU  710  CZ  TYR H  94     5958   4070   4525    468    496   -186       C  
ATOM    711  OH  TYR H  94      38.634  14.418  11.480  1.00 38.94           O  
ANISOU  711  OH  TYR H  94     5901   4161   4732    438    535   -231       O  
ATOM    712  N   TYR H  95      33.004  11.096  16.366  1.00 37.70           N  
ANISOU  712  N   TYR H  95     6206   4032   4085    503    507    219       N  
ATOM    713  CA  TYR H  95      31.715  10.651  16.885  1.00 37.51           C  
ANISOU  713  CA  TYR H  95     6231   3980   4040    445    571    338       C  
ATOM    714  C   TYR H  95      30.601  10.843  15.872  1.00 38.87           C  
ANISOU  714  C   TYR H  95     6416   4055   4299    226    579    291       C  
ATOM    715  O   TYR H  95      30.527  11.905  15.255  1.00 37.92           O  
ANISOU  715  O   TYR H  95     6219   3992   4196    158    508    186       O  
ATOM    716  CB  TYR H  95      31.353  11.539  18.033  1.00 36.78           C  
ANISOU  716  CB  TYR H  95     6028   4105   3840    527    515    327       C  
ATOM    717  CG  TYR H  95      32.251  11.399  19.191  1.00 37.82           C  
ANISOU  717  CG  TYR H  95     6115   4420   3835    769    490    356       C  
ATOM    718  CD1 TYR H  95      32.374  10.190  19.857  1.00 39.18           C  
ANISOU  718  CD1 TYR H  95     6380   4575   3931    922    593    561       C  
ATOM    719  CD2 TYR H  95      32.960  12.480  19.652  1.00 38.00           C  
ANISOU  719  CD2 TYR H  95     5987   4642   3810    861    371    175       C  
ATOM    720  CE1 TYR H  95      33.202  10.056  20.950  1.00 40.92           C  
ANISOU  720  CE1 TYR H  95     6546   5025   3978   1195    565    606       C  
ATOM    721  CE2 TYR H  95      33.799  12.363  20.740  1.00 39.45           C  
ANISOU  721  CE2 TYR H  95     6094   5058   3836   1106    323    160       C  
ATOM    722  CZ  TYR H  95      33.920  11.154  21.392  1.00 41.53           C  
ANISOU  722  CZ  TYR H  95     6453   5356   3971   1290    413    385       C  
ATOM    723  OH  TYR H  95      34.756  11.068  22.504  1.00 44.08           O  
ANISOU  723  OH  TYR H  95     6683   5976   4089   1582    357    380       O  
ATOM    724  N   CYS H  96      29.708   9.862  15.703  1.00 41.27           N  
ANISOU  724  N   CYS H  96     6795   4217   4667    121    669    366       N  
ATOM    725  CA  CYS H  96      28.494  10.186  14.981  1.00 43.15           C  
ANISOU  725  CA  CYS H  96     6993   4449   4954    -67    652    300       C  
ATOM    726  C   CYS H  96      27.455  10.412  16.049  1.00 44.29           C  
ANISOU  726  C   CYS H  96     7079   4691   5057    -71    684    400       C  
ATOM    727  O   CYS H  96      27.580   9.920  17.157  1.00 47.27           O  
ANISOU  727  O   CYS H  96     7482   5088   5388     50    757    542       O  
ATOM    728  CB  CYS H  96      28.085   9.139  13.956  1.00 45.19           C  
ANISOU  728  CB  CYS H  96     7317   4523   5329   -213    708    237       C  
ATOM    729  SG  CYS H  96      27.505   7.665  14.688  1.00 52.69           S  
ANISOU  729  SG  CYS H  96     8340   5263   6415   -252    875    377       S  
ATOM    730  N   ALA H  97      26.463  11.223  15.740  1.00 43.42           N  
ANISOU  730  N   ALA H  97     6881   4675   4943   -176    633    339       N  
ATOM    731  CA  ALA H  97      25.563  11.702  16.748  1.00 41.88           C  
ANISOU  731  CA  ALA H  97     6607   4618   4688   -152    648    410       C  
ATOM    732  C   ALA H  97      24.219  11.902  16.096  1.00 40.84           C  
ANISOU  732  C   ALA H  97     6400   4506   4611   -324    639    360       C  
ATOM    733  O   ALA H  97      24.142  12.324  14.947  1.00 40.44           O  
ANISOU  733  O   ALA H  97     6325   4459   4581   -398    567    247       O  
ATOM    734  CB  ALA H  97      26.089  12.997  17.300  1.00 39.69           C  
ANISOU  734  CB  ALA H  97     6252   4510   4318    -17    554    343       C  
ATOM    735  N   ARG H  98      23.165  11.561  16.815  1.00 41.15           N  
ANISOU  735  N   ARG H  98     6391   4580   4664   -373    722    456       N  
ATOM    736  CA  ARG H  98      21.810  11.733  16.323  1.00 42.28           C  
ANISOU  736  CA  ARG H  98     6428   4778   4860   -530    715    403       C  
ATOM    737  C   ARG H  98      21.273  13.127  16.712  1.00 39.92           C  
ANISOU  737  C   ARG H  98     6017   4692   4459   -452    638    380       C  
ATOM    738  O   ARG H  98      21.519  13.586  17.812  1.00 39.99           O  
ANISOU  738  O   ARG H  98     6014   4802   4377   -308    651    438       O  
ATOM    739  CB  ARG H  98      20.949  10.637  16.930  1.00 46.22           C  
ANISOU  739  CB  ARG H  98     6908   5189   5465   -631    872    525       C  
ATOM    740  CG  ARG H  98      19.632  10.361  16.252  1.00 48.22           C  
ANISOU  740  CG  ARG H  98     7038   5441   5840   -845    884    433       C  
ATOM    741  CD  ARG H  98      18.577  10.422  17.313  1.00 50.56           C  
ANISOU  741  CD  ARG H  98     7228   5847   6135   -852    991    573       C  
ATOM    742  NE  ARG H  98      17.644   9.310  17.295  1.00 52.67           N  
ANISOU  742  NE  ARG H  98     7424   5972   6618  -1055   1142    607       N  
ATOM    743  CZ  ARG H  98      16.784   9.077  18.281  1.00 54.72           C  
ANISOU  743  CZ  ARG H  98     7594   6280   6917  -1072   1298    779       C  
ATOM    744  NH1 ARG H  98      16.774   9.863  19.346  1.00 53.02           N  
ANISOU  744  NH1 ARG H  98     7363   6279   6501   -877   1305    915       N  
ATOM    745  NH2 ARG H  98      15.943   8.054  18.212  1.00 58.64           N  
ANISOU  745  NH2 ARG H  98     8004   6611   7665  -1283   1458    803       N  
ATOM    746  N   GLU H  99      20.614  13.821  15.781  1.00 38.84           N  
ANISOU  746  N   GLU H  99     5794   4633   4330   -521    557    281       N  
ATOM    747  CA  GLU H  99      19.986  15.106  16.056  1.00 37.87           C  
ANISOU  747  CA  GLU H  99     5561   4679   4148   -446    503    265       C  
ATOM    748  C   GLU H  99      18.560  14.850  16.456  1.00 39.47           C  
ANISOU  748  C   GLU H  99     5646   4986   4364   -533    561    306       C  
ATOM    749  O   GLU H  99      17.941  13.934  15.957  1.00 41.39           O  
ANISOU  749  O   GLU H  99     5857   5178   4691   -693    601    288       O  
ATOM    750  CB  GLU H  99      20.037  16.021  14.829  1.00 38.15           C  
ANISOU  750  CB  GLU H  99     5562   4752   4182   -432    407    185       C  
ATOM    751  CG  GLU H  99      19.502  17.449  15.048  1.00 37.65           C  
ANISOU  751  CG  GLU H  99     5395   4813   4096   -325    367    180       C  
ATOM    752  CD  GLU H  99      20.116  18.509  14.118  1.00 38.03           C  
ANISOU  752  CD  GLU H  99     5448   4828   4171   -239    316    161       C  
ATOM    753  OE1 GLU H  99      19.432  19.545  13.910  1.00 40.09           O  
ANISOU  753  OE1 GLU H  99     5615   5175   4441   -168    298    177       O  
ATOM    754  OE2 GLU H  99      21.265  18.346  13.628  1.00 34.89           O  
ANISOU  754  OE2 GLU H  99     5140   4318   3799   -228    314    151       O  
ATOM    755  N   ARG H 100      18.052  15.627  17.404  1.00 40.36           N  
ANISOU  755  N   ARG H 100     5680   5245   4412   -429    574    343       N  
ATOM    756  CA  ARG H 100      16.655  15.559  17.756  1.00 42.35           C  
ANISOU  756  CA  ARG H 100     5791   5631   4671   -494    630    382       C  
ATOM    757  C   ARG H 100      16.174  16.935  18.182  1.00 42.94           C  
ANISOU  757  C   ARG H 100     5765   5879   4671   -350    579    345       C  
ATOM    758  O   ARG H 100      16.864  17.624  18.931  1.00 44.06           O  
ANISOU  758  O   ARG H 100     5945   6043   4751   -191    561    322       O  
ATOM    759  CB  ARG H 100      16.439  14.557  18.882  1.00 45.26           C  
ANISOU  759  CB  ARG H 100     6172   5982   5044   -513    787    529       C  
ATOM    760  CG  ARG H 100      15.051  14.658  19.463  1.00 48.56           C  
ANISOU  760  CG  ARG H 100     6425   6569   5458   -547    868    589       C  
ATOM    761  CD  ARG H 100      14.601  13.403  20.121  1.00 52.41           C  
ANISOU  761  CD  ARG H 100     6896   6986   6030   -648   1062    756       C  
ATOM    762  NE  ARG H 100      13.150  13.338  20.148  1.00 55.36           N  
ANISOU  762  NE  ARG H 100     7073   7482   6480   -774   1132    768       N  
ATOM    763  CZ  ARG H 100      12.456  12.896  21.186  1.00 59.19           C  
ANISOU  763  CZ  ARG H 100     7474   8044   6970   -768   1319    946       C  
ATOM    764  NH1 ARG H 100      13.096  12.500  22.285  1.00 60.57           N  
ANISOU  764  NH1 ARG H 100     7758   8210   7048   -613   1447   1141       N  
ATOM    765  NH2 ARG H 100      11.130  12.860  21.136  1.00 61.53           N  
ANISOU  765  NH2 ARG H 100     7565   8456   7356   -898   1382    940       N  
ATOM    766  N   TRP H 101      14.982  17.323  17.734  1.00 43.64           N  
ANISOU  766  N   TRP H 101     5708   6097   4775   -398    556    319       N  
ATOM    767  CA  TRP H 101      14.444  18.650  18.024  1.00 43.29           C  
ANISOU  767  CA  TRP H 101     5562   6199   4686   -250    515    283       C  
ATOM    768  C   TRP H 101      13.281  18.588  18.974  1.00 45.66           C  
ANISOU  768  C   TRP H 101     5724   6681   4945   -238    602    336       C  
ATOM    769  O   TRP H 101      12.446  17.704  18.877  1.00 46.31           O  
ANISOU  769  O   TRP H 101     5718   6806   5072   -392    671    386       O  
ATOM    770  CB  TRP H 101      13.967  19.298  16.733  1.00 43.73           C  
ANISOU  770  CB  TRP H 101     5543   6303   4769   -253    423    235       C  
ATOM    771  CG  TRP H 101      15.084  19.734  15.879  1.00 42.18           C  
ANISOU  771  CG  TRP H 101     5464   5964   4598   -201    358    209       C  
ATOM    772  CD1 TRP H 101      16.203  19.020  15.586  1.00 41.90           C  
ANISOU  772  CD1 TRP H 101     5569   5768   4582   -264    358    203       C  
ATOM    773  CD2 TRP H 101      15.223  20.994  15.231  1.00 41.88           C  
ANISOU  773  CD2 TRP H 101     5406   5919   4587    -62    310    209       C  
ATOM    774  NE1 TRP H 101      17.034  19.749  14.793  1.00 41.69           N  
ANISOU  774  NE1 TRP H 101     5603   5655   4583   -183    311    192       N  
ATOM    775  CE2 TRP H 101      16.459  20.974  14.555  1.00 41.64           C  
ANISOU  775  CE2 TRP H 101     5502   5727   4593    -59    291    209       C  
ATOM    776  CE3 TRP H 101      14.430  22.153  15.175  1.00 42.66           C  
ANISOU  776  CE3 TRP H 101     5389   6121   4699     77    300    225       C  
ATOM    777  CZ2 TRP H 101      16.928  22.062  13.811  1.00 40.22           C  
ANISOU  777  CZ2 TRP H 101     5334   5475   4474     64    281    246       C  
ATOM    778  CZ3 TRP H 101      14.879  23.216  14.445  1.00 42.73           C  
ANISOU  778  CZ3 TRP H 101     5420   6042   4775    209    288    265       C  
ATOM    779  CH2 TRP H 101      16.125  23.163  13.756  1.00 42.03           C  
ANISOU  779  CH2 TRP H 101     5456   5781   4733    197    287    285       C  
ATOM    780  N   HIS H 102      13.248  19.511  19.924  1.00 47.16           N  
ANISOU  780  N   HIS H 102     5880   6976   5063    -57    611    310       N  
ATOM    781  CA  HIS H 102      12.027  19.783  20.632  1.00 48.68           C  
ANISOU  781  CA  HIS H 102     5910   7382   5204     -6    677    338       C  
ATOM    782  C   HIS H 102      11.570  21.046  19.932  1.00 48.61           C  
ANISOU  782  C   HIS H 102     5816   7417   5235     91    583    251       C  
ATOM    783  O   HIS H 102      11.006  20.993  18.842  1.00 47.50           O  
ANISOU  783  O   HIS H 102     5606   7298   5144      4    532    256       O  
ATOM    784  CB  HIS H 102      12.263  19.985  22.132  1.00 49.67           C  
ANISOU  784  CB  HIS H 102     6043   7629   5199    166    751    347       C  
ATOM    785  CG  HIS H 102      11.000  19.945  22.948  1.00 52.54           C  
ANISOU  785  CG  HIS H 102     6241   8234   5490    204    863    418       C  
ATOM    786  ND1 HIS H 102      10.053  18.950  22.813  1.00 53.83           N  
ANISOU  786  ND1 HIS H 102     6301   8442   5708     24    975    553       N  
ATOM    787  CD2 HIS H 102      10.521  20.785  23.901  1.00 54.36           C  
ANISOU  787  CD2 HIS H 102     6371   8674   5608    401    890    359       C  
ATOM    788  CE1 HIS H 102       9.039  19.188  23.629  1.00 56.02           C  
ANISOU  788  CE1 HIS H 102     6419   8954   5910    106   1073    600       C  
ATOM    789  NE2 HIS H 102       9.296  20.298  24.300  1.00 56.57           N  
ANISOU  789  NE2 HIS H 102     6494   9139   5860    346   1021    484       N  
ATOM    790  N   VAL H 103      11.892  22.185  20.524  1.00 49.47           N  
ANISOU  790  N   VAL H 103     5930   7535   5330    286    560    161       N  
ATOM    791  CA  VAL H 103      11.747  23.454  19.838  1.00 48.41           C  
ANISOU  791  CA  VAL H 103     5754   7355   5286    404    493     97       C  
ATOM    792  C   VAL H 103      12.917  23.609  18.903  1.00 47.00           C  
ANISOU  792  C   VAL H 103     5713   6944   5200    374    431     86       C  
ATOM    793  O   VAL H 103      12.738  24.000  17.767  1.00 47.82           O  
ANISOU  793  O   VAL H 103     5799   7009   5361    379    390    133       O  
ATOM    794  CB  VAL H 103      11.727  24.624  20.822  1.00 48.77           C  
ANISOU  794  CB  VAL H 103     5750   7441   5340    616    508    -30       C  
ATOM    795  CG1 VAL H 103      11.640  25.950  20.073  1.00 47.38           C  
ANISOU  795  CG1 VAL H 103     5541   7146   5316    745    471    -70       C  
ATOM    796  CG2 VAL H 103      10.563  24.457  21.797  1.00 50.72           C  
ANISOU  796  CG2 VAL H 103     5851   7956   5463    670    585    -12       C  
ATOM    797  N   ARG H 104      14.119  23.293  19.385  1.00 46.05           N  
ANISOU  797  N   ARG H 104     5718   6699   5079    361    431     36       N  
ATOM    798  CA  ARG H 104      15.297  23.326  18.527  1.00 44.49           C  
ANISOU  798  CA  ARG H 104     5643   6290   4973    320    388     32       C  
ATOM    799  C   ARG H 104      16.227  22.137  18.710  1.00 41.61           C  
ANISOU  799  C   ARG H 104     5399   5858   4552    211    395     54       C  
ATOM    800  O   ARG H 104      16.143  21.427  19.701  1.00 40.67           O  
ANISOU  800  O   ARG H 104     5285   5837   4332    205    441     72       O  
ATOM    801  CB  ARG H 104      16.057  24.618  18.743  1.00 46.50           C  
ANISOU  801  CB  ARG H 104     5903   6397   5368    461    376    -92       C  
ATOM    802  CG  ARG H 104      15.178  25.841  18.633  1.00 48.56           C  
ANISOU  802  CG  ARG H 104     6050   6680   5719    598    393   -108       C  
ATOM    803  CD  ARG H 104      15.190  26.328  17.228  1.00 48.83           C  
ANISOU  803  CD  ARG H 104     6097   6596   5859    609    392     16       C  
ATOM    804  NE  ARG H 104      14.475  27.583  17.078  1.00 50.31           N  
ANISOU  804  NE  ARG H 104     6186   6763   6165    777    427     31       N  
ATOM    805  CZ  ARG H 104      13.255  27.632  16.585  1.00 53.02           C  
ANISOU  805  CZ  ARG H 104     6430   7290   6425    826    421    142       C  
ATOM    806  NH1 ARG H 104      12.672  26.486  16.255  1.00 52.51           N  
ANISOU  806  NH1 ARG H 104     6340   7430   6183    690    378    205       N  
ATOM    807  NH2 ARG H 104      12.607  28.790  16.457  1.00 55.17           N  
ANISOU  807  NH2 ARG H 104     6611   7542   6807   1012    462    174       N  
ATOM    808  N   GLY H 105      17.126  21.938  17.756  1.00 38.66           N  
ANISOU  808  N   GLY H 105     5123   5326   4242    149    363     71       N  
ATOM    809  CA  GLY H 105      17.955  20.733  17.745  1.00 38.30           C  
ANISOU  809  CA  GLY H 105     5192   5205   4155     48    373    102       C  
ATOM    810  C   GLY H 105      18.928  20.529  18.908  1.00 38.93           C  
ANISOU  810  C   GLY H 105     5327   5276   4188    127    385     44       C  
ATOM    811  O   GLY H 105      19.489  21.491  19.451  1.00 38.38           O  
ANISOU  811  O   GLY H 105     5225   5195   4161    249    355    -83       O  
ATOM    812  N   TYR H 106      19.084  19.264  19.305  1.00 39.60           N  
ANISOU  812  N   TYR H 106     5478   5375   4192     67    434    131       N  
ATOM    813  CA  TYR H 106      20.124  18.819  20.228  1.00 39.88           C  
ANISOU  813  CA  TYR H 106     5579   5422   4150    159    446    118       C  
ATOM    814  C   TYR H 106      20.559  17.428  19.777  1.00 40.60           C  
ANISOU  814  C   TYR H 106     5787   5390   4250     50    495    237       C  
ATOM    815  O   TYR H 106      19.827  16.771  19.016  1.00 39.91           O  
ANISOU  815  O   TYR H 106     5703   5242   4221   -103    531    306       O  
ATOM    816  CB  TYR H 106      19.626  18.779  21.658  1.00 40.82           C  
ANISOU  816  CB  TYR H 106     5633   5757   4118    289    500    141       C  
ATOM    817  CG  TYR H 106      18.301  18.074  21.838  1.00 43.97           C  
ANISOU  817  CG  TYR H 106     5983   6242   4480    204    607    300       C  
ATOM    818  CD1 TYR H 106      18.245  16.729  22.191  1.00 44.58           C  
ANISOU  818  CD1 TYR H 106     6120   6298   4521    152    726    484       C  
ATOM    819  CD2 TYR H 106      17.097  18.763  21.682  1.00 45.04           C  
ANISOU  819  CD2 TYR H 106     5997   6474   4643    182    606    273       C  
ATOM    820  CE1 TYR H 106      17.030  16.079  22.349  1.00 46.89           C  
ANISOU  820  CE1 TYR H 106     6342   6640   4835     48    850    627       C  
ATOM    821  CE2 TYR H 106      15.869  18.119  21.843  1.00 46.77           C  
ANISOU  821  CE2 TYR H 106     6135   6785   4850     90    710    404       C  
ATOM    822  CZ  TYR H 106      15.839  16.779  22.184  1.00 47.93           C  
ANISOU  822  CZ  TYR H 106     6331   6890   4989     10    837    576       C  
ATOM    823  OH  TYR H 106      14.621  16.149  22.357  1.00 49.62           O  
ANISOU  823  OH  TYR H 106     6441   7170   5243   -103    965    703       O  
ATOM    824  N   PHE H 107      21.766  17.023  20.186  1.00 39.15           N  
ANISOU  824  N   PHE H 107     5682   5170   4025    134    488    231       N  
ATOM    825  CA  PHE H 107      22.288  15.686  19.912  1.00 39.30           C  
ANISOU  825  CA  PHE H 107     5817   5058   4059     73    550    347       C  
ATOM    826  C   PHE H 107      22.050  14.767  21.115  1.00 40.31           C  
ANISOU  826  C   PHE H 107     5964   5282   4073    161    669    517       C  
ATOM    827  O   PHE H 107      22.809  14.807  22.110  1.00 36.92           O  
ANISOU  827  O   PHE H 107     5538   4985   3504    356    662    523       O  
ATOM    828  CB  PHE H 107      23.802  15.720  19.633  1.00 39.71           C  
ANISOU  828  CB  PHE H 107     5936   5021   4129    140    487    269       C  
ATOM    829  CG  PHE H 107      24.201  16.653  18.550  1.00 39.20           C  
ANISOU  829  CG  PHE H 107     5850   4866   4179     85    406    141       C  
ATOM    830  CD1 PHE H 107      23.397  16.833  17.430  1.00 40.41           C  
ANISOU  830  CD1 PHE H 107     5989   4960   4406    -47    402    151       C  
ATOM    831  CD2 PHE H 107      25.400  17.330  18.617  1.00 38.35           C  
ANISOU  831  CD2 PHE H 107     5720   4743   4109    173    344     18       C  
ATOM    832  CE1 PHE H 107      23.791  17.718  16.411  1.00 39.64           C  
ANISOU  832  CE1 PHE H 107     5870   4794   4395    -59    353     85       C  
ATOM    833  CE2 PHE H 107      25.788  18.218  17.614  1.00 37.28           C  
ANISOU  833  CE2 PHE H 107     5555   4500   4109    126    308    -60       C  
ATOM    834  CZ  PHE H 107      24.978  18.428  16.530  1.00 37.71           C  
ANISOU  834  CZ  PHE H 107     5611   4500   4216     25    322     -3       C  
ATOM    835  N   ASP H 108      21.053  13.890  20.993  1.00 41.82           N  
ANISOU  835  N   ASP H 108     6154   5408   4328     28    788    658       N  
ATOM    836  CA  ASP H 108      20.632  13.084  22.132  1.00 45.12           C  
ANISOU  836  CA  ASP H 108     6570   5910   4665    109    949    871       C  
ATOM    837  C   ASP H 108      21.410  11.803  22.342  1.00 47.22           C  
ANISOU  837  C   ASP H 108     6963   6024   4956    157   1062   1046       C  
ATOM    838  O   ASP H 108      21.387  11.228  23.446  1.00 50.95           O  
ANISOU  838  O   ASP H 108     7446   6597   5315    313   1201   1260       O  
ATOM    839  CB  ASP H 108      19.099  12.861  22.207  1.00 46.61           C  
ANISOU  839  CB  ASP H 108     6653   6133   4924    -32   1062    963       C  
ATOM    840  CG  ASP H 108      18.507  12.110  20.992  1.00 47.31           C  
ANISOU  840  CG  ASP H 108     6740   5988   5246   -306   1095    935       C  
ATOM    841  OD1 ASP H 108      19.266  11.684  20.082  1.00 46.32           O  
ANISOU  841  OD1 ASP H 108     6714   5670   5217   -380   1042    856       O  
ATOM    842  OD2 ASP H 108      17.246  11.956  20.970  1.00 47.57           O  
ANISOU  842  OD2 ASP H 108     6652   6061   5363   -443   1173    970       O  
ATOM    843  N   HIS H 109      22.112  11.355  21.310  1.00 44.88           N  
ANISOU  843  N   HIS H 109     6759   5499   4793     54   1018    971       N  
ATOM    844  CA  HIS H 109      22.758  10.053  21.392  1.00 45.78           C  
ANISOU  844  CA  HIS H 109     6996   5419   4978     87   1145   1135       C  
ATOM    845  C   HIS H 109      23.993  10.047  20.553  1.00 44.98           C  
ANISOU  845  C   HIS H 109     6981   5195   4914     99   1033    996       C  
ATOM    846  O   HIS H 109      23.983  10.501  19.408  1.00 43.62           O  
ANISOU  846  O   HIS H 109     6796   4951   4828    -46    923    808       O  
ATOM    847  CB  HIS H 109      21.817   8.959  20.900  1.00 47.13           C  
ANISOU  847  CB  HIS H 109     7174   5343   5389   -142   1306   1229       C  
ATOM    848  CG  HIS H 109      20.802   8.528  21.914  1.00 49.58           C  
ANISOU  848  CG  HIS H 109     7418   5719   5702   -129   1503   1466       C  
ATOM    849  ND1 HIS H 109      19.517   9.025  21.937  1.00 50.11           N  
ANISOU  849  ND1 HIS H 109     7340   5906   5793   -259   1511   1425       N  
ATOM    850  CD2 HIS H 109      20.880   7.633  22.928  1.00 51.88           C  
ANISOU  850  CD2 HIS H 109     7758   5978   5976     15   1719   1772       C  
ATOM    851  CE1 HIS H 109      18.849   8.462  22.928  1.00 52.64           C  
ANISOU  851  CE1 HIS H 109     7617   6268   6116   -211   1727   1687       C  
ATOM    852  NE2 HIS H 109      19.654   7.615  23.544  1.00 53.72           N  
ANISOU  852  NE2 HIS H 109     7874   6312   6226    -41   1864   1916       N  
ATOM    853  N   TRP H 110      25.068   9.544  21.129  1.00 47.03           N  
ANISOU  853  N   TRP H 110     7318   5461   5089    299   1066   1100       N  
ATOM    854  CA  TRP H 110      26.364   9.573  20.462  1.00 47.58           C  
ANISOU  854  CA  TRP H 110     7451   5454   5175    347    964    973       C  
ATOM    855  C   TRP H 110      26.947   8.179  20.457  1.00 50.18           C  
ANISOU  855  C   TRP H 110     7908   5563   5595    407   1105   1142       C  
ATOM    856  O   TRP H 110      26.769   7.432  21.430  1.00 52.31           O  
ANISOU  856  O   TRP H 110     8210   5842   5823    543   1263   1396       O  
ATOM    857  CB  TRP H 110      27.350  10.464  21.230  1.00 46.35           C  
ANISOU  857  CB  TRP H 110     7229   5565   4817    580    837    886       C  
ATOM    858  CG  TRP H 110      26.930  11.912  21.451  1.00 45.34           C  
ANISOU  858  CG  TRP H 110     6966   5646   4614    570    709    703       C  
ATOM    859  CD1 TRP H 110      25.808  12.367  22.070  1.00 44.44           C  
ANISOU  859  CD1 TRP H 110     6773   5678   4435    560    738    735       C  
ATOM    860  CD2 TRP H 110      27.711  13.071  21.139  1.00 43.96           C  
ANISOU  860  CD2 TRP H 110     6712   5547   4443    594    553    464       C  
ATOM    861  NE1 TRP H 110      25.819  13.739  22.120  1.00 43.55           N  
ANISOU  861  NE1 TRP H 110     6546   5709   4290    579    603    517       N  
ATOM    862  CE2 TRP H 110      26.986  14.188  21.560  1.00 43.86           C  
ANISOU  862  CE2 TRP H 110     6584   5692   4390    592    496    353       C  
ATOM    863  CE3 TRP H 110      28.954  13.262  20.531  1.00 42.79           C  
ANISOU  863  CE3 TRP H 110     6569   5333   4356    612    474    338       C  
ATOM    864  CZ2 TRP H 110      27.454  15.474  21.387  1.00 43.86           C  
ANISOU  864  CZ2 TRP H 110     6480   5744   4442    599    373    118       C  
ATOM    865  CZ3 TRP H 110      29.417  14.518  20.364  1.00 42.42           C  
ANISOU  865  CZ3 TRP H 110     6408   5353   4356    609    359    121       C  
ATOM    866  CH2 TRP H 110      28.671  15.619  20.792  1.00 43.74           C  
ANISOU  866  CH2 TRP H 110     6466   5638   4514    599    313     11       C  
ATOM    867  N   GLY H 111      27.692   7.852  19.396  1.00 50.06           N  
ANISOU  867  N   GLY H 111     7962   5362   5696    337   1060   1018       N  
ATOM    868  CA  GLY H 111      28.544   6.660  19.397  1.00 51.66           C  
ANISOU  868  CA  GLY H 111     8286   5371   5973    451   1171   1145       C  
ATOM    869  C   GLY H 111      29.669   6.826  20.400  1.00 52.91           C  
ANISOU  869  C   GLY H 111     8433   5755   5916    767   1132   1238       C  
ATOM    870  O   GLY H 111      29.732   7.814  21.097  1.00 53.75           O  
ANISOU  870  O   GLY H 111     8433   6158   5832    875   1022   1178       O  
ATOM    871  N   GLN H 112      30.562   5.863  20.533  1.00 55.76           N  
ANISOU  871  N   GLN H 112     8888   5999   6300    937   1219   1372       N  
ATOM    872  CA  GLN H 112      31.657   6.100  21.456  1.00 55.95           C  
ANISOU  872  CA  GLN H 112     8865   6305   6087   1257   1151   1428       C  
ATOM    873  C   GLN H 112      32.954   6.410  20.708  1.00 53.58           C  
ANISOU  873  C   GLN H 112     8545   6019   5795   1293   1010   1213       C  
ATOM    874  O   GLN H 112      34.035   6.311  21.264  1.00 55.25           O  
ANISOU  874  O   GLN H 112     8723   6405   5863   1555    969   1247       O  
ATOM    875  CB  GLN H 112      31.799   4.958  22.467  1.00 60.69           C  
ANISOU  875  CB  GLN H 112     9545   6886   6626   1525   1349   1785       C  
ATOM    876  CG  GLN H 112      32.067   5.431  23.954  1.00 64.13           C  
ANISOU  876  CG  GLN H 112     9876   7779   6713   1863   1304   1908       C  
ATOM    877  CD  GLN H 112      30.793   5.656  24.826  1.00 65.87           C  
ANISOU  877  CD  GLN H 112    10049   8146   6834   1851   1402   2069       C  
ATOM    878  OE1 GLN H 112      29.799   6.279  24.405  1.00 64.10           O  
ANISOU  878  OE1 GLN H 112     9778   7866   6710   1579   1363   1924       O  
ATOM    879  NE2 GLN H 112      30.850   5.162  26.067  1.00 70.12           N  
ANISOU  879  NE2 GLN H 112    10586   8909   7149   2180   1533   2384       N  
ATOM    880  N   GLY H 113      32.826   6.792  19.443  1.00 49.78           N  
ANISOU  880  N   GLY H 113     8067   5380   5467   1042    942    998       N  
ATOM    881  CA  GLY H 113      33.951   7.273  18.622  1.00 48.91           C  
ANISOU  881  CA  GLY H 113     7913   5297   5374   1042    820    789       C  
ATOM    882  C   GLY H 113      35.067   6.332  18.167  1.00 49.42           C  
ANISOU  882  C   GLY H 113     8059   5217   5500   1168    874    818       C  
ATOM    883  O   GLY H 113      35.484   5.445  18.917  1.00 52.07           O  
ANISOU  883  O   GLY H 113     8454   5545   5786   1397    970   1019       O  
ATOM    884  N   THR H 114      35.539   6.512  16.931  1.00 46.61           N  
ANISOU  884  N   THR H 114     7707   4759   5245   1043    827    636       N  
ATOM    885  CA  THR H 114      36.845   5.973  16.525  1.00 47.25           C  
ANISOU  885  CA  THR H 114     7810   4797   5344   1194    837    607       C  
ATOM    886  C   THR H 114      37.888   7.042  16.439  1.00 45.99           C  
ANISOU  886  C   THR H 114     7488   4879   5108   1253    698    440       C  
ATOM    887  O   THR H 114      37.634   8.138  15.923  1.00 42.30           O  
ANISOU  887  O   THR H 114     6929   4477   4667   1084    617    290       O  
ATOM    888  CB  THR H 114      36.917   5.342  15.130  1.00 47.61           C  
ANISOU  888  CB  THR H 114     7955   4586   5549   1057    896    500       C  
ATOM    889  OG1 THR H 114      35.707   5.579  14.389  1.00 48.57           O  
ANISOU  889  OG1 THR H 114     8099   4602   5752    791    897    410       O  
ATOM    890  CG2 THR H 114      37.246   3.873  15.233  1.00 50.49           C  
ANISOU  890  CG2 THR H 114     8459   4709   6014   1201   1046    636       C  
ATOM    891  N   LEU H 115      39.098   6.658  16.837  1.00 47.58           N  
ANISOU  891  N   LEU H 115     7648   5186   5245   1495    688    468       N  
ATOM    892  CA  LEU H 115      40.237   7.535  16.747  1.00 47.33           C  
ANISOU  892  CA  LEU H 115     7433   5370   5179   1556    572    292       C  
ATOM    893  C   LEU H 115      40.754   7.543  15.321  1.00 47.33           C  
ANISOU  893  C   LEU H 115     7449   5225   5309   1431    601    174       C  
ATOM    894  O   LEU H 115      41.064   6.490  14.750  1.00 51.15           O  
ANISOU  894  O   LEU H 115     8058   5532   5845   1491    694    226       O  
ATOM    895  CB  LEU H 115      41.346   7.048  17.668  1.00 49.45           C  
ANISOU  895  CB  LEU H 115     7628   5841   5318   1880    548    358       C  
ATOM    896  CG  LEU H 115      42.386   8.105  18.067  1.00 50.43           C  
ANISOU  896  CG  LEU H 115     7492   6287   5384   1963    396    147       C  
ATOM    897  CD1 LEU H 115      43.738   7.491  18.305  1.00 52.14           C  
ANISOU  897  CD1 LEU H 115     7630   6648   5532   2244    384    159       C  
ATOM    898  CD2 LEU H 115      42.532   9.204  17.054  1.00 49.19           C  
ANISOU  898  CD2 LEU H 115     7225   6074   5390   1708    355    -64       C  
ATOM    899  N   VAL H 116      40.853   8.717  14.725  1.00 44.93           N  
ANISOU  899  N   VAL H 116     7018   4992   5063   1272    538     19       N  
ATOM    900  CA  VAL H 116      41.628   8.820  13.483  1.00 44.66           C  
ANISOU  900  CA  VAL H 116     6953   4902   5115   1219    574    -73       C  
ATOM    901  C   VAL H 116      42.952   9.514  13.780  1.00 43.72           C  
ANISOU  901  C   VAL H 116     6608   4990   5013   1326    510   -188       C  
ATOM    902  O   VAL H 116      42.970  10.577  14.374  1.00 43.40           O  
ANISOU  902  O   VAL H 116     6401   5096   4994   1283    427   -285       O  
ATOM    903  CB  VAL H 116      40.897   9.638  12.428  1.00 41.96           C  
ANISOU  903  CB  VAL H 116     6612   4488   4843    983    589   -129       C  
ATOM    904  CG1 VAL H 116      41.774   9.784  11.233  1.00 40.25           C  
ANISOU  904  CG1 VAL H 116     6344   4266   4681    972    643   -194       C  
ATOM    905  CG2 VAL H 116      39.620   8.957  12.074  1.00 42.03           C  
ANISOU  905  CG2 VAL H 116     6803   4327   4840    872    636    -65       C  
ATOM    906  N   THR H 117      44.071   8.922  13.420  1.00 43.28           N  
ANISOU  906  N   THR H 117     6526   4954   4965   1468    547   -203       N  
ATOM    907  CA  THR H 117      45.303   9.650  13.680  1.00 44.47           C  
ANISOU  907  CA  THR H 117     6420   5317   5159   1543    486   -338       C  
ATOM    908  C   THR H 117      46.111   9.830  12.406  1.00 43.74           C  
ANISOU  908  C   THR H 117     6263   5179   5178   1482    571   -395       C  
ATOM    909  O   THR H 117      46.473   8.865  11.769  1.00 43.70           O  
ANISOU  909  O   THR H 117     6373   5087   5143   1577    649   -343       O  
ATOM    910  CB  THR H 117      46.190   9.036  14.791  1.00 46.16           C  
ANISOU  910  CB  THR H 117     6546   5739   5254   1837    420   -330       C  
ATOM    911  OG1 THR H 117      47.414   8.618  14.212  1.00 46.32           O  
ANISOU  911  OG1 THR H 117     6489   5797   5314   1959    465   -368       O  
ATOM    912  CG2 THR H 117      45.523   7.865  15.525  1.00 47.75           C  
ANISOU  912  CG2 THR H 117     6961   5867   5315   2003    452   -127       C  
ATOM    913  N   VAL H 118      46.363  11.075  12.019  1.00 43.55           N  
ANISOU  913  N   VAL H 118     6051   5201   5294   1326    574   -495       N  
ATOM    914  CA  VAL H 118      46.996  11.322  10.733  1.00 44.16           C  
ANISOU  914  CA  VAL H 118     6071   5236   5472   1260    692   -501       C  
ATOM    915  C   VAL H 118      48.487  11.606  10.886  1.00 47.49           C  
ANISOU  915  C   VAL H 118     6223   5827   5995   1358    691   -616       C  
ATOM    916  O   VAL H 118      48.875  12.649  11.406  1.00 51.45           O  
ANISOU  916  O   VAL H 118     6478   6426   6643   1284    641   -747       O  
ATOM    917  CB  VAL H 118      46.377  12.513  10.026  1.00 41.53           C  
ANISOU  917  CB  VAL H 118     5694   4822   5264   1037    752   -484       C  
ATOM    918  CG1 VAL H 118      47.133  12.796   8.762  1.00 42.09           C  
ANISOU  918  CG1 VAL H 118     5680   4890   5422   1008    898   -453       C  
ATOM    919  CG2 VAL H 118      44.925  12.264   9.734  1.00 39.98           C  
ANISOU  919  CG2 VAL H 118     5732   4494   4963    944    752   -385       C  
ATOM    920  N   SER H 119      49.344  10.723  10.420  1.00 46.73           N  
ANISOU  920  N   SER H 119     6146   5763   5847   1517    751   -595       N  
ATOM    921  CA  SER H 119      50.712  10.998  10.652  1.00 49.49           C  
ANISOU  921  CA  SER H 119     6213   6300   6292   1613    740   -714       C  
ATOM    922  C   SER H 119      51.613  10.187   9.778  1.00 51.11           C  
ANISOU  922  C   SER H 119     6435   6520   6465   1755    850   -677       C  
ATOM    923  O   SER H 119      51.389   9.001   9.537  1.00 51.63           O  
ANISOU  923  O   SER H 119     6734   6493   6390   1896    880   -592       O  
ATOM    924  CB  SER H 119      51.044  10.780  12.126  1.00 52.13           C  
ANISOU  924  CB  SER H 119     6432   6835   6540   1793    576   -806       C  
ATOM    925  OG  SER H 119      52.423  10.492  12.311  1.00 56.49           O  
ANISOU  925  OG  SER H 119     6761   7597   7105   1983    558   -901       O  
ATOM    926  N   SER H 120      52.639  10.861   9.285  1.00 52.55           N  
ANISOU  926  N   SER H 120     6353   6805   6809   1711    929   -752       N  
ATOM    927  CA  SER H 120      53.599  10.235   8.416  1.00 53.08           C  
ANISOU  927  CA  SER H 120     6388   6924   6857   1846   1050   -729       C  
ATOM    928  C   SER H 120      54.667   9.748   9.344  1.00 51.27           C  
ANISOU  928  C   SER H 120     5972   6908   6600   2080    948   -834       C  
ATOM    929  O   SER H 120      55.707   9.314   8.909  1.00 52.01           O  
ANISOU  929  O   SER H 120     5950   7108   6701   2227   1021   -855       O  
ATOM    930  CB  SER H 120      54.140  11.229   7.366  1.00 56.00           C  
ANISOU  930  CB  SER H 120     6552   7306   7418   1685   1221   -718       C  
ATOM    931  OG  SER H 120      54.187  12.564   7.871  1.00 58.23           O  
ANISOU  931  OG  SER H 120     6581   7605   7940   1488   1195   -807       O  
ATOM    932  N   ALA H 121      54.383   9.823  10.638  1.00101.05           N  
ANISOU  932  N   ALA H 121    15092  14220   9084    674     83  -3578       N  
ATOM    933  CA  ALA H 121      55.263   9.246  11.621  1.00 96.22           C  
ANISOU  933  CA  ALA H 121    14738  12800   9019    753    351  -3494       C  
ATOM    934  C   ALA H 121      55.134   7.748  11.511  1.00100.84           C  
ANISOU  934  C   ALA H 121    15967  12802   9547    367    292  -4083       C  
ATOM    935  O   ALA H 121      54.059   7.216  11.219  1.00105.33           O  
ANISOU  935  O   ALA H 121    16616  13525   9879   -219    -62  -4487       O  
ATOM    936  CB  ALA H 121      54.895   9.698  12.998  1.00 90.63           C  
ANISOU  936  CB  ALA H 121    13589  11994   8850    525    287  -3100       C  
ATOM    937  N   SER H 122      56.263   7.086  11.713  1.00 99.64           N  
ANISOU  937  N   SER H 122    16268  11983   9608    713    657  -4110       N  
ATOM    938  CA  SER H 122      56.359   5.645  11.683  1.00103.32           C  
ANISOU  938  CA  SER H 122    17439  11726  10094    470    725  -4617       C  
ATOM    939  C   SER H 122      57.744   5.368  12.233  1.00 99.73           C  
ANISOU  939  C   SER H 122    17206  10683  10002   1036   1212  -4314       C  
ATOM    940  O   SER H 122      58.751   5.461  11.502  1.00100.61           O  
ANISOU  940  O   SER H 122    17546  10816   9865   1666   1524  -4260       O  
ATOM    941  CB  SER H 122      56.268   5.144  10.250  1.00110.85           C  
ANISOU  941  CB  SER H 122    18924  12824  10371    524    651  -5211       C  
ATOM    942  OG  SER H 122      57.321   5.700   9.487  1.00110.37           O  
ANISOU  942  OG  SER H 122    18903  13016  10018   1315    979  -4995       O  
ATOM    943  N   THR H 123      57.800   5.096  13.541  1.00 95.16           N  
ANISOU  943  N   THR H 123    16489   9669   9997    853   1282  -4044       N  
ATOM    944  CA  THR H 123      59.073   4.834  14.194  1.00 91.99           C  
ANISOU  944  CA  THR H 123    16210   8789   9954   1366   1717  -3694       C  
ATOM    945  C   THR H 123      60.177   5.824  13.796  1.00 88.56           C  
ANISOU  945  C   THR H 123    15476   8747   9425   2062   1963  -3260       C  
ATOM    946  O   THR H 123      60.636   5.841  12.655  1.00 92.02           O  
ANISOU  946  O   THR H 123    16178   9353   9433   2458   2112  -3409       O  
ATOM    947  CB  THR H 123      59.538   3.372  13.943  1.00 97.93           C  
ANISOU  947  CB  THR H 123    17788   8750  10671   1457   2013  -4086       C  
ATOM    948  OG1 THR H 123      58.658   2.466  14.635  1.00 99.93           O  
ANISOU  948  OG1 THR H 123    18244   8512  11214    801   1850  -4334       O  
ATOM    949  CG2 THR H 123      60.952   3.160  14.459  1.00 96.18           C  
ANISOU  949  CG2 THR H 123    17653   8161  10729   2121   2510  -3650       C  
ATOM    950  N   LYS H 124      60.565   6.671  14.748  1.00 82.34           N  
ANISOU  950  N   LYS H 124    14123   8124   9037   2187   1990  -2719       N  
ATOM    951  CA  LYS H 124      61.793   7.458  14.653  1.00 79.46           C  
ANISOU  951  CA  LYS H 124    13466   7970   8757   2791   2264  -2233       C  
ATOM    952  C   LYS H 124      62.287   7.670  16.078  1.00 74.83           C  
ANISOU  952  C   LYS H 124    12516   7205   8710   2798   2319  -1794       C  
ATOM    953  O   LYS H 124      61.513   8.073  16.943  1.00 71.31           O  
ANISOU  953  O   LYS H 124    11743   6867   8487   2397   2046  -1730       O  
ATOM    954  CB  LYS H 124      61.541   8.807  13.974  1.00 77.06           C  
ANISOU  954  CB  LYS H 124    12698   8346   8237   2884   2109  -2048       C  
ATOM    955  CG  LYS H 124      62.663   9.826  14.169  1.00 73.08           C  
ANISOU  955  CG  LYS H 124    11734   8047   7986   3341   2322  -1458       C  
ATOM    956  CD  LYS H 124      62.211  11.237  13.801  1.00 69.94           C  
ANISOU  956  CD  LYS H 124    10834   8225   7517   3315   2147  -1228       C  
ATOM    957  CE  LYS H 124      63.292  12.258  14.118  1.00 66.75           C  
ANISOU  957  CE  LYS H 124     9967   7930   7464   3653   2331   -649       C  
ATOM    958  NZ  LYS H 124      63.807  12.081  15.507  1.00 63.24           N  
ANISOU  958  NZ  LYS H 124     9375   7141   7512   3536   2329   -450       N  
ATOM    959  N   GLY H 125      63.557   7.354  16.329  1.00 75.60           N  
ANISOU  959  N   GLY H 125    12678   7066   8980   3273   2675  -1489       N  
ATOM    960  CA  GLY H 125      64.163   7.552  17.649  1.00 71.89           C  
ANISOU  960  CA  GLY H 125    11838   6512   8967   3331   2723  -1053       C  
ATOM    961  C   GLY H 125      64.271   9.022  18.017  1.00 66.87           C  
ANISOU  961  C   GLY H 125    10546   6355   8509   3297   2522   -695       C  
ATOM    962  O   GLY H 125      64.249   9.891  17.142  1.00 67.65           O  
ANISOU  962  O   GLY H 125    10467   6822   8416   3404   2481   -647       O  
ATOM    963  N   PRO H 126      64.382   9.319  19.316  1.00 62.74           N  
ANISOU  963  N   PRO H 126     9678   5817   8341   3161   2406   -442       N  
ATOM    964  CA  PRO H 126      64.352  10.695  19.737  1.00 59.43           C  
ANISOU  964  CA  PRO H 126     8723   5766   8093   3059   2184   -193       C  
ATOM    965  C   PRO H 126      65.738  11.276  19.807  1.00 59.99           C  
ANISOU  965  C   PRO H 126     8459   5975   8360   3424   2357    254       C  
ATOM    966  O   PRO H 126      66.703  10.545  19.933  1.00 62.99           O  
ANISOU  966  O   PRO H 126     8941   6190   8803   3742   2624    440       O  
ATOM    967  CB  PRO H 126      63.784  10.595  21.145  1.00 56.33           C  
ANISOU  967  CB  PRO H 126     8193   5275   7934   2747   1974   -190       C  
ATOM    968  CG  PRO H 126      64.326   9.357  21.635  1.00 58.48           C  
ANISOU  968  CG  PRO H 126     8737   5182   8301   2907   2206   -148       C  
ATOM    969  CD  PRO H 126      64.388   8.409  20.467  1.00 62.65           C  
ANISOU  969  CD  PRO H 126     9787   5454   8562   3068   2454   -410       C  
ATOM    970  N   SER H 127      65.834  12.591  19.721  1.00 59.52           N  
ANISOU  970  N   SER H 127     7989   6214   8412   3378   2219    454       N  
ATOM    971  CA  SER H 127      67.086  13.259  19.987  1.00 60.49           C  
ANISOU  971  CA  SER H 127     7703   6472   8811   3587   2306    898       C  
ATOM    972  C   SER H 127      67.041  13.692  21.448  1.00 58.38           C  
ANISOU  972  C   SER H 127     7143   6200   8837   3314   2036    970       C  
ATOM    973  O   SER H 127      66.032  14.257  21.903  1.00 56.58           O  
ANISOU  973  O   SER H 127     6878   6007   8613   3000   1771    773       O  
ATOM    974  CB  SER H 127      67.223  14.489  19.088  1.00 60.93           C  
ANISOU  974  CB  SER H 127     7486   6796   8868   3657   2317   1088       C  
ATOM    975  OG  SER H 127      66.665  14.271  17.805  1.00 62.44           O  
ANISOU  975  OG  SER H 127     7972   7077   8677   3794   2437    883       O  
ATOM    976  N   VAL H 128      68.112  13.432  22.190  1.00 58.53           N  
ANISOU  976  N   VAL H 128     6951   6225   9062   3465   2106   1262       N  
ATOM    977  CA  VAL H 128      68.167  13.892  23.572  1.00 57.00           C  
ANISOU  977  CA  VAL H 128     6465   6098   9093   3234   1827   1323       C  
ATOM    978  C   VAL H 128      69.070  15.109  23.772  1.00 58.32           C  
ANISOU  978  C   VAL H 128     6141   6482   9538   3172   1697   1627       C  
ATOM    979  O   VAL H 128      70.221  15.144  23.296  1.00 61.08           O  
ANISOU  979  O   VAL H 128     6256   6957   9996   3411   1891   1988       O  
ATOM    980  CB  VAL H 128      68.609  12.786  24.530  1.00 57.50           C  
ANISOU  980  CB  VAL H 128     6585   6078   9183   3377   1914   1425       C  
ATOM    981  CG1 VAL H 128      68.655  13.312  25.961  1.00 55.67           C  
ANISOU  981  CG1 VAL H 128     6040   6001   9110   3167   1598   1473       C  
ATOM    982  CG2 VAL H 128      67.693  11.586  24.414  1.00 57.66           C  
ANISOU  982  CG2 VAL H 128     7105   5798   9005   3371   2044   1131       C  
ATOM    983  N   PHE H 129      68.532  16.102  24.480  1.00 56.58           N  
ANISOU  983  N   PHE H 129     5773   6289   9434   2849   1377   1487       N  
ATOM    984  CA  PHE H 129      69.300  17.244  24.935  1.00 58.08           C  
ANISOU  984  CA  PHE H 129     5545   6601   9920   2683   1183   1688       C  
ATOM    985  C   PHE H 129      69.249  17.388  26.464  1.00 59.00           C  
ANISOU  985  C   PHE H 129     5547   6772  10099   2472    858   1567       C  
ATOM    986  O   PHE H 129      68.198  17.157  27.090  1.00 57.25           O  
ANISOU  986  O   PHE H 129     5571   6475   9709   2380    733   1275       O  
ATOM    987  CB  PHE H 129      68.768  18.503  24.285  1.00 57.61           C  
ANISOU  987  CB  PHE H 129     5459   6485   9946   2517   1121   1625       C  
ATOM    988  CG  PHE H 129      68.685  18.425  22.789  1.00 58.44           C  
ANISOU  988  CG  PHE H 129     5677   6609   9920   2752   1424   1734       C  
ATOM    989  CD1 PHE H 129      69.774  18.040  22.042  1.00 60.39           C  
ANISOU  989  CD1 PHE H 129     5776   6964  10206   3046   1702   2084       C  
ATOM    990  CD2 PHE H 129      67.521  18.782  22.128  1.00 57.35           C  
ANISOU  990  CD2 PHE H 129     5767   6441   9583   2715   1434   1518       C  
ATOM    991  CE1 PHE H 129      69.698  17.979  20.683  1.00 61.28           C  
ANISOU  991  CE1 PHE H 129     6011   7134  10137   3313   1983   2175       C  
ATOM    992  CE2 PHE H 129      67.450  18.726  20.755  1.00 58.19           C  
ANISOU  992  CE2 PHE H 129     5964   6641   9507   2955   1691   1612       C  
ATOM    993  CZ  PHE H 129      68.538  18.325  20.038  1.00 59.81           C  
ANISOU  993  CZ  PHE H 129     6062   6934   9730   3260   1964   1923       C  
ATOM    994  N   PRO H 130      70.380  17.797  27.071  1.00 61.56           N  
ANISOU  994  N   PRO H 130     5469   7275  10645   2394    710   1806       N  
ATOM    995  CA  PRO H 130      70.453  17.963  28.513  1.00 62.25           C  
ANISOU  995  CA  PRO H 130     5425   7489  10737   2216    375   1686       C  
ATOM    996  C   PRO H 130      69.842  19.292  28.990  1.00 62.40           C  
ANISOU  996  C   PRO H 130     5477   7388  10846   1874     53   1389       C  
ATOM    997  O   PRO H 130      70.125  20.361  28.428  1.00 64.53           O  
ANISOU  997  O   PRO H 130     5606   7550  11363   1693     20   1455       O  
ATOM    998  CB  PRO H 130      71.952  17.957  28.778  1.00 66.06           C  
ANISOU  998  CB  PRO H 130     5426   8263  11412   2243    333   2075       C  
ATOM    999  CG  PRO H 130      72.585  18.469  27.497  1.00 67.87           C  
ANISOU  999  CG  PRO H 130     5465   8455  11865   2277    551   2374       C  
ATOM   1000  CD  PRO H 130      71.558  18.363  26.393  1.00 64.62           C  
ANISOU 1000  CD  PRO H 130     5473   7780  11299   2411    805   2191       C  
ATOM   1001  N   LEU H 131      69.010  19.221  30.023  1.00 60.76           N  
ANISOU 1001  N   LEU H 131     5468   7179  10441   1820   -146   1093       N  
ATOM   1002  CA  LEU H 131      68.489  20.423  30.657  1.00 60.42           C  
ANISOU 1002  CA  LEU H 131     5500   7025  10433   1565   -442    801       C  
ATOM   1003  C   LEU H 131      69.410  20.948  31.776  1.00 64.40           C  
ANISOU 1003  C   LEU H 131     5720   7713  11035   1351   -807    766       C  
ATOM   1004  O   LEU H 131      69.300  20.559  32.944  1.00 63.92           O  
ANISOU 1004  O   LEU H 131     5678   7861  10748   1405  -1002    635       O  
ATOM   1005  CB  LEU H 131      67.062  20.187  31.134  1.00 56.86           C  
ANISOU 1005  CB  LEU H 131     5409   6510   9687   1652   -451    521       C  
ATOM   1006  CG  LEU H 131      66.142  19.882  29.950  1.00 53.66           C  
ANISOU 1006  CG  LEU H 131     5232   5957   9198   1764   -160    530       C  
ATOM   1007  CD1 LEU H 131      64.693  19.837  30.395  1.00 51.01           C  
ANISOU 1007  CD1 LEU H 131     5174   5601   8606   1799   -194    302       C  
ATOM   1008  CD2 LEU H 131      66.329  20.912  28.828  1.00 53.64           C  
ANISOU 1008  CD2 LEU H 131     5169   5796   9418   1674    -63    619       C  
ATOM   1009  N   ALA H 132      70.315  21.844  31.378  1.00 68.58           N  
ANISOU 1009  N   ALA H 132     5971   8185  11903   1098   -900    902       N  
ATOM   1010  CA  ALA H 132      71.373  22.373  32.232  1.00 74.20           C  
ANISOU 1010  CA  ALA H 132     6330   9095  12768    805  -1269    909       C  
ATOM   1011  C   ALA H 132      70.831  23.179  33.400  1.00 76.49           C  
ANISOU 1011  C   ALA H 132     6849   9296  12918    591  -1652    436       C  
ATOM   1012  O   ALA H 132      70.091  24.146  33.197  1.00 76.80           O  
ANISOU 1012  O   ALA H 132     7192   8952  13034    466  -1662    178       O  
ATOM   1013  CB  ALA H 132      72.325  23.230  31.407  1.00 77.34           C  
ANISOU 1013  CB  ALA H 132     6391   9378  13618    527  -1253   1178       C  
ATOM   1014  N   PRO H 133      71.238  22.807  34.624  1.00 79.46           N  
ANISOU 1014  N   PRO H 133     7079  10047  13066    586  -1953    342       N  
ATOM   1015  CA  PRO H 133      70.762  23.446  35.850  1.00 81.43           C  
ANISOU 1015  CA  PRO H 133     7570  10294  13078    459  -2327   -128       C  
ATOM   1016  C   PRO H 133      71.273  24.864  36.035  1.00 86.35           C  
ANISOU 1016  C   PRO H 133     8155  10667  13988    -39  -2679   -393       C  
ATOM   1017  O   PRO H 133      72.427  25.161  35.724  1.00 89.49           O  
ANISOU 1017  O   PRO H 133     8121  11153  14729   -358  -2805   -161       O  
ATOM   1018  CB  PRO H 133      71.325  22.545  36.955  1.00 83.68           C  
ANISOU 1018  CB  PRO H 133     7589  11159  13045    621  -2526    -38       C  
ATOM   1019  CG  PRO H 133      72.538  21.902  36.344  1.00 84.85           C  
ANISOU 1019  CG  PRO H 133     7226  11590  13424    637  -2384    482       C  
ATOM   1020  CD  PRO H 133      72.241  21.753  34.883  1.00 80.97           C  
ANISOU 1020  CD  PRO H 133     6848  10730  13187    753  -1931    721       C  
ATOM   1021  N   SER H 134      70.396  25.724  36.538  1.00 87.98           N  
ANISOU 1021  N   SER H 134     8823  10545  14062    -96  -2815   -857       N  
ATOM   1022  CA  SER H 134      70.770  27.057  36.986  1.00 94.72           C  
ANISOU 1022  CA  SER H 134     9774  11100  15117   -562  -3191  -1233       C  
ATOM   1023  C   SER H 134      70.953  27.061  38.509  1.00 99.15           C  
ANISOU 1023  C   SER H 134    10383  12026  15262   -617  -3669  -1635       C  
ATOM   1024  O   SER H 134      70.246  26.341  39.229  1.00 96.32           O  
ANISOU 1024  O   SER H 134    10214  11968  14417   -197  -3627  -1723       O  
ATOM   1025  CB  SER H 134      69.691  28.074  36.592  1.00 94.39           C  
ANISOU 1025  CB  SER H 134    10279  10422  15162   -531  -3005  -1505       C  
ATOM   1026  OG  SER H 134      69.809  28.453  35.229  1.00 93.99           O  
ANISOU 1026  OG  SER H 134    10122  10017  15572   -624  -2671  -1167       O  
ATOM   1027  N   SER H 135      71.900  27.873  38.990  1.00106.06           N  
ANISOU 1027  N   SER H 135    11074  12897  16327  -1143  -4129  -1866       N  
ATOM   1028  CA  SER H 135      72.131  28.033  40.428  1.00111.07           C  
ANISOU 1028  CA  SER H 135    11772  13891  16537  -1253  -4653  -2324       C  
ATOM   1029  C   SER H 135      71.475  29.318  40.933  1.00114.61           C  
ANISOU 1029  C   SER H 135    12866  13759  16921  -1437  -4856  -2986       C  
ATOM   1030  O   SER H 135      70.241  29.448  40.917  1.00110.46           O  
ANISOU 1030  O   SER H 135    12881  12919  16171  -1030  -4565  -3153       O  
ATOM   1031  CB  SER H 135      73.635  28.052  40.749  1.00117.42           C  
ANISOU 1031  CB  SER H 135    11933  15163  17519  -1747  -5104  -2193       C  
ATOM   1032  OG  SER H 135      74.167  29.369  40.675  1.00123.80           O  
ANISOU 1032  OG  SER H 135    12789  15498  18753  -2427  -5440  -2516       O  
ATOM   1033  N   ALA H 143      68.856  22.897  43.337  1.00 87.99           N  
ANISOU 1033  N   ALA H 143     9211  12937  11285   1454  -3770  -1667       N  
ATOM   1034  CA  ALA H 143      69.121  22.871  41.896  1.00 84.08           C  
ANISOU 1034  CA  ALA H 143     8572  12029  11343   1229  -3474  -1373       C  
ATOM   1035  C   ALA H 143      68.257  21.856  41.152  1.00 77.85           C  
ANISOU 1035  C   ALA H 143     7883  11096  10599   1591  -2940  -1005       C  
ATOM   1036  O   ALA H 143      68.042  20.737  41.616  1.00 76.86           O  
ANISOU 1036  O   ALA H 143     7669  11314  10219   1960  -2769   -738       O  
ATOM   1037  CB  ALA H 143      70.596  22.603  41.630  1.00 86.46           C  
ANISOU 1037  CB  ALA H 143     8296  12644  11910    962  -3626  -1062       C  
ATOM   1038  N   ALA H 144      67.770  22.251  39.982  1.00 74.88           N  
ANISOU 1038  N   ALA H 144     7688  10211  10552   1469  -2678   -984       N  
ATOM   1039  CA  ALA H 144      67.046  21.330  39.103  1.00 69.59           C  
ANISOU 1039  CA  ALA H 144     7088   9394   9958   1712  -2215   -667       C  
ATOM   1040  C   ALA H 144      67.747  21.179  37.747  1.00 67.24           C  
ANISOU 1040  C   ALA H 144     6564   8894  10089   1533  -2001   -375       C  
ATOM   1041  O   ALA H 144      68.305  22.141  37.217  1.00 69.10           O  
ANISOU 1041  O   ALA H 144     6722   8903  10629   1210  -2124   -457       O  
ATOM   1042  CB  ALA H 144      65.598  21.810  38.912  1.00 67.86           C  
ANISOU 1042  CB  ALA H 144     7300   8857   9626   1833  -2051   -867       C  
ATOM   1043  N   LEU H 145      67.711  19.970  37.196  1.00 63.91           N  
ANISOU 1043  N   LEU H 145     6059   8535   9688   1761  -1662    -29       N  
ATOM   1044  CA  LEU H 145      68.287  19.682  35.881  1.00 62.37           C  
ANISOU 1044  CA  LEU H 145     5709   8174   9816   1701  -1398    258       C  
ATOM   1045  C   LEU H 145      67.523  18.515  35.242  1.00 59.64           C  
ANISOU 1045  C   LEU H 145     5555   7709   9395   1967   -994    436       C  
ATOM   1046  O   LEU H 145      66.808  17.798  35.931  1.00 58.81           O  
ANISOU 1046  O   LEU H 145     5594   7709   9044   2173   -931    428       O  
ATOM   1047  CB  LEU H 145      69.771  19.358  36.016  1.00 65.20           C  
ANISOU 1047  CB  LEU H 145     5611   8860  10301   1663  -1492    555       C  
ATOM   1048  CG  LEU H 145      70.138  18.276  37.027  1.00 66.15           C  
ANISOU 1048  CG  LEU H 145     5554   9431  10150   1956  -1504    760       C  
ATOM   1049  CD1 LEU H 145      69.785  16.943  36.460  1.00 64.43           C  
ANISOU 1049  CD1 LEU H 145     5471   9103   9907   2294  -1045   1049       C  
ATOM   1050  CD2 LEU H 145      71.609  18.309  37.352  1.00 70.73           C  
ANISOU 1050  CD2 LEU H 145     5621  10436  10817   1865  -1714   1014       C  
ATOM   1051  N   GLY H 146      67.624  18.349  33.928  1.00 59.08           N  
ANISOU 1051  N   GLY H 146     5505   7414   9529   1951   -724    585       N  
ATOM   1052  CA  GLY H 146      66.826  17.322  33.249  1.00 58.08           C  
ANISOU 1052  CA  GLY H 146     5620   7128   9318   2131   -384    661       C  
ATOM   1053  C   GLY H 146      67.335  16.793  31.908  1.00 59.35           C  
ANISOU 1053  C   GLY H 146     5765   7147   9636   2207    -73    877       C  
ATOM   1054  O   GLY H 146      68.489  16.993  31.531  1.00 61.51           O  
ANISOU 1054  O   GLY H 146     5769   7509  10092   2202    -56   1092       O  
ATOM   1055  N   CYS H 147      66.470  16.075  31.201  1.00 58.28           N  
ANISOU 1055  N   CYS H 147     5915   6821   9409   2286    175    830       N  
ATOM   1056  CA  CYS H 147      66.726  15.699  29.818  1.00 58.71           C  
ANISOU 1056  CA  CYS H 147     6054   6720   9533   2364    458    936       C  
ATOM   1057  C   CYS H 147      65.521  16.028  28.956  1.00 57.43           C  
ANISOU 1057  C   CYS H 147     6142   6401   9276   2248    506    718       C  
ATOM   1058  O   CYS H 147      64.387  15.659  29.280  1.00 56.63           O  
ANISOU 1058  O   CYS H 147     6239   6261   9017   2193    483    559       O  
ATOM   1059  CB  CYS H 147      67.030  14.218  29.701  1.00 60.48           C  
ANISOU 1059  CB  CYS H 147     6412   6873   9694   2614    751   1102       C  
ATOM   1060  SG  CYS H 147      68.739  13.814  30.019  1.00 64.54           S  
ANISOU 1060  SG  CYS H 147     6578   7615  10331   2870    850   1513       S  
ATOM   1061  N   LEU H 148      65.770  16.742  27.866  1.00 57.06           N  
ANISOU 1061  N   LEU H 148     6043   6315   9322   2220    576    759       N  
ATOM   1062  CA  LEU H 148      64.747  17.017  26.875  1.00 55.15           C  
ANISOU 1062  CA  LEU H 148     5995   6008   8953   2166    653    613       C  
ATOM   1063  C   LEU H 148      64.801  15.883  25.887  1.00 56.05           C  
ANISOU 1063  C   LEU H 148     6316   6043   8938   2315    923    628       C  
ATOM   1064  O   LEU H 148      65.769  15.756  25.152  1.00 58.26           O  
ANISOU 1064  O   LEU H 148     6524   6324   9287   2490   1107    815       O  
ATOM   1065  CB  LEU H 148      65.091  18.322  26.169  1.00 55.90           C  
ANISOU 1065  CB  LEU H 148     5921   6110   9207   2121    640    706       C  
ATOM   1066  CG  LEU H 148      64.455  18.709  24.836  1.00 55.98           C  
ANISOU 1066  CG  LEU H 148     6034   6135   9102   2165    791    692       C  
ATOM   1067  CD1 LEU H 148      62.966  18.459  24.885  1.00 55.26           C  
ANISOU 1067  CD1 LEU H 148     6159   6093   8745   2085    732    463       C  
ATOM   1068  CD2 LEU H 148      64.746  20.185  24.513  1.00 56.16           C  
ANISOU 1068  CD2 LEU H 148     5864   6128   9348   2111    763    830       C  
ATOM   1069  N   VAL H 149      63.814  14.999  25.909  1.00 55.86           N  
ANISOU 1069  N   VAL H 149     6556   5941   8729   2253    956    444       N  
ATOM   1070  CA  VAL H 149      63.828  13.865  24.968  1.00 56.97           C  
ANISOU 1070  CA  VAL H 149     6980   5934   8731   2359   1199    378       C  
ATOM   1071  C   VAL H 149      62.778  14.144  23.918  1.00 56.69           C  
ANISOU 1071  C   VAL H 149     7087   5974   8480   2229   1173    174       C  
ATOM   1072  O   VAL H 149      61.580  14.215  24.213  1.00 56.42           O  
ANISOU 1072  O   VAL H 149     7091   6007   8339   2010   1017     20       O  
ATOM   1073  CB  VAL H 149      63.638  12.493  25.660  1.00 57.46           C  
ANISOU 1073  CB  VAL H 149     7265   5792   8777   2364   1291    334       C  
ATOM   1074  CG1 VAL H 149      63.284  12.672  27.115  1.00 55.54           C  
ANISOU 1074  CG1 VAL H 149     6857   5635   8611   2265   1095    384       C  
ATOM   1075  CG2 VAL H 149      62.618  11.649  24.925  1.00 58.62           C  
ANISOU 1075  CG2 VAL H 149     7768   5773   8735   2205   1360     67       C  
ATOM   1076  N   LYS H 150      63.246  14.365  22.698  1.00 56.61           N  
ANISOU 1076  N   LYS H 150     7103   6021   8386   2394   1328    220       N  
ATOM   1077  CA  LYS H 150      62.481  15.147  21.740  1.00 54.58           C  
ANISOU 1077  CA  LYS H 150     6819   5974   7943   2337   1278    141       C  
ATOM   1078  C   LYS H 150      62.276  14.412  20.416  1.00 56.01           C  
ANISOU 1078  C   LYS H 150     7291   6179   7810   2430   1432    -37       C  
ATOM   1079  O   LYS H 150      63.153  13.681  19.942  1.00 57.40           O  
ANISOU 1079  O   LYS H 150     7644   6212   7952   2669   1659     -3       O  
ATOM   1080  CB  LYS H 150      63.181  16.506  21.536  1.00 54.00           C  
ANISOU 1080  CB  LYS H 150     6430   6023   8065   2460   1293    415       C  
ATOM   1081  CG  LYS H 150      62.776  17.317  20.312  1.00 55.19           C  
ANISOU 1081  CG  LYS H 150     6528   6398   8045   2551   1364    467       C  
ATOM   1082  CD  LYS H 150      61.787  18.435  20.693  1.00 55.13           C  
ANISOU 1082  CD  LYS H 150     6376   6511   8058   2395   1189    466       C  
ATOM   1083  CE  LYS H 150      61.417  19.311  19.491  1.00 56.47           C  
ANISOU 1083  CE  LYS H 150     6454   6935   8066   2546   1300    602       C  
ATOM   1084  NZ  LYS H 150      60.839  20.611  19.919  1.00 55.98           N  
ANISOU 1084  NZ  LYS H 150     6228   6906   8137   2496   1220    721       N  
ATOM   1085  N   ASP H 151      61.080  14.579  19.868  1.00 54.93           N  
ANISOU 1085  N   ASP H 151     7211   6249   7411   2250   1302   -232       N  
ATOM   1086  CA  ASP H 151      60.787  14.248  18.485  1.00 57.36           C  
ANISOU 1086  CA  ASP H 151     7727   6720   7347   2330   1382   -411       C  
ATOM   1087  C   ASP H 151      60.726  12.771  18.161  1.00 59.72           C  
ANISOU 1087  C   ASP H 151     8470   6758   7461   2264   1457   -735       C  
ATOM   1088  O   ASP H 151      61.102  12.384  17.068  1.00 62.47           O  
ANISOU 1088  O   ASP H 151     9061   7131   7543   2485   1620   -850       O  
ATOM   1089  CB  ASP H 151      61.807  14.907  17.554  1.00 59.08           C  
ANISOU 1089  CB  ASP H 151     7826   7076   7547   2721   1609   -150       C  
ATOM   1090  CG  ASP H 151      61.361  16.281  17.036  1.00 58.91           C  
ANISOU 1090  CG  ASP H 151     7499   7416   7468   2776   1562     50       C  
ATOM   1091  OD1 ASP H 151      60.162  16.678  17.137  1.00 56.52           O  
ANISOU 1091  OD1 ASP H 151     7115   7333   7028   2560   1368    -48       O  
ATOM   1092  OD2 ASP H 151      62.257  16.958  16.490  1.00 60.33           O  
ANISOU 1092  OD2 ASP H 151     7504   7667   7750   3074   1760    360       O  
ATOM   1093  N   TYR H 152      60.234  11.946  19.078  1.00 59.58           N  
ANISOU 1093  N   TYR H 152     8588   6477   7573   1978   1358   -882       N  
ATOM   1094  CA  TYR H 152      60.179  10.495  18.831  1.00 62.86           C  
ANISOU 1094  CA  TYR H 152     9480   6525   7878   1883   1458  -1193       C  
ATOM   1095  C   TYR H 152      58.779   9.984  18.491  1.00 64.68           C  
ANISOU 1095  C   TYR H 152     9870   6835   7869   1420   1219  -1560       C  
ATOM   1096  O   TYR H 152      57.820  10.755  18.459  1.00 63.77           O  
ANISOU 1096  O   TYR H 152     9452   7132   7648   1209    982  -1529       O  
ATOM   1097  CB  TYR H 152      60.675   9.735  20.047  1.00 63.08           C  
ANISOU 1097  CB  TYR H 152     9582   6140   8244   1893   1572  -1066       C  
ATOM   1098  CG  TYR H 152      59.745   9.857  21.240  1.00 61.89           C  
ANISOU 1098  CG  TYR H 152     9204   6030   8281   1546   1343  -1009       C  
ATOM   1099  CD1 TYR H 152      58.703   8.956  21.434  1.00 64.30           C  
ANISOU 1099  CD1 TYR H 152     9712   6159   8560   1145   1237  -1244       C  
ATOM   1100  CD2 TYR H 152      59.906  10.879  22.172  1.00 57.96           C  
ANISOU 1100  CD2 TYR H 152     8296   5746   7981   1618   1238   -716       C  
ATOM   1101  CE1 TYR H 152      57.854   9.077  22.531  1.00 62.35           C  
ANISOU 1101  CE1 TYR H 152     9217   5999   8475    879   1063  -1117       C  
ATOM   1102  CE2 TYR H 152      59.067  10.999  23.263  1.00 56.19           C  
ANISOU 1102  CE2 TYR H 152     7889   5589   7870   1382   1059   -652       C  
ATOM   1103  CZ  TYR H 152      58.047  10.098  23.440  1.00 57.81           C  
ANISOU 1103  CZ  TYR H 152     8256   5668   8042   1040    988   -819       C  
ATOM   1104  OH  TYR H 152      57.222  10.221  24.530  1.00 55.74           O  
ANISOU 1104  OH  TYR H 152     7776   5517   7885    857    845   -686       O  
ATOM   1105  N   PHE H 153      58.666   8.672  18.289  1.00 67.74           N  
ANISOU 1105  N   PHE H 153    10728   6814   8195   1255   1290  -1883       N  
ATOM   1106  CA  PHE H 153      57.406   8.041  17.890  1.00 70.48           C  
ANISOU 1106  CA  PHE H 153    11261   7189   8331    738   1046  -2275       C  
ATOM   1107  C   PHE H 153      57.618   6.560  17.693  1.00 75.23           C  
ANISOU 1107  C   PHE H 153    12478   7166   8940    626   1209  -2625       C  
ATOM   1108  O   PHE H 153      58.690   6.160  17.264  1.00 76.19           O  
ANISOU 1108  O   PHE H 153    12943   6997   9009   1055   1517  -2651       O  
ATOM   1109  CB  PHE H 153      56.917   8.627  16.568  1.00 72.23           C  
ANISOU 1109  CB  PHE H 153    11427   7945   8071    735    884  -2470       C  
ATOM   1110  CG  PHE H 153      55.676   7.967  16.028  1.00 76.83           C  
ANISOU 1110  CG  PHE H 153    12180   8639   8372    176    589  -2905       C  
ATOM   1111  CD1 PHE H 153      54.419   8.492  16.297  1.00 75.92           C  
ANISOU 1111  CD1 PHE H 153    11628   9006   8214   -225    266  -2815       C  
ATOM   1112  CD2 PHE H 153      55.766   6.837  15.235  1.00 83.11           C  
ANISOU 1112  CD2 PHE H 153    13573   9076   8930     54    632  -3400       C  
ATOM   1113  CE1 PHE H 153      53.276   7.898  15.800  1.00 80.69           C  
ANISOU 1113  CE1 PHE H 153    12309   9787   8563   -788    -40  -3177       C  
ATOM   1114  CE2 PHE H 153      54.627   6.236  14.734  1.00 88.21           C  
ANISOU 1114  CE2 PHE H 153    14367   9828   9321   -541    310  -3838       C  
ATOM   1115  CZ  PHE H 153      53.380   6.768  15.016  1.00 87.29           C  
ANISOU 1115  CZ  PHE H 153    13733  10252   9182   -987    -44  -3711       C  
ATOM   1116  N   PRO H 154      56.621   5.736  18.062  1.00 78.46           N  
ANISOU 1116  N   PRO H 154    13026   7336   9451     66   1036  -2853       N  
ATOM   1117  CA  PRO H 154      55.474   6.115  18.855  1.00 77.12           C  
ANISOU 1117  CA  PRO H 154    12401   7467   9435   -373    748  -2683       C  
ATOM   1118  C   PRO H 154      55.796   5.751  20.298  1.00 75.82           C  
ANISOU 1118  C   PRO H 154    12149   6915   9742   -309    922  -2340       C  
ATOM   1119  O   PRO H 154      56.930   5.362  20.585  1.00 75.25           O  
ANISOU 1119  O   PRO H 154    12309   6446   9838     98   1239  -2217       O  
ATOM   1120  CB  PRO H 154      54.385   5.191  18.323  1.00 82.43           C  
ANISOU 1120  CB  PRO H 154    13343   8018   9958  -1012    513  -3132       C  
ATOM   1121  CG  PRO H 154      55.105   3.940  18.074  1.00 87.34           C  
ANISOU 1121  CG  PRO H 154    14651   7878  10655   -935    794  -3435       C  
ATOM   1122  CD  PRO H 154      56.513   4.329  17.638  1.00 85.45           C  
ANISOU 1122  CD  PRO H 154    14562   7613  10292   -195   1122  -3310       C  
ATOM   1123  N   GLU H 155      54.814   5.866  21.189  1.00 75.93           N  
ANISOU 1123  N   GLU H 155    11813   7098   9938   -664    732  -2149       N  
ATOM   1124  CA  GLU H 155      55.000   5.538  22.605  1.00 75.57           C  
ANISOU 1124  CA  GLU H 155    11648   6773  10290   -589    883  -1796       C  
ATOM   1125  C   GLU H 155      55.444   4.065  22.786  1.00 81.33           C  
ANISOU 1125  C   GLU H 155    12910   6731  11260   -642   1168  -1921       C  
ATOM   1126  O   GLU H 155      55.147   3.214  21.935  1.00 87.09           O  
ANISOU 1126  O   GLU H 155    14086   7122  11883   -959   1155  -2338       O  
ATOM   1127  CB  GLU H 155      53.694   5.815  23.347  1.00 74.80           C  
ANISOU 1127  CB  GLU H 155    11118   7026  10276   -985    634  -1596       C  
ATOM   1128  CG  GLU H 155      53.842   6.177  24.812  1.00 71.68           C  
ANISOU 1128  CG  GLU H 155    10393   6703  10140   -735    721  -1138       C  
ATOM   1129  CD  GLU H 155      54.400   7.566  25.027  1.00 66.33           C  
ANISOU 1129  CD  GLU H 155     9396   6457   9349   -285    685   -934       C  
ATOM   1130  OE1 GLU H 155      55.515   7.810  24.533  1.00 65.80           O  
ANISOU 1130  OE1 GLU H 155     9486   6285   9229     65    823  -1000       O  
ATOM   1131  OE2 GLU H 155      53.740   8.402  25.694  1.00 63.34           O  
ANISOU 1131  OE2 GLU H 155     8625   6498   8945   -275    538   -697       O  
ATOM   1132  N   PRO H 156      56.159   3.751  23.886  1.00 80.58           N  
ANISOU 1132  N   PRO H 156    12794   6351  11471   -317   1434  -1567       N  
ATOM   1133  CA  PRO H 156      56.578   4.600  24.993  1.00 76.25           C  
ANISOU 1133  CA  PRO H 156    11784   6145  11040     42   1445  -1121       C  
ATOM   1134  C   PRO H 156      58.098   4.846  25.081  1.00 75.20           C  
ANISOU 1134  C   PRO H 156    11694   5954  10925    651   1698   -939       C  
ATOM   1135  O   PRO H 156      58.871   4.220  24.367  1.00 78.43           O  
ANISOU 1135  O   PRO H 156    12513   6004  11284    862   1942  -1093       O  
ATOM   1136  CB  PRO H 156      56.121   3.784  26.210  1.00 77.79           C  
ANISOU 1136  CB  PRO H 156    11937   6060  11559   -117   1552   -851       C  
ATOM   1137  CG  PRO H 156      56.103   2.324  25.728  1.00 83.42           C  
ANISOU 1137  CG  PRO H 156    13235   6044  12418   -359   1777  -1108       C  
ATOM   1138  CD  PRO H 156      56.327   2.330  24.235  1.00 85.43           C  
ANISOU 1138  CD  PRO H 156    13860   6232  12366   -405   1724  -1592       C  
ATOM   1139  N   VAL H 157      58.515   5.741  25.974  1.00 72.17           N  
ANISOU 1139  N   VAL H 157    10886   5934  10601    928   1639   -606       N  
ATOM   1140  CA  VAL H 157      59.936   5.986  26.227  1.00 71.97           C  
ANISOU 1140  CA  VAL H 157    10794   5925  10626   1442   1834   -369       C  
ATOM   1141  C   VAL H 157      60.183   5.951  27.731  1.00 71.78           C  
ANISOU 1141  C   VAL H 157    10495   5985  10793   1623   1872     11       C  
ATOM   1142  O   VAL H 157      59.453   6.617  28.482  1.00 70.56           O  
ANISOU 1142  O   VAL H 157    10017   6163  10629   1476   1637    104       O  
ATOM   1143  CB  VAL H 157      60.357   7.376  25.689  1.00 68.44           C  
ANISOU 1143  CB  VAL H 157    10052   5935  10019   1596   1662   -368       C  
ATOM   1144  CG1 VAL H 157      61.417   8.028  26.574  1.00 66.26           C  
ANISOU 1144  CG1 VAL H 157     9436   5878   9862   1951   1681    -28       C  
ATOM   1145  CG2 VAL H 157      60.828   7.277  24.266  1.00 70.01           C  
ANISOU 1145  CG2 VAL H 157    10532   6039  10029   1714   1786   -592       C  
ATOM   1146  N   THR H 158      61.200   5.197  28.167  1.00 73.21           N  
ANISOU 1146  N   THR H 158    10800   5912  11105   1987   2180    248       N  
ATOM   1147  CA  THR H 158      61.633   5.209  29.569  1.00 73.18           C  
ANISOU 1147  CA  THR H 158    10497   6091  11216   2250   2220    643       C  
ATOM   1148  C   THR H 158      62.902   6.039  29.803  1.00 71.82           C  
ANISOU 1148  C   THR H 158    10001   6294  10993   2629   2178    853       C  
ATOM   1149  O   THR H 158      63.828   6.002  28.996  1.00 73.06           O  
ANISOU 1149  O   THR H 158    10264   6377  11119   2856   2340    851       O  
ATOM   1150  CB  THR H 158      61.925   3.809  30.075  1.00 78.00           C  
ANISOU 1150  CB  THR H 158    11381   6244  12010   2442   2604    872       C  
ATOM   1151  OG1 THR H 158      63.151   3.337  29.492  1.00 81.01           O  
ANISOU 1151  OG1 THR H 158    11990   6405  12387   2843   2923    949       O  
ATOM   1152  CG2 THR H 158      60.781   2.853  29.739  1.00 81.94           C  
ANISOU 1152  CG2 THR H 158    12256   6251  12625   2011   2679    653       C  
ATOM   1153  N   VAL H 159      62.945   6.782  30.909  1.00 70.02           N  
ANISOU 1153  N   VAL H 159     9375   6482  10746   2692   1958   1037       N  
ATOM   1154  CA  VAL H 159      64.173   7.461  31.346  1.00 69.74           C  
ANISOU 1154  CA  VAL H 159     8999   6808  10690   2995   1886   1258       C  
ATOM   1155  C   VAL H 159      64.546   6.960  32.726  1.00 72.22           C  
ANISOU 1155  C   VAL H 159     9126   7288  11028   3269   1964   1612       C  
ATOM   1156  O   VAL H 159      63.727   7.033  33.646  1.00 71.85           O  
ANISOU 1156  O   VAL H 159     8983   7377  10938   3170   1828   1640       O  
ATOM   1157  CB  VAL H 159      63.976   8.975  31.542  1.00 66.41           C  
ANISOU 1157  CB  VAL H 159     8257   6795  10182   2824   1489   1121       C  
ATOM   1158  CG1 VAL H 159      64.161   9.756  30.240  1.00 64.70           C  
ANISOU 1158  CG1 VAL H 159     8070   6566   9945   2707   1426    918       C  
ATOM   1159  CG2 VAL H 159      62.628   9.249  32.160  1.00 65.45           C  
ANISOU 1159  CG2 VAL H 159     8121   6760   9987   2582   1294    999       C  
ATOM   1160  N   SER H 160      65.769   6.462  32.891  1.00 73.80           N  
ANISOU 1160  N   SER H 160     9244   7534  11264   3656   2195   1926       N  
ATOM   1161  CA  SER H 160      66.293   6.299  34.234  1.00 73.81           C  
ANISOU 1161  CA  SER H 160     8932   7895  11216   3953   2186   2291       C  
ATOM   1162  C   SER H 160      67.361   7.368  34.456  1.00 71.49           C  
ANISOU 1162  C   SER H 160     8193   8128  10842   4037   1902   2370       C  
ATOM   1163  O   SER H 160      67.751   8.054  33.514  1.00 70.51           O  
ANISOU 1163  O   SER H 160     8036   7998  10759   3909   1812   2214       O  
ATOM   1164  CB  SER H 160      66.853   4.902  34.425  1.00 79.70           C  
ANISOU 1164  CB  SER H 160     9857   8373  12053   4357   2666   2670       C  
ATOM   1165  OG  SER H 160      68.006   4.707  33.624  1.00 83.89           O  
ANISOU 1165  OG  SER H 160    10414   8848  12612   4633   2898   2811       O  
ATOM   1166  N   TRP H 161      67.790   7.558  35.699  1.00 70.45           N  
ANISOU 1166  N   TRP H 161     7707   8471  10591   4222   1739   2604       N  
ATOM   1167  CA  TRP H 161      68.967   8.383  35.948  1.00 70.22           C  
ANISOU 1167  CA  TRP H 161     7231   8945  10505   4291   1484   2726       C  
ATOM   1168  C   TRP H 161      70.139   7.567  36.543  1.00 75.22           C  
ANISOU 1168  C   TRP H 161     7596   9890  11092   4771   1725   3257       C  
ATOM   1169  O   TRP H 161      69.933   6.570  37.252  1.00 76.99           O  
ANISOU 1169  O   TRP H 161     7910  10078  11266   5072   1991   3533       O  
ATOM   1170  CB  TRP H 161      68.635   9.608  36.799  1.00 67.33           C  
ANISOU 1170  CB  TRP H 161     6621   8975   9986   4041    975   2474       C  
ATOM   1171  CG  TRP H 161      67.805  10.669  36.088  1.00 62.56           C  
ANISOU 1171  CG  TRP H 161     6188   8145   9436   3623    739   2021       C  
ATOM   1172  CD1 TRP H 161      66.446  10.740  36.038  1.00 58.95           C  
ANISOU 1172  CD1 TRP H 161     6014   7447   8939   3436    719   1765       C  
ATOM   1173  CD2 TRP H 161      68.292  11.822  35.369  1.00 61.03           C  
ANISOU 1173  CD2 TRP H 161     5853   7989   9349   3372    511   1840       C  
ATOM   1174  NE1 TRP H 161      66.057  11.842  35.323  1.00 56.58           N  
ANISOU 1174  NE1 TRP H 161     5767   7047   8683   3129    511   1442       N  
ATOM   1175  CE2 TRP H 161      67.170  12.528  34.909  1.00 57.60           C  
ANISOU 1175  CE2 TRP H 161     5656   7312   8916   3083    390   1478       C  
ATOM   1176  CE3 TRP H 161      69.570  12.323  35.075  1.00 62.08           C  
ANISOU 1176  CE3 TRP H 161     5645   8353   9592   3366    416   2002       C  
ATOM   1177  CZ2 TRP H 161      67.284  13.703  34.157  1.00 56.12           C  
ANISOU 1177  CZ2 TRP H 161     5419   7063   8841   2824    210   1274       C  
ATOM   1178  CZ3 TRP H 161      69.683  13.487  34.346  1.00 60.07           C  
ANISOU 1178  CZ3 TRP H 161     5325   8020   9478   3060    220   1796       C  
ATOM   1179  CH2 TRP H 161      68.548  14.163  33.887  1.00 57.76           C  
ANISOU 1179  CH2 TRP H 161     5315   7440   9189   2809    134   1435       C  
ATOM   1180  N   ASN H 162      71.365   7.993  36.226  1.00 76.96           N  
ANISOU 1180  N   ASN H 162     7464  10434  11344   4855   1655   3451       N  
ATOM   1181  CA  ASN H 162      72.574   7.265  36.601  1.00 80.47           C  
ANISOU 1181  CA  ASN H 162     7599  11234  11741   5339   1910   4017       C  
ATOM   1182  C   ASN H 162      72.232   5.802  36.762  1.00 82.63           C  
ANISOU 1182  C   ASN H 162     8240  11123  12031   5746   2446   4290       C  
ATOM   1183  O   ASN H 162      72.175   5.295  37.882  1.00 85.28           O  
ANISOU 1183  O   ASN H 162     8441  11731  12231   6010   2497   4566       O  
ATOM   1184  CB  ASN H 162      73.191   7.843  37.877  1.00 82.06           C  
ANISOU 1184  CB  ASN H 162     7231  12215  11733   5368   1496   4182       C  
ATOM   1185  CG  ASN H 162      73.547   9.323  37.732  1.00 80.76           C  
ANISOU 1185  CG  ASN H 162     6738  12346  11600   4897    951   3876       C  
ATOM   1186  OD1 ASN H 162      73.459  10.086  38.689  1.00 81.10           O  
ANISOU 1186  OD1 ASN H 162     6544  12803  11468   4693    486   3683       O  
ATOM   1187  ND2 ASN H 162      73.933   9.732  36.524  1.00 79.29           N  
ANISOU 1187  ND2 ASN H 162     6572  11921  11635   4733   1023   3827       N  
ATOM   1188  N   SER H 163      71.968   5.160  35.619  1.00 82.11           N  
ANISOU 1188  N   SER H 163     8665  10406  12127   5779   2841   4189       N  
ATOM   1189  CA  SER H 163      71.520   3.754  35.507  1.00 84.27           C  
ANISOU 1189  CA  SER H 163     9445  10083  12489   6063   3384   4336       C  
ATOM   1190  C   SER H 163      70.799   3.136  36.711  1.00 85.47           C  
ANISOU 1190  C   SER H 163     9636  10239  12599   6159   3449   4494       C  
ATOM   1191  O   SER H 163      71.133   2.034  37.152  1.00 88.49           O  
ANISOU 1191  O   SER H 163    10102  10511  13008   6633   3901   4954       O  
ATOM   1192  CB  SER H 163      72.649   2.840  35.031  1.00 88.65           C  
ANISOU 1192  CB  SER H 163    10065  10538  13082   6642   3924   4814       C  
ATOM   1193  OG  SER H 163      73.075   3.212  33.732  1.00 88.25           O  
ANISOU 1193  OG  SER H 163    10133  10319  13079   6577   3973   4642       O  
ATOM   1194  N   GLY H 164      69.781   3.835  37.204  1.00 82.77           N  
ANISOU 1194  N   GLY H 164     9251  10002  12194   5747   3043   4145       N  
ATOM   1195  CA  GLY H 164      68.958   3.311  38.274  1.00 84.27           C  
ANISOU 1195  CA  GLY H 164     9482  10193  12342   5819   3108   4290       C  
ATOM   1196  C   GLY H 164      69.355   3.850  39.630  1.00 86.13           C  
ANISOU 1196  C   GLY H 164     9185  11245  12297   6019   2787   4521       C  
ATOM   1197  O   GLY H 164      68.520   3.965  40.526  1.00 86.58           O  
ANISOU 1197  O   GLY H 164     9200  11467  12231   5961   2635   4485       O  
ATOM   1198  N   ALA H 165      70.629   4.183  39.788  1.00 88.55           N  
ANISOU 1198  N   ALA H 165     9066  12103  12475   6260   2675   4769       N  
ATOM   1199  CA  ALA H 165      71.116   4.699  41.060  1.00 90.95           C  
ANISOU 1199  CA  ALA H 165     8840  13253  12462   6432   2320   4960       C  
ATOM   1200  C   ALA H 165      70.313   5.918  41.570  1.00 88.25           C  
ANISOU 1200  C   ALA H 165     8429  13162  11942   5997   1739   4447       C  
ATOM   1201  O   ALA H 165      69.929   5.960  42.743  1.00 89.91           O  
ANISOU 1201  O   ALA H 165     8492  13783  11886   6153   1589   4530       O  
ATOM   1202  CB  ALA H 165      72.606   5.016  40.969  1.00 93.84           C  
ANISOU 1202  CB  ALA H 165     8719  14189  12748   6621   2209   5244       C  
ATOM   1203  N   LEU H 166      70.042   6.886  40.693  1.00 84.00           N  
ANISOU 1203  N   LEU H 166     8018  12368  11528   5509   1454   3949       N  
ATOM   1204  CA  LEU H 166      69.340   8.109  41.088  1.00 81.64           C  
ANISOU 1204  CA  LEU H 166     7696  12250  11073   5132    944   3466       C  
ATOM   1205  C   LEU H 166      67.835   7.936  40.980  1.00 79.55           C  
ANISOU 1205  C   LEU H 166     7840  11517  10870   4955   1055   3232       C  
ATOM   1206  O   LEU H 166      67.289   7.864  39.882  1.00 76.70           O  
ANISOU 1206  O   LEU H 166     7800  10598  10747   4687   1202   3014       O  
ATOM   1207  CB  LEU H 166      69.775   9.286  40.217  1.00 79.12           C  
ANISOU 1207  CB  LEU H 166     7298  11885  10880   4717    615   3102       C  
ATOM   1208  CG  LEU H 166      70.100  10.567  40.980  1.00 79.36           C  
ANISOU 1208  CG  LEU H 166     7019  12446  10689   4501     34   2828       C  
ATOM   1209  CD1 LEU H 166      70.658  11.607  40.040  1.00 78.06           C  
ANISOU 1209  CD1 LEU H 166     6757  12162  10741   4101   -204   2575       C  
ATOM   1210  CD2 LEU H 166      68.894  11.087  41.726  1.00 77.62           C  
ANISOU 1210  CD2 LEU H 166     7011  12233  10246   4401   -190   2484       C  
ATOM   1211  N   THR H 167      67.166   7.916  42.124  1.00 81.42           N  
ANISOU 1211  N   THR H 167     8030  12048  10859   5109    962   3287       N  
ATOM   1212  CA  THR H 167      65.781   7.478  42.180  1.00 82.20           C  
ANISOU 1212  CA  THR H 167     8430  11778  11022   5035   1158   3254       C  
ATOM   1213  C   THR H 167      64.884   8.519  42.854  1.00 81.66           C  
ANISOU 1213  C   THR H 167     8352  11991  10684   4898    779   2928       C  
ATOM   1214  O   THR H 167      63.808   8.878  42.349  1.00 79.05           O  
ANISOU 1214  O   THR H 167     8255  11336  10445   4602    749   2660       O  
ATOM   1215  CB  THR H 167      65.677   6.090  42.908  1.00 86.97           C  
ANISOU 1215  CB  THR H 167     9035  12369  11642   5474   1614   3817       C  
ATOM   1216  OG1 THR H 167      64.375   5.925  43.490  1.00 87.35           O  
ANISOU 1216  OG1 THR H 167     9200  12359  11632   5457   1673   3851       O  
ATOM   1217  CG2 THR H 167      66.750   5.934  44.017  1.00 91.23           C  
ANISOU 1217  CG2 THR H 167     9167  13618  11878   5964   1562   4208       C  
ATOM   1218  N   SER H 168      65.360   9.001  43.995  1.00 84.75           N  
ANISOU 1218  N   SER H 168     8472  13020  10710   5142    492   2961       N  
ATOM   1219  CA  SER H 168      64.723  10.056  44.761  1.00 84.83           C  
ANISOU 1219  CA  SER H 168     8491  13360  10379   5104    114   2631       C  
ATOM   1220  C   SER H 168      64.705  11.396  43.999  1.00 82.08           C  
ANISOU 1220  C   SER H 168     8263  12812  10111   4654   -244   2077       C  
ATOM   1221  O   SER H 168      65.675  11.738  43.323  1.00 81.78           O  
ANISOU 1221  O   SER H 168     8115  12708  10251   4448   -366   1974       O  
ATOM   1222  CB  SER H 168      65.491  10.202  46.082  1.00 89.89           C  
ANISOU 1222  CB  SER H 168     8817  14757  10580   5473   -131   2766       C  
ATOM   1223  OG  SER H 168      64.821  11.054  46.992  1.00 91.36           O  
ANISOU 1223  OG  SER H 168     9069  15285  10356   5553   -440   2478       O  
ATOM   1224  N   GLY H 169      63.604  12.144  44.104  1.00 80.23           N  
ANISOU 1224  N   GLY H 169     8240  12489   9754   4538   -374   1780       N  
ATOM   1225  CA  GLY H 169      63.521  13.499  43.548  1.00 77.86           C  
ANISOU 1225  CA  GLY H 169     8075  12019   9490   4188   -692   1284       C  
ATOM   1226  C   GLY H 169      63.332  13.582  42.041  1.00 74.38           C  
ANISOU 1226  C   GLY H 169     7785  11023   9454   3823   -541   1173       C  
ATOM   1227  O   GLY H 169      63.556  14.632  41.432  1.00 72.98           O  
ANISOU 1227  O   GLY H 169     7664  10689   9378   3541   -758    847       O  
ATOM   1228  N   VAL H 170      62.932  12.474  41.426  1.00 73.12           N  
ANISOU 1228  N   VAL H 170     7704  10557   9523   3827   -164   1445       N  
ATOM   1229  CA  VAL H 170      62.761  12.454  39.974  1.00 70.24           C  
ANISOU 1229  CA  VAL H 170     7497   9714   9478   3511    -22   1329       C  
ATOM   1230  C   VAL H 170      61.314  12.608  39.556  1.00 67.51           C  
ANISOU 1230  C   VAL H 170     7356   9151   9144   3348     56   1217       C  
ATOM   1231  O   VAL H 170      60.405  12.059  40.168  1.00 68.39           O  
ANISOU 1231  O   VAL H 170     7491   9340   9153   3481    191   1406       O  
ATOM   1232  CB  VAL H 170      63.313  11.178  39.316  1.00 70.77           C  
ANISOU 1232  CB  VAL H 170     7583   9511   9796   3563    332   1618       C  
ATOM   1233  CG1 VAL H 170      62.622  10.939  37.976  1.00 68.47           C  
ANISOU 1233  CG1 VAL H 170     7544   8738   9734   3274    515   1486       C  
ATOM   1234  CG2 VAL H 170      64.794  11.307  39.105  1.00 72.37           C  
ANISOU 1234  CG2 VAL H 170     7578   9848  10071   3621    263   1688       C  
ATOM   1235  N   HIS H 171      61.121  13.330  38.471  1.00 64.36           N  
ANISOU 1235  N   HIS H 171     7064   8513   8879   3069    -12    962       N  
ATOM   1236  CA  HIS H 171      59.809  13.574  37.949  1.00 61.97           C  
ANISOU 1236  CA  HIS H 171     6902   8075   8568   2906     40    870       C  
ATOM   1237  C   HIS H 171      59.979  13.489  36.460  1.00 60.15           C  
ANISOU 1237  C   HIS H 171     6766   7514   8573   2641    141    765       C  
ATOM   1238  O   HIS H 171      60.497  14.409  35.843  1.00 60.78           O  
ANISOU 1238  O   HIS H 171     6837   7543   8714   2536     10    578       O  
ATOM   1239  CB  HIS H 171      59.375  14.994  38.332  1.00 61.30           C  
ANISOU 1239  CB  HIS H 171     6851   8160   8279   2933   -212    623       C  
ATOM   1240  CG  HIS H 171      57.935  15.300  38.056  1.00 59.30           C  
ANISOU 1240  CG  HIS H 171     6688   7904   7939   2878   -148    616       C  
ATOM   1241  ND1 HIS H 171      57.158  14.550  37.200  1.00 58.91           N  
ANISOU 1241  ND1 HIS H 171     6660   7693   8029   2676     45    738       N  
ATOM   1242  CD2 HIS H 171      57.151  16.322  38.473  1.00 58.85           C  
ANISOU 1242  CD2 HIS H 171     6699   8003   7659   2999   -253    503       C  
ATOM   1243  CE1 HIS H 171      55.947  15.074  37.128  1.00 57.72           C  
ANISOU 1243  CE1 HIS H 171     6519   7669   7742   2666     41    746       C  
ATOM   1244  NE2 HIS H 171      55.922  16.157  37.882  1.00 57.89           N  
ANISOU 1244  NE2 HIS H 171     6580   7873   7544   2896   -111    623       N  
ATOM   1245  N   THR H 172      59.608  12.367  35.876  1.00 58.85           N  
ANISOU 1245  N   THR H 172     6704   7113   8543   2538    383    888       N  
ATOM   1246  CA  THR H 172      59.505  12.326  34.441  1.00 55.94           C  
ANISOU 1246  CA  THR H 172     6469   6479   8306   2294    461    739       C  
ATOM   1247  C   THR H 172      58.096  12.737  34.071  1.00 53.79           C  
ANISOU 1247  C   THR H 172     6231   6269   7938   2100    404    647       C  
ATOM   1248  O   THR H 172      57.143  12.300  34.697  1.00 53.28           O  
ANISOU 1248  O   THR H 172     6134   6304   7808   2095    446    793       O  
ATOM   1249  CB  THR H 172      59.748  10.951  33.963  1.00 58.39           C  
ANISOU 1249  CB  THR H 172     6931   6481   8773   2260    730    851       C  
ATOM   1250  OG1 THR H 172      61.159  10.707  34.043  1.00 61.10           O  
ANISOU 1250  OG1 THR H 172     7223   6795   9197   2479    811    961       O  
ATOM   1251  CG2 THR H 172      59.214  10.779  32.529  1.00 57.60           C  
ANISOU 1251  CG2 THR H 172     7023   6142   8723   1975    795    652       C  
ATOM   1252  N   PHE H 173      57.968  13.613  33.080  1.00 51.78           N  
ANISOU 1252  N   PHE H 173     6001   6006   7669   1970    321    463       N  
ATOM   1253  CA  PHE H 173      56.664  14.168  32.691  1.00 49.10           C  
ANISOU 1253  CA  PHE H 173     5641   5816   7198   1837    263    417       C  
ATOM   1254  C   PHE H 173      56.021  13.403  31.542  1.00 48.86           C  
ANISOU 1254  C   PHE H 173     5697   5666   7200   1552    358    368       C  
ATOM   1255  O   PHE H 173      56.704  12.906  30.653  1.00 49.53           O  
ANISOU 1255  O   PHE H 173     5917   5521   7383   1476    449    264       O  
ATOM   1256  CB  PHE H 173      56.811  15.620  32.268  1.00 47.22           C  
ANISOU 1256  CB  PHE H 173     5376   5660   6905   1892    141    280       C  
ATOM   1257  CG  PHE H 173      56.929  16.589  33.411  1.00 47.24           C  
ANISOU 1257  CG  PHE H 173     5340   5805   6804   2112      1    261       C  
ATOM   1258  CD1 PHE H 173      58.088  16.664  34.168  1.00 47.34           C  
ANISOU 1258  CD1 PHE H 173     5326   5787   6876   2231    -89    229       C  
ATOM   1259  CD2 PHE H 173      55.896  17.469  33.690  1.00 46.92           C  
ANISOU 1259  CD2 PHE H 173     5299   5949   6579   2212    -43    266       C  
ATOM   1260  CE1 PHE H 173      58.195  17.575  35.193  1.00 47.63           C  
ANISOU 1260  CE1 PHE H 173     5368   5951   6776   2399   -259    137       C  
ATOM   1261  CE2 PHE H 173      55.994  18.381  34.722  1.00 47.45           C  
ANISOU 1261  CE2 PHE H 173     5415   6100   6514   2441   -161    192       C  
ATOM   1262  CZ  PHE H 173      57.141  18.424  35.480  1.00 48.46           C  
ANISOU 1262  CZ  PHE H 173     5549   6173   6689   2511   -288     94       C  
ATOM   1263  N   PRO H 174      54.691  13.328  31.541  1.00 48.95           N  
ANISOU 1263  N   PRO H 174     5627   5868   7103   1398    329    442       N  
ATOM   1264  CA  PRO H 174      54.028  12.727  30.393  1.00 49.32           C  
ANISOU 1264  CA  PRO H 174     5732   5868   7141   1065    349    347       C  
ATOM   1265  C   PRO H 174      54.247  13.576  29.132  1.00 47.90           C  
ANISOU 1265  C   PRO H 174     5578   5761   6861   1054    297    167       C  
ATOM   1266  O   PRO H 174      54.475  14.797  29.233  1.00 47.35           O  
ANISOU 1266  O   PRO H 174     5426   5831   6733   1270    243    181       O  
ATOM   1267  CB  PRO H 174      52.553  12.695  30.814  1.00 50.92           C  
ANISOU 1267  CB  PRO H 174     5732   6384   7232    926    293    537       C  
ATOM   1268  CG  PRO H 174      52.558  12.836  32.311  1.00 51.12           C  
ANISOU 1268  CG  PRO H 174     5660   6514   7249   1218    322    763       C  
ATOM   1269  CD  PRO H 174      53.742  13.713  32.601  1.00 49.45           C  
ANISOU 1269  CD  PRO H 174     5528   6232   7028   1527    281    637       C  
ATOM   1270  N   ALA H 175      54.173  12.925  27.967  1.00 48.50           N  
ANISOU 1270  N   ALA H 175     5789   5728   6912    816    325      1       N  
ATOM   1271  CA  ALA H 175      54.607  13.477  26.673  1.00 46.65           C  
ANISOU 1271  CA  ALA H 175     5618   5533   6574    855    329   -157       C  
ATOM   1272  C   ALA H 175      53.532  14.293  25.972  1.00 46.33           C  
ANISOU 1272  C   ALA H 175     5395   5916   6294    778    219   -135       C  
ATOM   1273  O   ALA H 175      52.353  14.033  26.184  1.00 48.19           O  
ANISOU 1273  O   ALA H 175     5487   6393   6430    568    131    -52       O  
ATOM   1274  CB  ALA H 175      55.034  12.343  25.771  1.00 48.11           C  
ANISOU 1274  CB  ALA H 175     6079   5427   6772    695    424   -367       C  
ATOM   1275  N   VAL H 176      53.940  15.264  25.142  1.00 44.11           N  
ANISOU 1275  N   VAL H 176     5084   5749   5926    963    244   -152       N  
ATOM   1276  CA  VAL H 176      53.037  15.925  24.173  1.00 45.01           C  
ANISOU 1276  CA  VAL H 176     5043   6288   5771    931    185   -118       C  
ATOM   1277  C   VAL H 176      52.955  15.209  22.832  1.00 47.69           C  
ANISOU 1277  C   VAL H 176     5508   6699   5914    728    163   -337       C  
ATOM   1278  O   VAL H 176      53.946  14.667  22.326  1.00 48.47           O  
ANISOU 1278  O   VAL H 176     5848   6493   6075    776    263   -505       O  
ATOM   1279  CB  VAL H 176      53.472  17.370  23.790  1.00 43.69           C  
ANISOU 1279  CB  VAL H 176     4787   6221   5594   1262    266     12       C  
ATOM   1280  CG1 VAL H 176      52.997  18.420  24.802  1.00 43.01           C  
ANISOU 1280  CG1 VAL H 176     4562   6235   5545   1460    260    215       C  
ATOM   1281  CG2 VAL H 176      54.960  17.442  23.532  1.00 42.85           C  
ANISOU 1281  CG2 VAL H 176     4826   5762   5692   1420    384    -50       C  
ATOM   1282  N   LEU H 177      51.775  15.257  22.227  1.00 50.41           N  
ANISOU 1282  N   LEU H 177     5678   7495   5979    535     32   -326       N  
ATOM   1283  CA  LEU H 177      51.617  14.793  20.859  1.00 53.25           C  
ANISOU 1283  CA  LEU H 177     6136   8044   6054    368    -32   -559       C  
ATOM   1284  C   LEU H 177      51.595  16.054  20.069  1.00 52.14           C  
ANISOU 1284  C   LEU H 177     5808   8301   5703    695     29   -381       C  
ATOM   1285  O   LEU H 177      50.650  16.833  20.153  1.00 52.23           O  
ANISOU 1285  O   LEU H 177     5518   8762   5564    759    -22   -137       O  
ATOM   1286  CB  LEU H 177      50.312  14.033  20.656  1.00 58.15           C  
ANISOU 1286  CB  LEU H 177     6635   8984   6476   -104   -257   -653       C  
ATOM   1287  CG  LEU H 177      50.443  12.935  19.588  1.00 64.11           C  
ANISOU 1287  CG  LEU H 177     7698   9616   7043   -413   -342  -1072       C  
ATOM   1288  CD1 LEU H 177      49.413  11.787  19.760  1.00 68.47           C  
ANISOU 1288  CD1 LEU H 177     8245  10175   7594  -1026   -563  -1237       C  
ATOM   1289  CD2 LEU H 177      50.385  13.541  18.174  1.00 66.55           C  
ANISOU 1289  CD2 LEU H 177     7948  10416   6923   -243   -381  -1147       C  
ATOM   1290  N   GLN H 178      52.689  16.294  19.368  1.00 51.31           N  
ANISOU 1290  N   GLN H 178     5868   8015   5614    959    185   -440       N  
ATOM   1291  CA  GLN H 178      52.852  17.517  18.624  1.00 51.15           C  
ANISOU 1291  CA  GLN H 178     5682   8290   5463   1317    307   -214       C  
ATOM   1292  C   GLN H 178      52.080  17.470  17.303  1.00 54.79           C  
ANISOU 1292  C   GLN H 178     6039   9339   5438   1267    213   -279       C  
ATOM   1293  O   GLN H 178      51.627  16.401  16.882  1.00 56.97           O  
ANISOU 1293  O   GLN H 178     6442   9712   5491    920     35   -587       O  
ATOM   1294  CB  GLN H 178      54.332  17.734  18.359  1.00 50.93           C  
ANISOU 1294  CB  GLN H 178     5821   7879   5650   1604    520   -196       C  
ATOM   1295  CG  GLN H 178      55.176  17.935  19.600  1.00 48.71           C  
ANISOU 1295  CG  GLN H 178     5579   7115   5814   1669    587   -105       C  
ATOM   1296  CD  GLN H 178      56.634  18.167  19.246  1.00 48.86           C  
ANISOU 1296  CD  GLN H 178     5678   6849   6039   1924    782    -27       C  
ATOM   1297  OE1 GLN H 178      57.272  17.318  18.607  1.00 51.09           O  
ANISOU 1297  OE1 GLN H 178     6160   7014   6237   1952    863   -180       O  
ATOM   1298  NE2 GLN H 178      57.167  19.321  19.646  1.00 47.21           N  
ANISOU 1298  NE2 GLN H 178     5316   6520   6100   2113    870    221       N  
ATOM   1299  N   SER H 179      51.926  18.630  16.660  1.00 55.14           N  
ANISOU 1299  N   SER H 179     5859   9776   5316   1609    331     14       N  
ATOM   1300  CA  SER H 179      51.252  18.704  15.363  1.00 59.62           C  
ANISOU 1300  CA  SER H 179     6281  11005   5366   1648    257     10       C  
ATOM   1301  C   SER H 179      51.909  17.766  14.378  1.00 62.02           C  
ANISOU 1301  C   SER H 179     6897  11224   5444   1591    240   -361       C  
ATOM   1302  O   SER H 179      51.223  17.019  13.681  1.00 66.56           O  
ANISOU 1302  O   SER H 179     7512  12170   5609   1309     16   -647       O  
ATOM   1303  CB  SER H 179      51.285  20.117  14.775  1.00 60.22           C  
ANISOU 1303  CB  SER H 179     6111  11422   5346   2142    486    441       C  
ATOM   1304  OG  SER H 179      50.540  21.020  15.564  1.00 59.19           O  
ANISOU 1304  OG  SER H 179     5730  11418   5343   2249    527    781       O  
ATOM   1305  N   SER H 180      53.239  17.818  14.312  1.00 59.43           N  
ANISOU 1305  N   SER H 180     6790  10425   5366   1864    476   -351       N  
ATOM   1306  CA  SER H 180      53.982  16.963  13.382  1.00 61.48           C  
ANISOU 1306  CA  SER H 180     7387  10572   5399   1928    534   -662       C  
ATOM   1307  C   SER H 180      53.455  15.536  13.445  1.00 63.61           C  
ANISOU 1307  C   SER H 180     7946  10712   5510   1433    281  -1159       C  
ATOM   1308  O   SER H 180      53.320  14.871  12.420  1.00 68.82           O  
ANISOU 1308  O   SER H 180     8828  11590   5729   1364    189  -1497       O  
ATOM   1309  CB  SER H 180      55.485  16.981  13.681  1.00 58.82           C  
ANISOU 1309  CB  SER H 180     7234   9653   5462   2211    812   -560       C  
ATOM   1310  OG  SER H 180      55.783  16.334  14.908  1.00 55.38           O  
ANISOU 1310  OG  SER H 180     6945   8660   5436   1959    766   -677       O  
ATOM   1311  N   GLY H 181      53.124  15.088  14.652  1.00 60.25           N  
ANISOU 1311  N   GLY H 181     7523   9935   5435   1088    170  -1199       N  
ATOM   1312  CA  GLY H 181      52.642  13.739  14.859  1.00 60.94           C  
ANISOU 1312  CA  GLY H 181     7876   9788   5489    582    -34  -1610       C  
ATOM   1313  C   GLY H 181      53.673  13.016  15.676  1.00 57.74           C  
ANISOU 1313  C   GLY H 181     7800   8623   5516    615    148  -1689       C  
ATOM   1314  O   GLY H 181      53.532  11.839  15.976  1.00 59.93           O  
ANISOU 1314  O   GLY H 181     8374   8518   5879    264     75  -1989       O  
ATOM   1315  N   LEU H 182      54.721  13.742  16.037  1.00 54.00           N  
ANISOU 1315  N   LEU H 182     7255   7938   5324   1036    393  -1388       N  
ATOM   1316  CA  LEU H 182      55.762  13.194  16.883  1.00 52.01           C  
ANISOU 1316  CA  LEU H 182     7219   7070   5475   1126    570  -1369       C  
ATOM   1317  C   LEU H 182      55.564  13.631  18.321  1.00 49.46           C  
ANISOU 1317  C   LEU H 182     6640   6617   5536   1042    521  -1109       C  
ATOM   1318  O   LEU H 182      54.811  14.548  18.600  1.00 47.30           O  
ANISOU 1318  O   LEU H 182     6040   6693   5236   1024    413   -903       O  
ATOM   1319  CB  LEU H 182      57.142  13.609  16.384  1.00 51.29           C  
ANISOU 1319  CB  LEU H 182     7190   6852   5446   1616    854  -1198       C  
ATOM   1320  CG  LEU H 182      57.462  13.270  14.925  1.00 55.40           C  
ANISOU 1320  CG  LEU H 182     7971   7542   5537   1836    962  -1404       C  
ATOM   1321  CD1 LEU H 182      58.768  13.888  14.516  1.00 54.56           C  
ANISOU 1321  CD1 LEU H 182     7796   7400   5534   2356   1267  -1088       C  
ATOM   1322  CD2 LEU H 182      57.491  11.782  14.708  1.00 59.30           C  
ANISOU 1322  CD2 LEU H 182     8978   7658   5895   1639    962  -1853       C  
ATOM   1323  N   TYR H 183      56.239  12.945  19.233  1.00 51.88           N  
ANISOU 1323  N   TYR H 183     7112   6437   6162   1034    619  -1111       N  
ATOM   1324  CA  TYR H 183      56.090  13.193  20.655  1.00 52.78           C  
ANISOU 1324  CA  TYR H 183     7032   6433   6589    974    568   -902       C  
ATOM   1325  C   TYR H 183      57.375  13.825  21.228  1.00 52.71           C  
ANISOU 1325  C   TYR H 183     6934   6227   6868   1321    725   -662       C  
ATOM   1326  O   TYR H 183      58.458  13.694  20.630  1.00 53.66           O  
ANISOU 1326  O   TYR H 183     7181   6199   7006   1568    907   -649       O  
ATOM   1327  CB  TYR H 183      55.850  11.866  21.383  1.00 54.70           C  
ANISOU 1327  CB  TYR H 183     7493   6308   6981    692    556  -1043       C  
ATOM   1328  CG  TYR H 183      54.524  11.152  21.135  1.00 58.70           C  
ANISOU 1328  CG  TYR H 183     8041   6946   7317    222    362  -1250       C  
ATOM   1329  CD1 TYR H 183      54.458  10.009  20.341  1.00 63.42           C  
ANISOU 1329  CD1 TYR H 183     9020   7302   7776    -17    367  -1608       C  
ATOM   1330  CD2 TYR H 183      53.355  11.569  21.763  1.00 58.28           C  
ANISOU 1330  CD2 TYR H 183     7654   7233   7258      6    179  -1079       C  
ATOM   1331  CE1 TYR H 183      53.261   9.338  20.153  1.00 67.03           C  
ANISOU 1331  CE1 TYR H 183     9493   7858   8116   -536    150  -1810       C  
ATOM   1332  CE2 TYR H 183      52.165  10.901  21.582  1.00 61.36           C  
ANISOU 1332  CE2 TYR H 183     8005   7780   7529   -465    -10  -1208       C  
ATOM   1333  CZ  TYR H 183      52.125   9.798  20.779  1.00 66.30           C  
ANISOU 1333  CZ  TYR H 183     8983   8163   8047   -772    -45  -1581       C  
ATOM   1334  OH  TYR H 183      50.929   9.161  20.596  1.00 71.48           O  
ANISOU 1334  OH  TYR H 183     9572   8981   8606  -1323   -276  -1721       O  
ATOM   1335  N   SER H 184      57.252  14.475  22.392  1.00 51.85           N  
ANISOU 1335  N   SER H 184     6603   6135   6962   1336    648   -471       N  
ATOM   1336  CA  SER H 184      58.408  14.859  23.225  1.00 51.23           C  
ANISOU 1336  CA  SER H 184     6443   5849   7173   1551    723   -294       C  
ATOM   1337  C   SER H 184      58.026  14.752  24.694  1.00 51.88           C  
ANISOU 1337  C   SER H 184     6440   5877   7393   1462    612   -227       C  
ATOM   1338  O   SER H 184      56.875  14.949  25.068  1.00 51.77           O  
ANISOU 1338  O   SER H 184     6335   6060   7276   1317    488   -223       O  
ATOM   1339  CB  SER H 184      58.847  16.296  22.963  1.00 49.13           C  
ANISOU 1339  CB  SER H 184     5961   5726   6980   1744    736   -115       C  
ATOM   1340  OG  SER H 184      59.508  16.441  21.734  1.00 49.93           O  
ANISOU 1340  OG  SER H 184     6096   5867   7007   1917    892    -78       O  
ATOM   1341  N   LEU H 185      58.999  14.466  25.540  1.00 53.46           N  
ANISOU 1341  N   LEU H 185     6640   5873   7800   1588    665   -134       N  
ATOM   1342  CA  LEU H 185      58.746  14.435  26.973  1.00 53.27           C  
ANISOU 1342  CA  LEU H 185     6523   5856   7863   1576    565    -50       C  
ATOM   1343  C   LEU H 185      59.977  14.954  27.688  1.00 53.92           C  
ANISOU 1343  C   LEU H 185     6473   5889   8124   1769    548     75       C  
ATOM   1344  O   LEU H 185      61.039  15.131  27.069  1.00 56.84           O  
ANISOU 1344  O   LEU H 185     6814   6191   8593   1884    641    132       O  
ATOM   1345  CB  LEU H 185      58.460  13.010  27.447  1.00 54.13           C  
ANISOU 1345  CB  LEU H 185     6791   5779   7998   1469    645    -63       C  
ATOM   1346  CG  LEU H 185      59.685  12.096  27.603  1.00 54.59           C  
ANISOU 1346  CG  LEU H 185     6979   5560   8204   1644    835     11       C  
ATOM   1347  CD1 LEU H 185      60.601  12.569  28.738  1.00 53.11           C  
ANISOU 1347  CD1 LEU H 185     6579   5460   8141   1860    781    201       C  
ATOM   1348  CD2 LEU H 185      59.282  10.641  27.813  1.00 56.43           C  
ANISOU 1348  CD2 LEU H 185     7447   5517   8477   1524    976    -12       C  
ATOM   1349  N   SER H 186      59.843  15.162  28.996  1.00 52.53           N  
ANISOU 1349  N   SER H 186     6200   5787   7971   1806    425    131       N  
ATOM   1350  CA  SER H 186      60.955  15.596  29.807  1.00 51.34           C  
ANISOU 1350  CA  SER H 186     5907   5650   7950   1940    346    215       C  
ATOM   1351  C   SER H 186      61.034  14.809  31.112  1.00 52.86           C  
ANISOU 1351  C   SER H 186     6078   5885   8122   2033    328    310       C  
ATOM   1352  O   SER H 186      60.008  14.400  31.656  1.00 52.82           O  
ANISOU 1352  O   SER H 186     6128   5936   8006   1997    323    316       O  
ATOM   1353  CB  SER H 186      60.871  17.096  30.026  1.00 49.20           C  
ANISOU 1353  CB  SER H 186     5532   5469   7692   1928    172    154       C  
ATOM   1354  OG  SER H 186      61.168  17.739  28.805  1.00 46.50           O  
ANISOU 1354  OG  SER H 186     5169   5068   7431   1899    248    161       O  
ATOM   1355  N   SER H 187      62.260  14.505  31.541  1.00 53.83           N  
ANISOU 1355  N   SER H 187     6091   6013   8348   2174    351    441       N  
ATOM   1356  CA  SER H 187      62.507  13.975  32.874  1.00 54.98           C  
ANISOU 1356  CA  SER H 187     6151   6296   8445   2326    310    574       C  
ATOM   1357  C   SER H 187      63.360  15.005  33.622  1.00 56.80           C  
ANISOU 1357  C   SER H 187     6158   6742   8681   2365     53    552       C  
ATOM   1358  O   SER H 187      64.445  15.357  33.175  1.00 58.92           O  
ANISOU 1358  O   SER H 187     6279   7013   9097   2349     31    610       O  
ATOM   1359  CB  SER H 187      63.249  12.639  32.792  1.00 55.63           C  
ANISOU 1359  CB  SER H 187     6277   6250   8612   2490    570    787       C  
ATOM   1360  OG  SER H 187      63.438  12.059  34.076  1.00 55.74           O  
ANISOU 1360  OG  SER H 187     6190   6430   8560   2686    573    979       O  
ATOM   1361  N   VAL H 188      62.880  15.498  34.753  1.00 57.28           N  
ANISOU 1361  N   VAL H 188     6193   6995   8576   2409   -147    468       N  
ATOM   1362  CA  VAL H 188      63.679  16.414  35.548  1.00 59.61           C  
ANISOU 1362  CA  VAL H 188     6321   7488   8842   2411   -433    381       C  
ATOM   1363  C   VAL H 188      63.887  15.866  36.974  1.00 62.26           C  
ANISOU 1363  C   VAL H 188     6549   8141   8967   2635   -523    493       C  
ATOM   1364  O   VAL H 188      62.933  15.412  37.611  1.00 62.48           O  
ANISOU 1364  O   VAL H 188     6683   8245   8810   2777   -452    537       O  
ATOM   1365  CB  VAL H 188      63.021  17.799  35.601  1.00 59.22           C  
ANISOU 1365  CB  VAL H 188     6389   7379   8732   2289   -627    106       C  
ATOM   1366  CG1 VAL H 188      61.712  17.719  36.327  1.00 58.60           C  
ANISOU 1366  CG1 VAL H 188     6470   7404   8392   2430   -615     58       C  
ATOM   1367  CG2 VAL H 188      63.928  18.793  36.288  1.00 62.30           C  
ANISOU 1367  CG2 VAL H 188     6657   7878   9137   2205   -943    -52       C  
ATOM   1368  N   VAL H 189      65.134  15.913  37.459  1.00 64.47           N  
ANISOU 1368  N   VAL H 189     6578   8654   9265   2677   -676    581       N  
ATOM   1369  CA  VAL H 189      65.504  15.461  38.813  1.00 66.58           C  
ANISOU 1369  CA  VAL H 189     6682   9328   9287   2920   -792    712       C  
ATOM   1370  C   VAL H 189      65.966  16.647  39.679  1.00 69.53           C  
ANISOU 1370  C   VAL H 189     6950   9973   9497   2815  -1232    433       C  
ATOM   1371  O   VAL H 189      66.639  17.557  39.187  1.00 70.55           O  
ANISOU 1371  O   VAL H 189     6988   9998   9819   2534  -1425    276       O  
ATOM   1372  CB  VAL H 189      66.635  14.414  38.735  1.00 68.03           C  
ANISOU 1372  CB  VAL H 189     6620   9659   9571   3098   -606   1094       C  
ATOM   1373  CG1 VAL H 189      67.860  15.002  38.078  1.00 68.18           C  
ANISOU 1373  CG1 VAL H 189     6391   9704   9811   2904   -734   1114       C  
ATOM   1374  CG2 VAL H 189      66.975  13.880  40.110  1.00 71.12           C  
ANISOU 1374  CG2 VAL H 189     6814  10528   9678   3406   -687   1296       C  
ATOM   1375  N   THR H 190      65.598  16.661  40.957  1.00 71.81           N  
ANISOU 1375  N   THR H 190     7264  10593   9427   3030  -1392    363       N  
ATOM   1376  CA  THR H 190      66.036  17.760  41.829  1.00 76.91           C  
ANISOU 1376  CA  THR H 190     7869  11493   9860   2927  -1840     25       C  
ATOM   1377  C   THR H 190      67.177  17.290  42.742  1.00 81.33           C  
ANISOU 1377  C   THR H 190     8059  12613  10229   3069  -2035    214       C  
ATOM   1378  O   THR H 190      67.054  16.272  43.428  1.00 82.20           O  
ANISOU 1378  O   THR H 190     8075  13041  10115   3443  -1863    524       O  
ATOM   1379  CB  THR H 190      64.866  18.386  42.656  1.00 78.44           C  
ANISOU 1379  CB  THR H 190     8389  11717   9698   3088  -1948   -275       C  
ATOM   1380  OG1 THR H 190      63.601  17.948  42.142  1.00 75.73           O  
ANISOU 1380  OG1 THR H 190     8261  11108   9406   3207  -1595   -138       O  
ATOM   1381  CG2 THR H 190      64.910  19.917  42.600  1.00 80.18           C  
ANISOU 1381  CG2 THR H 190     8816  11705   9945   2798  -2268   -761       C  
ATOM   1382  N   VAL H 191      68.293  18.020  42.720  1.00 84.42           N  
ANISOU 1382  N   VAL H 191     8207  13142  10728   2765  -2380     72       N  
ATOM   1383  CA  VAL H 191      69.517  17.601  43.400  1.00 88.81           C  
ANISOU 1383  CA  VAL H 191     8310  14293  11142   2846  -2582    309       C  
ATOM   1384  C   VAL H 191      70.274  18.838  43.931  1.00 94.10           C  
ANISOU 1384  C   VAL H 191     8843  15182  11731   2455  -3165   -102       C  
ATOM   1385  O   VAL H 191      69.922  19.971  43.600  1.00 92.49           O  
ANISOU 1385  O   VAL H 191     8921  14548  11675   2116  -3338   -532       O  
ATOM   1386  CB  VAL H 191      70.419  16.762  42.425  1.00 88.29           C  
ANISOU 1386  CB  VAL H 191     7921  14187  11438   2863  -2267    809       C  
ATOM   1387  CG1 VAL H 191      71.426  17.656  41.701  1.00 89.87           C  
ANISOU 1387  CG1 VAL H 191     7865  14293  11986   2400  -2506    730       C  
ATOM   1388  CG2 VAL H 191      71.141  15.617  43.153  1.00 91.13           C  
ANISOU 1388  CG2 VAL H 191     7912  15142  11573   3275  -2155   1298       C  
ATOM   1389  N   PRO H 192      71.271  18.625  44.816  1.00100.35           N  
ANISOU 1389  N   PRO H 192     9214  16653  12261   2509  -3474     22       N  
ATOM   1390  CA  PRO H 192      72.190  19.687  45.234  1.00106.56           C  
ANISOU 1390  CA  PRO H 192     9775  17693  13021   2044  -4065   -327       C  
ATOM   1391  C   PRO H 192      73.639  19.184  45.181  1.00111.10           C  
ANISOU 1391  C   PRO H 192     9668  18841  13705   1973  -4169    144       C  
ATOM   1392  O   PRO H 192      73.860  17.971  45.129  1.00110.51           O  
ANISOU 1392  O   PRO H 192     9353  19055  13581   2416  -3794    710       O  
ATOM   1393  CB  PRO H 192      71.803  19.868  46.699  1.00110.34           C  
ANISOU 1393  CB  PRO H 192    10414  18652  12858   2284  -4403   -670       C  
ATOM   1394  CG  PRO H 192      71.437  18.405  47.145  1.00108.26           C  
ANISOU 1394  CG  PRO H 192    10043  18781  12310   2961  -3971   -120       C  
ATOM   1395  CD  PRO H 192      71.182  17.595  45.870  1.00101.94           C  
ANISOU 1395  CD  PRO H 192     9276  17454  12001   3050  -3375    328       C  
ATOM   1396  N   SER H 193      74.625  20.080  45.233  1.00116.53           N  
ANISOU 1396  N   SER H 193    10031  19711  14534   1435  -4662    -52       N  
ATOM   1397  CA  SER H 193      76.021  19.618  45.343  1.00121.39           C  
ANISOU 1397  CA  SER H 193     9909  21035  15179   1389  -4811    441       C  
ATOM   1398  C   SER H 193      77.011  20.705  45.786  1.00129.21           C  
ANISOU 1398  C   SER H 193    10530  22372  16191    732  -5519    111       C  
ATOM   1399  O   SER H 193      76.601  21.864  46.089  1.00131.86           O  
ANISOU 1399  O   SER H 193    11265  22337  16500    304  -5915   -583       O  
ATOM   1400  CB  SER H 193      76.477  18.967  44.034  1.00117.64           C  
ANISOU 1400  CB  SER H 193     9190  20301  15206   1483  -4289   1051       C  
ATOM   1401  OG  SER H 193      75.910  19.639  42.920  1.00112.80           O  
ANISOU 1401  OG  SER H 193     8970  18840  15047   1184  -4096    817       O  
ATOM   1402  N   THR H 200      77.597  15.464  37.605  1.00 87.97           N  
ANISOU 1402  N   THR H 200     5344  14939  13140   2723  -1385   3478       N  
ATOM   1403  CA  THR H 200      77.865  14.030  37.693  1.00 88.91           C  
ANISOU 1403  CA  THR H 200     5430  15271  13081   3368   -908   3992       C  
ATOM   1404  C   THR H 200      76.684  13.156  37.211  1.00 84.74           C  
ANISOU 1404  C   THR H 200     5596  14095  12506   3698   -415   3846       C  
ATOM   1405  O   THR H 200      76.702  11.938  37.394  1.00 85.27           O  
ANISOU 1405  O   THR H 200     5764  14206  12429   4216     -7   4191       O  
ATOM   1406  CB  THR H 200      78.367  13.623  39.130  1.00 93.10           C  
ANISOU 1406  CB  THR H 200     5554  16581  13239   3583  -1166   4206       C  
ATOM   1407  OG1 THR H 200      78.659  12.221  39.181  1.00 93.37           O  
ANISOU 1407  OG1 THR H 200     5560  16782  13133   4262   -633   4778       O  
ATOM   1408  CG2 THR H 200      77.366  13.985  40.232  1.00 90.82           C  
ANISOU 1408  CG2 THR H 200     5580  16284  12642   3438  -1530   3654       C  
ATOM   1409  N   TYR H 201      75.709  13.766  36.522  1.00 81.26           N  
ANISOU 1409  N   TYR H 201     5612  13050  12212   3394   -429   3377       N  
ATOM   1410  CA  TYR H 201      74.410  13.108  36.240  1.00 76.94           C  
ANISOU 1410  CA  TYR H 201     5696  11949  11588   3566   -106   3133       C  
ATOM   1411  C   TYR H 201      74.093  12.747  34.772  1.00 74.41           C  
ANISOU 1411  C   TYR H 201     5742  11070  11462   3654    336   3147       C  
ATOM   1412  O   TYR H 201      74.404  13.499  33.848  1.00 73.84           O  
ANISOU 1412  O   TYR H 201     5579  10872  11605   3429    301   3115       O  
ATOM   1413  CB  TYR H 201      73.271  13.930  36.847  1.00 74.10           C  
ANISOU 1413  CB  TYR H 201     5617  11425  11111   3233   -470   2572       C  
ATOM   1414  CG  TYR H 201      73.519  14.315  38.286  1.00 78.13           C  
ANISOU 1414  CG  TYR H 201     5846  12482  11360   3171   -919   2482       C  
ATOM   1415  CD1 TYR H 201      73.645  13.342  39.270  1.00 80.95           C  
ANISOU 1415  CD1 TYR H 201     6088  13235  11433   3584   -814   2769       C  
ATOM   1416  CD2 TYR H 201      73.648  15.646  38.665  1.00 80.11           C  
ANISOU 1416  CD2 TYR H 201     5958  12851  11628   2716  -1438   2111       C  
ATOM   1417  CE1 TYR H 201      73.892  13.682  40.602  1.00 84.79           C  
ANISOU 1417  CE1 TYR H 201     6303  14312  11604   3572  -1239   2689       C  
ATOM   1418  CE2 TYR H 201      73.892  15.999  39.999  1.00 84.19           C  
ANISOU 1418  CE2 TYR H 201     6254  13893  11842   2657  -1885   1965       C  
ATOM   1419  CZ  TYR H 201      74.010  15.008  40.963  1.00 86.43           C  
ANISOU 1419  CZ  TYR H 201     6400  14651  11788   3100  -1793   2256       C  
ATOM   1420  OH  TYR H 201      74.252  15.329  42.285  1.00 90.63           O  
ANISOU 1420  OH  TYR H 201     6706  15782  11947   3091  -2240   2117       O  
ATOM   1421  N   ILE H 202      73.425  11.607  34.584  1.00 73.61           N  
ANISOU 1421  N   ILE H 202     6070  10628  11271   3969    741   3177       N  
ATOM   1422  CA  ILE H 202      73.149  11.034  33.250  1.00 73.26           C  
ANISOU 1422  CA  ILE H 202     6425  10078  11332   4111   1179   3174       C  
ATOM   1423  C   ILE H 202      71.704  10.499  33.094  1.00 71.10           C  
ANISOU 1423  C   ILE H 202     6735   9296  10985   4049   1324   2814       C  
ATOM   1424  O   ILE H 202      71.194   9.839  33.999  1.00 71.79           O  
ANISOU 1424  O   ILE H 202     6938   9389  10951   4171   1363   2834       O  
ATOM   1425  CB  ILE H 202      74.128   9.847  32.970  1.00 75.89           C  
ANISOU 1425  CB  ILE H 202     6698  10482  11656   4658   1666   3708       C  
ATOM   1426  CG1 ILE H 202      75.561  10.362  32.829  1.00 79.64           C  
ANISOU 1426  CG1 ILE H 202     6561  11468  12229   4724   1582   4135       C  
ATOM   1427  CG2 ILE H 202      73.717   9.034  31.728  1.00 73.65           C  
ANISOU 1427  CG2 ILE H 202     6971   9613  11401   4865   2149   3632       C  
ATOM   1428  CD1 ILE H 202      76.613   9.375  33.322  1.00 84.23           C  
ANISOU 1428  CD1 ILE H 202     6842  12446  12716   5271   1884   4753       C  
ATOM   1429  N   CYS H 203      71.059  10.745  31.952  1.00 68.67           N  
ANISOU 1429  N   CYS H 203     6756   8594  10744   3869   1412   2530       N  
ATOM   1430  CA  CYS H 203      69.767  10.099  31.699  1.00 68.45           C  
ANISOU 1430  CA  CYS H 203     7237   8124  10647   3798   1566   2241       C  
ATOM   1431  C   CYS H 203      69.850   8.940  30.711  1.00 70.56           C  
ANISOU 1431  C   CYS H 203     7904   7984  10922   4067   2044   2318       C  
ATOM   1432  O   CYS H 203      70.499   9.044  29.676  1.00 71.43           O  
ANISOU 1432  O   CYS H 203     8021   8054  11067   4198   2217   2406       O  
ATOM   1433  CB  CYS H 203      68.693  11.108  31.264  1.00 67.00           C  
ANISOU 1433  CB  CYS H 203     7187   7813  10459   3389   1296   1815       C  
ATOM   1434  SG  CYS H 203      68.883  11.848  29.606  1.00 67.77           S  
ANISOU 1434  SG  CYS H 203     7341   7770  10640   3281   1366   1705       S  
ATOM   1435  N   ASN H 204      69.194   7.831  31.049  1.00 72.73           N  
ANISOU 1435  N   ASN H 204     8530   7942  11162   4160   2269   2293       N  
ATOM   1436  CA  ASN H 204      69.179   6.634  30.205  1.00 76.02           C  
ANISOU 1436  CA  ASN H 204     9433   7866  11585   4388   2728   2299       C  
ATOM   1437  C   ASN H 204      67.862   6.503  29.425  1.00 75.62           C  
ANISOU 1437  C   ASN H 204     9841   7392  11500   4021   2692   1823       C  
ATOM   1438  O   ASN H 204      66.937   5.805  29.847  1.00 76.16           O  
ANISOU 1438  O   ASN H 204    10169   7174  11594   3870   2741   1707       O  
ATOM   1439  CB  ASN H 204      69.386   5.379  31.052  1.00 79.74           C  
ANISOU 1439  CB  ASN H 204    10025   8185  12086   4734   3059   2624       C  
ATOM   1440  CG  ASN H 204      70.683   5.400  31.853  1.00 82.44           C  
ANISOU 1440  CG  ASN H 204     9878   9034  12413   5141   3108   3149       C  
ATOM   1441  OD1 ASN H 204      70.673   5.692  33.051  1.00 82.31           O  
ANISOU 1441  OD1 ASN H 204     9507   9417  12351   5116   2861   3291       O  
ATOM   1442  ND2 ASN H 204      71.800   5.057  31.204  1.00 84.89           N  
ANISOU 1442  ND2 ASN H 204    10158   9371  12726   5549   3437   3460       N  
ATOM   1443  N   VAL H 205      67.786   7.199  28.295  1.00 75.58           N  
ANISOU 1443  N   VAL H 205     9885   7396  11435   3874   2600   1588       N  
ATOM   1444  CA  VAL H 205      66.592   7.229  27.452  1.00 74.38           C  
ANISOU 1444  CA  VAL H 205    10084   6983  11194   3523   2513   1147       C  
ATOM   1445  C   VAL H 205      66.494   5.959  26.618  1.00 76.99           C  
ANISOU 1445  C   VAL H 205    10991   6794  11466   3655   2888   1000       C  
ATOM   1446  O   VAL H 205      67.371   5.671  25.820  1.00 79.78           O  
ANISOU 1446  O   VAL H 205    11496   7063  11754   4005   3173   1098       O  
ATOM   1447  CB  VAL H 205      66.613   8.467  26.520  1.00 72.97           C  
ANISOU 1447  CB  VAL H 205     9725   7059  10941   3386   2306   1002       C  
ATOM   1448  CG1 VAL H 205      66.377   8.066  25.063  1.00 76.03           C  
ANISOU 1448  CG1 VAL H 205    10535   7191  11160   3413   2499    740       C  
ATOM   1449  CG2 VAL H 205      65.624   9.485  26.966  1.00 68.94           C  
ANISOU 1449  CG2 VAL H 205     9004   6766  10426   3002   1915    816       C  
ATOM   1450  N   ASN H 206      65.403   5.226  26.798  1.00 77.54           N  
ANISOU 1450  N   ASN H 206    11389   6513  11559   3363   2886    760       N  
ATOM   1451  CA  ASN H 206      65.224   3.897  26.224  1.00 81.60           C  
ANISOU 1451  CA  ASN H 206    12512   6426  12067   3414   3231    585       C  
ATOM   1452  C   ASN H 206      63.948   3.914  25.387  1.00 80.08           C  
ANISOU 1452  C   ASN H 206    12608   6068  11750   2904   3015     77       C  
ATOM   1453  O   ASN H 206      62.876   4.209  25.893  1.00 79.03           O  
ANISOU 1453  O   ASN H 206    12303   6060  11665   2485   2726    -24       O  
ATOM   1454  CB  ASN H 206      65.096   2.881  27.370  1.00 85.50           C  
ANISOU 1454  CB  ASN H 206    13098   6620  12768   3485   3439    835       C  
ATOM   1455  CG  ASN H 206      65.700   1.522  27.037  1.00 93.77           C  
ANISOU 1455  CG  ASN H 206    14691   7068  13870   3859   3968    918       C  
ATOM   1456  OD1 ASN H 206      66.296   1.325  25.970  1.00 97.85           O  
ANISOU 1456  OD1 ASN H 206    15528   7414  14238   4119   4190    789       O  
ATOM   1457  ND2 ASN H 206      65.553   0.568  27.958  1.00 96.92           N  
ANISOU 1457  ND2 ASN H 206    15218   7133  14475   3937   4211   1162       N  
ATOM   1458  N   HIS H 207      64.051   3.642  24.098  1.00 80.70           N  
ANISOU 1458  N   HIS H 207    13094   5939  11629   2957   3142   -229       N  
ATOM   1459  CA  HIS H 207      62.879   3.736  23.243  1.00 80.19           C  
ANISOU 1459  CA  HIS H 207    13244   5842  11382   2470   2887   -715       C  
ATOM   1460  C   HIS H 207      62.720   2.435  22.445  1.00 85.97           C  
ANISOU 1460  C   HIS H 207    14708   5931  12025   2426   3150  -1087       C  
ATOM   1461  O   HIS H 207      62.843   2.414  21.220  1.00 88.20           O  
ANISOU 1461  O   HIS H 207    15316   6184  12012   2511   3194  -1406       O  
ATOM   1462  CB  HIS H 207      62.985   5.005  22.372  1.00 77.50           C  
ANISOU 1462  CB  HIS H 207    12611   6034  10800   2511   2667   -784       C  
ATOM   1463  CG  HIS H 207      62.039   5.049  21.209  1.00 79.76           C  
ANISOU 1463  CG  HIS H 207    13154   6361  10792   2168   2476  -1261       C  
ATOM   1464  ND1 HIS H 207      60.673   5.186  21.356  1.00 79.35           N  
ANISOU 1464  ND1 HIS H 207    13001   6430  10719   1607   2138  -1484       N  
ATOM   1465  CD2 HIS H 207      62.270   5.015  19.872  1.00 82.64           C  
ANISOU 1465  CD2 HIS H 207    13827   6746  10826   2333   2564  -1528       C  
ATOM   1466  CE1 HIS H 207      60.101   5.204  20.162  1.00 81.91           C  
ANISOU 1466  CE1 HIS H 207    13550   6856  10714   1408   2004  -1881       C  
ATOM   1467  NE2 HIS H 207      61.048   5.097  19.245  1.00 83.63           N  
ANISOU 1467  NE2 HIS H 207    14043   7009  10724   1850   2257  -1936       N  
ATOM   1468  N   LYS H 208      62.451   1.348  23.176  1.00 88.48           N  
ANISOU 1468  N   LYS H 208    15300   5720  12598   2307   3337  -1038       N  
ATOM   1469  CA  LYS H 208      62.408  -0.024  22.639  1.00 94.23           C  
ANISOU 1469  CA  LYS H 208    16794   5675  13336   2288   3660  -1349       C  
ATOM   1470  C   LYS H 208      61.872  -0.136  21.223  1.00 97.82           C  
ANISOU 1470  C   LYS H 208    17704   6019  13443   2005   3511  -1973       C  
ATOM   1471  O   LYS H 208      62.444  -0.853  20.407  1.00102.79           O  
ANISOU 1471  O   LYS H 208    18947   6210  13897   2319   3834  -2208       O  
ATOM   1472  CB  LYS H 208      61.571  -0.929  23.541  1.00 96.55           C  
ANISOU 1472  CB  LYS H 208    17224   5485  13977   1868   3692  -1315       C  
ATOM   1473  CG  LYS H 208      62.112  -1.128  24.948  1.00 94.46           C  
ANISOU 1473  CG  LYS H 208    16638   5227  14026   2215   3930   -700       C  
ATOM   1474  CD  LYS H 208      61.031  -1.720  25.852  1.00 95.43           C  
ANISOU 1474  CD  LYS H 208    16722   5066  14470   1717   3859   -624       C  
ATOM   1475  CE  LYS H 208      60.322  -2.905  25.184  1.00101.67           C  
ANISOU 1475  CE  LYS H 208    18224   5043  15364   1253   3976  -1089       C  
ATOM   1476  NZ  LYS H 208      61.241  -4.034  24.978  1.00106.28           N  
ANISOU 1476  NZ  LYS H 208    19469   4873  16039   1736   4552  -1048       N  
ATOM   1477  N   PRO H 209      60.738   0.528  20.945  1.00 96.29           N  
ANISOU 1477  N   PRO H 209    17229   6235  13120   1430   3032  -2240       N  
ATOM   1478  CA  PRO H 209      60.146   0.615  19.611  1.00 99.70           C  
ANISOU 1478  CA  PRO H 209    17955   6775  13151   1139   2799  -2807       C  
ATOM   1479  C   PRO H 209      61.128   0.921  18.466  1.00101.14           C  
ANISOU 1479  C   PRO H 209    18365   7126  12938   1721   2999  -2906       C  
ATOM   1480  O   PRO H 209      60.794   0.709  17.301  1.00105.37           O  
ANISOU 1480  O   PRO H 209    19316   7634  13088   1592   2904  -3416       O  
ATOM   1481  CB  PRO H 209      59.139   1.764  19.756  1.00 94.56           C  
ANISOU 1481  CB  PRO H 209    16649   6851  12430    705   2300  -2761       C  
ATOM   1482  CG  PRO H 209      58.707   1.705  21.189  1.00 91.81           C  
ANISOU 1482  CG  PRO H 209    15921   6459  12502    486   2252  -2378       C  
ATOM   1483  CD  PRO H 209      59.823   1.051  21.982  1.00 92.47           C  
ANISOU 1483  CD  PRO H 209    16171   6091  12870   1001   2707  -2007       C  
ATOM   1484  N   SER H 210      62.319   1.418  18.787  1.00 98.20           N  
ANISOU 1484  N   SER H 210    17698   6973  12641   2353   3261  -2410       N  
ATOM   1485  CA  SER H 210      63.272   1.803  17.750  1.00 99.19           C  
ANISOU 1485  CA  SER H 210    17925   7340  12421   2934   3469  -2384       C  
ATOM   1486  C   SER H 210      64.718   1.527  18.144  1.00 99.57           C  
ANISOU 1486  C   SER H 210    17978   7230  12624   3662   3959  -1880       C  
ATOM   1487  O   SER H 210      65.611   2.298  17.799  1.00 97.48           O  
ANISOU 1487  O   SER H 210    17376   7415  12246   4132   4065  -1545       O  
ATOM   1488  CB  SER H 210      63.119   3.291  17.438  1.00 94.70           C  
ANISOU 1488  CB  SER H 210    16705   7574  11701   2899   3142  -2222       C  
ATOM   1489  OG  SER H 210      63.617   4.085  18.551  1.00 89.79           O  
ANISOU 1489  OG  SER H 210    15428   7261  11430   3031   3110  -1652       O  
ATOM   1490  N   ASN H 211      64.946   0.432  18.862  1.00102.86           N  
ANISOU 1490  N   ASN H 211    18744   7032  13309   3759   4272  -1778       N  
ATOM   1491  CA  ASN H 211      66.283   0.085  19.347  1.00103.83           C  
ANISOU 1491  CA  ASN H 211    18831   7039  13581   4468   4757  -1231       C  
ATOM   1492  C   ASN H 211      67.219   1.276  19.592  1.00 98.94           C  
ANISOU 1492  C   ASN H 211    17443   7156  12993   4843   4708   -662       C  
ATOM   1493  O   ASN H 211      68.381   1.249  19.179  1.00101.27           O  
ANISOU 1493  O   ASN H 211    17749   7558  13171   5494   5075   -338       O  
ATOM   1494  CB  ASN H 211      66.955  -0.917  18.407  1.00111.04           C  
ANISOU 1494  CB  ASN H 211    20542   7418  14230   5013   5267  -1427       C  
ATOM   1495  CG  ASN H 211      68.092  -1.658  19.080  1.00113.81           C  
ANISOU 1495  CG  ASN H 211    20990   7460  14792   5686   5832   -877       C  
ATOM   1496  OD1 ASN H 211      68.151  -1.741  20.310  1.00111.78           O  
ANISOU 1496  OD1 ASN H 211    20355   7217  14900   5622   5834   -464       O  
ATOM   1497  ND2 ASN H 211      69.007  -2.189  18.284  1.00118.99           N  
ANISOU 1497  ND2 ASN H 211    22136   7890  15184   6387   6330   -830       N  
ATOM   1498  N   THR H 212      66.706   2.310  20.259  1.00 92.67           N  
ANISOU 1498  N   THR H 212    15995   6854  12362   4428   4265   -535       N  
ATOM   1499  CA  THR H 212      67.490   3.494  20.614  1.00 88.20           C  
ANISOU 1499  CA  THR H 212    14697   6927  11889   4647   4152    -43       C  
ATOM   1500  C   THR H 212      67.803   3.542  22.106  1.00 85.49           C  
ANISOU 1500  C   THR H 212    13900   6696  11887   4650   4112    401       C  
ATOM   1501  O   THR H 212      66.896   3.662  22.935  1.00 82.32           O  
ANISOU 1501  O   THR H 212    13342   6293  11641   4188   3815    296       O  
ATOM   1502  CB  THR H 212      66.718   4.806  20.317  1.00 83.85           C  
ANISOU 1502  CB  THR H 212    13723   6880  11258   4205   3671   -215       C  
ATOM   1503  OG1 THR H 212      66.517   4.955  18.909  1.00 86.88           O  
ANISOU 1503  OG1 THR H 212    14402   7333  11275   4264   3686   -547       O  
ATOM   1504  CG2 THR H 212      67.494   6.006  20.824  1.00 79.28           C  
ANISOU 1504  CG2 THR H 212    12425   6845  10854   4351   3545    271       C  
ATOM   1505  N   LYS H 213      69.085   3.496  22.450  1.00 85.90           N  
ANISOU 1505  N   LYS H 213    13692   6923  12023   5188   4398    926       N  
ATOM   1506  CA  LYS H 213      69.489   3.774  23.821  1.00 82.85           C  
ANISOU 1506  CA  LYS H 213    12753   6834  11890   5207   4286   1371       C  
ATOM   1507  C   LYS H 213      70.504   4.915  23.859  1.00 80.80           C  
ANISOU 1507  C   LYS H 213    11821   7209  11670   5398   4161   1787       C  
ATOM   1508  O   LYS H 213      71.635   4.774  23.422  1.00 83.36           O  
ANISOU 1508  O   LYS H 213    12066   7665  11942   5913   4487   2152       O  
ATOM   1509  CB  LYS H 213      70.021   2.509  24.493  1.00 86.30           C  
ANISOU 1509  CB  LYS H 213    13448   6905  12436   5622   4728   1679       C  
ATOM   1510  CG  LYS H 213      68.934   1.489  24.812  1.00 87.45           C  
ANISOU 1510  CG  LYS H 213    14134   6423  12671   5304   4786   1340       C  
ATOM   1511  CD  LYS H 213      69.453   0.068  24.749  1.00 94.14           C  
ANISOU 1511  CD  LYS H 213    15565   6658  13548   5798   5384   1492       C  
ATOM   1512  CE  LYS H 213      69.766  -0.319  23.304  1.00 98.01           C  
ANISOU 1512  CE  LYS H 213    16652   6818  13770   6090   5687   1196       C  
ATOM   1513  NZ  LYS H 213      70.271  -1.691  23.201  1.00104.82           N  
ANISOU 1513  NZ  LYS H 213    18170   7014  14645   6616   6311   1314       N  
ATOM   1514  N   VAL H 214      70.066   6.072  24.334  1.00 77.52           N  
ANISOU 1514  N   VAL H 214    10932   7171  11350   4970   3695   1730       N  
ATOM   1515  CA  VAL H 214      70.943   7.235  24.453  1.00 76.45           C  
ANISOU 1515  CA  VAL H 214    10154   7579  11314   5025   3517   2082       C  
ATOM   1516  C   VAL H 214      71.182   7.560  25.909  1.00 74.58           C  
ANISOU 1516  C   VAL H 214     9433   7648  11257   4903   3263   2338       C  
ATOM   1517  O   VAL H 214      70.231   7.732  26.678  1.00 70.69           O  
ANISOU 1517  O   VAL H 214     8947   7113  10800   4531   2971   2093       O  
ATOM   1518  CB  VAL H 214      70.334   8.514  23.841  1.00 73.56           C  
ANISOU 1518  CB  VAL H 214     9611   7416  10923   4635   3168   1821       C  
ATOM   1519  CG1 VAL H 214      71.412   9.585  23.700  1.00 74.14           C  
ANISOU 1519  CG1 VAL H 214     9099   7938  11134   4745   3099   2226       C  
ATOM   1520  CG2 VAL H 214      69.694   8.230  22.500  1.00 75.04           C  
ANISOU 1520  CG2 VAL H 214    10303   7347  10860   4637   3305   1442       C  
ATOM   1521  N   ASP H 215      72.452   7.660  26.277  1.00 76.24           N  
ANISOU 1521  N   ASP H 215     9200   8219  11550   5231   3368   2846       N  
ATOM   1522  CA  ASP H 215      72.812   8.175  27.580  1.00 75.59           C  
ANISOU 1522  CA  ASP H 215     8573   8558  11591   5095   3053   3080       C  
ATOM   1523  C   ASP H 215      73.383   9.565  27.391  1.00 74.94           C  
ANISOU 1523  C   ASP H 215     7945   8896  11633   4867   2738   3197       C  
ATOM   1524  O   ASP H 215      74.322   9.742  26.638  1.00 77.93           O  
ANISOU 1524  O   ASP H 215     8116   9445  12049   5120   2936   3521       O  
ATOM   1525  CB  ASP H 215      73.805   7.240  28.242  1.00 78.58           C  
ANISOU 1525  CB  ASP H 215     8797   9094  11964   5596   3368   3594       C  
ATOM   1526  CG  ASP H 215      73.259   5.843  28.354  1.00 80.14           C  
ANISOU 1526  CG  ASP H 215     9591   8769  12088   5836   3748   3504       C  
ATOM   1527  OD1 ASP H 215      72.031   5.703  28.210  1.00 77.33           O  
ANISOU 1527  OD1 ASP H 215     9659   8010  11711   5487   3640   3026       O  
ATOM   1528  OD2 ASP H 215      74.032   4.886  28.553  1.00 84.18           O  
ANISOU 1528  OD2 ASP H 215    10153   9256  12577   6365   4170   3926       O  
ATOM   1529  N   LYS H 216      72.773  10.566  28.017  1.00 72.40           N  
ANISOU 1529  N   LYS H 216     7424   8702  11382   4395   2273   2933       N  
ATOM   1530  CA  LYS H 216      73.290  11.921  27.895  1.00 72.04           C  
ANISOU 1530  CA  LYS H 216     6902   8965  11506   4126   1970   3020       C  
ATOM   1531  C   LYS H 216      73.707  12.473  29.235  1.00 72.21           C  
ANISOU 1531  C   LYS H 216     6453   9376  11608   3916   1577   3123       C  
ATOM   1532  O   LYS H 216      72.875  12.651  30.124  1.00 70.46           O  
ANISOU 1532  O   LYS H 216     6344   9116  11313   3678   1299   2811       O  
ATOM   1533  CB  LYS H 216      72.296  12.860  27.220  1.00 68.74           C  
ANISOU 1533  CB  LYS H 216     6680   8332  11106   3761   1783   2610       C  
ATOM   1534  CG  LYS H 216      72.992  14.079  26.626  1.00 70.90           C  
ANISOU 1534  CG  LYS H 216     6547   8801  11592   3612   1670   2805       C  
ATOM   1535  CD  LYS H 216      72.546  14.359  25.193  1.00 71.09           C  
ANISOU 1535  CD  LYS H 216     6831   8622  11560   3663   1875   2689       C  
ATOM   1536  CE  LYS H 216      73.173  13.396  24.191  1.00 74.80           C  
ANISOU 1536  CE  LYS H 216     7476   9057  11887   4170   2355   2953       C  
ATOM   1537  NZ  LYS H 216      74.570  13.804  23.868  1.00 78.95           N  
ANISOU 1537  NZ  LYS H 216     7477   9916  12606   4368   2485   3517       N  
ATOM   1538  N   LYS H 217      75.009  12.700  29.382  1.00 74.58           N  
ANISOU 1538  N   LYS H 217     6218  10091  12028   4028   1559   3578       N  
ATOM   1539  CA  LYS H 217      75.531  13.338  30.575  1.00 75.26           C  
ANISOU 1539  CA  LYS H 217     5800  10620  12176   3772   1123   3661       C  
ATOM   1540  C   LYS H 217      75.104  14.812  30.580  1.00 72.89           C  
ANISOU 1540  C   LYS H 217     5413  10241  12043   3211    687   3298       C  
ATOM   1541  O   LYS H 217      75.394  15.578  29.662  1.00 72.61           O  
ANISOU 1541  O   LYS H 217     5248  10123  12218   3061    715   3374       O  
ATOM   1542  CB  LYS H 217      77.062  13.164  30.693  1.00 79.70           C  
ANISOU 1542  CB  LYS H 217     5749  11712  12820   4013   1206   4289       C  
ATOM   1543  CG  LYS H 217      77.673  13.865  31.910  1.00 82.35           C  
ANISOU 1543  CG  LYS H 217     5508  12585  13195   3685    686   4356       C  
ATOM   1544  CD  LYS H 217      79.039  13.317  32.349  1.00 88.62           C  
ANISOU 1544  CD  LYS H 217     5697  14022  13954   4015    776   5012       C  
ATOM   1545  CE  LYS H 217      80.099  13.343  31.256  1.00 91.75           C  
ANISOU 1545  CE  LYS H 217     5740  14573  14547   4234   1099   5568       C  
ATOM   1546  NZ  LYS H 217      80.303  14.698  30.699  1.00 92.98           N  
ANISOU 1546  NZ  LYS H 217     5615  14685  15027   3696    805   5477       N  
ATOM   1547  N   VAL H 218      74.377  15.193  31.614  1.00 71.14           N  
ANISOU 1547  N   VAL H 218     5295  10018  11717   2947    325   2919       N  
ATOM   1548  CA  VAL H 218      73.950  16.560  31.735  1.00 71.43           C  
ANISOU 1548  CA  VAL H 218     5319   9934  11889   2467    -61   2560       C  
ATOM   1549  C   VAL H 218      74.864  17.245  32.720  1.00 74.34           C  
ANISOU 1549  C   VAL H 218     5178  10731  12339   2187   -500   2640       C  
ATOM   1550  O   VAL H 218      75.172  16.684  33.768  1.00 75.87           O  
ANISOU 1550  O   VAL H 218     5200  11302  12327   2331   -629   2734       O  
ATOM   1551  CB  VAL H 218      72.479  16.650  32.230  1.00 69.80           C  
ANISOU 1551  CB  VAL H 218     5594   9445  11481   2367   -181   2059       C  
ATOM   1552  CG1 VAL H 218      71.605  15.666  31.470  1.00 67.47           C  
ANISOU 1552  CG1 VAL H 218     5758   8824  11055   2641    223   2009       C  
ATOM   1553  CG2 VAL H 218      72.384  16.357  33.730  1.00 71.95           C  
ANISOU 1553  CG2 VAL H 218     5798  10022  11516   2405   -446   1965       C  
ATOM   1554  N   GLU H 219      75.285  18.460  32.392  1.00 75.70           N  
ANISOU 1554  N   GLU H 219     5105  10850  12807   1777   -735   2605       N  
ATOM   1555  CA  GLU H 219      76.163  19.218  33.274  1.00 80.72           C  
ANISOU 1555  CA  GLU H 219     5257  11857  13555   1394  -1214   2623       C  
ATOM   1556  C   GLU H 219      75.726  20.669  33.444  1.00 81.14           C  
ANISOU 1556  C   GLU H 219     5449  11580  13800    854  -1591   2161       C  
ATOM   1557  O   GLU H 219      74.616  21.030  33.054  1.00 77.42           O  
ANISOU 1557  O   GLU H 219     5468  10642  13306    847  -1480   1824       O  
ATOM   1558  CB  GLU H 219      77.579  19.176  32.729  1.00 85.61           C  
ANISOU 1558  CB  GLU H 219     5255  12834  14437   1403  -1113   3226       C  
ATOM   1559  CG  GLU H 219      78.070  17.777  32.472  1.00 86.28           C  
ANISOU 1559  CG  GLU H 219     5236  13206  14340   2009   -668   3727       C  
ATOM   1560  CD  GLU H 219      79.125  17.743  31.391  1.00 89.37           C  
ANISOU 1560  CD  GLU H 219     5210  13747  14998   2158   -355   4330       C  
ATOM   1561  OE1 GLU H 219      79.037  18.573  30.455  1.00 88.92           O  
ANISOU 1561  OE1 GLU H 219     5184  13370  15230   1927   -293   4308       O  
ATOM   1562  OE2 GLU H 219      80.034  16.889  31.480  1.00 92.68           O  
ANISOU 1562  OE2 GLU H 219     5263  14624  15325   2551   -139   4867       O  
ATOM   1563  N   PRO H 220      76.588  21.491  34.077  1.00 86.53           N  
ANISOU 1563  N   PRO H 220     5705  12516  14656    400  -2047   2142       N  
ATOM   1564  CA  PRO H 220      76.486  22.960  34.161  1.00 88.31           C  
ANISOU 1564  CA  PRO H 220     5997  12383  15172   -181  -2402   1771       C  
ATOM   1565  C   PRO H 220      76.966  23.669  32.898  1.00 88.54           C  
ANISOU 1565  C   PRO H 220     5816  12116  15711   -396  -2190   2097       C  
ATOM   1566  O   PRO H 220      77.658  24.708  33.024  1.00 92.79           O  
ANISOU 1566  O   PRO H 220     6036  12602  16619   -948  -2518   2088       O  
ATOM   1567  CB  PRO H 220      77.419  23.309  35.325  1.00 94.83           C  
ANISOU 1567  CB  PRO H 220     6369  13700  15964   -573  -2969   1698       C  
ATOM   1568  CG  PRO H 220      77.500  22.049  36.133  1.00 94.64           C  
ANISOU 1568  CG  PRO H 220     6244  14247  15467   -106  -2934   1850       C  
ATOM   1569  CD  PRO H 220      77.487  20.956  35.115  1.00 90.89           C  
ANISOU 1569  CD  PRO H 220     5787  13745  15003    441  -2320   2346       C  
TER    1570      PRO H 220                                                      
ATOM   1571  N   ILE L   2      27.852  33.060  16.869  1.00 66.34           N  
ANISOU 1571  N   ILE L   2     8737   8567   7902   -359   -560   3173       N  
ATOM   1572  CA  ILE L   2      28.927  32.504  15.983  1.00 67.59           C  
ANISOU 1572  CA  ILE L   2     8906   9206   7570   -366   -384   3302       C  
ATOM   1573  C   ILE L   2      30.143  31.987  16.782  1.00 65.66           C  
ANISOU 1573  C   ILE L   2     8731   8877   7339   -330   -183   3037       C  
ATOM   1574  O   ILE L   2      30.932  31.204  16.233  1.00 66.80           O  
ANISOU 1574  O   ILE L   2     8919   9402   7059   -296    -21   2961       O  
ATOM   1575  CB  ILE L   2      29.398  33.519  14.887  1.00 71.58           C  
ANISOU 1575  CB  ILE L   2     9187   9969   8039   -464   -435   3958       C  
ATOM   1576  CG1 ILE L   2      29.975  32.803  13.645  1.00 74.38           C  
ANISOU 1576  CG1 ILE L   2     9543  11007   7711   -449   -289   4062       C  
ATOM   1577  CG2 ILE L   2      30.413  34.512  15.452  1.00 72.51           C  
ANISOU 1577  CG2 ILE L   2     9138   9769   8641   -542   -410   4229       C  
ATOM   1578  CD1 ILE L   2      29.117  32.915  12.354  1.00 77.07           C  
ANISOU 1578  CD1 ILE L   2     9821  11791   7672   -457   -431   4359       C  
ATOM   1579  N   GLU L   3      30.302  32.398  18.053  1.00 62.64           N  
ANISOU 1579  N   GLU L   3     8344   8033   7425   -320   -203   2869       N  
ATOM   1580  CA  GLU L   3      31.482  31.958  18.842  1.00 60.41           C  
ANISOU 1580  CA  GLU L   3     8110   7678   7165   -277    -38   2635       C  
ATOM   1581  C   GLU L   3      31.286  31.946  20.359  1.00 56.95           C  
ANISOU 1581  C   GLU L   3     7741   6815   7082   -219    -65   2267       C  
ATOM   1582  O   GLU L   3      31.105  32.976  20.987  1.00 58.09           O  
ANISOU 1582  O   GLU L   3     7754   6624   7696   -242   -192   2337       O  
ATOM   1583  CB  GLU L   3      32.731  32.775  18.503  1.00 62.81           C  
ANISOU 1583  CB  GLU L   3     8211   8045   7609   -355     17   3020       C  
ATOM   1584  CG  GLU L   3      34.023  32.079  18.945  1.00 62.56           C  
ANISOU 1584  CG  GLU L   3     8225   8104   7439   -299    209   2787       C  
ATOM   1585  CD  GLU L   3      35.181  33.050  19.275  1.00 65.22           C  
ANISOU 1585  CD  GLU L   3     8344   8269   8170   -371    223   3036       C  
ATOM   1586  OE1 GLU L   3      35.181  34.222  18.792  1.00 68.13           O  
ANISOU 1586  OE1 GLU L   3     8494   8555   8836   -492    117   3503       O  
ATOM   1587  OE2 GLU L   3      36.094  32.617  20.026  1.00 63.55           O  
ANISOU 1587  OE2 GLU L   3     8166   7990   7992   -309    326   2767       O  
ATOM   1588  N   LEU L   4      31.352  30.778  20.961  1.00 54.00           N  
ANISOU 1588  N   LEU L   4     7556   6468   6492   -135     46   1873       N  
ATOM   1589  CA  LEU L   4      30.949  30.659  22.340  1.00 51.73           C  
ANISOU 1589  CA  LEU L   4     7339   5871   6445    -77     21   1547       C  
ATOM   1590  C   LEU L   4      32.179  30.636  23.266  1.00 51.40           C  
ANISOU 1590  C   LEU L   4     7284   5721   6526    -26    107   1411       C  
ATOM   1591  O   LEU L   4      33.191  29.974  22.990  1.00 50.76           O  
ANISOU 1591  O   LEU L   4     7250   5832   6204      4    237   1388       O  
ATOM   1592  CB  LEU L   4      30.056  29.422  22.512  1.00 50.33           C  
ANISOU 1592  CB  LEU L   4     7359   5758   6007    -32     61   1245       C  
ATOM   1593  CG  LEU L   4      28.545  29.555  22.245  1.00 50.64           C  
ANISOU 1593  CG  LEU L   4     7393   5757   6092    -66    -64   1243       C  
ATOM   1594  CD1 LEU L   4      28.198  30.671  21.302  1.00 53.50           C  
ANISOU 1594  CD1 LEU L   4     7587   6158   6584   -133   -207   1608       C  
ATOM   1595  CD2 LEU L   4      27.954  28.266  21.740  1.00 49.97           C  
ANISOU 1595  CD2 LEU L   4     7463   5860   5664    -55    -20   1057       C  
ATOM   1596  N   THR L   5      32.099  31.381  24.364  1.00 50.82           N  
ANISOU 1596  N   THR L   5     7121   5355   6832     -2     21   1292       N  
ATOM   1597  CA  THR L   5      33.244  31.500  25.239  1.00 50.78           C  
ANISOU 1597  CA  THR L   5     7069   5255   6971     51     63   1161       C  
ATOM   1598  C   THR L   5      32.948  30.955  26.624  1.00 49.79           C  
ANISOU 1598  C   THR L   5     7054   5027   6836    154     79    783       C  
ATOM   1599  O   THR L   5      32.076  31.491  27.302  1.00 51.22           O  
ANISOU 1599  O   THR L   5     7176   5047   7239    173    -23    650       O  
ATOM   1600  CB  THR L   5      33.694  32.969  25.369  1.00 52.73           C  
ANISOU 1600  CB  THR L   5     7056   5266   7714     -3    -71   1342       C  
ATOM   1601  OG1 THR L   5      34.369  33.390  24.169  1.00 54.90           O  
ANISOU 1601  OG1 THR L   5     7205   5681   7973   -107    -44   1755       O  
ATOM   1602  CG2 THR L   5      34.641  33.138  26.536  1.00 51.69           C  
ANISOU 1602  CG2 THR L   5     6860   4995   7783     72    -74   1096       C  
ATOM   1603  N   GLN L   6      33.670  29.911  27.043  1.00 47.78           N  
ANISOU 1603  N   GLN L   6     6940   4887   6329    227    200    621       N  
ATOM   1604  CA  GLN L   6      33.547  29.383  28.391  1.00 46.05           C  
ANISOU 1604  CA  GLN L   6     6810   4614   6073    325    217    328       C  
ATOM   1605  C   GLN L   6      34.863  29.490  29.160  1.00 46.27           C  
ANISOU 1605  C   GLN L   6     6776   4622   6182    404    227    222       C  
ATOM   1606  O   GLN L   6      35.929  29.343  28.588  1.00 46.54           O  
ANISOU 1606  O   GLN L   6     6783   4738   6162    396    285    335       O  
ATOM   1607  CB  GLN L   6      33.206  27.909  28.318  1.00 45.80           C  
ANISOU 1607  CB  GLN L   6     7000   4708   5692    352    325    243       C  
ATOM   1608  CG  GLN L   6      31.843  27.570  27.803  1.00 45.04           C  
ANISOU 1608  CG  GLN L   6     6977   4632   5505    288    312    267       C  
ATOM   1609  CD  GLN L   6      31.700  26.097  27.636  1.00 44.39           C  
ANISOU 1609  CD  GLN L   6     7084   4634   5147    306    401    183       C  
ATOM   1610  OE1 GLN L   6      31.502  25.607  26.521  1.00 46.24           O  
ANISOU 1610  OE1 GLN L   6     7368   4975   5224    266    416    244       O  
ATOM   1611  NE2 GLN L   6      31.837  25.361  28.731  1.00 42.89           N  
ANISOU 1611  NE2 GLN L   6     6986   4405   4904    373    448     42       N  
ATOM   1612  N   PRO L   7      34.797  29.692  30.487  1.00 47.00           N  
ANISOU 1612  N   PRO L   7     6835   4647   6375    491    173    -19       N  
ATOM   1613  CA  PRO L   7      36.063  29.711  31.241  1.00 46.52           C  
ANISOU 1613  CA  PRO L   7     6716   4599   6362    581    163   -144       C  
ATOM   1614  C   PRO L   7      36.642  28.311  31.292  1.00 45.80           C  
ANISOU 1614  C   PRO L   7     6817   4653   5931    647    284   -161       C  
ATOM   1615  O   PRO L   7      35.879  27.339  31.367  1.00 44.74           O  
ANISOU 1615  O   PRO L   7     6860   4575   5563    654    348   -180       O  
ATOM   1616  CB  PRO L   7      35.630  30.140  32.646  1.00 46.74           C  
ANISOU 1616  CB  PRO L   7     6672   4595   6492    676     72   -427       C  
ATOM   1617  CG  PRO L   7      34.217  29.648  32.785  1.00 46.39           C  
ANISOU 1617  CG  PRO L   7     6748   4607   6273    658    117   -456       C  
ATOM   1618  CD  PRO L   7      33.613  29.765  31.377  1.00 46.79           C  
ANISOU 1618  CD  PRO L   7     6820   4597   6360    527    132   -206       C  
ATOM   1619  N   PRO L   8      37.985  28.196  31.251  1.00 47.13           N  
ANISOU 1619  N   PRO L   8     6932   4861   6112    695    305   -155       N  
ATOM   1620  CA  PRO L   8      38.570  26.878  30.989  1.00 45.94           C  
ANISOU 1620  CA  PRO L   8     6941   4826   5687    757    409   -149       C  
ATOM   1621  C   PRO L   8      38.257  25.942  32.109  1.00 45.79           C  
ANISOU 1621  C   PRO L   8     7078   4829   5491    860    410   -290       C  
ATOM   1622  O   PRO L   8      38.122  24.723  31.888  1.00 46.60           O  
ANISOU 1622  O   PRO L   8     7351   4963   5393    886    478   -268       O  
ATOM   1623  CB  PRO L   8      40.076  27.148  30.978  1.00 46.36           C  
ANISOU 1623  CB  PRO L   8     6850   4911   5854    805    405   -156       C  
ATOM   1624  CG  PRO L   8      40.207  28.600  30.660  1.00 48.15           C  
ANISOU 1624  CG  PRO L   8     6841   5039   6415    704    329    -54       C  
ATOM   1625  CD  PRO L   8      39.004  29.260  31.298  1.00 47.69           C  
ANISOU 1625  CD  PRO L   8     6771   4857   6492    684    227   -145       C  
ATOM   1626  N   SER L   9      38.168  26.493  33.313  1.00 45.64           N  
ANISOU 1626  N   SER L   9     6983   4804   5554    923    326   -436       N  
ATOM   1627  CA  SER L   9      37.992  25.639  34.471  1.00 45.70           C  
ANISOU 1627  CA  SER L   9     7111   4899   5354   1027    329   -525       C  
ATOM   1628  C   SER L   9      37.302  26.343  35.604  1.00 46.37           C  
ANISOU 1628  C   SER L   9     7104   5047   5469   1065    257   -685       C  
ATOM   1629  O   SER L   9      37.531  27.534  35.806  1.00 47.40           O  
ANISOU 1629  O   SER L   9     7039   5133   5838   1073    158   -820       O  
ATOM   1630  CB  SER L   9      39.339  25.187  35.006  1.00 45.91           C  
ANISOU 1630  CB  SER L   9     7128   4985   5332   1158    299   -582       C  
ATOM   1631  OG  SER L   9      39.657  25.946  36.152  1.00 46.65           O  
ANISOU 1631  OG  SER L   9     7080   5151   5496   1248    189   -766       O  
ATOM   1632  N   VAL L  10      36.516  25.573  36.368  1.00 45.73           N  
ANISOU 1632  N   VAL L  10     7140   5080   5156   1094    303   -678       N  
ATOM   1633  CA  VAL L  10      35.735  26.072  37.487  1.00 46.06           C  
ANISOU 1633  CA  VAL L  10     7090   5272   5138   1141    268   -838       C  
ATOM   1634  C   VAL L  10      35.714  24.996  38.538  1.00 47.29           C  
ANISOU 1634  C   VAL L  10     7361   5629   4978   1226    313   -777       C  
ATOM   1635  O   VAL L  10      35.578  23.827  38.209  1.00 47.28           O  
ANISOU 1635  O   VAL L  10     7534   5573   4857   1183    392   -567       O  
ATOM   1636  CB  VAL L  10      34.277  26.330  37.091  1.00 45.53           C  
ANISOU 1636  CB  VAL L  10     7017   5164   5119   1026    314   -810       C  
ATOM   1637  CG1 VAL L  10      33.394  26.408  38.297  1.00 45.83           C  
ANISOU 1637  CG1 VAL L  10     6989   5431   4994   1082    330   -945       C  
ATOM   1638  CG2 VAL L  10      34.166  27.597  36.247  1.00 45.67           C  
ANISOU 1638  CG2 VAL L  10     6878   5000   5475    957    233   -863       C  
ATOM   1639  N   SER L  11      35.814  25.397  39.806  1.00 49.06           N  
ANISOU 1639  N   SER L  11     7470   6095   5077   1349    250   -960       N  
ATOM   1640  CA  SER L  11      35.910  24.457  40.898  1.00 50.34           C  
ANISOU 1640  CA  SER L  11     7712   6509   4905   1444    277   -862       C  
ATOM   1641  C   SER L  11      34.997  24.855  42.051  1.00 52.04           C  
ANISOU 1641  C   SER L  11     7803   7060   4909   1497    292  -1010       C  
ATOM   1642  O   SER L  11      34.746  26.016  42.247  1.00 52.21           O  
ANISOU 1642  O   SER L  11     7636   7132   5070   1533    222  -1308       O  
ATOM   1643  CB  SER L  11      37.359  24.356  41.365  1.00 51.32           C  
ANISOU 1643  CB  SER L  11     7812   6693   4996   1592    169   -923       C  
ATOM   1644  OG  SER L  11      37.807  25.591  41.854  1.00 52.52           O  
ANISOU 1644  OG  SER L  11     7744   6936   5275   1685     39  -1256       O  
ATOM   1645  N   VAL L  12      34.496  23.869  42.796  1.00 53.98           N  
ANISOU 1645  N   VAL L  12     8138   7539   4833   1502    384   -792       N  
ATOM   1646  CA  VAL L  12      33.565  24.091  43.909  1.00 56.13           C  
ANISOU 1646  CA  VAL L  12     8282   8220   4827   1545    439   -885       C  
ATOM   1647  C   VAL L  12      33.864  23.166  45.052  1.00 58.35           C  
ANISOU 1647  C   VAL L  12     8611   8853   4705   1641    461   -666       C  
ATOM   1648  O   VAL L  12      34.398  22.096  44.869  1.00 59.09           O  
ANISOU 1648  O   VAL L  12     8878   8801   4773   1622    468   -347       O  
ATOM   1649  CB  VAL L  12      32.112  23.779  43.518  1.00 55.65           C  
ANISOU 1649  CB  VAL L  12     8249   8117   4779   1377    589   -728       C  
ATOM   1650  CG1 VAL L  12      31.509  24.945  42.853  1.00 54.68           C  
ANISOU 1650  CG1 VAL L  12     7991   7829   4955   1328    554  -1007       C  
ATOM   1651  CG2 VAL L  12      32.044  22.545  42.596  1.00 54.39           C  
ANISOU 1651  CG2 VAL L  12     8319   7626   4719   1229    661   -349       C  
ATOM   1652  N   ALA L  13      33.489  23.555  46.245  1.00 61.30           N  
ANISOU 1652  N   ALA L  13     8818   9713   4759   1752    468   -829       N  
ATOM   1653  CA  ALA L  13      33.619  22.640  47.361  1.00 64.61           C  
ANISOU 1653  CA  ALA L  13     9271  10541   4736   1829    506   -544       C  
ATOM   1654  C   ALA L  13      32.446  21.666  47.338  1.00 65.43           C  
ANISOU 1654  C   ALA L  13     9458  10679   4722   1652    699   -123       C  
ATOM   1655  O   ALA L  13      31.381  21.999  46.832  1.00 65.15           O  
ANISOU 1655  O   ALA L  13     9370  10543   4839   1522    800   -199       O  
ATOM   1656  CB  ALA L  13      33.636  23.410  48.648  1.00 67.73           C  
ANISOU 1656  CB  ALA L  13     9431  11526   4777   2021    448   -885       C  
ATOM   1657  N   PRO L  14      32.630  20.459  47.894  1.00 67.11           N  
ANISOU 1657  N   PRO L  14     9781  11023   4695   1644    737    338       N  
ATOM   1658  CA  PRO L  14      31.544  19.488  47.860  1.00 68.13           C  
ANISOU 1658  CA  PRO L  14     9968  11136   4783   1452    909    777       C  
ATOM   1659  C   PRO L  14      30.306  20.081  48.476  1.00 69.53           C  
ANISOU 1659  C   PRO L  14     9931  11769   4717   1419   1056    632       C  
ATOM   1660  O   PRO L  14      30.405  20.710  49.506  1.00 72.81           O  
ANISOU 1660  O   PRO L  14    10167  12728   4770   1584   1038    394       O  
ATOM   1661  CB  PRO L  14      32.061  18.345  48.733  1.00 71.56           C  
ANISOU 1661  CB  PRO L  14    10479  11779   4933   1504    890   1263       C  
ATOM   1662  CG  PRO L  14      33.271  18.863  49.419  1.00 72.27           C  
ANISOU 1662  CG  PRO L  14    10512  12143   4805   1750    720   1016       C  
ATOM   1663  CD  PRO L  14      33.825  19.927  48.560  1.00 68.88           C  
ANISOU 1663  CD  PRO L  14    10064  11387   4721   1803    609    500       C  
ATOM   1664  N   GLY L  15      29.158  19.898  47.839  1.00 68.65           N  
ANISOU 1664  N   GLY L  15     9819  11457   4808   1219   1191    734       N  
ATOM   1665  CA  GLY L  15      27.911  20.466  48.316  1.00 70.78           C  
ANISOU 1665  CA  GLY L  15     9863  12132   4900   1180   1339    575       C  
ATOM   1666  C   GLY L  15      27.575  21.840  47.765  1.00 68.98           C  
ANISOU 1666  C   GLY L  15     9496  11791   4921   1230   1281      4       C  
ATOM   1667  O   GLY L  15      26.418  22.226  47.761  1.00 69.79           O  
ANISOU 1667  O   GLY L  15     9438  12041   5040   1156   1396   -121       O  
ATOM   1668  N   GLN L  16      28.572  22.595  47.309  1.00 66.82           N  
ANISOU 1668  N   GLN L  16     9262  11254   4871   1352   1098   -330       N  
ATOM   1669  CA  GLN L  16      28.303  23.966  46.886  1.00 65.55           C  
ANISOU 1669  CA  GLN L  16     8938  10987   4982   1409   1014   -847       C  
ATOM   1670  C   GLN L  16      27.800  24.054  45.476  1.00 62.11           C  
ANISOU 1670  C   GLN L  16     8598  10002   4998   1235   1014   -807       C  
ATOM   1671  O   GLN L  16      27.850  23.085  44.755  1.00 61.79           O  
ANISOU 1671  O   GLN L  16     8764   9638   5075   1091   1054   -445       O  
ATOM   1672  CB  GLN L  16      29.479  24.899  47.154  1.00 65.30           C  
ANISOU 1672  CB  GLN L  16     8829  10974   5008   1614    813  -1250       C  
ATOM   1673  CG  GLN L  16      29.199  25.735  48.395  1.00 70.61           C  
ANISOU 1673  CG  GLN L  16     9212  12246   5372   1807    794  -1676       C  
ATOM   1674  CD  GLN L  16      30.418  25.914  49.259  1.00 73.12           C  
ANISOU 1674  CD  GLN L  16     9483  12847   5451   2020    642  -1857       C  
ATOM   1675  OE1 GLN L  16      30.951  27.021  49.359  1.00 73.29           O  
ANISOU 1675  OE1 GLN L  16     9342  12836   5670   2168    461  -2357       O  
ATOM   1676  NE2 GLN L  16      30.874  24.807  49.861  1.00 74.70           N  
ANISOU 1676  NE2 GLN L  16     9820  13298   5266   2033    695  -1434       N  
ATOM   1677  N   THR L  17      27.273  25.206  45.096  1.00 61.17           N  
ANISOU 1677  N   THR L  17     8313   9793   5137   1257    956  -1185       N  
ATOM   1678  CA  THR L  17      26.675  25.352  43.778  1.00 58.18           C  
ANISOU 1678  CA  THR L  17     7998   8955   5151   1098    948  -1135       C  
ATOM   1679  C   THR L  17      27.724  25.707  42.739  1.00 55.73           C  
ANISOU 1679  C   THR L  17     7817   8188   5171   1101    791  -1169       C  
ATOM   1680  O   THR L  17      28.602  26.517  42.976  1.00 56.55           O  
ANISOU 1680  O   THR L  17     7836   8290   5359   1239    654  -1434       O  
ATOM   1681  CB  THR L  17      25.577  26.402  43.840  1.00 58.88           C  
ANISOU 1681  CB  THR L  17     7830   9154   5387   1122    946  -1482       C  
ATOM   1682  OG1 THR L  17      24.576  25.946  44.752  1.00 61.95           O  
ANISOU 1682  OG1 THR L  17     8090  10008   5442   1100   1127  -1408       O  
ATOM   1683  CG2 THR L  17      24.942  26.629  42.486  1.00 56.79           C  
ANISOU 1683  CG2 THR L  17     7613   8444   5522    973    909  -1426       C  
ATOM   1684  N   ALA L  18      27.663  25.095  41.578  1.00 53.54           N  
ANISOU 1684  N   ALA L  18     7723   7541   5080    950    809   -909       N  
ATOM   1685  CA  ALA L  18      28.624  25.460  40.565  1.00 51.60           C  
ANISOU 1685  CA  ALA L  18     7566   6933   5105    951    684   -932       C  
ATOM   1686  C   ALA L  18      27.884  26.199  39.476  1.00 50.97           C  
ANISOU 1686  C   ALA L  18     7421   6594   5351    856    636  -1007       C  
ATOM   1687  O   ALA L  18      26.772  25.824  39.091  1.00 50.12           O  
ANISOU 1687  O   ALA L  18     7325   6459   5261    735    714   -896       O  
ATOM   1688  CB  ALA L  18      29.337  24.223  40.008  1.00 49.82           C  
ANISOU 1688  CB  ALA L  18     7585   6515   4827    887    717   -613       C  
ATOM   1689  N   ARG L  19      28.512  27.253  38.979  1.00 50.34           N  
ANISOU 1689  N   ARG L  19     7257   6322   5549    906    494  -1173       N  
ATOM   1690  CA  ARG L  19      27.952  27.986  37.870  1.00 49.10           C  
ANISOU 1690  CA  ARG L  19     7038   5902   5717    819    421  -1180       C  
ATOM   1691  C   ARG L  19      28.930  28.021  36.720  1.00 48.11           C  
ANISOU 1691  C   ARG L  19     7023   5505   5753    768    356  -1014       C  
ATOM   1692  O   ARG L  19      30.056  28.522  36.898  1.00 49.67           O  
ANISOU 1692  O   ARG L  19     7170   5658   6045    850    273  -1100       O  
ATOM   1693  CB  ARG L  19      27.592  29.389  38.328  1.00 50.51           C  
ANISOU 1693  CB  ARG L  19     6944   6099   6147    917    297  -1519       C  
ATOM   1694  CG  ARG L  19      26.235  29.423  39.016  1.00 51.89           C  
ANISOU 1694  CG  ARG L  19     6979   6519   6219    930    374  -1672       C  
ATOM   1695  CD  ARG L  19      25.969  30.684  39.740  1.00 53.69           C  
ANISOU 1695  CD  ARG L  19     6914   6838   6647   1076    254  -2093       C  
ATOM   1696  NE  ARG L  19      26.340  30.539  41.144  1.00 56.71           N  
ANISOU 1696  NE  ARG L  19     7218   7624   6705   1226    300  -2316       N  
ATOM   1697  CZ  ARG L  19      25.464  30.353  42.131  1.00 59.08           C  
ANISOU 1697  CZ  ARG L  19     7384   8338   6725   1286    417  -2471       C  
ATOM   1698  NH1 ARG L  19      24.165  30.265  41.854  1.00 59.13           N  
ANISOU 1698  NH1 ARG L  19     7321   8370   6775   1198    503  -2431       N  
ATOM   1699  NH2 ARG L  19      25.885  30.240  43.389  1.00 60.90           N  
ANISOU 1699  NH2 ARG L  19     7535   8993   6612   1434    449  -2659       N  
ATOM   1700  N   ILE L  20      28.549  27.456  35.568  1.00 45.74           N  
ANISOU 1700  N   ILE L  20     6854   5058   5466    640    395   -790       N  
ATOM   1701  CA  ILE L  20      29.437  27.501  34.410  1.00 45.00           C  
ANISOU 1701  CA  ILE L  20     6837   4783   5477    597    350   -636       C  
ATOM   1702  C   ILE L  20      28.887  28.389  33.315  1.00 45.24           C  
ANISOU 1702  C   ILE L  20     6768   4653   5768    517    258   -572       C  
ATOM   1703  O   ILE L  20      27.815  28.135  32.780  1.00 45.62           O  
ANISOU 1703  O   ILE L  20     6841   4690   5804    434    275   -504       O  
ATOM   1704  CB  ILE L  20      29.715  26.102  33.861  1.00 44.40           C  
ANISOU 1704  CB  ILE L  20     6982   4702   5185    542    448   -448       C  
ATOM   1705  CG1 ILE L  20      30.215  25.206  34.984  1.00 44.48           C  
ANISOU 1705  CG1 ILE L  20     7081   4848   4972    622    517   -458       C  
ATOM   1706  CG2 ILE L  20      30.697  26.149  32.698  1.00 42.43           C  
ANISOU 1706  CG2 ILE L  20     6780   4347   4994    520    419   -330       C  
ATOM   1707  CD1 ILE L  20      30.342  23.785  34.558  1.00 44.69           C  
ANISOU 1707  CD1 ILE L  20     7300   4820   4859    575    589   -291       C  
ATOM   1708  N   SER L  21      29.605  29.446  32.979  1.00 46.12           N  
ANISOU 1708  N   SER L  21     6749   4635   6139    537    146   -572       N  
ATOM   1709  CA  SER L  21      29.061  30.420  32.045  1.00 46.24           C  
ANISOU 1709  CA  SER L  21     6635   4489   6444    467     31   -469       C  
ATOM   1710  C   SER L  21      29.436  30.115  30.599  1.00 45.44           C  
ANISOU 1710  C   SER L  21     6633   4361   6273    368     49   -174       C  
ATOM   1711  O   SER L  21      30.376  29.385  30.345  1.00 44.80           O  
ANISOU 1711  O   SER L  21     6675   4352   5994    372    134    -96       O  
ATOM   1712  CB  SER L  21      29.523  31.805  32.442  1.00 47.01           C  
ANISOU 1712  CB  SER L  21     6497   4432   6934    528   -124   -601       C  
ATOM   1713  OG  SER L  21      30.908  31.917  32.248  1.00 48.03           O  
ANISOU 1713  OG  SER L  21     6625   4516   7108    534   -131   -510       O  
ATOM   1714  N   CYS L  22      28.705  30.713  29.667  1.00 46.34           N  
ANISOU 1714  N   CYS L  22     6667   4393   6547    293    -40    -21       N  
ATOM   1715  CA  CYS L  22      28.892  30.523  28.231  1.00 46.52           C  
ANISOU 1715  CA  CYS L  22     6749   4464   6462    204    -36    265       C  
ATOM   1716  C   CYS L  22      28.403  31.786  27.550  1.00 48.59           C  
ANISOU 1716  C   CYS L  22     6820   4584   7059    153   -202    448       C  
ATOM   1717  O   CYS L  22      27.211  32.101  27.620  1.00 49.59           O  
ANISOU 1717  O   CYS L  22     6879   4649   7316    150   -285    384       O  
ATOM   1718  CB  CYS L  22      28.044  29.338  27.771  1.00 45.44           C  
ANISOU 1718  CB  CYS L  22     6782   4462   6021    161     43    258       C  
ATOM   1719  SG  CYS L  22      27.997  29.056  26.002  1.00 46.38           S  
ANISOU 1719  SG  CYS L  22     6953   4725   5946     76     25    525       S  
ATOM   1720  N   SER L  23      29.299  32.537  26.914  1.00 49.76           N  
ANISOU 1720  N   SER L  23     6857   4670   7379    112   -260    692       N  
ATOM   1721  CA  SER L  23      28.888  33.839  26.395  1.00 51.88           C  
ANISOU 1721  CA  SER L  23     6912   4744   8054     65   -447    906       C  
ATOM   1722  C   SER L  23      29.326  34.090  24.957  1.00 53.57           C  
ANISOU 1722  C   SER L  23     7091   5066   8199    -40   -463   1355       C  
ATOM   1723  O   SER L  23      30.350  33.520  24.514  1.00 53.53           O  
ANISOU 1723  O   SER L  23     7166   5256   7915    -63   -328   1466       O  
ATOM   1724  CB  SER L  23      29.381  34.944  27.309  1.00 52.87           C  
ANISOU 1724  CB  SER L  23     6827   4600   8662    117   -569    761       C  
ATOM   1725  OG  SER L  23      30.776  35.019  27.235  1.00 53.62           O  
ANISOU 1725  OG  SER L  23     6894   4706   8774     95   -515    875       O  
ATOM   1726  N   GLY L  24      28.522  34.900  24.240  1.00 54.80           N  
ANISOU 1726  N   GLY L  24     7113   5125   8582    -92   -629   1607       N  
ATOM   1727  CA  GLY L  24      28.792  35.321  22.859  1.00 57.56           C  
ANISOU 1727  CA  GLY L  24     7384   5603   8884   -194   -677   2105       C  
ATOM   1728  C   GLY L  24      27.775  36.363  22.394  1.00 60.33           C  
ANISOU 1728  C   GLY L  24     7557   5758   9607   -225   -913   2345       C  
ATOM   1729  O   GLY L  24      26.747  36.543  23.048  1.00 59.66           O  
ANISOU 1729  O   GLY L  24     7441   5491   9736   -158  -1014   2071       O  
ATOM   1730  N   ASP L  25      28.045  37.047  21.271  1.00 62.86           N  
ANISOU 1730  N   ASP L  25     7743   6135  10007   -322  -1003   2872       N  
ATOM   1731  CA  ASP L  25      27.132  38.091  20.772  1.00 65.81           C  
ANISOU 1731  CA  ASP L  25     7928   6300  10779   -350  -1259   3174       C  
ATOM   1732  C   ASP L  25      25.673  37.633  20.690  1.00 64.75           C  
ANISOU 1732  C   ASP L  25     7883   6243  10477   -288  -1330   2965       C  
ATOM   1733  O   ASP L  25      25.327  36.738  19.917  1.00 64.39           O  
ANISOU 1733  O   ASP L  25     7992   6570   9902   -303  -1244   3007       O  
ATOM   1734  CB  ASP L  25      27.550  38.640  19.388  1.00 70.45           C  
ANISOU 1734  CB  ASP L  25     8389   7071  11308   -472  -1320   3852       C  
ATOM   1735  CG  ASP L  25      28.788  39.544  19.438  1.00 74.00           C  
ANISOU 1735  CG  ASP L  25     8632   7310  12174   -563  -1337   4178       C  
ATOM   1736  OD1 ASP L  25      29.549  39.529  20.443  1.00 72.85           O  
ANISOU 1736  OD1 ASP L  25     8481   6967  12233   -529  -1259   3847       O  
ATOM   1737  OD2 ASP L  25      29.024  40.253  18.429  1.00 77.79           O  
ANISOU 1737  OD2 ASP L  25     8943   7853  12762   -677  -1429   4798       O  
ATOM   1738  N   SER L  26      24.816  38.273  21.472  1.00 64.62           N  
ANISOU 1738  N   SER L  26     7739   5879  10936   -215  -1497   2718       N  
ATOM   1739  CA  SER L  26      23.386  38.021  21.413  1.00 64.45           C  
ANISOU 1739  CA  SER L  26     7737   5892  10859   -162  -1589   2542       C  
ATOM   1740  C   SER L  26      23.017  36.567  21.679  1.00 61.17           C  
ANISOU 1740  C   SER L  26     7573   5785   9886   -135  -1375   2167       C  
ATOM   1741  O   SER L  26      22.034  36.076  21.140  1.00 60.74           O  
ANISOU 1741  O   SER L  26     7572   5905   9601   -137  -1414   2153       O  
ATOM   1742  CB  SER L  26      22.839  38.424  20.050  1.00 68.26           C  
ANISOU 1742  CB  SER L  26     8139   6501  11294   -221  -1767   3048       C  
ATOM   1743  OG  SER L  26      23.311  39.715  19.693  1.00 72.05           O  
ANISOU 1743  OG  SER L  26     8385   6705  12287   -273  -1959   3506       O  
ATOM   1744  N   LEU L  27      23.799  35.882  22.512  1.00 58.84           N  
ANISOU 1744  N   LEU L  27     7413   5538   9407   -111  -1167   1873       N  
ATOM   1745  CA  LEU L  27      23.518  34.488  22.842  1.00 56.63           C  
ANISOU 1745  CA  LEU L  27     7356   5494   8668    -93   -974   1548       C  
ATOM   1746  C   LEU L  27      22.073  34.296  23.307  1.00 56.48           C  
ANISOU 1746  C   LEU L  27     7303   5423   8732    -51  -1033   1266       C  
ATOM   1747  O   LEU L  27      21.436  33.288  23.013  1.00 55.74           O  
ANISOU 1747  O   LEU L  27     7339   5533   8305    -75   -961   1158       O  
ATOM   1748  CB  LEU L  27      24.466  33.971  23.917  1.00 54.27           C  
ANISOU 1748  CB  LEU L  27     7160   5178   8282    -52   -788   1269       C  
ATOM   1749  CG  LEU L  27      25.045  32.581  23.640  1.00 52.66           C  
ANISOU 1749  CG  LEU L  27     7193   5259   7556    -72   -582   1209       C  
ATOM   1750  CD1 LEU L  27      25.474  31.929  24.923  1.00 50.52           C  
ANISOU 1750  CD1 LEU L  27     7024   4952   7220    -11   -431    870       C  
ATOM   1751  CD2 LEU L  27      24.076  31.701  22.892  1.00 52.21           C  
ANISOU 1751  CD2 LEU L  27     7241   5408   7187   -104   -581   1185       C  
ATOM   1752  N   GLY L  28      21.557  35.274  24.030  1.00 57.16           N  
ANISOU 1752  N   GLY L  28     7187   5236   9295     13  -1171   1128       N  
ATOM   1753  CA  GLY L  28      20.226  35.154  24.569  1.00 56.85           C  
ANISOU 1753  CA  GLY L  28     7074   5170   9358     63  -1210    833       C  
ATOM   1754  C   GLY L  28      19.107  35.163  23.541  1.00 58.75           C  
ANISOU 1754  C   GLY L  28     7265   5488   9570     29  -1363   1012       C  
ATOM   1755  O   GLY L  28      17.948  35.033  23.908  1.00 58.77           O  
ANISOU 1755  O   GLY L  28     7185   5484   9660     62  -1398    776       O  
ATOM   1756  N   SER L  29      19.433  35.358  22.264  1.00 60.28           N  
ANISOU 1756  N   SER L  29     7480   5782   9640    -32  -1462   1434       N  
ATOM   1757  CA  SER L  29      18.431  35.258  21.196  1.00 61.82           C  
ANISOU 1757  CA  SER L  29     7642   6127   9718    -59  -1616   1616       C  
ATOM   1758  C   SER L  29      18.607  33.912  20.482  1.00 60.20           C  
ANISOU 1758  C   SER L  29     7666   6295   8911   -121  -1465   1606       C  
ATOM   1759  O   SER L  29      18.011  33.657  19.450  1.00 61.26           O  
ANISOU 1759  O   SER L  29     7803   6643   8828   -146  -1575   1753       O  
ATOM   1760  CB  SER L  29      18.542  36.427  20.212  1.00 65.16           C  
ANISOU 1760  CB  SER L  29     7899   6457  10402    -73  -1864   2115       C  
ATOM   1761  OG  SER L  29      19.755  36.364  19.475  1.00 66.60           O  
ANISOU 1761  OG  SER L  29     8172   6822  10312   -142  -1784   2473       O  
ATOM   1762  N   LYS L  30      19.443  33.059  21.053  1.00 57.46           N  
ANISOU 1762  N   LYS L  30     7496   6022   8316   -133  -1231   1408       N  
ATOM   1763  CA  LYS L  30      19.689  31.747  20.503  1.00 56.78           C  
ANISOU 1763  CA  LYS L  30     7610   6231   7732   -173  -1093   1330       C  
ATOM   1764  C   LYS L  30      19.453  30.697  21.576  1.00 54.34           C  
ANISOU 1764  C   LYS L  30     7418   5877   7353   -171   -911    929       C  
ATOM   1765  O   LYS L  30      19.673  30.953  22.757  1.00 52.98           O  
ANISOU 1765  O   LYS L  30     7216   5522   7394   -135   -827    766       O  
ATOM   1766  CB  LYS L  30      21.133  31.637  20.036  1.00 56.87           C  
ANISOU 1766  CB  LYS L  30     7716   6393   7497   -189   -982   1535       C  
ATOM   1767  CG  LYS L  30      21.630  32.807  19.220  1.00 59.86           C  
ANISOU 1767  CG  LYS L  30     7951   6786   8007   -208  -1121   1998       C  
ATOM   1768  CD  LYS L  30      22.984  32.479  18.609  1.00 60.67           C  
ANISOU 1768  CD  LYS L  30     8138   7146   7767   -235   -979   2189       C  
ATOM   1769  CE  LYS L  30      23.710  33.728  18.168  1.00 62.91           C  
ANISOU 1769  CE  LYS L  30     8250   7365   8287   -275  -1068   2665       C  
ATOM   1770  NZ  LYS L  30      22.824  34.618  17.336  1.00 66.92           N  
ANISOU 1770  NZ  LYS L  30     8590   7874   8961   -296  -1321   3030       N  
ATOM   1771  N   TYR L  31      19.021  29.512  21.173  1.00 53.83           N  
ANISOU 1771  N   TYR L  31     7470   5988   6996   -210   -861    777       N  
ATOM   1772  CA  TYR L  31      18.795  28.438  22.139  1.00 52.52           C  
ANISOU 1772  CA  TYR L  31     7404   5767   6786   -230   -694    466       C  
ATOM   1773  C   TYR L  31      20.076  27.669  22.395  1.00 51.36           C  
ANISOU 1773  C   TYR L  31     7437   5665   6413   -219   -516    423       C  
ATOM   1774  O   TYR L  31      20.738  27.220  21.460  1.00 52.08           O  
ANISOU 1774  O   TYR L  31     7619   5939   6231   -219   -510    502       O  
ATOM   1775  CB  TYR L  31      17.697  27.492  21.658  1.00 53.28           C  
ANISOU 1775  CB  TYR L  31     7511   5963   6771   -288   -743    308       C  
ATOM   1776  CG  TYR L  31      16.304  27.995  21.957  1.00 54.58           C  
ANISOU 1776  CG  TYR L  31     7486   6034   7217   -300   -857    234       C  
ATOM   1777  CD1 TYR L  31      15.521  28.594  20.977  1.00 56.28           C  
ANISOU 1777  CD1 TYR L  31     7570   6326   7489   -293  -1082    366       C  
ATOM   1778  CD2 TYR L  31      15.782  27.890  23.236  1.00 53.87           C  
ANISOU 1778  CD2 TYR L  31     7329   5814   7325   -308   -741     38       C  
ATOM   1779  CE1 TYR L  31      14.254  29.060  21.274  1.00 57.45           C  
ANISOU 1779  CE1 TYR L  31     7522   6380   7925   -289  -1194    277       C  
ATOM   1780  CE2 TYR L  31      14.522  28.363  23.537  1.00 55.20           C  
ANISOU 1780  CE2 TYR L  31     7292   5929   7754   -307   -830    -58       C  
ATOM   1781  CZ  TYR L  31      13.763  28.936  22.558  1.00 56.93           C  
ANISOU 1781  CZ  TYR L  31     7382   6184   8065   -296  -1059     48       C  
ATOM   1782  OH  TYR L  31      12.514  29.384  22.920  1.00 58.45           O  
ANISOU 1782  OH  TYR L  31     7351   6315   8544   -284  -1146    -77       O  
ATOM   1783  N   VAL L  32      20.431  27.547  23.670  1.00 50.27           N  
ANISOU 1783  N   VAL L  32     7329   5391   6381   -195   -378    289       N  
ATOM   1784  CA  VAL L  32      21.679  26.914  24.066  1.00 48.27           C  
ANISOU 1784  CA  VAL L  32     7226   5152   5962   -168   -226    255       C  
ATOM   1785  C   VAL L  32      21.442  25.526  24.622  1.00 47.84           C  
ANISOU 1785  C   VAL L  32     7295   5083   5798   -201   -104     61       C  
ATOM   1786  O   VAL L  32      20.427  25.280  25.278  1.00 47.49           O  
ANISOU 1786  O   VAL L  32     7193   4979   5873   -243    -84    -50       O  
ATOM   1787  CB  VAL L  32      22.416  27.761  25.094  1.00 47.20           C  
ANISOU 1787  CB  VAL L  32     7031   4892   6011   -105   -179    264       C  
ATOM   1788  CG1 VAL L  32      23.624  27.013  25.683  1.00 45.30           C  
ANISOU 1788  CG1 VAL L  32     6937   4667   5609    -67    -26    200       C  
ATOM   1789  CG2 VAL L  32      22.834  29.098  24.468  1.00 48.01           C  
ANISOU 1789  CG2 VAL L  32     7001   4958   6285    -87   -312    497       C  
ATOM   1790  N   ILE L  33      22.398  24.634  24.331  1.00 47.95           N  
ANISOU 1790  N   ILE L  33     7458   5153   5608   -182    -27     35       N  
ATOM   1791  CA  ILE L  33      22.362  23.202  24.665  1.00 47.93           C  
ANISOU 1791  CA  ILE L  33     7579   5099   5534   -210     59   -117       C  
ATOM   1792  C   ILE L  33      23.629  22.825  25.440  1.00 47.59           C  
ANISOU 1792  C   ILE L  33     7643   5005   5434   -143    184   -119       C  
ATOM   1793  O   ILE L  33      24.710  23.291  25.083  1.00 47.93           O  
ANISOU 1793  O   ILE L  33     7699   5121   5390    -78    192    -42       O  
ATOM   1794  CB  ILE L  33      22.457  22.419  23.394  1.00 49.05           C  
ANISOU 1794  CB  ILE L  33     7783   5359   5496   -216     -7   -191       C  
ATOM   1795  CG1 ILE L  33      21.809  23.191  22.250  1.00 50.88           C  
ANISOU 1795  CG1 ILE L  33     7904   5753   5674   -233   -159   -105       C  
ATOM   1796  CG2 ILE L  33      21.863  21.095  23.569  1.00 50.34           C  
ANISOU 1796  CG2 ILE L  33     8001   5410   5715   -276      5   -366       C  
ATOM   1797  CD1 ILE L  33      20.405  22.784  21.966  1.00 51.59           C  
ANISOU 1797  CD1 ILE L  33     7927   5824   5850   -310   -261   -223       C  
ATOM   1798  N   TRP L  34      23.531  21.967  26.456  1.00 46.72           N  
ANISOU 1798  N   TRP L  34     7595   4787   5371   -159    277   -181       N  
ATOM   1799  CA  TRP L  34      24.712  21.643  27.263  1.00 46.10           C  
ANISOU 1799  CA  TRP L  34     7606   4671   5239    -82    373   -165       C  
ATOM   1800  C   TRP L  34      25.043  20.154  27.364  1.00 47.34           C  
ANISOU 1800  C   TRP L  34     7891   4724   5371    -84    413   -225       C  
ATOM   1801  O   TRP L  34      24.168  19.314  27.646  1.00 48.27           O  
ANISOU 1801  O   TRP L  34     8014   4739   5589   -170    419   -247       O  
ATOM   1802  CB  TRP L  34      24.537  22.137  28.678  1.00 45.28           C  
ANISOU 1802  CB  TRP L  34     7438   4556   5210    -64    443   -138       C  
ATOM   1803  CG  TRP L  34      24.528  23.631  28.866  1.00 45.32           C  
ANISOU 1803  CG  TRP L  34     7303   4612   5306    -21    395   -125       C  
ATOM   1804  CD1 TRP L  34      23.444  24.455  28.804  1.00 45.13           C  
ANISOU 1804  CD1 TRP L  34     7131   4596   5420    -58    329   -146       C  
ATOM   1805  CD2 TRP L  34      25.631  24.449  29.260  1.00 44.10           C  
ANISOU 1805  CD2 TRP L  34     7116   4471   5169     73    394   -111       C  
ATOM   1806  NE1 TRP L  34      23.813  25.734  29.115  1.00 45.27           N  
ANISOU 1806  NE1 TRP L  34     7028   4607   5566     12    276   -150       N  
ATOM   1807  CE2 TRP L  34      25.155  25.755  29.383  1.00 44.15           C  
ANISOU 1807  CE2 TRP L  34     6953   4466   5357     84    314   -129       C  
ATOM   1808  CE3 TRP L  34      26.982  24.200  29.496  1.00 43.92           C  
ANISOU 1808  CE3 TRP L  34     7173   4454   5060    150    438    -97       C  
ATOM   1809  CZ2 TRP L  34      25.969  26.807  29.735  1.00 44.03           C  
ANISOU 1809  CZ2 TRP L  34     6841   4420   5467    160    269   -139       C  
ATOM   1810  CZ3 TRP L  34      27.797  25.261  29.847  1.00 43.55           C  
ANISOU 1810  CZ3 TRP L  34     7031   4408   5107    221    404   -101       C  
ATOM   1811  CH2 TRP L  34      27.285  26.542  29.960  1.00 43.75           C  
ANISOU 1811  CH2 TRP L  34     6884   4399   5339    221    317   -124       C  
ATOM   1812  N   TYR L  35      26.322  19.826  27.201  1.00 46.17           N  
ANISOU 1812  N   TYR L  35     7825   4583   5133     11    436   -244       N  
ATOM   1813  CA  TYR L  35      26.739  18.451  27.369  1.00 46.66           C  
ANISOU 1813  CA  TYR L  35     7994   4507   5228     35    452   -306       C  
ATOM   1814  C   TYR L  35      27.757  18.289  28.492  1.00 46.62           C  
ANISOU 1814  C   TYR L  35     8044   4456   5213    124    524   -226       C  
ATOM   1815  O   TYR L  35      28.584  19.158  28.726  1.00 45.57           O  
ANISOU 1815  O   TYR L  35     7882   4429   5004    201    548   -190       O  
ATOM   1816  CB  TYR L  35      27.303  17.878  26.079  1.00 47.33           C  
ANISOU 1816  CB  TYR L  35     8114   4638   5230     90    392   -468       C  
ATOM   1817  CG  TYR L  35      26.413  18.092  24.890  1.00 48.13           C  
ANISOU 1817  CG  TYR L  35     8151   4858   5279     27    302   -557       C  
ATOM   1818  CD1 TYR L  35      26.532  19.236  24.112  1.00 47.67           C  
ANISOU 1818  CD1 TYR L  35     8017   5028   5068     41    277   -485       C  
ATOM   1819  CD2 TYR L  35      25.429  17.179  24.558  1.00 49.44           C  
ANISOU 1819  CD2 TYR L  35     8313   4905   5568    -53    226   -690       C  
ATOM   1820  CE1 TYR L  35      25.698  19.457  23.044  1.00 48.66           C  
ANISOU 1820  CE1 TYR L  35     8074   5295   5119     -9    177   -532       C  
ATOM   1821  CE2 TYR L  35      24.593  17.403  23.487  1.00 50.76           C  
ANISOU 1821  CE2 TYR L  35     8405   5208   5671   -102    122   -786       C  
ATOM   1822  CZ  TYR L  35      24.738  18.546  22.742  1.00 50.44           C  
ANISOU 1822  CZ  TYR L  35     8301   5429   5433    -72     98   -700       C  
ATOM   1823  OH  TYR L  35      23.949  18.800  21.663  1.00 52.33           O  
ANISOU 1823  OH  TYR L  35     8462   5844   5576   -107    -20   -761       O  
ATOM   1824  N   GLN L  36      27.652  17.173  29.202  1.00 47.51           N  
ANISOU 1824  N   GLN L  36     8220   4404   5425    105    541   -179       N  
ATOM   1825  CA  GLN L  36      28.596  16.790  30.208  1.00 46.86           C  
ANISOU 1825  CA  GLN L  36     8197   4278   5331    197    582    -85       C  
ATOM   1826  C   GLN L  36      29.406  15.665  29.600  1.00 48.69           C  
ANISOU 1826  C   GLN L  36     8508   4354   5638    275    525   -194       C  
ATOM   1827  O   GLN L  36      28.871  14.786  28.890  1.00 49.57           O  
ANISOU 1827  O   GLN L  36     8634   4316   5886    220    459   -305       O  
ATOM   1828  CB  GLN L  36      27.869  16.293  31.450  1.00 48.37           C  
ANISOU 1828  CB  GLN L  36     8381   4410   5587    120    634    100       C  
ATOM   1829  CG  GLN L  36      28.659  15.266  32.231  1.00 49.94           C  
ANISOU 1829  CG  GLN L  36     8662   4477   5836    191    631    231       C  
ATOM   1830  CD  GLN L  36      27.890  14.702  33.384  1.00 51.49           C  
ANISOU 1830  CD  GLN L  36     8834   4648   6081     94    688    482       C  
ATOM   1831  OE1 GLN L  36      27.684  15.393  34.368  1.00 51.25           O  
ANISOU 1831  OE1 GLN L  36     8740   4847   5886    100    767    586       O  
ATOM   1832  NE2 GLN L  36      27.479  13.440  33.285  1.00 53.65           N  
ANISOU 1832  NE2 GLN L  36     9136   4657   6590      6    645    581       N  
ATOM   1833  N   GLN L  37      30.710  15.702  29.832  1.00 48.25           N  
ANISOU 1833  N   GLN L  37     8482   4332   5517    414    533   -204       N  
ATOM   1834  CA  GLN L  37      31.565  14.667  29.314  1.00 50.09           C  
ANISOU 1834  CA  GLN L  37     8766   4428   5839    519    475   -340       C  
ATOM   1835  C   GLN L  37      32.633  14.138  30.281  1.00 51.58           C  
ANISOU 1835  C   GLN L  37     9001   4521   6075    645    468   -239       C  
ATOM   1836  O   GLN L  37      33.566  14.860  30.641  1.00 51.90           O  
ANISOU 1836  O   GLN L  37     9016   4719   5987    741    502   -218       O  
ATOM   1837  CB  GLN L  37      32.233  15.113  28.028  1.00 49.55           C  
ANISOU 1837  CB  GLN L  37     8649   4540   5635    593    470   -548       C  
ATOM   1838  CG  GLN L  37      33.150  14.006  27.489  1.00 52.40           C  
ANISOU 1838  CG  GLN L  37     9031   4790   6086    729    412   -754       C  
ATOM   1839  CD  GLN L  37      34.026  14.495  26.365  1.00 53.35           C  
ANISOU 1839  CD  GLN L  37     9075   5181   6014    824    442   -937       C  
ATOM   1840  OE1 GLN L  37      34.838  15.406  26.550  1.00 52.45           O  
ANISOU 1840  OE1 GLN L  37     8911   5248   5770    870    511   -845       O  
ATOM   1841  NE2 GLN L  37      33.868  13.906  25.185  1.00 54.77           N  
ANISOU 1841  NE2 GLN L  37     9222   5415   6173    854    389  -1201       N  
ATOM   1842  N   LYS L  38      32.529  12.861  30.640  1.00 52.91           N  
ANISOU 1842  N   LYS L  38     9222   4416   6463    647    403   -178       N  
ATOM   1843  CA  LYS L  38      33.503  12.243  31.541  1.00 54.96           C  
ANISOU 1843  CA  LYS L  38     9523   4562   6797    774    365    -47       C  
ATOM   1844  C   LYS L  38      34.634  11.519  30.782  1.00 56.17           C  
ANISOU 1844  C   LYS L  38     9676   4592   7073    942    282   -291       C  
ATOM   1845  O   LYS L  38      34.425  10.983  29.695  1.00 57.53           O  
ANISOU 1845  O   LYS L  38     9829   4666   7363    942    227   -545       O  
ATOM   1846  CB  LYS L  38      32.799  11.310  32.543  1.00 56.46           C  
ANISOU 1846  CB  LYS L  38     9750   4527   7177    682    335    247       C  
ATOM   1847  CG  LYS L  38      31.671  12.017  33.271  1.00 55.32           C  
ANISOU 1847  CG  LYS L  38     9569   4567   6881    526    437    455       C  
ATOM   1848  CD  LYS L  38      30.892  11.112  34.197  1.00 58.05           C  
ANISOU 1848  CD  LYS L  38     9917   4748   7392    407    436    786       C  
ATOM   1849  CE  LYS L  38      29.974  11.935  35.141  1.00 57.28           C  
ANISOU 1849  CE  LYS L  38     9752   4950   7060    294    567    989       C  
ATOM   1850  NZ  LYS L  38      29.191  11.071  36.087  1.00 60.30           N  
ANISOU 1850  NZ  LYS L  38    10105   5244   7562    160    596   1370       N  
ATOM   1851  N   PRO L  39      35.842  11.519  31.353  1.00 56.10           N  
ANISOU 1851  N   PRO L  39     9667   4618   7031   1100    265   -248       N  
ATOM   1852  CA  PRO L  39      37.007  10.875  30.763  1.00 57.21           C  
ANISOU 1852  CA  PRO L  39     9779   4668   7292   1284    192   -483       C  
ATOM   1853  C   PRO L  39      36.667   9.525  30.152  1.00 60.55           C  
ANISOU 1853  C   PRO L  39    10211   4748   8047   1296     70   -651       C  
ATOM   1854  O   PRO L  39      36.056   8.685  30.822  1.00 63.30           O  
ANISOU 1854  O   PRO L  39    10607   4796   8648   1223     -6   -433       O  
ATOM   1855  CB  PRO L  39      37.917  10.629  31.965  1.00 58.76           C  
ANISOU 1855  CB  PRO L  39     9994   4808   7525   1411    142   -272       C  
ATOM   1856  CG  PRO L  39      37.295  11.397  33.154  1.00 57.62           C  
ANISOU 1856  CG  PRO L  39     9877   4832   7183   1298    213     47       C  
ATOM   1857  CD  PRO L  39      36.158  12.204  32.619  1.00 55.47           C  
ANISOU 1857  CD  PRO L  39     9590   4706   6781   1122    310     -2       C  
ATOM   1858  N   GLY L  40      37.077   9.293  28.907  1.00 61.08           N  
ANISOU 1858  N   GLY L  40    10212   4866   8130   1391     44  -1036       N  
ATOM   1859  CA  GLY L  40      36.855   8.007  28.281  1.00 63.94           C  
ANISOU 1859  CA  GLY L  40    10552   4902   8841   1438   -101  -1292       C  
ATOM   1860  C   GLY L  40      35.467   7.765  27.712  1.00 65.14           C  
ANISOU 1860  C   GLY L  40    10709   4952   9092   1260   -134  -1369       C  
ATOM   1861  O   GLY L  40      35.171   6.666  27.248  1.00 67.50           O  
ANISOU 1861  O   GLY L  40    10974   4934   9740   1282   -280  -1595       O  
ATOM   1862  N   GLN L  41      34.597   8.775  27.720  1.00 62.59           N  
ANISOU 1862  N   GLN L  41    10406   4876   8501   1090    -18  -1213       N  
ATOM   1863  CA  GLN L  41      33.289   8.526  27.129  1.00 63.25           C  
ANISOU 1863  CA  GLN L  41    10471   4871   8691    931    -65  -1312       C  
ATOM   1864  C   GLN L  41      32.635   9.633  26.301  1.00 59.85           C  
ANISOU 1864  C   GLN L  41    10005   4818   7918    834     24  -1399       C  
ATOM   1865  O   GLN L  41      33.138  10.723  26.201  1.00 58.11           O  
ANISOU 1865  O   GLN L  41     9772   4931   7377    868    136  -1339       O  
ATOM   1866  CB  GLN L  41      32.345   7.892  28.163  1.00 64.93           C  
ANISOU 1866  CB  GLN L  41    10726   4736   9210    766   -109   -972       C  
ATOM   1867  CG  GLN L  41      32.356   8.549  29.528  1.00 63.24           C  
ANISOU 1867  CG  GLN L  41    10567   4635   8826    706      9   -522       C  
ATOM   1868  CD  GLN L  41      31.314   7.936  30.444  1.00 65.22           C  
ANISOU 1868  CD  GLN L  41    10824   4627   9328    525     -9   -172       C  
ATOM   1869  OE1 GLN L  41      31.407   6.762  30.799  1.00 68.80           O  
ANISOU 1869  OE1 GLN L  41    11279   4698  10166    533   -129    -62       O  
ATOM   1870  NE2 GLN L  41      30.310   8.726  30.821  1.00 63.01           N  
ANISOU 1870  NE2 GLN L  41    10528   4556   8858    359    108     15       N  
ATOM   1871  N   ALA L  42      31.524   9.303  25.671  1.00 60.97           N  
ANISOU 1871  N   ALA L  42    10112   4882   8171    717    -50  -1543       N  
ATOM   1872  CA  ALA L  42      30.813  10.224  24.811  1.00 60.17           C  
ANISOU 1872  CA  ALA L  42     9965   5114   7782    633     -6  -1627       C  
ATOM   1873  C   ALA L  42      30.191  11.365  25.610  1.00 57.73           C  
ANISOU 1873  C   ALA L  42     9684   4944   7309    490    115  -1258       C  
ATOM   1874  O   ALA L  42      29.842  11.204  26.783  1.00 58.06           O  
ANISOU 1874  O   ALA L  42     9766   4792   7501    406    147   -971       O  
ATOM   1875  CB  ALA L  42      29.721   9.476  24.081  1.00 63.26           C  
ANISOU 1875  CB  ALA L  42    10301   5348   8387    543   -145  -1874       C  
ATOM   1876  N   PRO L  43      30.042  12.527  24.982  1.00 55.88           N  
ANISOU 1876  N   PRO L  43     9406   5058   6767    468    177  -1259       N  
ATOM   1877  CA  PRO L  43      29.330  13.545  25.735  1.00 53.95           C  
ANISOU 1877  CA  PRO L  43     9161   4891   6445    342    259   -965       C  
ATOM   1878  C   PRO L  43      27.890  13.099  25.996  1.00 54.75           C  
ANISOU 1878  C   PRO L  43     9242   4800   6758    173    210   -909       C  
ATOM   1879  O   PRO L  43      27.395  12.192  25.289  1.00 57.00           O  
ANISOU 1879  O   PRO L  43     9501   4939   7218    145     96  -1134       O  
ATOM   1880  CB  PRO L  43      29.373  14.758  24.797  1.00 53.08           C  
ANISOU 1880  CB  PRO L  43     8985   5141   6044    349    289   -997       C  
ATOM   1881  CG  PRO L  43      30.576  14.548  23.954  1.00 53.67           C  
ANISOU 1881  CG  PRO L  43     9039   5382   5971    504    289  -1199       C  
ATOM   1882  CD  PRO L  43      30.646  13.052  23.744  1.00 56.10           C  
ANISOU 1882  CD  PRO L  43     9371   5439   6506    567    187  -1467       C  
ATOM   1883  N   VAL L  44      27.250  13.708  27.002  1.00 53.03           N  
ANISOU 1883  N   VAL L  44     9014   4594   6540     69    292   -643       N  
ATOM   1884  CA  VAL L  44      25.897  13.353  27.392  1.00 53.45           C  
ANISOU 1884  CA  VAL L  44     9018   4503   6788   -101    278   -547       C  
ATOM   1885  C   VAL L  44      25.048  14.614  27.467  1.00 51.28           C  
ANISOU 1885  C   VAL L  44     8664   4457   6365   -181    333   -456       C  
ATOM   1886  O   VAL L  44      25.479  15.592  28.041  1.00 49.22           O  
ANISOU 1886  O   VAL L  44     8400   4360   5942   -128    415   -333       O  
ATOM   1887  CB  VAL L  44      25.909  12.651  28.746  1.00 54.06           C  
ANISOU 1887  CB  VAL L  44     9126   4372   7041   -146    333   -284       C  
ATOM   1888  CG1 VAL L  44      24.514  12.556  29.308  1.00 54.82           C  
ANISOU 1888  CG1 VAL L  44     9134   4415   7280   -337    371   -115       C  
ATOM   1889  CG2 VAL L  44      26.520  11.315  28.608  1.00 55.70           C  
ANISOU 1889  CG2 VAL L  44     9386   4276   7501    -86    236   -366       C  
ATOM   1890  N   LEU L  45      23.860  14.598  26.866  1.00 52.40           N  
ANISOU 1890  N   LEU L  45     8723   4595   6590   -296    267   -544       N  
ATOM   1891  CA  LEU L  45      22.927  15.718  26.920  1.00 51.23           C  
ANISOU 1891  CA  LEU L  45     8475   4627   6363   -369    293   -472       C  
ATOM   1892  C   LEU L  45      22.522  15.975  28.364  1.00 51.33           C  
ANISOU 1892  C   LEU L  45     8444   4638   6420   -431    420   -241       C  
ATOM   1893  O   LEU L  45      22.116  15.051  29.044  1.00 54.27           O  
ANISOU 1893  O   LEU L  45     8808   4845   6968   -523    455   -129       O  
ATOM   1894  CB  LEU L  45      21.679  15.343  26.135  1.00 52.97           C  
ANISOU 1894  CB  LEU L  45     8602   4797   6727   -488    182   -612       C  
ATOM   1895  CG  LEU L  45      20.818  16.341  25.371  1.00 52.44           C  
ANISOU 1895  CG  LEU L  45     8427   4932   6567   -519    111   -668       C  
ATOM   1896  CD1 LEU L  45      19.377  16.011  25.595  1.00 53.48           C  
ANISOU 1896  CD1 LEU L  45     8431   4965   6924   -679     83   -667       C  
ATOM   1897  CD2 LEU L  45      21.096  17.759  25.789  1.00 51.30           C  
ANISOU 1897  CD2 LEU L  45     8255   4974   6264   -457    183   -518       C  
ATOM   1898  N   VAL L  46      22.643  17.210  28.847  1.00 49.55           N  
ANISOU 1898  N   VAL L  46     8172   4608   6047   -378    484   -170       N  
ATOM   1899  CA  VAL L  46      22.129  17.536  30.174  1.00 49.60           C  
ANISOU 1899  CA  VAL L  46     8097   4694   6056   -422    600    -17       C  
ATOM   1900  C   VAL L  46      21.110  18.648  30.147  1.00 49.59           C  
ANISOU 1900  C   VAL L  46     7938   4843   6060   -461    596    -62       C  
ATOM   1901  O   VAL L  46      20.244  18.675  31.001  1.00 51.06           O  
ANISOU 1901  O   VAL L  46     8007   5099   6293   -536    681      9       O  
ATOM   1902  CB  VAL L  46      23.226  17.861  31.213  1.00 48.82           C  
ANISOU 1902  CB  VAL L  46     8053   4688   5809   -300    684     80       C  
ATOM   1903  CG1 VAL L  46      24.230  16.730  31.289  1.00 49.99           C  
ANISOU 1903  CG1 VAL L  46     8342   4671   5981   -248    673    136       C  
ATOM   1904  CG2 VAL L  46      23.915  19.132  30.873  1.00 46.99           C  
ANISOU 1904  CG2 VAL L  46     7804   4587   5463   -184    649    -12       C  
ATOM   1905  N   ILE L  47      21.190  19.561  29.176  1.00 48.73           N  
ANISOU 1905  N   ILE L  47     7804   4800   5912   -408    497   -164       N  
ATOM   1906  CA  ILE L  47      20.184  20.627  29.066  1.00 48.68           C  
ANISOU 1906  CA  ILE L  47     7632   4896   5970   -434    455   -204       C  
ATOM   1907  C   ILE L  47      19.966  21.050  27.609  1.00 49.58           C  
ANISOU 1907  C   ILE L  47     7729   5025   6084   -432    299   -273       C  
ATOM   1908  O   ILE L  47      20.934  21.241  26.869  1.00 49.50           O  
ANISOU 1908  O   ILE L  47     7806   5046   5956   -355    250   -269       O  
ATOM   1909  CB  ILE L  47      20.511  21.792  29.998  1.00 47.37           C  
ANISOU 1909  CB  ILE L  47     7382   4849   5766   -337    509   -196       C  
ATOM   1910  CG1 ILE L  47      20.101  21.402  31.406  1.00 48.35           C  
ANISOU 1910  CG1 ILE L  47     7443   5058   5871   -369    655   -147       C  
ATOM   1911  CG2 ILE L  47      19.791  23.036  29.594  1.00 46.91           C  
ANISOU 1911  CG2 ILE L  47     7160   4843   5820   -320    411   -261       C  
ATOM   1912  CD1 ILE L  47      20.464  22.395  32.399  1.00 49.11           C  
ANISOU 1912  CD1 ILE L  47     7448   5308   5902   -254    703   -201       C  
ATOM   1913  N   TYR L  48      18.707  21.167  27.177  1.00 50.71           N  
ANISOU 1913  N   TYR L  48     7744   5181   6342   -515    222   -325       N  
ATOM   1914  CA  TYR L  48      18.462  21.212  25.746  1.00 51.72           C  
ANISOU 1914  CA  TYR L  48     7869   5348   6432   -522     60   -387       C  
ATOM   1915  C   TYR L  48      17.732  22.422  25.083  1.00 54.10           C  
ANISOU 1915  C   TYR L  48     8022   5750   6785   -504    -81   -364       C  
ATOM   1916  O   TYR L  48      18.161  22.882  24.017  1.00 57.33           O  
ANISOU 1916  O   TYR L  48     8454   6258   7071   -450   -194   -316       O  
ATOM   1917  CB  TYR L  48      18.001  19.868  25.176  1.00 52.38           C  
ANISOU 1917  CB  TYR L  48     7991   5343   6566   -613      7   -509       C  
ATOM   1918  CG  TYR L  48      16.585  19.442  25.532  1.00 54.24           C  
ANISOU 1918  CG  TYR L  48     8081   5508   7019   -751      3   -551       C  
ATOM   1919  CD1 TYR L  48      15.476  20.042  24.947  1.00 54.35           C  
ANISOU 1919  CD1 TYR L  48     7935   5603   7112   -787   -123   -607       C  
ATOM   1920  CD2 TYR L  48      16.365  18.388  26.409  1.00 54.95           C  
ANISOU 1920  CD2 TYR L  48     8177   5449   7253   -853    116   -513       C  
ATOM   1921  CE1 TYR L  48      14.206  19.617  25.260  1.00 55.92           C  
ANISOU 1921  CE1 TYR L  48     7976   5745   7525   -918   -122   -656       C  
ATOM   1922  CE2 TYR L  48      15.112  17.972  26.715  1.00 56.59           C  
ANISOU 1922  CE2 TYR L  48     8227   5602   7673   -998    126   -522       C  
ATOM   1923  CZ  TYR L  48      14.051  18.579  26.161  1.00 57.18           C  
ANISOU 1923  CZ  TYR L  48     8137   5766   7821  -1031     16   -609       C  
ATOM   1924  OH  TYR L  48      12.837  18.094  26.525  1.00 60.11           O  
ANISOU 1924  OH  TYR L  48     8331   6084   8425  -1185     41   -618       O  
ATOM   1925  N   ASP L  49      16.629  22.939  25.582  1.00 53.19           N  
ANISOU 1925  N   ASP L  49     7734   5631   6844   -543    -92   -384       N  
ATOM   1926  CA  ASP L  49      16.300  24.254  25.020  1.00 52.78           C  
ANISOU 1926  CA  ASP L  49     7553   5638   6864   -483   -240   -327       C  
ATOM   1927  C   ASP L  49      16.891  25.027  26.157  1.00 52.60           C  
ANISOU 1927  C   ASP L  49     7500   5581   6903   -404   -132   -299       C  
ATOM   1928  O   ASP L  49      17.477  24.373  26.987  1.00 55.32           O  
ANISOU 1928  O   ASP L  49     7946   5910   7165   -408     21   -317       O  
ATOM   1929  CB  ASP L  49      14.822  24.384  24.748  1.00 54.43           C  
ANISOU 1929  CB  ASP L  49     7576   5862   7243   -546   -351   -402       C  
ATOM   1930  CG  ASP L  49      14.419  23.604  23.482  1.00 55.51           C  
ANISOU 1930  CG  ASP L  49     7750   6056   7284   -606   -493   -460       C  
ATOM   1931  OD1 ASP L  49      15.340  23.240  22.727  1.00 55.19           O  
ANISOU 1931  OD1 ASP L  49     7862   6079   7029   -569   -519   -433       O  
ATOM   1932  OD2 ASP L  49      13.216  23.367  23.227  1.00 56.24           O  
ANISOU 1932  OD2 ASP L  49     7703   6155   7511   -679   -584   -557       O  
ATOM   1933  N   ASP L  50      16.901  26.340  26.240  1.00 51.14           N  
ANISOU 1933  N   ASP L  50     7186   5378   6865   -324   -218   -260       N  
ATOM   1934  CA  ASP L  50      17.969  26.823  27.103  1.00 49.09           C  
ANISOU 1934  CA  ASP L  50     6964   5089   6601   -239   -126   -252       C  
ATOM   1935  C   ASP L  50      17.995  26.117  28.474  1.00 48.37           C  
ANISOU 1935  C   ASP L  50     6898   5039   6441   -249     70   -364       C  
ATOM   1936  O   ASP L  50      19.002  26.142  29.161  1.00 45.84           O  
ANISOU 1936  O   ASP L  50     6654   4727   6036   -185    157   -362       O  
ATOM   1937  CB  ASP L  50      18.004  28.337  27.335  1.00 51.22           C  
ANISOU 1937  CB  ASP L  50     7055   5284   7123   -143   -240   -252       C  
ATOM   1938  CG  ASP L  50      17.314  29.135  26.298  1.00 53.00           C  
ANISOU 1938  CG  ASP L  50     7151   5464   7523   -145   -450   -146       C  
ATOM   1939  OD1 ASP L  50      16.421  29.927  26.645  1.00 55.26           O  
ANISOU 1939  OD1 ASP L  50     7226   5692   8079   -103   -540   -246       O  
ATOM   1940  OD2 ASP L  50      17.726  29.066  25.155  1.00 53.98           O  
ANISOU 1940  OD2 ASP L  50     7363   5625   7521   -171   -536     43       O  
ATOM   1941  N   SER L  51      16.891  25.482  28.870  1.00 49.50           N  
ANISOU 1941  N   SER L  51     6961   5230   6615   -333    136   -436       N  
ATOM   1942  CA  SER L  51      16.759  25.035  30.239  1.00 49.82           C  
ANISOU 1942  CA  SER L  51     6963   5369   6598   -343    321   -494       C  
ATOM   1943  C   SER L  51      15.906  23.782  30.489  1.00 51.82           C  
ANISOU 1943  C   SER L  51     7208   5652   6829   -489    430   -461       C  
ATOM   1944  O   SER L  51      15.330  23.645  31.568  1.00 54.03           O  
ANISOU 1944  O   SER L  51     7356   6071   7103   -516    570   -490       O  
ATOM   1945  CB  SER L  51      16.168  26.172  31.046  1.00 50.37           C  
ANISOU 1945  CB  SER L  51     6789   5533   6816   -254    315   -652       C  
ATOM   1946  OG  SER L  51      14.903  26.503  30.532  1.00 50.36           O  
ANISOU 1946  OG  SER L  51     6608   5521   7005   -298    215   -715       O  
ATOM   1947  N   ASN L  52      15.820  22.862  29.532  1.00 51.73           N  
ANISOU 1947  N   ASN L  52     7313   5527   6814   -586    367   -406       N  
ATOM   1948  CA  ASN L  52      15.022  21.640  29.731  1.00 53.12           C  
ANISOU 1948  CA  ASN L  52     7461   5670   7054   -742    444   -372       C  
ATOM   1949  C   ASN L  52      15.944  20.521  30.116  1.00 54.12           C  
ANISOU 1949  C   ASN L  52     7778   5709   7074   -768    543   -255       C  
ATOM   1950  O   ASN L  52      17.030  20.397  29.545  1.00 53.06           O  
ANISOU 1950  O   ASN L  52     7823   5496   6840   -693    482   -250       O  
ATOM   1951  CB  ASN L  52      14.342  21.170  28.448  1.00 54.57           C  
ANISOU 1951  CB  ASN L  52     7635   5750   7349   -832    282   -433       C  
ATOM   1952  CG  ASN L  52      13.123  21.995  28.068  1.00 56.29           C  
ANISOU 1952  CG  ASN L  52     7628   6038   7722   -842    170   -528       C  
ATOM   1953  OD1 ASN L  52      12.216  21.485  27.395  1.00 57.81           O  
ANISOU 1953  OD1 ASN L  52     7738   6187   8039   -946     73   -590       O  
ATOM   1954  ND2 ASN L  52      13.089  23.276  28.487  1.00 56.32           N  
ANISOU 1954  ND2 ASN L  52     7511   6135   7753   -726    161   -565       N  
ATOM   1955  N   ARG L  53      15.514  19.673  31.054  1.00 55.96           N  
ANISOU 1955  N   ARG L  53     7958   5962   7343   -877    690   -141       N  
ATOM   1956  CA  ARG L  53      16.333  18.534  31.452  1.00 55.24           C  
ANISOU 1956  CA  ARG L  53     8033   5751   7206   -906    761     13       C  
ATOM   1957  C   ARG L  53      15.804  17.295  30.794  1.00 56.95           C  
ANISOU 1957  C   ARG L  53     8263   5736   7640  -1062    691     30       C  
ATOM   1958  O   ARG L  53      14.631  16.959  30.948  1.00 59.38           O  
ANISOU 1958  O   ARG L  53     8397   6042   8123  -1213    722     59       O  
ATOM   1959  CB  ARG L  53      16.300  18.318  32.946  1.00 56.51           C  
ANISOU 1959  CB  ARG L  53     8123   6083   7267   -929    957    194       C  
ATOM   1960  CG  ARG L  53      17.319  19.068  33.688  1.00 55.44           C  
ANISOU 1960  CG  ARG L  53     8048   6118   6899   -757   1012    185       C  
ATOM   1961  CD  ARG L  53      17.146  18.802  35.174  1.00 57.80           C  
ANISOU 1961  CD  ARG L  53     8245   6668   7049   -780   1203    362       C  
ATOM   1962  NE  ARG L  53      15.980  19.501  35.725  1.00 59.13           N  
ANISOU 1962  NE  ARG L  53     8147   7108   7212   -808   1294    270       N  
ATOM   1963  CZ  ARG L  53      14.852  18.877  36.067  1.00 62.53           C  
ANISOU 1963  CZ  ARG L  53     8407   7613   7739   -981   1405    406       C  
ATOM   1964  NH1 ARG L  53      14.764  17.545  35.940  1.00 63.62           N  
ANISOU 1964  NH1 ARG L  53     8619   7534   8019  -1150   1423    658       N  
ATOM   1965  NH2 ARG L  53      13.821  19.563  36.571  1.00 63.72           N  
ANISOU 1965  NH2 ARG L  53     8289   8049   7875   -987   1496    289       N  
ATOM   1966  N   PRO L  54      16.663  16.599  30.047  1.00 56.20           N  
ANISOU 1966  N   PRO L  54     8349   5444   7560  -1024    589    -18       N  
ATOM   1967  CA  PRO L  54      16.168  15.321  29.575  1.00 59.02           C  
ANISOU 1967  CA  PRO L  54     8693   5549   8182  -1169    513    -33       C  
ATOM   1968  C   PRO L  54      15.768  14.455  30.777  1.00 61.94           C  
ANISOU 1968  C   PRO L  54     8984   5850   8702  -1316    663    245       C  
ATOM   1969  O   PRO L  54      16.415  14.520  31.833  1.00 61.13           O  
ANISOU 1969  O   PRO L  54     8934   5856   8434  -1258    801    447       O  
ATOM   1970  CB  PRO L  54      17.367  14.716  28.841  1.00 57.88           C  
ANISOU 1970  CB  PRO L  54     8748   5235   8007  -1062    405   -140       C  
ATOM   1971  CG  PRO L  54      18.533  15.506  29.272  1.00 55.78           C  
ANISOU 1971  CG  PRO L  54     8600   5130   7464   -892    480    -82       C  
ATOM   1972  CD  PRO L  54      18.061  16.850  29.672  1.00 54.19           C  
ANISOU 1972  CD  PRO L  54     8282   5183   7124   -858    544    -70       C  
ATOM   1973  N   SER L  55      14.686  13.689  30.633  1.00 64.69           N  
ANISOU 1973  N   SER L  55     9181   6044   9353  -1510    634    272       N  
ATOM   1974  CA  SER L  55      14.260  12.848  31.727  1.00 67.66           C  
ANISOU 1974  CA  SER L  55     9452   6359   9896  -1679    780    599       C  
ATOM   1975  C   SER L  55      15.435  11.928  32.141  1.00 68.18           C  
ANISOU 1975  C   SER L  55     9704   6210   9992  -1630    782    793       C  
ATOM   1976  O   SER L  55      15.998  11.193  31.316  1.00 68.56           O  
ANISOU 1976  O   SER L  55     9874   5950  10224  -1594    614    640       O  
ATOM   1977  CB  SER L  55      13.034  12.042  31.322  1.00 70.02           C  
ANISOU 1977  CB  SER L  55     9559   6445  10602  -1907    709    585       C  
ATOM   1978  OG  SER L  55      13.201  10.696  31.743  1.00 73.84           O  
ANISOU 1978  OG  SER L  55    10051   6609  11395  -2047    713    843       O  
ATOM   1979  N   GLY L  56      15.841  11.992  33.402  1.00 67.22           N  
ANISOU 1979  N   GLY L  56     9592   6275   9675  -1606    958   1102       N  
ATOM   1980  CA  GLY L  56      16.921  11.132  33.831  1.00 67.63           C  
ANISOU 1980  CA  GLY L  56     9803   6127   9766  -1553    942   1314       C  
ATOM   1981  C   GLY L  56      18.237  11.828  34.094  1.00 65.49           C  
ANISOU 1981  C   GLY L  56     9712   6040   9133  -1312    960   1254       C  
ATOM   1982  O   GLY L  56      19.193  11.168  34.471  1.00 65.78           O  
ANISOU 1982  O   GLY L  56     9876   5931   9188  -1245    937   1420       O  
ATOM   1983  N   ILE L  57      18.296  13.144  33.860  1.00 62.44           N  
ANISOU 1983  N   ILE L  57     9321   5939   8465  -1184    979   1015       N  
ATOM   1984  CA  ILE L  57      19.346  14.006  34.372  1.00 59.57           C  
ANISOU 1984  CA  ILE L  57     9055   5817   7763   -983   1028    985       C  
ATOM   1985  C   ILE L  57      18.777  14.634  35.631  1.00 60.84           C  
ANISOU 1985  C   ILE L  57     9052   6366   7700  -1002   1212   1141       C  
ATOM   1986  O   ILE L  57      17.656  15.164  35.603  1.00 61.71           O  
ANISOU 1986  O   ILE L  57     8980   6631   7837  -1086   1264   1056       O  
ATOM   1987  CB  ILE L  57      19.640  15.119  33.345  1.00 57.24           C  
ANISOU 1987  CB  ILE L  57     8805   5585   7359   -851    926    642       C  
ATOM   1988  CG1 ILE L  57      20.350  14.547  32.127  1.00 56.10           C  
ANISOU 1988  CG1 ILE L  57     8810   5164   7340   -799    764    471       C  
ATOM   1989  CG2 ILE L  57      20.448  16.271  33.934  1.00 54.75           C  
ANISOU 1989  CG2 ILE L  57     8514   5541   6749   -673    980    588       C  
ATOM   1990  CD1 ILE L  57      21.370  13.551  32.463  1.00 57.28           C  
ANISOU 1990  CD1 ILE L  57     9094   5119   7550   -745    746    606       C  
ATOM   1991  N   PRO L  58      19.542  14.606  36.737  1.00 61.76           N  
ANISOU 1991  N   PRO L  58     9211   6675   7578   -908   1302   1340       N  
ATOM   1992  CA  PRO L  58      19.031  15.016  38.083  1.00 63.51           C  
ANISOU 1992  CA  PRO L  58     9255   7339   7536   -919   1489   1510       C  
ATOM   1993  C   PRO L  58      18.622  16.473  38.167  1.00 62.27           C  
ANISOU 1993  C   PRO L  58     8959   7505   7198   -814   1525   1194       C  
ATOM   1994  O   PRO L  58      19.270  17.292  37.513  1.00 59.45           O  
ANISOU 1994  O   PRO L  58     8693   7073   6822   -670   1407    915       O  
ATOM   1995  CB  PRO L  58      20.209  14.758  39.023  1.00 64.10           C  
ANISOU 1995  CB  PRO L  58     9444   7545   7367   -785   1515   1714       C  
ATOM   1996  CG  PRO L  58      21.299  14.112  38.198  1.00 62.73           C  
ANISOU 1996  CG  PRO L  58     9500   6952   7384   -719   1347   1677       C  
ATOM   1997  CD  PRO L  58      20.914  14.065  36.761  1.00 61.35           C  
ANISOU 1997  CD  PRO L  58     9361   6449   7500   -784   1221   1416       C  
ATOM   1998  N   GLU L  59      17.568  16.776  38.949  1.00 64.39           N  
ANISOU 1998  N   GLU L  59     8986   8120   7361   -887   1682   1243       N  
ATOM   1999  CA  GLU L  59      17.032  18.151  39.110  1.00 63.57           C  
ANISOU 1999  CA  GLU L  59     8695   8322   7138   -780   1709    910       C  
ATOM   2000  C   GLU L  59      18.106  19.177  39.470  1.00 61.43           C  
ANISOU 2000  C   GLU L  59     8486   8217   6638   -536   1651    675       C  
ATOM   2001  O   GLU L  59      17.931  20.384  39.245  1.00 60.67           O  
ANISOU 2001  O   GLU L  59     8284   8201   6566   -422   1587    341       O  
ATOM   2002  CB  GLU L  59      15.925  18.179  40.180  1.00 67.56           C  
ANISOU 2002  CB  GLU L  59     8910   9268   7490   -865   1921   1022       C  
ATOM   2003  CG  GLU L  59      14.666  17.351  39.844  1.00 70.56           C  
ANISOU 2003  CG  GLU L  59     9149   9516   8144  -1124   1987   1220       C  
ATOM   2004  CD  GLU L  59      13.514  17.564  40.864  1.00 75.18           C  
ANISOU 2004  CD  GLU L  59     9393  10607   8565  -1198   2217   1287       C  
ATOM   2005  OE1 GLU L  59      13.543  16.941  41.954  1.00 78.33           O  
ANISOU 2005  OE1 GLU L  59     9715  11318   8728  -1260   2396   1645       O  
ATOM   2006  OE2 GLU L  59      12.567  18.349  40.572  1.00 75.47           O  
ANISOU 2006  OE2 GLU L  59     9219  10752   8704  -1192   2217    995       O  
ATOM   2007  N   ARG L  60      19.173  18.663  40.080  1.00 61.53           N  
ANISOU 2007  N   ARG L  60     8643   8271   6463   -462   1663    865       N  
ATOM   2008  CA  ARG L  60      20.401  19.368  40.428  1.00 60.31           C  
ANISOU 2008  CA  ARG L  60     8575   8223   6118   -245   1588    692       C  
ATOM   2009  C   ARG L  60      20.944  20.261  39.328  1.00 57.18           C  
ANISOU 2009  C   ARG L  60     8266   7549   5911   -148   1413    383       C  
ATOM   2010  O   ARG L  60      21.603  21.263  39.619  1.00 57.39           O  
ANISOU 2010  O   ARG L  60     8255   7704   5845     23   1352    143       O  
ATOM   2011  CB  ARG L  60      21.471  18.330  40.690  1.00 60.96           C  
ANISOU 2011  CB  ARG L  60     8861   8175   6127   -229   1565    989       C  
ATOM   2012  CG  ARG L  60      22.131  18.402  42.024  1.00 63.18           C  
ANISOU 2012  CG  ARG L  60     9104   8861   6041    -91   1629   1086       C  
ATOM   2013  CD  ARG L  60      23.416  17.609  41.954  1.00 62.44           C  
ANISOU 2013  CD  ARG L  60     9237   8531   5958    -29   1531   1285       C  
ATOM   2014  NE  ARG L  60      23.199  16.193  41.680  1.00 64.20           N  
ANISOU 2014  NE  ARG L  60     9559   8445   6389   -201   1542   1674       N  
ATOM   2015  CZ  ARG L  60      24.146  15.401  41.202  1.00 63.65           C  
ANISOU 2015  CZ  ARG L  60     9685   8010   6487   -173   1423   1791       C  
ATOM   2016  NH1 ARG L  60      25.330  15.916  40.931  1.00 61.70           N  
ANISOU 2016  NH1 ARG L  60     9549   7703   6192      8   1308   1563       N  
ATOM   2017  NH2 ARG L  60      23.915  14.119  40.979  1.00 65.12           N  
ANISOU 2017  NH2 ARG L  60     9934   7882   6926   -322   1409   2113       N  
ATOM   2018  N   PHE L  61      20.699  19.856  38.082  1.00 54.90           N  
ANISOU 2018  N   PHE L  61     8079   6893   5888   -261   1327    403       N  
ATOM   2019  CA  PHE L  61      21.114  20.571  36.890  1.00 52.40           C  
ANISOU 2019  CA  PHE L  61     7837   6335   5738   -202   1170    189       C  
ATOM   2020  C   PHE L  61      20.035  21.452  36.319  1.00 52.18           C  
ANISOU 2020  C   PHE L  61     7640   6311   5873   -239   1124     -6       C  
ATOM   2021  O   PHE L  61      18.924  21.016  36.114  1.00 52.88           O  
ANISOU 2021  O   PHE L  61     7640   6383   6070   -379   1167     53       O  
ATOM   2022  CB  PHE L  61      21.506  19.593  35.798  1.00 51.63           C  
ANISOU 2022  CB  PHE L  61     7933   5891   5792   -281   1088    300       C  
ATOM   2023  CG  PHE L  61      22.761  18.834  36.087  1.00 51.70           C  
ANISOU 2023  CG  PHE L  61     8118   5815   5711   -210   1080    441       C  
ATOM   2024  CD1 PHE L  61      22.721  17.645  36.772  1.00 53.84           C  
ANISOU 2024  CD1 PHE L  61     8431   6067   5960   -284   1155    715       C  
ATOM   2025  CD2 PHE L  61      23.988  19.303  35.673  1.00 50.29           C  
ANISOU 2025  CD2 PHE L  61     8043   5567   5499    -72    991    323       C  
ATOM   2026  CE1 PHE L  61      23.884  16.935  37.040  1.00 53.94           C  
ANISOU 2026  CE1 PHE L  61     8594   5978   5923   -203   1122    853       C  
ATOM   2027  CE2 PHE L  61      25.157  18.589  35.953  1.00 50.43           C  
ANISOU 2027  CE2 PHE L  61     8202   5511   5450      7    975    437       C  
ATOM   2028  CZ  PHE L  61      25.095  17.401  36.638  1.00 51.51           C  
ANISOU 2028  CZ  PHE L  61     8387   5615   5572    -50   1032    695       C  
ATOM   2029  N   SER L  62      20.381  22.699  36.038  1.00 51.23           N  
ANISOU 2029  N   SER L  62     7463   6190   5811   -114   1019   -230       N  
ATOM   2030  CA  SER L  62      19.449  23.627  35.422  1.00 51.30           C  
ANISOU 2030  CA  SER L  62     7309   6161   6021   -126    934   -402       C  
ATOM   2031  C   SER L  62      20.297  24.533  34.555  1.00 49.67           C  
ANISOU 2031  C   SER L  62     7164   5770   5938    -32    769   -492       C  
ATOM   2032  O   SER L  62      21.520  24.619  34.762  1.00 48.76           O  
ANISOU 2032  O   SER L  62     7156   5636   5735     60    752   -481       O  
ATOM   2033  CB  SER L  62      18.633  24.419  36.468  1.00 52.34           C  
ANISOU 2033  CB  SER L  62     7172   6591   6125    -59   1005   -595       C  
ATOM   2034  OG  SER L  62      19.465  25.096  37.371  1.00 52.16           O  
ANISOU 2034  OG  SER L  62     7103   6741   5973    108   1005   -747       O  
ATOM   2035  N   GLY L  63      19.665  25.161  33.563  1.00 49.23           N  
ANISOU 2035  N   GLY L  63     7031   5584   6088    -63    644   -548       N  
ATOM   2036  CA  GLY L  63      20.328  26.162  32.738  1.00 48.20           C  
ANISOU 2036  CA  GLY L  63     6907   5301   6104     10    483   -580       C  
ATOM   2037  C   GLY L  63      19.454  27.374  32.506  1.00 49.54           C  
ANISOU 2037  C   GLY L  63     6852   5438   6534     48    358   -718       C  
ATOM   2038  O   GLY L  63      18.236  27.274  32.543  1.00 50.74           O  
ANISOU 2038  O   GLY L  63     6874   5651   6754    -10    374   -772       O  
ATOM   2039  N   SER L  64      20.066  28.525  32.265  1.00 49.26           N  
ANISOU 2039  N   SER L  64     6745   5286   6685    142    220   -768       N  
ATOM   2040  CA  SER L  64      19.309  29.720  31.968  1.00 50.65           C  
ANISOU 2040  CA  SER L  64     6697   5366   7183    187     59   -874       C  
ATOM   2041  C   SER L  64      20.077  30.467  30.899  1.00 50.46           C  
ANISOU 2041  C   SER L  64     6707   5131   7334    195   -111   -702       C  
ATOM   2042  O   SER L  64      21.274  30.207  30.719  1.00 49.45           O  
ANISOU 2042  O   SER L  64     6734   4979   7077    195    -76   -582       O  
ATOM   2043  CB  SER L  64      19.172  30.577  33.226  1.00 52.22           C  
ANISOU 2043  CB  SER L  64     6669   5661   7511    326     59  -1181       C  
ATOM   2044  OG  SER L  64      20.450  31.005  33.708  1.00 52.07           O  
ANISOU 2044  OG  SER L  64     6682   5608   7494    422     36  -1242       O  
ATOM   2045  N   ASN L  65      19.418  31.413  30.226  1.00 51.41           N  
ANISOU 2045  N   ASN L  65     6664   5110   7760    205   -294   -671       N  
ATOM   2046  CA  ASN L  65      20.055  32.174  29.159  1.00 51.24           C  
ANISOU 2046  CA  ASN L  65     6642   4907   7919    194   -463   -429       C  
ATOM   2047  C   ASN L  65      19.442  33.558  28.945  1.00 53.34           C  
ANISOU 2047  C   ASN L  65     6646   4970   8653    257   -693   -454       C  
ATOM   2048  O   ASN L  65      18.252  33.683  28.628  1.00 53.59           O  
ANISOU 2048  O   ASN L  65     6562   4998   8801    246   -777   -482       O  
ATOM   2049  CB  ASN L  65      20.001  31.358  27.862  1.00 50.80           C  
ANISOU 2049  CB  ASN L  65     6765   4923   7613     81   -457   -161       C  
ATOM   2050  CG  ASN L  65      20.794  31.979  26.742  1.00 51.15           C  
ANISOU 2050  CG  ASN L  65     6823   4883   7728     59   -584    144       C  
ATOM   2051  OD1 ASN L  65      20.584  31.639  25.578  1.00 52.10           O  
ANISOU 2051  OD1 ASN L  65     7015   5092   7688     -9   -635    352       O  
ATOM   2052  ND2 ASN L  65      21.714  32.885  27.077  1.00 50.97           N  
ANISOU 2052  ND2 ASN L  65     6712   4714   7938    114   -639    174       N  
ATOM   2053  N   SER L  66      20.273  34.591  29.098  1.00 54.51           N  
ANISOU 2053  N   SER L  66     6682   4922   9107    322   -813   -441       N  
ATOM   2054  CA  SER L  66      19.889  35.947  28.725  1.00 57.15           C  
ANISOU 2054  CA  SER L  66     6766   4982   9966    373  -1073   -388       C  
ATOM   2055  C   SER L  66      21.107  36.828  28.439  1.00 58.16           C  
ANISOU 2055  C   SER L  66     6839   4877  10383    373  -1195   -186       C  
ATOM   2056  O   SER L  66      22.240  36.494  28.814  1.00 57.09           O  
ANISOU 2056  O   SER L  66     6821   4803  10069    367  -1072   -201       O  
ATOM   2057  CB  SER L  66      19.085  36.568  29.849  1.00 59.26           C  
ANISOU 2057  CB  SER L  66     6779   5204  10532    509  -1128   -827       C  
ATOM   2058  OG  SER L  66      19.898  36.592  31.007  1.00 58.95           O  
ANISOU 2058  OG  SER L  66     6728   5226  10442    595  -1030  -1116       O  
ATOM   2059  N   GLY L  67      20.854  37.976  27.811  1.00 60.53           N  
ANISOU 2059  N   GLY L  67     6934   4894  11170    380  -1449     10       N  
ATOM   2060  CA  GLY L  67      21.904  38.912  27.475  1.00 62.04           C  
ANISOU 2060  CA  GLY L  67     7021   4818  11732    356  -1592    261       C  
ATOM   2061  C   GLY L  67      22.849  38.252  26.515  1.00 60.77           C  
ANISOU 2061  C   GLY L  67     7084   4841  11165    223  -1461    684       C  
ATOM   2062  O   GLY L  67      22.437  37.802  25.444  1.00 60.52           O  
ANISOU 2062  O   GLY L  67     7160   4977  10857    142  -1453    993       O  
ATOM   2063  N   ASN L  68      24.113  38.183  26.914  1.00 59.82           N  
ANISOU 2063  N   ASN L  68     7014   4719  10997    215  -1363    661       N  
ATOM   2064  CA  ASN L  68      25.132  37.532  26.114  1.00 58.74           C  
ANISOU 2064  CA  ASN L  68     7063   4784  10470    109  -1216   1000       C  
ATOM   2065  C   ASN L  68      25.580  36.245  26.804  1.00 56.04           C  
ANISOU 2065  C   ASN L  68     6958   4715   9618    138   -960    721       C  
ATOM   2066  O   ASN L  68      26.588  35.630  26.426  1.00 55.71           O  
ANISOU 2066  O   ASN L  68     7062   4837   9270     87   -820    879       O  
ATOM   2067  CB  ASN L  68      26.330  38.473  25.915  1.00 60.85           C  
ANISOU 2067  CB  ASN L  68     7172   4826  11121     61  -1313   1256       C  
ATOM   2068  CG  ASN L  68      26.009  39.663  25.010  1.00 65.55           C  
ANISOU 2068  CG  ASN L  68     7541   5155  12208     -3  -1567   1685       C  
ATOM   2069  OD1 ASN L  68      25.107  39.595  24.149  1.00 66.16           O  
ANISOU 2069  OD1 ASN L  68     7639   5327  12170    -36  -1638   1927       O  
ATOM   2070  ND2 ASN L  68      26.770  40.771  25.190  1.00 67.65           N  
ANISOU 2070  ND2 ASN L  68     7572   5075  13056    -23  -1725   1803       N  
ATOM   2071  N   THR L  69      24.841  35.830  27.824  1.00 54.61           N  
ANISOU 2071  N   THR L  69     6799   4596   9355    224   -898    321       N  
ATOM   2072  CA  THR L  69      25.349  34.787  28.722  1.00 52.39           C  
ANISOU 2072  CA  THR L  69     6693   4521   8691    266   -688     67       C  
ATOM   2073  C   THR L  69      24.389  33.644  29.054  1.00 51.03           C  
ANISOU 2073  C   THR L  69     6669   4572   8148    266   -541   -102       C  
ATOM   2074  O   THR L  69      23.275  33.866  29.508  1.00 52.34           O  
ANISOU 2074  O   THR L  69     6720   4728   8439    307   -587   -300       O  
ATOM   2075  CB  THR L  69      25.829  35.397  30.043  1.00 52.83           C  
ANISOU 2075  CB  THR L  69     6599   4473   9000    384   -728   -285       C  
ATOM   2076  OG1 THR L  69      26.855  36.362  29.777  1.00 54.49           O  
ANISOU 2076  OG1 THR L  69     6666   4452   9585    368   -860   -134       O  
ATOM   2077  CG2 THR L  69      26.386  34.323  30.930  1.00 51.35           C  
ANISOU 2077  CG2 THR L  69     6590   4527   8394    429   -528   -481       C  
ATOM   2078  N   ALA L  70      24.831  32.414  28.826  1.00 49.02           N  
ANISOU 2078  N   ALA L  70     6649   4509   7469    218   -370    -25       N  
ATOM   2079  CA  ALA L  70      24.057  31.234  29.195  1.00 47.38           C  
ANISOU 2079  CA  ALA L  70     6576   4475   6951    200   -230   -157       C  
ATOM   2080  C   ALA L  70      24.791  30.577  30.347  1.00 47.07           C  
ANISOU 2080  C   ALA L  70     6630   4542   6711    262    -84   -333       C  
ATOM   2081  O   ALA L  70      26.019  30.648  30.427  1.00 46.65           O  
ANISOU 2081  O   ALA L  70     6620   4469   6637    293    -68   -289       O  
ATOM   2082  CB  ALA L  70      23.952  30.293  28.033  1.00 46.69           C  
ANISOU 2082  CB  ALA L  70     6661   4493   6587    105   -183     48       C  
ATOM   2083  N   THR L  71      24.058  29.963  31.268  1.00 46.95           N  
ANISOU 2083  N   THR L  71     6627   4659   6553    281     18   -514       N  
ATOM   2084  CA  THR L  71      24.690  29.462  32.488  1.00 46.88           C  
ANISOU 2084  CA  THR L  71     6671   4786   6354    356    136   -659       C  
ATOM   2085  C   THR L  71      24.182  28.057  32.886  1.00 47.13           C  
ANISOU 2085  C   THR L  71     6852   4980   6077    300    301   -625       C  
ATOM   2086  O   THR L  71      22.968  27.808  32.938  1.00 47.61           O  
ANISOU 2086  O   THR L  71     6854   5097   6137    242    334   -655       O  
ATOM   2087  CB  THR L  71      24.514  30.451  33.693  1.00 48.39           C  
ANISOU 2087  CB  THR L  71     6635   5025   6724    483     79   -964       C  
ATOM   2088  OG1 THR L  71      25.004  31.768  33.351  1.00 48.71           O  
ANISOU 2088  OG1 THR L  71     6513   4849   7148    529   -103  -1000       O  
ATOM   2089  CG2 THR L  71      25.269  29.939  34.903  1.00 48.42           C  
ANISOU 2089  CG2 THR L  71     6693   5229   6477    571    184  -1092       C  
ATOM   2090  N   LEU L  72      25.118  27.134  33.144  1.00 46.45           N  
ANISOU 2090  N   LEU L  72     6937   4944   5767    311    393   -546       N  
ATOM   2091  CA  LEU L  72      24.763  25.816  33.671  1.00 45.97           C  
ANISOU 2091  CA  LEU L  72     6997   4996   5473    263    532   -481       C  
ATOM   2092  C   LEU L  72      25.069  25.882  35.121  1.00 46.76           C  
ANISOU 2092  C   LEU L  72     7032   5292   5441    365    596   -599       C  
ATOM   2093  O   LEU L  72      26.188  26.234  35.521  1.00 46.64           O  
ANISOU 2093  O   LEU L  72     7022   5293   5405    469    559   -662       O  
ATOM   2094  CB  LEU L  72      25.561  24.673  33.035  1.00 45.10           C  
ANISOU 2094  CB  LEU L  72     7102   4802   5231    224    569   -318       C  
ATOM   2095  CG  LEU L  72      25.190  23.231  33.438  1.00 44.61           C  
ANISOU 2095  CG  LEU L  72     7159   4768   5024    157    677   -212       C  
ATOM   2096  CD1 LEU L  72      23.806  22.903  33.070  1.00 45.07           C  
ANISOU 2096  CD1 LEU L  72     7165   4805   5153     32    692   -191       C  
ATOM   2097  CD2 LEU L  72      26.083  22.218  32.818  1.00 43.62           C  
ANISOU 2097  CD2 LEU L  72     7214   4521   4839    154    677   -114       C  
ATOM   2098  N   THR L  73      24.047  25.548  35.896  1.00 47.82           N  
ANISOU 2098  N   THR L  73     7085   5608   5475    335    693   -630       N  
ATOM   2099  CA  THR L  73      24.062  25.658  37.334  1.00 49.65           C  
ANISOU 2099  CA  THR L  73     7207   6133   5524    434    768   -754       C  
ATOM   2100  C   THR L  73      23.861  24.253  37.907  1.00 51.01           C  
ANISOU 2100  C   THR L  73     7495   6444   5443    357    920   -516       C  
ATOM   2101  O   THR L  73      22.866  23.590  37.615  1.00 51.26           O  
ANISOU 2101  O   THR L  73     7530   6446   5501    219    991   -383       O  
ATOM   2102  CB  THR L  73      22.886  26.524  37.802  1.00 51.34           C  
ANISOU 2102  CB  THR L  73     7164   6510   5832    463    769   -987       C  
ATOM   2103  OG1 THR L  73      22.629  27.544  36.833  1.00 51.54           O  
ANISOU 2103  OG1 THR L  73     7102   6289   6191    461    615  -1091       O  
ATOM   2104  CG2 THR L  73      23.151  27.130  39.130  1.00 52.79           C  
ANISOU 2104  CG2 THR L  73     7179   7005   5875    626    782  -1245       C  
ATOM   2105  N   ILE L  74      24.808  23.802  38.729  1.00 51.77           N  
ANISOU 2105  N   ILE L  74     7668   6678   5323    443    953   -447       N  
ATOM   2106  CA  ILE L  74      24.708  22.493  39.365  1.00 52.48           C  
ANISOU 2106  CA  ILE L  74     7853   6889   5199    378   1077   -165       C  
ATOM   2107  C   ILE L  74      24.612  22.726  40.839  1.00 54.65           C  
ANISOU 2107  C   ILE L  74     7975   7606   5182    483   1158   -231       C  
ATOM   2108  O   ILE L  74      25.603  23.114  41.454  1.00 55.33           O  
ANISOU 2108  O   ILE L  74     8054   7831   5136    638   1098   -351       O  
ATOM   2109  CB  ILE L  74      25.947  21.645  39.076  1.00 51.21           C  
ANISOU 2109  CB  ILE L  74     7910   6531   5017    404   1031     15       C  
ATOM   2110  CG1 ILE L  74      26.222  21.616  37.578  1.00 48.74           C  
ANISOU 2110  CG1 ILE L  74     7715   5855   4949    344    939     -3       C  
ATOM   2111  CG2 ILE L  74      25.716  20.259  39.493  1.00 51.95           C  
ANISOU 2111  CG2 ILE L  74     8096   6635   5009    311   1123    341       C  
ATOM   2112  CD1 ILE L  74      27.428  20.834  37.210  1.00 48.55           C  
ANISOU 2112  CD1 ILE L  74     7870   5651   4925    387    894    112       C  
ATOM   2113  N   SER L  75      23.421  22.555  41.406  1.00 57.00           N  
ANISOU 2113  N   SER L  75     8122   8164   5372    407   1292   -182       N  
ATOM   2114  CA  SER L  75      23.227  22.869  42.829  1.00 60.60           C  
ANISOU 2114  CA  SER L  75     8384   9148   5492    520   1385   -283       C  
ATOM   2115  C   SER L  75      23.793  21.705  43.626  1.00 62.05           C  
ANISOU 2115  C   SER L  75     8686   9510   5380    511   1465     94       C  
ATOM   2116  O   SER L  75      24.115  20.692  43.040  1.00 61.14           O  
ANISOU 2116  O   SER L  75     8773   9065   5392    401   1450    402       O  
ATOM   2117  CB  SER L  75      21.742  23.121  43.159  1.00 62.87           C  
ANISOU 2117  CB  SER L  75     8428   9708   5751    447   1518   -365       C  
ATOM   2118  OG  SER L  75      21.002  21.918  43.153  1.00 65.24           O  
ANISOU 2118  OG  SER L  75     8769  10004   6015    246   1665     37       O  
ATOM   2119  N   GLY L  76      23.936  21.850  44.939  1.00 65.07           N  
ANISOU 2119  N   GLY L  76     8932  10414   5376    638   1532     61       N  
ATOM   2120  CA  GLY L  76      24.595  20.822  45.757  1.00 67.49           C  
ANISOU 2120  CA  GLY L  76     9343  10921   5380    656   1576    448       C  
ATOM   2121  C   GLY L  76      25.365  19.752  44.980  1.00 65.78           C  
ANISOU 2121  C   GLY L  76     9406  10199   5390    569   1496    784       C  
ATOM   2122  O   GLY L  76      24.856  18.671  44.758  1.00 68.01           O  
ANISOU 2122  O   GLY L  76     9761  10306   5773    391   1573   1169       O  
ATOM   2123  N   THR L  77      26.613  20.023  44.614  1.00 63.16           N  
ANISOU 2123  N   THR L  77     9206   9641   5152    700   1336    631       N  
ATOM   2124  CA  THR L  77      27.315  19.205  43.623  1.00 60.67           C  
ANISOU 2124  CA  THR L  77     9124   8809   5118    636   1247    819       C  
ATOM   2125  C   THR L  77      28.163  18.105  44.236  1.00 62.56           C  
ANISOU 2125  C   THR L  77     9488   9068   5212    683   1219   1187       C  
ATOM   2126  O   THR L  77      28.661  18.243  45.334  1.00 65.05           O  
ANISOU 2126  O   THR L  77     9738   9782   5197    825   1210   1214       O  
ATOM   2127  CB  THR L  77      28.180  20.077  42.688  1.00 57.53           C  
ANISOU 2127  CB  THR L  77     8783   8120   4955    730   1099    472       C  
ATOM   2128  OG1 THR L  77      29.307  20.580  43.385  1.00 59.91           O  
ANISOU 2128  OG1 THR L  77     9054   8625   5083    926   1004    312       O  
ATOM   2129  CG2 THR L  77      27.432  21.266  42.262  1.00 56.49           C  
ANISOU 2129  CG2 THR L  77     8500   8003   4960    713   1096    137       C  
ATOM   2130  N   GLN L  78      28.357  17.019  43.501  1.00 62.23           N  
ANISOU 2130  N   GLN L  78     9616   8590   5437    580   1181   1448       N  
ATOM   2131  CA  GLN L  78      29.010  15.849  44.066  1.00 64.52           C  
ANISOU 2131  CA  GLN L  78    10009   8839   5668    607   1142   1852       C  
ATOM   2132  C   GLN L  78      30.239  15.424  43.298  1.00 62.28           C  
ANISOU 2132  C   GLN L  78     9897   8137   5630    696    986   1798       C  
ATOM   2133  O   GLN L  78      30.480  15.902  42.220  1.00 59.42           O  
ANISOU 2133  O   GLN L  78     9581   7509   5487    700    932   1496       O  
ATOM   2134  CB  GLN L  78      28.016  14.698  44.097  1.00 67.62           C  
ANISOU 2134  CB  GLN L  78    10401   9092   6201    391   1238   2286       C  
ATOM   2135  CG  GLN L  78      26.590  15.150  44.375  1.00 68.76           C  
ANISOU 2135  CG  GLN L  78    10360   9533   6233    251   1409   2264       C  
ATOM   2136  CD  GLN L  78      26.061  14.873  45.784  1.00 73.44           C  
ANISOU 2136  CD  GLN L  78    10794  10675   6435    225   1556   2624       C  
ATOM   2137  OE1 GLN L  78      26.508  15.447  46.786  1.00 75.62           O  
ANISOU 2137  OE1 GLN L  78    10982  11454   6294    398   1567   2540       O  
ATOM   2138  NE2 GLN L  78      25.035  14.049  45.842  1.00 75.30           N  
ANISOU 2138  NE2 GLN L  78    10962  10851   6799      2   1675   3002       N  
ATOM   2139  N   ALA L  79      31.006  14.493  43.849  1.00 64.94           N  
ANISOU 2139  N   ALA L  79    10312   8432   5931    769    911   2114       N  
ATOM   2140  CA  ALA L  79      32.192  13.988  43.160  1.00 64.26           C  
ANISOU 2140  CA  ALA L  79    10366   7955   6097    871    760   2058       C  
ATOM   2141  C   ALA L  79      31.820  13.566  41.745  1.00 62.57           C  
ANISOU 2141  C   ALA L  79    10233   7252   6289    740    747   1941       C  
ATOM   2142  O   ALA L  79      32.525  13.884  40.774  1.00 60.12           O  
ANISOU 2142  O   ALA L  79     9977   6729   6138    812    674   1637       O  
ATOM   2143  CB  ALA L  79      32.779  12.824  43.900  1.00 67.11           C  
ANISOU 2143  CB  ALA L  79    10785   8263   6449    931    677   2490       C  
ATOM   2144  N   GLU L  80      30.688  12.877  41.638  1.00 64.07           N  
ANISOU 2144  N   GLU L  80    10407   7305   6631    544    821   2177       N  
ATOM   2145  CA  GLU L  80      30.262  12.302  40.369  1.00 62.93           C  
ANISOU 2145  CA  GLU L  80    10325   6707   6881    419    785   2077       C  
ATOM   2146  C   GLU L  80      29.988  13.360  39.287  1.00 59.08           C  
ANISOU 2146  C   GLU L  80     9815   6216   6417    402    807   1642       C  
ATOM   2147  O   GLU L  80      29.862  13.033  38.110  1.00 58.09           O  
ANISOU 2147  O   GLU L  80     9740   5774   6556    345    755   1478       O  
ATOM   2148  CB  GLU L  80      29.058  11.366  40.585  1.00 65.71           C  
ANISOU 2148  CB  GLU L  80    10628   6924   7415    199    850   2432       C  
ATOM   2149  CG  GLU L  80      27.697  11.984  40.285  1.00 65.80           C  
ANISOU 2149  CG  GLU L  80    10526   7071   7402     29    978   2306       C  
ATOM   2150  CD  GLU L  80      26.589  11.445  41.202  1.00 70.50           C  
ANISOU 2150  CD  GLU L  80    10996   7836   7954   -153   1106   2733       C  
ATOM   2151  OE1 GLU L  80      26.915  11.003  42.331  1.00 73.39           O  
ANISOU 2151  OE1 GLU L  80    11342   8412   8132   -114   1131   3116       O  
ATOM   2152  OE2 GLU L  80      25.388  11.494  40.797  1.00 71.01           O  
ANISOU 2152  OE2 GLU L  80    10964   7859   8159   -336   1185   2696       O  
ATOM   2153  N   ASP L  81      29.938  14.625  39.677  1.00 57.31           N  
ANISOU 2153  N   ASP L  81     9501   6347   5926    463    866   1451       N  
ATOM   2154  CA  ASP L  81      29.688  15.689  38.721  1.00 54.27           C  
ANISOU 2154  CA  ASP L  81     9076   5954   5589    448    870   1100       C  
ATOM   2155  C   ASP L  81      30.961  16.207  38.075  1.00 52.24           C  
ANISOU 2155  C   ASP L  81     8869   5618   5362    596    777    854       C  
ATOM   2156  O   ASP L  81      30.891  17.104  37.249  1.00 50.03           O  
ANISOU 2156  O   ASP L  81     8549   5330   5131    586    769    613       O  
ATOM   2157  CB  ASP L  81      28.965  16.851  39.397  1.00 54.19           C  
ANISOU 2157  CB  ASP L  81     8912   6314   5362    442    956    986       C  
ATOM   2158  CG  ASP L  81      27.554  16.495  39.802  1.00 56.72           C  
ANISOU 2158  CG  ASP L  81     9141   6739   5670    274   1072   1175       C  
ATOM   2159  OD1 ASP L  81      26.880  15.820  38.992  1.00 57.41           O  
ANISOU 2159  OD1 ASP L  81     9267   6542   6005    124   1070   1241       O  
ATOM   2160  OD2 ASP L  81      27.119  16.889  40.918  1.00 58.53           O  
ANISOU 2160  OD2 ASP L  81     9240   7358   5640    294   1164   1236       O  
ATOM   2161  N   GLU L  82      32.123  15.683  38.467  1.00 53.39           N  
ANISOU 2161  N   GLU L  82     9079   5723   5484    732    705    935       N  
ATOM   2162  CA  GLU L  82      33.385  16.110  37.847  1.00 52.11           C  
ANISOU 2162  CA  GLU L  82     8937   5496   5367    869    628    710       C  
ATOM   2163  C   GLU L  82      33.480  15.640  36.436  1.00 51.62           C  
ANISOU 2163  C   GLU L  82     8938   5143   5531    826    597    585       C  
ATOM   2164  O   GLU L  82      33.412  14.435  36.165  1.00 53.44           O  
ANISOU 2164  O   GLU L  82     9246   5122   5938    799    557    693       O  
ATOM   2165  CB  GLU L  82      34.595  15.598  38.579  1.00 54.06           C  
ANISOU 2165  CB  GLU L  82     9219   5767   5556   1033    546    813       C  
ATOM   2166  CG  GLU L  82      35.047  16.521  39.674  1.00 55.09           C  
ANISOU 2166  CG  GLU L  82     9251   6248   5430   1149    535    756       C  
ATOM   2167  CD  GLU L  82      36.417  16.166  40.187  1.00 56.63           C  
ANISOU 2167  CD  GLU L  82     9465   6465   5586   1333    425    790       C  
ATOM   2168  OE1 GLU L  82      37.251  15.722  39.368  1.00 56.73           O  
ANISOU 2168  OE1 GLU L  82     9529   6231   5795   1391    366    711       O  
ATOM   2169  OE2 GLU L  82      36.671  16.334  41.396  1.00 58.20           O  
ANISOU 2169  OE2 GLU L  82     9610   6957   5547   1432    392    878       O  
ATOM   2170  N   ALA L  83      33.656  16.595  35.526  1.00 49.69           N  
ANISOU 2170  N   ALA L  83     8644   4941   5294    825    603    354       N  
ATOM   2171  CA  ALA L  83      33.510  16.312  34.111  1.00 48.67           C  
ANISOU 2171  CA  ALA L  83     8546   4641   5304    769    590    219       C  
ATOM   2172  C   ALA L  83      33.826  17.548  33.335  1.00 47.09           C  
ANISOU 2172  C   ALA L  83     8263   4572   5058    777    602     47       C  
ATOM   2173  O   ALA L  83      34.030  18.609  33.905  1.00 46.74           O  
ANISOU 2173  O   ALA L  83     8133   4690   4939    808    610     24       O  
ATOM   2174  CB  ALA L  83      32.075  15.871  33.822  1.00 49.24           C  
ANISOU 2174  CB  ALA L  83     8632   4613   5465    602    618    282       C  
ATOM   2175  N   ASP L  84      33.868  17.427  32.017  1.00 47.63           N  
ANISOU 2175  N   ASP L  84     8337   4580   5181    750    594    -73       N  
ATOM   2176  CA  ASP L  84      33.901  18.622  31.180  1.00 46.78           C  
ANISOU 2176  CA  ASP L  84     8134   4608   5031    715    609   -155       C  
ATOM   2177  C   ASP L  84      32.479  18.943  30.724  1.00 45.96           C  
ANISOU 2177  C   ASP L  84     8010   4506   4946    572    615   -140       C  
ATOM   2178  O   ASP L  84      31.700  18.048  30.381  1.00 46.65           O  
ANISOU 2178  O   ASP L  84     8158   4480   5087    503    603   -148       O  
ATOM   2179  CB  ASP L  84      34.814  18.429  29.972  1.00 47.09           C  
ANISOU 2179  CB  ASP L  84     8158   4680   5054    777    606   -273       C  
ATOM   2180  CG  ASP L  84      36.261  18.271  30.358  1.00 48.06           C  
ANISOU 2180  CG  ASP L  84     8260   4823   5177    923    600   -306       C  
ATOM   2181  OD1 ASP L  84      36.621  18.709  31.461  1.00 47.04           O  
ANISOU 2181  OD1 ASP L  84     8104   4723   5045    971    587   -242       O  
ATOM   2182  OD2 ASP L  84      37.043  17.700  29.556  1.00 50.14           O  
ANISOU 2182  OD2 ASP L  84     8516   5097   5438   1003    601   -425       O  
ATOM   2183  N   TYR L  85      32.152  20.225  30.732  1.00 44.30           N  
ANISOU 2183  N   TYR L  85     7696   4404   4734    531    615   -129       N  
ATOM   2184  CA  TYR L  85      30.873  20.680  30.240  1.00 44.44           C  
ANISOU 2184  CA  TYR L  85     7666   4433   4787    413    602   -120       C  
ATOM   2185  C   TYR L  85      31.100  21.579  29.048  1.00 44.30           C  
ANISOU 2185  C   TYR L  85     7567   4501   4766    392    570   -123       C  
ATOM   2186  O   TYR L  85      31.970  22.446  29.064  1.00 44.11           O  
ANISOU 2186  O   TYR L  85     7459   4534   4766    441    563    -97       O  
ATOM   2187  CB  TYR L  85      30.094  21.376  31.353  1.00 44.12           C  
ANISOU 2187  CB  TYR L  85     7545   4438   4780    385    614    -96       C  
ATOM   2188  CG  TYR L  85      29.770  20.433  32.479  1.00 45.18           C  
ANISOU 2188  CG  TYR L  85     7743   4555   4869    386    664    -32       C  
ATOM   2189  CD1 TYR L  85      30.674  20.219  33.515  1.00 45.65           C  
ANISOU 2189  CD1 TYR L  85     7826   4667   4851    495    677      1       C  
ATOM   2190  CD2 TYR L  85      28.582  19.716  32.483  1.00 45.75           C  
ANISOU 2190  CD2 TYR L  85     7836   4566   4980    273    690     25       C  
ATOM   2191  CE1 TYR L  85      30.386  19.331  34.552  1.00 46.37           C  
ANISOU 2191  CE1 TYR L  85     7967   4775   4878    492    719    130       C  
ATOM   2192  CE2 TYR L  85      28.281  18.834  33.503  1.00 46.99           C  
ANISOU 2192  CE2 TYR L  85     8030   4714   5111    252    743    155       C  
ATOM   2193  CZ  TYR L  85      29.188  18.644  34.534  1.00 47.39           C  
ANISOU 2193  CZ  TYR L  85     8110   4840   5058    362    759    228       C  
ATOM   2194  OH  TYR L  85      28.895  17.759  35.541  1.00 48.73           O  
ANISOU 2194  OH  TYR L  85     8304   5030   5179    337    808    422       O  
ATOM   2195  N   TYR L  86      30.338  21.323  27.993  1.00 44.73           N  
ANISOU 2195  N   TYR L  86     7631   4571   4792    318    541   -139       N  
ATOM   2196  CA  TYR L  86      30.366  22.137  26.790  1.00 44.11           C  
ANISOU 2196  CA  TYR L  86     7467   4624   4671    286    502    -87       C  
ATOM   2197  C   TYR L  86      29.004  22.749  26.534  1.00 44.36           C  
ANISOU 2197  C   TYR L  86     7430   4651   4775    188    438    -40       C  
ATOM   2198  O   TYR L  86      27.982  22.044  26.590  1.00 45.53           O  
ANISOU 2198  O   TYR L  86     7623   4737   4939    130    425   -106       O  
ATOM   2199  CB  TYR L  86      30.680  21.249  25.614  1.00 44.84           C  
ANISOU 2199  CB  TYR L  86     7612   4814   4613    309    502   -177       C  
ATOM   2200  CG  TYR L  86      32.045  20.687  25.675  1.00 45.31           C  
ANISOU 2200  CG  TYR L  86     7706   4898   4612    420    556   -247       C  
ATOM   2201  CD1 TYR L  86      32.283  19.457  26.245  1.00 45.46           C  
ANISOU 2201  CD1 TYR L  86     7832   4765   4677    482    565   -364       C  
ATOM   2202  CD2 TYR L  86      33.115  21.390  25.154  1.00 46.26           C  
ANISOU 2202  CD2 TYR L  86     7730   5188   4659    462    591   -175       C  
ATOM   2203  CE1 TYR L  86      33.549  18.956  26.315  1.00 46.42           C  
ANISOU 2203  CE1 TYR L  86     7967   4897   4772    602    596   -438       C  
ATOM   2204  CE2 TYR L  86      34.390  20.895  25.214  1.00 46.82           C  
ANISOU 2204  CE2 TYR L  86     7805   5299   4687    571    644   -254       C  
ATOM   2205  CZ  TYR L  86      34.599  19.680  25.793  1.00 46.93           C  
ANISOU 2205  CZ  TYR L  86     7929   5155   4746    651    640   -402       C  
ATOM   2206  OH  TYR L  86      35.872  19.191  25.791  1.00 47.78           O  
ANISOU 2206  OH  TYR L  86     8023   5301   4832    776    675   -496       O  
ATOM   2207  N   CYS L  87      28.978  24.039  26.225  1.00 43.53           N  
ANISOU 2207  N   CYS L  87     7197   4594   4749    166    387     81       N  
ATOM   2208  CA  CYS L  87      27.750  24.601  25.698  1.00 44.47           C  
ANISOU 2208  CA  CYS L  87     7237   4723   4937     88    299    136       C  
ATOM   2209  C   CYS L  87      27.790  24.553  24.187  1.00 46.12           C  
ANISOU 2209  C   CYS L  87     7432   5114   4977     63    251    218       C  
ATOM   2210  O   CYS L  87      28.842  24.293  23.597  1.00 46.80           O  
ANISOU 2210  O   CYS L  87     7540   5338   4903    108    301    239       O  
ATOM   2211  CB  CYS L  87      27.513  26.025  26.197  1.00 44.53           C  
ANISOU 2211  CB  CYS L  87     7089   4651   5181     83    232    221       C  
ATOM   2212  SG  CYS L  87      28.773  27.149  25.739  1.00 44.70           S  
ANISOU 2212  SG  CYS L  87     6992   4700   5291    106    202    410       S  
ATOM   2213  N   SER L  88      26.650  24.786  23.553  1.00 46.47           N  
ANISOU 2213  N   SER L  88     7424   5201   5033      0    154    253       N  
ATOM   2214  CA  SER L  88      26.621  24.847  22.113  1.00 48.33           C  
ANISOU 2214  CA  SER L  88     7623   5673   5066    -16     90    349       C  
ATOM   2215  C   SER L  88      25.349  25.517  21.652  1.00 49.64           C  
ANISOU 2215  C   SER L  88     7688   5850   5324    -77    -51    447       C  
ATOM   2216  O   SER L  88      24.403  25.667  22.424  1.00 48.81           O  
ANISOU 2216  O   SER L  88     7553   5564   5430   -107    -84    373       O  
ATOM   2217  CB  SER L  88      26.699  23.443  21.520  1.00 49.41           C  
ANISOU 2217  CB  SER L  88     7871   5929   4973     13    118    126       C  
ATOM   2218  OG  SER L  88      25.491  22.739  21.736  1.00 49.81           O  
ANISOU 2218  OG  SER L  88     7958   5857   5110    -38     63    -42       O  
ATOM   2219  N   THR L  89      25.328  25.893  20.376  1.00 51.62           N  
ANISOU 2219  N   THR L  89     7870   6348   5395    -89   -134    618       N  
ATOM   2220  CA  THR L  89      24.143  26.462  19.762  1.00 52.93           C  
ANISOU 2220  CA  THR L  89     7933   6564   5614   -135   -298    731       C  
ATOM   2221  C   THR L  89      24.189  26.268  18.247  1.00 55.56           C  
ANISOU 2221  C   THR L  89     8239   7283   5587   -127   -369    826       C  
ATOM   2222  O   THR L  89      25.220  25.907  17.705  1.00 56.80           O  
ANISOU 2222  O   THR L  89     8428   7676   5477    -87   -277    836       O  
ATOM   2223  CB  THR L  89      23.998  27.947  20.117  1.00 52.40           C  
ANISOU 2223  CB  THR L  89     7715   6325   5870   -154   -385    996       C  
ATOM   2224  OG1 THR L  89      22.658  28.369  19.849  1.00 52.49           O  
ANISOU 2224  OG1 THR L  89     7628   6297   6019   -184   -550   1031       O  
ATOM   2225  CG2 THR L  89      24.977  28.783  19.332  1.00 53.91           C  
ANISOU 2225  CG2 THR L  89     7815   6682   5986   -159   -397   1347       C  
ATOM   2226  N   PHE L  90      23.066  26.484  17.579  1.00 56.97           N  
ANISOU 2226  N   PHE L  90     8342   7561   5741   -155   -533    875       N  
ATOM   2227  CA  PHE L  90      22.978  26.384  16.135  1.00 59.93           C  
ANISOU 2227  CA  PHE L  90     8667   8362   5742   -138   -631    972       C  
ATOM   2228  C   PHE L  90      23.589  27.616  15.468  1.00 62.86           C  
ANISOU 2228  C   PHE L  90     8906   8926   6052   -151   -668   1454       C  
ATOM   2229  O   PHE L  90      23.140  28.744  15.693  1.00 63.69           O  
ANISOU 2229  O   PHE L  90     8897   8832   6469   -190   -782   1737       O  
ATOM   2230  CB  PHE L  90      21.498  26.265  15.736  1.00 62.27           C  
ANISOU 2230  CB  PHE L  90     8907   8680   6073   -163   -823    872       C  
ATOM   2231  CG  PHE L  90      21.201  26.586  14.270  1.00 67.16           C  
ANISOU 2231  CG  PHE L  90     9422   9751   6346   -143   -988   1077       C  
ATOM   2232  CD1 PHE L  90      21.880  27.633  13.599  1.00 68.83           C  
ANISOU 2232  CD1 PHE L  90     9528  10199   6424   -144  -1006   1550       C  
ATOM   2233  CD2 PHE L  90      20.209  25.852  13.560  1.00 69.51           C  
ANISOU 2233  CD2 PHE L  90     9703  10251   6458   -129  -1139    815       C  
ATOM   2234  CE1 PHE L  90      21.616  27.933  12.236  1.00 72.52           C  
ANISOU 2234  CE1 PHE L  90     9887  11151   6519   -125  -1157   1798       C  
ATOM   2235  CE2 PHE L  90      19.913  26.146  12.183  1.00 73.22           C  
ANISOU 2235  CE2 PHE L  90    10063  11207   6549    -94  -1312    998       C  
ATOM   2236  CZ  PHE L  90      20.635  27.197  11.524  1.00 74.81           C  
ANISOU 2236  CZ  PHE L  90    10170  11692   6564    -90  -1313   1515       C  
ATOM   2237  N   THR L  91      24.591  27.377  14.620  1.00 64.74           N  
ANISOU 2237  N   THR L  91     9137   9559   5901   -118   -578   1545       N  
ATOM   2238  CA  THR L  91      25.193  28.364  13.720  1.00 66.97           C  
ANISOU 2238  CA  THR L  91     9272  10158   6016   -143   -600   2043       C  
ATOM   2239  C   THR L  91      24.601  28.205  12.307  1.00 71.45           C  
ANISOU 2239  C   THR L  91     9766  11253   6129   -118   -739   2132       C  
ATOM   2240  O   THR L  91      24.122  27.114  11.943  1.00 72.23           O  
ANISOU 2240  O   THR L  91     9940  11539   5965    -59   -771   1714       O  
ATOM   2241  CB  THR L  91      26.712  28.110  13.595  1.00 67.68           C  
ANISOU 2241  CB  THR L  91     9367  10466   5882   -116   -386   2073       C  
ATOM   2242  OG1 THR L  91      27.304  29.077  12.719  1.00 71.28           O  
ANISOU 2242  OG1 THR L  91     9650  11254   6180   -164   -389   2610       O  
ATOM   2243  CG2 THR L  91      26.967  26.716  13.006  1.00 68.65           C  
ANISOU 2243  CG2 THR L  91     9579  10958   5548    -21   -305   1637       C  
ATOM   2244  N   MET L  92      24.638  29.275  11.509  1.00 74.37           N  
ANISOU 2244  N   MET L  92     9974  11868   6415   -160   -838   2676       N  
ATOM   2245  CA  MET L  92      24.155  29.205  10.143  1.00 78.50           C  
ANISOU 2245  CA  MET L  92    10407  12969   6448   -127   -976   2821       C  
ATOM   2246  C   MET L  92      25.342  28.897   9.181  1.00 81.39           C  
ANISOU 2246  C   MET L  92    10712  13977   6233    -87   -809   2931       C  
ATOM   2247  O   MET L  92      25.239  29.075   7.958  1.00 85.63           O  
ANISOU 2247  O   MET L  92    11127  15120   6289    -64   -889   3194       O  
ATOM   2248  CB  MET L  92      23.427  30.518   9.766  1.00 82.04           C  
ANISOU 2248  CB  MET L  92    10694  13360   7116   -189  -1206   3393       C  
ATOM   2249  CG  MET L  92      22.079  30.371   8.966  1.00 85.09           C  
ANISOU 2249  CG  MET L  92    11034  14003   7294   -147  -1469   3341       C  
ATOM   2250  SD  MET L  92      20.601  30.005  10.003  1.00 85.77           S  
ANISOU 2250  SD  MET L  92    11204  13488   7897   -142  -1616   2852       S  
ATOM   2251  CE  MET L  92      19.245  30.170   8.818  1.00 86.28           C  
ANISOU 2251  CE  MET L  92    11137  13944   7701   -102  -1950   2980       C  
ATOM   2252  N   SER L  93      26.447  28.395   9.736  1.00 79.69           N  
ANISOU 2252  N   SER L  93    10570  13669   6040    -66   -577   2707       N  
ATOM   2253  CA  SER L  93      27.684  28.100   8.970  1.00 82.61           C  
ANISOU 2253  CA  SER L  93    10858  14616   5913    -21   -384   2769       C  
ATOM   2254  C   SER L  93      28.159  26.607   8.920  1.00 81.96           C  
ANISOU 2254  C   SER L  93    10885  14738   5519    113   -250   2090       C  
ATOM   2255  O   SER L  93      28.423  26.031   9.990  1.00 77.16           O  
ANISOU 2255  O   SER L  93    10419  13642   5256    131   -162   1731       O  
ATOM   2256  CB  SER L  93      28.835  28.905   9.624  1.00 81.36           C  
ANISOU 2256  CB  SER L  93    10634  14189   6091   -107   -217   3137       C  
ATOM   2257  OG  SER L  93      29.991  28.961   8.807  1.00 84.80           O  
ANISOU 2257  OG  SER L  93    10921  15206   6091    -99    -38   3376       O  
ATOM   2258  N   GLY L  94      28.198  25.901   7.776  1.00 85.52           N  
ANISOU 2258  N   GLY L  94    11271  15861   5363    221   -257   1853       N  
ATOM   2259  CA  GLY L  94      27.114  25.558   6.875  1.00 88.28           C  
ANISOU 2259  CA  GLY L  94    11590  16583   5370    280   -470   1681       C  
ATOM   2260  C   GLY L  94      25.993  24.807   7.599  1.00 85.51           C  
ANISOU 2260  C   GLY L  94    11401  15687   5401    290   -625   1172       C  
ATOM   2261  O   GLY L  94      25.876  23.571   7.553  1.00 85.69           O  
ANISOU 2261  O   GLY L  94    11496  15737   5325    391   -638    546       O  
ATOM   2262  N   ASN L  95      25.178  25.595   8.295  1.00 82.97           N  
ANISOU 2262  N   ASN L  95    11112  14852   5562    181   -745   1458       N  
ATOM   2263  CA  ASN L  95      23.891  25.165   8.824  1.00 80.34           C  
ANISOU 2263  CA  ASN L  95    10869  14093   5564    164   -920   1128       C  
ATOM   2264  C   ASN L  95      24.079  24.161   9.947  1.00 76.29           C  
ANISOU 2264  C   ASN L  95    10520  13065   5401    176   -802    629       C  
ATOM   2265  O   ASN L  95      23.187  23.359  10.233  1.00 74.89           O  
ANISOU 2265  O   ASN L  95    10409  12647   5399    180   -910    217       O  
ATOM   2266  CB  ASN L  95      23.033  24.586   7.695  1.00 84.67           C  
ANISOU 2266  CB  ASN L  95    11348  15134   5688    243  -1125    854       C  
ATOM   2267  CG  ASN L  95      21.587  25.076   7.734  1.00 84.80           C  
ANISOU 2267  CG  ASN L  95    11326  14936   5960    184  -1380    977       C  
ATOM   2268  OD1 ASN L  95      20.861  24.854   8.707  1.00 82.08           O  
ANISOU 2268  OD1 ASN L  95    11064  14014   6110    127  -1419    765       O  
ATOM   2269  ND2 ASN L  95      21.151  25.703   6.647  1.00 88.09           N  
ANISOU 2269  ND2 ASN L  95    11598  15859   6015    204  -1558   1317       N  
ATOM   2270  N   GLY L  96      25.239  24.252  10.603  1.00 74.11           N  
ANISOU 2270  N   GLY L  96    10292  12614   5253    171   -589    712       N  
ATOM   2271  CA  GLY L  96      25.642  23.307  11.629  1.00 70.99           C  
ANISOU 2271  CA  GLY L  96    10043  11795   5137    197   -466    303       C  
ATOM   2272  C   GLY L  96      25.459  23.814  13.035  1.00 66.92           C  
ANISOU 2272  C   GLY L  96     9606  10654   5167    107   -424    451       C  
ATOM   2273  O   GLY L  96      24.498  24.525  13.310  1.00 66.44           O  
ANISOU 2273  O   GLY L  96     9512  10379   5356     33   -549    650       O  
ATOM   2274  N   THR L  97      26.387  23.444  13.914  1.00 63.97           N  
ANISOU 2274  N   THR L  97     9318  10021   4965    130   -256    332       N  
ATOM   2275  CA  THR L  97      26.286  23.691  15.343  1.00 60.15           C  
ANISOU 2275  CA  THR L  97     8915   8989   4948     72   -205    368       C  
ATOM   2276  C   THR L  97      27.644  24.173  15.800  1.00 59.11           C  
ANISOU 2276  C   THR L  97     8770   8822   4869     87    -42    563       C  
ATOM   2277  O   THR L  97      28.662  23.821  15.225  1.00 60.85           O  
ANISOU 2277  O   THR L  97     8961   9353   4806    156     62    512       O  
ATOM   2278  CB  THR L  97      25.919  22.375  16.115  1.00 58.79           C  
ANISOU 2278  CB  THR L  97     8881   8495   4962     93   -191    -78       C  
ATOM   2279  OG1 THR L  97      24.611  21.929  15.747  1.00 59.90           O  
ANISOU 2279  OG1 THR L  97     9010   8629   5120     60   -351   -267       O  
ATOM   2280  CG2 THR L  97      25.933  22.584  17.611  1.00 55.55           C  
ANISOU 2280  CG2 THR L  97     8541   7616   4949     47   -115    -25       C  
ATOM   2281  N   VAL L  98      27.683  24.961  16.854  1.00 57.13           N  
ANISOU 2281  N   VAL L  98     8517   8203   4986     32    -21    749       N  
ATOM   2282  CA  VAL L  98      28.963  25.442  17.352  1.00 56.69           C  
ANISOU 2282  CA  VAL L  98     8428   8084   5027     44    111    908       C  
ATOM   2283  C   VAL L  98      29.097  25.138  18.828  1.00 53.46           C  
ANISOU 2283  C   VAL L  98     8125   7248   4940     59    170    717       C  
ATOM   2284  O   VAL L  98      28.108  25.171  19.541  1.00 52.45           O  
ANISOU 2284  O   VAL L  98     8037   6851   5040     23     99    639       O  
ATOM   2285  CB  VAL L  98      29.149  26.951  17.087  1.00 58.03           C  
ANISOU 2285  CB  VAL L  98     8431   8285   5334    -33     63   1388       C  
ATOM   2286  CG1 VAL L  98      28.179  27.769  17.899  1.00 56.46           C  
ANISOU 2286  CG1 VAL L  98     8205   7695   5554    -90    -64   1477       C  
ATOM   2287  CG2 VAL L  98      30.566  27.350  17.401  1.00 58.93           C  
ANISOU 2287  CG2 VAL L  98     8477   8394   5520    -27    199   1535       C  
ATOM   2288  N   PHE L  99      30.300  24.793  19.276  1.00 52.53           N  
ANISOU 2288  N   PHE L  99     8038   7107   4815    119    298    636       N  
ATOM   2289  CA  PHE L  99      30.511  24.384  20.662  1.00 50.07           C  
ANISOU 2289  CA  PHE L  99     7827   6451   4745    151    349    457       C  
ATOM   2290  C   PHE L  99      31.340  25.431  21.410  1.00 49.34           C  
ANISOU 2290  C   PHE L  99     7644   6216   4887    141    385    652       C  
ATOM   2291  O   PHE L  99      32.209  26.052  20.851  1.00 51.02           O  
ANISOU 2291  O   PHE L  99     7737   6603   5046    130    424    861       O  
ATOM   2292  CB  PHE L  99      31.238  23.031  20.739  1.00 49.96           C  
ANISOU 2292  CB  PHE L  99     7921   6470   4591    251    435    163       C  
ATOM   2293  CG  PHE L  99      30.371  21.837  20.436  1.00 51.15           C  
ANISOU 2293  CG  PHE L  99     8171   6600   4664    265    376   -116       C  
ATOM   2294  CD1 PHE L  99      30.379  21.253  19.174  1.00 53.66           C  
ANISOU 2294  CD1 PHE L  99     8460   7236   4693    310    350   -267       C  
ATOM   2295  CD2 PHE L  99      29.591  21.260  21.421  1.00 49.50           C  
ANISOU 2295  CD2 PHE L  99     8061   6072   4674    235    346   -241       C  
ATOM   2296  CE1 PHE L  99      29.579  20.144  18.902  1.00 54.47           C  
ANISOU 2296  CE1 PHE L  99     8630   7283   4784    323    266   -570       C  
ATOM   2297  CE2 PHE L  99      28.805  20.156  21.162  1.00 49.97           C  
ANISOU 2297  CE2 PHE L  99     8185   6068   4734    227    281   -481       C  
ATOM   2298  CZ  PHE L  99      28.793  19.597  19.905  1.00 52.74           C  
ANISOU 2298  CZ  PHE L  99     8505   6681   4852    272    229   -664       C  
ATOM   2299  N   GLY L 100      31.094  25.625  22.691  1.00 48.17           N  
ANISOU 2299  N   GLY L 100     7529   5771   5002    144    369    574       N  
ATOM   2300  CA  GLY L 100      32.056  26.357  23.490  1.00 47.86           C  
ANISOU 2300  CA  GLY L 100     7410   5607   5169    167    398    646       C  
ATOM   2301  C   GLY L 100      33.358  25.578  23.589  1.00 47.55           C  
ANISOU 2301  C   GLY L 100     7418   5658   4990    253    511    530       C  
ATOM   2302  O   GLY L 100      33.432  24.420  23.199  1.00 48.83           O  
ANISOU 2302  O   GLY L 100     7688   5929   4937    307    559    358       O  
ATOM   2303  N   GLY L 101      34.407  26.208  24.084  1.00 47.01           N  
ANISOU 2303  N   GLY L 101     7250   5537   5076    274    537    601       N  
ATOM   2304  CA  GLY L 101      35.669  25.501  24.240  1.00 47.11           C  
ANISOU 2304  CA  GLY L 101     7285   5629   4985    368    633    481       C  
ATOM   2305  C   GLY L 101      35.640  24.546  25.426  1.00 46.14           C  
ANISOU 2305  C   GLY L 101     7317   5327   4889    460    637    237       C  
ATOM   2306  O   GLY L 101      36.610  23.859  25.699  1.00 46.03           O  
ANISOU 2306  O   GLY L 101     7335   5334   4821    557    691    121       O  
ATOM   2307  N   GLY L 102      34.524  24.534  26.143  1.00 45.16           N  
ANISOU 2307  N   GLY L 102     7267   5039   4854    430    579    185       N  
ATOM   2308  CA  GLY L 102      34.304  23.589  27.222  1.00 44.95           C  
ANISOU 2308  CA  GLY L 102     7378   4879   4823    494    587     23       C  
ATOM   2309  C   GLY L 102      34.991  23.989  28.496  1.00 45.03           C  
ANISOU 2309  C   GLY L 102     7345   4806   4960    564    574    -16       C  
ATOM   2310  O   GLY L 102      36.040  24.601  28.456  1.00 46.36           O  
ANISOU 2310  O   GLY L 102     7398   5013   5202    594    576     21       O  
ATOM   2311  N   THR L 103      34.409  23.631  29.638  1.00 44.63           N  
ANISOU 2311  N   THR L 103     7366   4669   4923    589    561    -90       N  
ATOM   2312  CA  THR L 103      35.029  23.946  30.931  1.00 43.91           C  
ANISOU 2312  CA  THR L 103     7229   4561   4894    677    536   -157       C  
ATOM   2313  C   THR L 103      35.155  22.744  31.874  1.00 43.85           C  
ANISOU 2313  C   THR L 103     7356   4538   4765    760    560   -200       C  
ATOM   2314  O   THR L 103      34.270  21.913  31.953  1.00 44.52           O  
ANISOU 2314  O   THR L 103     7548   4581   4787    717    585   -171       O  
ATOM   2315  CB  THR L 103      34.333  25.158  31.652  1.00 43.58           C  
ANISOU 2315  CB  THR L 103     7055   4496   5008    650    469   -201       C  
ATOM   2316  OG1 THR L 103      33.714  24.737  32.864  1.00 43.65           O  
ANISOU 2316  OG1 THR L 103     7114   4541   4929    692    480   -280       O  
ATOM   2317  CG2 THR L 103      33.304  25.815  30.795  1.00 43.51           C  
ANISOU 2317  CG2 THR L 103     6986   4450   5095    538    439   -124       C  
ATOM   2318  N   LYS L 104      36.259  22.644  32.594  1.00 43.93           N  
ANISOU 2318  N   LYS L 104     7345   4578   4767    875    540   -244       N  
ATOM   2319  CA  LYS L 104      36.455  21.501  33.477  1.00 44.72           C  
ANISOU 2319  CA  LYS L 104     7564   4666   4761    962    542   -228       C  
ATOM   2320  C   LYS L 104      35.978  21.794  34.880  1.00 45.63           C  
ANISOU 2320  C   LYS L 104     7648   4879   4809    994    518   -239       C  
ATOM   2321  O   LYS L 104      36.451  22.729  35.510  1.00 46.37           O  
ANISOU 2321  O   LYS L 104     7614   5064   4939   1057    463   -344       O  
ATOM   2322  CB  LYS L 104      37.934  21.100  33.486  1.00 45.59           C  
ANISOU 2322  CB  LYS L 104     7664   4781   4878   1090    520   -267       C  
ATOM   2323  CG  LYS L 104      38.367  20.259  34.661  1.00 47.38           C  
ANISOU 2323  CG  LYS L 104     7962   5016   5025   1212    477   -232       C  
ATOM   2324  CD  LYS L 104      39.792  19.722  34.530  1.00 48.64           C  
ANISOU 2324  CD  LYS L 104     8108   5152   5220   1349    442   -278       C  
ATOM   2325  CE  LYS L 104      40.013  18.495  35.456  1.00 50.81           C  
ANISOU 2325  CE  LYS L 104     8494   5371   5440   1460    386   -176       C  
ATOM   2326  NZ  LYS L 104      41.220  17.692  35.019  1.00 52.49           N  
ANISOU 2326  NZ  LYS L 104     8709   5493   5741   1592    348   -234       N  
ATOM   2327  N   LEU L 105      35.031  21.005  35.371  1.00 45.98           N  
ANISOU 2327  N   LEU L 105     7787   4924   4761    951    556   -141       N  
ATOM   2328  CA  LEU L 105      34.465  21.232  36.692  1.00 46.15           C  
ANISOU 2328  CA  LEU L 105     7758   5119   4657    978    561   -134       C  
ATOM   2329  C   LEU L 105      35.180  20.360  37.681  1.00 47.38           C  
ANISOU 2329  C   LEU L 105     7978   5352   4672   1095    536    -29       C  
ATOM   2330  O   LEU L 105      35.038  19.144  37.654  1.00 48.96           O  
ANISOU 2330  O   LEU L 105     8302   5441   4859   1073    557    151       O  
ATOM   2331  CB  LEU L 105      32.982  20.859  36.731  1.00 46.87           C  
ANISOU 2331  CB  LEU L 105     7880   5212   4715    849    633    -37       C  
ATOM   2332  CG  LEU L 105      32.072  21.443  37.835  1.00 47.41           C  
ANISOU 2332  CG  LEU L 105     7832   5521   4662    846    666    -81       C  
ATOM   2333  CD1 LEU L 105      31.048  20.464  38.321  1.00 47.38           C  
ANISOU 2333  CD1 LEU L 105     7881   5570   4552    756    755    124       C  
ATOM   2334  CD2 LEU L 105      32.839  21.999  38.978  1.00 47.70           C  
ANISOU 2334  CD2 LEU L 105     7771   5788   4564    999    612   -201       C  
ATOM   2335  N   THR L 106      35.949  20.968  38.562  1.00 48.03           N  
ANISOU 2335  N   THR L 106     7964   5613   4674   1223    470   -140       N  
ATOM   2336  CA  THR L 106      36.567  20.232  39.655  1.00 50.40           C  
ANISOU 2336  CA  THR L 106     8303   6051   4794   1351    427    -24       C  
ATOM   2337  C   THR L 106      35.809  20.335  40.995  1.00 52.34           C  
ANISOU 2337  C   THR L 106     8488   6621   4780   1375    454     27       C  
ATOM   2338  O   THR L 106      35.476  21.432  41.446  1.00 51.39           O  
ANISOU 2338  O   THR L 106     8216   6700   4609   1399    441   -195       O  
ATOM   2339  CB  THR L 106      37.982  20.703  39.898  1.00 50.23           C  
ANISOU 2339  CB  THR L 106     8198   6083   4803   1502    319   -180       C  
ATOM   2340  OG1 THR L 106      38.749  20.409  38.741  1.00 49.92           O  
ANISOU 2340  OG1 THR L 106     8205   5804   4960   1492    316   -190       O  
ATOM   2341  CG2 THR L 106      38.570  19.989  41.094  1.00 51.99           C  
ANISOU 2341  CG2 THR L 106     8449   6490   4814   1649    250    -53       C  
ATOM   2342  N   VAL L 107      35.542  19.188  41.623  1.00 54.05           N  
ANISOU 2342  N   VAL L 107     8799   6895   4842   1371    486    323       N  
ATOM   2343  CA  VAL L 107      34.913  19.177  42.918  1.00 55.77           C  
ANISOU 2343  CA  VAL L 107     8944   7494   4753   1398    529    429       C  
ATOM   2344  C   VAL L 107      35.996  18.924  43.957  1.00 57.97           C  
ANISOU 2344  C   VAL L 107     9204   8007   4813   1586    420    489       C  
ATOM   2345  O   VAL L 107      36.411  17.788  44.221  1.00 59.69           O  
ANISOU 2345  O   VAL L 107     9531   8150   4998   1620    385    803       O  
ATOM   2346  CB  VAL L 107      33.763  18.167  42.988  1.00 57.42           C  
ANISOU 2346  CB  VAL L 107     9226   7661   4929   1241    646    772       C  
ATOM   2347  CG1 VAL L 107      33.405  17.858  44.429  1.00 61.09           C  
ANISOU 2347  CG1 VAL L 107     9620   8567   5026   1287    691   1001       C  
ATOM   2348  CG2 VAL L 107      32.554  18.732  42.266  1.00 55.56           C  
ANISOU 2348  CG2 VAL L 107     8938   7340   4831   1082    742    636       C  
ATOM   2349  N   LEU L 108      36.473  20.023  44.522  1.00 58.80           N  
ANISOU 2349  N   LEU L 108     9155   8378   4807   1717    341    166       N  
ATOM   2350  CA  LEU L 108      37.619  20.037  45.440  1.00 61.06           C  
ANISOU 2350  CA  LEU L 108     9386   8910   4904   1920    200    114       C  
ATOM   2351  C   LEU L 108      37.649  18.917  46.451  1.00 64.24           C  
ANISOU 2351  C   LEU L 108     9856   9558   4996   1982    193    513       C  
ATOM   2352  O   LEU L 108      36.919  18.944  47.440  1.00 67.27           O  
ANISOU 2352  O   LEU L 108    10160  10369   5033   1992    257    611       O  
ATOM   2353  CB  LEU L 108      37.659  21.352  46.214  1.00 61.78           C  
ANISOU 2353  CB  LEU L 108     9257   9372   4844   2037    131   -297       C  
ATOM   2354  CG  LEU L 108      37.904  22.649  45.453  1.00 59.46           C  
ANISOU 2354  CG  LEU L 108     8838   8861   4893   2018     72   -711       C  
ATOM   2355  CD1 LEU L 108      37.651  23.754  46.412  1.00 61.19           C  
ANISOU 2355  CD1 LEU L 108     8827   9468   4953   2133      3  -1095       C  
ATOM   2356  CD2 LEU L 108      39.310  22.756  44.888  1.00 57.48           C  
ANISOU 2356  CD2 LEU L 108     8589   8351   4898   2086    -52   -803       C  
ATOM   2357  N   GLY L 109      38.542  17.960  46.244  1.00 65.08           N  
ANISOU 2357  N   GLY L 109    10084   9423   5221   2040    107    745       N  
ATOM   2358  CA  GLY L 109      38.713  16.883  47.211  1.00 67.68           C  
ANISOU 2358  CA  GLY L 109    10466   9947   5301   2115     59   1173       C  
ATOM   2359  C   GLY L 109      39.931  17.093  48.072  1.00 69.73           C  
ANISOU 2359  C   GLY L 109    10643  10496   5355   2352   -125   1070       C  
ATOM   2360  O   GLY L 109      40.265  16.233  48.880  1.00 74.06           O  
ANISOU 2360  O   GLY L 109    11226  11216   5696   2447   -205   1435       O  
ATOM   2361  N   GLN L 110      40.626  18.209  47.885  1.00 68.14           N  
ANISOU 2361  N   GLN L 110    10318  10329   5240   2446   -211    595       N  
ATOM   2362  CA  GLN L 110      41.802  18.534  48.696  1.00 70.31           C  
ANISOU 2362  CA  GLN L 110    10477  10890   5346   2675   -408    419       C  
ATOM   2363  C   GLN L 110      42.045  20.023  48.661  1.00 69.19           C  
ANISOU 2363  C   GLN L 110    10140  10870   5279   2725   -465   -146       C  
ATOM   2364  O   GLN L 110      41.376  20.733  47.928  1.00 66.63           O  
ANISOU 2364  O   GLN L 110     9787  10357   5171   2583   -358   -351       O  
ATOM   2365  CB  GLN L 110      43.060  17.798  48.222  1.00 70.27           C  
ANISOU 2365  CB  GLN L 110    10552  10541   5606   2769   -541    531       C  
ATOM   2366  CG  GLN L 110      43.446  18.064  46.777  1.00 67.27           C  
ANISOU 2366  CG  GLN L 110    10202   9659   5697   2673   -497    311       C  
ATOM   2367  CD  GLN L 110      44.831  17.535  46.414  1.00 67.49           C  
ANISOU 2367  CD  GLN L 110    10238   9449   5956   2808   -638    311       C  
ATOM   2368  OE1 GLN L 110      45.843  18.027  46.902  1.00 67.98           O  
ANISOU 2368  OE1 GLN L 110    10160   9693   5977   2972   -794     89       O  
ATOM   2369  NE2 GLN L 110      44.874  16.549  45.525  1.00 67.35           N  
ANISOU 2369  NE2 GLN L 110    10361   9022   6208   2745   -590    517       N  
ATOM   2370  N   PRO L 111      43.003  20.513  49.467  1.00 71.84           N  
ANISOU 2370  N   PRO L 111    10322  11511   5463   2930   -657   -401       N  
ATOM   2371  CA  PRO L 111      43.248  21.964  49.432  1.00 70.66           C  
ANISOU 2371  CA  PRO L 111     9953  11422   5471   2971   -740   -967       C  
ATOM   2372  C   PRO L 111      43.909  22.367  48.132  1.00 67.61           C  
ANISOU 2372  C   PRO L 111     9565  10503   5619   2876   -744  -1123       C  
ATOM   2373  O   PRO L 111      44.753  21.642  47.592  1.00 66.90           O  
ANISOU 2373  O   PRO L 111     9571  10140   5706   2894   -776   -934       O  
ATOM   2374  CB  PRO L 111      44.192  22.233  50.619  1.00 73.95           C  
ANISOU 2374  CB  PRO L 111    10200  12290   5607   3222   -971  -1188       C  
ATOM   2375  CG  PRO L 111      44.567  20.863  51.208  1.00 76.80           C  
ANISOU 2375  CG  PRO L 111    10708  12807   5663   3321  -1017   -682       C  
ATOM   2376  CD  PRO L 111      43.970  19.780  50.312  1.00 75.00           C  
ANISOU 2376  CD  PRO L 111    10727  12142   5626   3128   -831   -198       C  
ATOM   2377  N   LYS L 112      43.490  23.526  47.650  1.00 66.02           N  
ANISOU 2377  N   LYS L 112     9235  10179   5671   2781   -712  -1457       N  
ATOM   2378  CA  LYS L 112      43.909  24.115  46.387  1.00 63.01           C  
ANISOU 2378  CA  LYS L 112     8814   9341   5784   2657   -692  -1584       C  
ATOM   2379  C   LYS L 112      45.362  24.549  46.415  1.00 63.71           C  
ANISOU 2379  C   LYS L 112     8737   9374   6097   2774   -875  -1818       C  
ATOM   2380  O   LYS L 112      45.804  25.132  47.375  1.00 66.19           O  
ANISOU 2380  O   LYS L 112     8865   9981   6303   2929  -1051  -2122       O  
ATOM   2381  CB  LYS L 112      42.971  25.281  46.147  1.00 62.28           C  
ANISOU 2381  CB  LYS L 112     8595   9206   5862   2549   -646  -1853       C  
ATOM   2382  CG  LYS L 112      43.444  26.478  45.383  1.00 62.15           C  
ANISOU 2382  CG  LYS L 112     8392   8886   6338   2478   -720  -2139       C  
ATOM   2383  CD  LYS L 112      42.273  27.525  45.398  1.00 62.69           C  
ANISOU 2383  CD  LYS L 112     8336   8959   6525   2402   -695  -2380       C  
ATOM   2384  CE  LYS L 112      40.901  26.811  45.194  1.00 61.96           C  
ANISOU 2384  CE  LYS L 112     8446   8910   6187   2287   -489  -2083       C  
ATOM   2385  NZ  LYS L 112      39.730  27.731  44.963  1.00 61.24           N  
ANISOU 2385  NZ  LYS L 112     8248   8758   6265   2194   -447  -2268       N  
ATOM   2386  N   ALA L 113      46.109  24.235  45.359  1.00 62.27           N  
ANISOU 2386  N   ALA L 113     8603   8841   6217   2706   -835  -1690       N  
ATOM   2387  CA  ALA L 113      47.580  24.358  45.374  1.00 63.56           C  
ANISOU 2387  CA  ALA L 113     8616   8961   6571   2821   -990  -1834       C  
ATOM   2388  C   ALA L 113      48.153  24.944  44.077  1.00 62.02           C  
ANISOU 2388  C   ALA L 113     8315   8401   6847   2679   -932  -1894       C  
ATOM   2389  O   ALA L 113      47.896  24.424  42.961  1.00 60.48           O  
ANISOU 2389  O   ALA L 113     8266   7961   6752   2546   -759  -1652       O  
ATOM   2390  CB  ALA L 113      48.233  22.987  45.661  1.00 64.12           C  
ANISOU 2390  CB  ALA L 113     8837   9088   6438   2958  -1028  -1549       C  
ATOM   2391  N   ALA L 114      48.941  26.012  44.220  1.00 62.34           N  
ANISOU 2391  N   ALA L 114     8081   8428   7177   2707  -1080  -2212       N  
ATOM   2392  CA  ALA L 114      49.544  26.663  43.052  1.00 61.37           C  
ANISOU 2392  CA  ALA L 114     7807   7997   7515   2558  -1028  -2230       C  
ATOM   2393  C   ALA L 114      50.697  25.835  42.495  1.00 61.41           C  
ANISOU 2393  C   ALA L 114     7826   7922   7584   2609   -996  -2077       C  
ATOM   2394  O   ALA L 114      51.385  25.153  43.240  1.00 62.85           O  
ANISOU 2394  O   ALA L 114     8022   8273   7584   2796  -1117  -2094       O  
ATOM   2395  CB  ALA L 114      50.010  28.056  43.385  1.00 62.43           C  
ANISOU 2395  CB  ALA L 114     7614   8099   8009   2554  -1208  -2596       C  
ATOM   2396  N   PRO L 115      50.918  25.909  41.174  1.00 60.04           N  
ANISOU 2396  N   PRO L 115     7628   7518   7665   2452   -839  -1931       N  
ATOM   2397  CA  PRO L 115      51.893  25.061  40.481  1.00 59.47           C  
ANISOU 2397  CA  PRO L 115     7566   7390   7640   2497   -768  -1800       C  
ATOM   2398  C   PRO L 115      53.309  25.578  40.630  1.00 60.82           C  
ANISOU 2398  C   PRO L 115     7431   7583   8095   2565   -902  -1995       C  
ATOM   2399  O   PRO L 115      53.499  26.749  40.844  1.00 61.32           O  
ANISOU 2399  O   PRO L 115     7256   7613   8431   2500  -1005  -2190       O  
ATOM   2400  CB  PRO L 115      51.468  25.188  39.024  1.00 57.96           C  
ANISOU 2400  CB  PRO L 115     7413   7024   7585   2290   -546  -1613       C  
ATOM   2401  CG  PRO L 115      50.925  26.599  38.944  1.00 57.43           C  
ANISOU 2401  CG  PRO L 115     7187   6870   7765   2130   -574  -1703       C  
ATOM   2402  CD  PRO L 115      50.203  26.811  40.246  1.00 58.06           C  
ANISOU 2402  CD  PRO L 115     7326   7079   7656   2230   -721  -1878       C  
ATOM   2403  N   SER L 116      54.292  24.696  40.515  1.00 62.02           N  
ANISOU 2403  N   SER L 116     7572   7772   8222   2698   -913  -1954       N  
ATOM   2404  CA  SER L 116      55.688  25.101  40.478  1.00 64.78           C  
ANISOU 2404  CA  SER L 116     7609   8138   8868   2750  -1011  -2119       C  
ATOM   2405  C   SER L 116      56.119  25.141  39.037  1.00 64.32           C  
ANISOU 2405  C   SER L 116     7442   7968   9030   2598   -793  -1981       C  
ATOM   2406  O   SER L 116      55.908  24.177  38.309  1.00 64.54           O  
ANISOU 2406  O   SER L 116     7653   7976   8894   2610   -633  -1813       O  
ATOM   2407  CB  SER L 116      56.569  24.058  41.168  1.00 67.15           C  
ANISOU 2407  CB  SER L 116     7932   8566   9014   3007  -1155  -2156       C  
ATOM   2408  OG  SER L 116      56.093  23.745  42.456  1.00 68.75           O  
ANISOU 2408  OG  SER L 116     8284   8937   8902   3163  -1330  -2192       O  
ATOM   2409  N   VAL L 117      56.793  26.207  38.642  1.00 64.72           N  
ANISOU 2409  N   VAL L 117     7168   7966   9457   2468   -798  -2058       N  
ATOM   2410  CA  VAL L 117      57.202  26.348  37.258  1.00 64.99           C  
ANISOU 2410  CA  VAL L 117     7058   7963   9674   2305   -573  -1886       C  
ATOM   2411  C   VAL L 117      58.711  26.388  37.126  1.00 67.44           C  
ANISOU 2411  C   VAL L 117     7036   8348  10242   2367   -607  -1992       C  
ATOM   2412  O   VAL L 117      59.356  27.274  37.666  1.00 69.58           O  
ANISOU 2412  O   VAL L 117     7020   8588  10830   2347   -774  -2160       O  
ATOM   2413  CB  VAL L 117      56.607  27.639  36.669  1.00 64.49           C  
ANISOU 2413  CB  VAL L 117     6864   7762   9877   2040   -504  -1773       C  
ATOM   2414  CG1 VAL L 117      56.830  27.715  35.198  1.00 64.75           C  
ANISOU 2414  CG1 VAL L 117     6787   7822   9994   1863   -248  -1517       C  
ATOM   2415  CG2 VAL L 117      55.136  27.671  36.939  1.00 63.07           C  
ANISOU 2415  CG2 VAL L 117     6975   7514   9473   2000   -503  -1720       C  
ATOM   2416  N   THR L 118      59.275  25.446  36.393  1.00 67.32           N  
ANISOU 2416  N   THR L 118     7030   8430  10118   2445   -457  -1922       N  
ATOM   2417  CA  THR L 118      60.699  25.508  36.072  1.00 70.78           C  
ANISOU 2417  CA  THR L 118     7112   8969  10814   2482   -440  -2007       C  
ATOM   2418  C   THR L 118      60.851  25.778  34.592  1.00 71.06           C  
ANISOU 2418  C   THR L 118     6982   9084  10932   2279   -147  -1796       C  
ATOM   2419  O   THR L 118      60.200  25.116  33.805  1.00 70.12           O  
ANISOU 2419  O   THR L 118     7085   9018  10538   2264     38  -1664       O  
ATOM   2420  CB  THR L 118      61.427  24.181  36.410  1.00 72.00           C  
ANISOU 2420  CB  THR L 118     7332   9219  10804   2772   -512  -2137       C  
ATOM   2421  OG1 THR L 118      61.584  24.067  37.825  1.00 72.24           O  
ANISOU 2421  OG1 THR L 118     7416   9238  10796   2964   -811  -2312       O  
ATOM   2422  CG2 THR L 118      62.807  24.158  35.784  1.00 74.60           C  
ANISOU 2422  CG2 THR L 118     7286   9683  11377   2797   -425  -2208       C  
ATOM   2423  N   LEU L 119      61.717  26.717  34.214  1.00 72.93           N  
ANISOU 2423  N   LEU L 119     6815   9355  11542   2125   -107  -1761       N  
ATOM   2424  CA  LEU L 119      61.862  27.090  32.810  1.00 74.02           C  
ANISOU 2424  CA  LEU L 119     6756   9626  11741   1906    182  -1496       C  
ATOM   2425  C   LEU L 119      63.277  26.940  32.352  1.00 77.54           C  
ANISOU 2425  C   LEU L 119     6816  10284  12363   1944    282  -1549       C  
ATOM   2426  O   LEU L 119      64.147  27.640  32.850  1.00 80.74           O  
ANISOU 2426  O   LEU L 119     6888  10633  13156   1907    144  -1645       O  
ATOM   2427  CB  LEU L 119      61.483  28.548  32.597  1.00 74.58           C  
ANISOU 2427  CB  LEU L 119     6643   9537  12158   1610    176  -1286       C  
ATOM   2428  CG  LEU L 119      60.958  28.970  31.226  1.00 74.54           C  
ANISOU 2428  CG  LEU L 119     6600   9631  12091   1359    449   -902       C  
ATOM   2429  CD1 LEU L 119      61.180  30.446  31.019  1.00 77.47           C  
ANISOU 2429  CD1 LEU L 119     6610   9846  12977   1076    418   -677       C  
ATOM   2430  CD2 LEU L 119      61.582  28.204  30.107  1.00 75.86           C  
ANISOU 2430  CD2 LEU L 119     6657  10153  12011   1395    728   -813       C  
ATOM   2431  N   PHE L 120      63.511  26.074  31.371  1.00 78.21           N  
ANISOU 2431  N   PHE L 120     6908  10624  12184   2012    521  -1508       N  
ATOM   2432  CA  PHE L 120      64.850  25.903  30.804  1.00 81.76           C  
ANISOU 2432  CA  PHE L 120     6954  11342  12770   2051    661  -1565       C  
ATOM   2433  C   PHE L 120      65.007  26.547  29.428  1.00 83.56           C  
ANISOU 2433  C   PHE L 120     6892  11834  13021   1782    981  -1239       C  
ATOM   2434  O   PHE L 120      64.164  26.348  28.567  1.00 82.11           O  
ANISOU 2434  O   PHE L 120     6906  11774  12518   1703   1167  -1056       O  
ATOM   2435  CB  PHE L 120      65.170  24.422  30.656  1.00 81.86           C  
ANISOU 2435  CB  PHE L 120     7104  11511  12488   2356    703  -1806       C  
ATOM   2436  CG  PHE L 120      65.346  23.699  31.953  1.00 80.83           C  
ANISOU 2436  CG  PHE L 120     7160  11182  12371   2640    394  -2082       C  
ATOM   2437  CD1 PHE L 120      66.544  23.772  32.654  1.00 83.29           C  
ANISOU 2437  CD1 PHE L 120     7172  11505  12971   2772    219  -2284       C  
ATOM   2438  CD2 PHE L 120      64.329  22.910  32.459  1.00 77.84           C  
ANISOU 2438  CD2 PHE L 120     7238  10626  11712   2778    275  -2118       C  
ATOM   2439  CE1 PHE L 120      66.713  23.087  33.848  1.00 82.77           C  
ANISOU 2439  CE1 PHE L 120     7271  11295  12882   3047    -81  -2504       C  
ATOM   2440  CE2 PHE L 120      64.495  22.216  33.648  1.00 77.63           C  
ANISOU 2440  CE2 PHE L 120     7371  10453  11673   3037     -6  -2304       C  
ATOM   2441  CZ  PHE L 120      65.690  22.306  34.343  1.00 80.19           C  
ANISOU 2441  CZ  PHE L 120     7405  10811  12254   3178   -190  -2492       C  
ATOM   2442  N   PRO L 121      66.126  27.265  29.199  1.00 69.52           N  
ANISOU 2442  N   PRO L 121     5942  11084   9386   1267  -1433    469       N  
ATOM   2443  CA  PRO L 121      66.377  27.855  27.885  1.00 68.94           C  
ANISOU 2443  CA  PRO L 121     5944  10822   9427   1111  -1280    354       C  
ATOM   2444  C   PRO L 121      66.817  26.763  26.908  1.00 69.82           C  
ANISOU 2444  C   PRO L 121     5910  10877   9740   1597   -886    570       C  
ATOM   2445  O   PRO L 121      66.955  25.616  27.302  1.00 71.87           O  
ANISOU 2445  O   PRO L 121     6038  11184  10085   2061   -702    820       O  
ATOM   2446  CB  PRO L 121      67.544  28.808  28.165  1.00 73.15           C  
ANISOU 2446  CB  PRO L 121     6072  11922   9800    602  -1499    464       C  
ATOM   2447  CG  PRO L 121      68.315  28.121  29.235  1.00 76.65           C  
ANISOU 2447  CG  PRO L 121     5966  13053  10104    748  -1643    861       C  
ATOM   2448  CD  PRO L 121      67.272  27.458  30.110  1.00 74.30           C  
ANISOU 2448  CD  PRO L 121     5977  12474   9779   1036  -1682    780       C  
ATOM   2449  N   PRO L 122      67.048  27.107  25.637  1.00 69.31           N  
ANISOU 2449  N   PRO L 122     5907  10681   9745   1498   -693    486       N  
ATOM   2450  CA  PRO L 122      67.591  26.110  24.741  1.00 71.16           C  
ANISOU 2450  CA  PRO L 122     6026  10882  10128   1914   -241    654       C  
ATOM   2451  C   PRO L 122      69.010  25.792  25.146  1.00 76.58           C  
ANISOU 2451  C   PRO L 122     6036  12194  10868   2145   -179   1138       C  
ATOM   2452  O   PRO L 122      69.778  26.688  25.490  1.00 78.85           O  
ANISOU 2452  O   PRO L 122     5910  13021  11030   1750   -484   1276       O  
ATOM   2453  CB  PRO L 122      67.617  26.822  23.389  1.00 70.79           C  
ANISOU 2453  CB  PRO L 122     6131  10710  10055   1622   -128    472       C  
ATOM   2454  CG  PRO L 122      66.695  27.951  23.512  1.00 67.50           C  
ANISOU 2454  CG  PRO L 122     6045  10071   9529   1195   -454    214       C  
ATOM   2455  CD  PRO L 122      66.765  28.372  24.947  1.00 68.46           C  
ANISOU 2455  CD  PRO L 122     6031  10400   9582   1037   -805    252       C  
ATOM   2456  N   SER L 123      69.359  24.516  25.106  1.00 79.81           N  
ANISOU 2456  N   SER L 123     6326  12548  11452   2768    258   1430       N  
ATOM   2457  CA  SER L 123      70.719  24.097  25.395  1.00 86.61           C  
ANISOU 2457  CA  SER L 123     6455  14055  12398   3148    419   2038       C  
ATOM   2458  C   SER L 123      71.644  24.673  24.339  1.00 89.56           C  
ANISOU 2458  C   SER L 123     6515  14733  12780   2967    568   2100       C  
ATOM   2459  O   SER L 123      71.179  24.991  23.232  1.00 87.18           O  
ANISOU 2459  O   SER L 123     6673  13979  12472   2740    729   1687       O  
ATOM   2460  CB  SER L 123      70.813  22.572  25.357  1.00 90.28           C  
ANISOU 2460  CB  SER L 123     6997  14184  13124   3966   1054   2344       C  
ATOM   2461  OG  SER L 123      70.829  22.086  24.019  1.00 91.19           O  
ANISOU 2461  OG  SER L 123     7483  13782  13381   4169   1678   2119       O  
ATOM   2462  N   SER L 124      72.939  24.792  24.650  1.00 95.05           N  
ANISOU 2462  N   SER L 124     6392  16271  13453   3047    520   2656       N  
ATOM   2463  CA  SER L 124      73.873  25.291  23.652  1.00 97.93           C  
ANISOU 2463  CA  SER L 124     6400  16987  13824   2885    699   2766       C  
ATOM   2464  C   SER L 124      74.122  24.193  22.633  1.00100.49           C  
ANISOU 2464  C   SER L 124     6864  16906  14410   3605   1503   2870       C  
ATOM   2465  O   SER L 124      74.499  24.471  21.486  1.00102.09           O  
ANISOU 2465  O   SER L 124     7096  17075  14620   3492   1794   2745       O  
ATOM   2466  CB  SER L 124      75.177  25.816  24.269  1.00104.45           C  
ANISOU 2466  CB  SER L 124     6244  18957  14484   2637    386   3342       C  
ATOM   2467  OG  SER L 124      75.924  24.791  24.902  1.00110.56           O  
ANISOU 2467  OG  SER L 124     6344  20289  15373   3374    632   4081       O  
ATOM   2468  N   GLU L 125      73.874  22.950  23.039  1.00101.76           N  
ANISOU 2468  N   GLU L 125     7191  16700  14773   4314   1918   3068       N  
ATOM   2469  CA  GLU L 125      74.018  21.827  22.123  1.00105.51           C  
ANISOU 2469  CA  GLU L 125     7983  16606  15499   4983   2819   3084       C  
ATOM   2470  C   GLU L 125      72.944  21.837  21.039  1.00100.47           C  
ANISOU 2470  C   GLU L 125     8293  15118  14764   4609   3029   2295       C  
ATOM   2471  O   GLU L 125      73.236  21.656  19.866  1.00102.48           O  
ANISOU 2471  O   GLU L 125     8740  15169  15026   4667   3568   2124       O  
ATOM   2472  CB  GLU L 125      74.003  20.508  22.874  1.00109.33           C  
ANISOU 2472  CB  GLU L 125     8489  16812  16239   5813   3284   3516       C  
ATOM   2473  CG  GLU L 125      74.100  19.295  21.973  1.00114.71           C  
ANISOU 2473  CG  GLU L 125     9667  16721  17195   6493   4362   3471       C  
ATOM   2474  CD  GLU L 125      74.331  18.017  22.768  1.00121.92           C  
ANISOU 2474  CD  GLU L 125    10493  17400  18432   7437   4932   4097       C  
ATOM   2475  OE1 GLU L 125      74.349  18.112  24.017  1.00122.01           O  
ANISOU 2475  OE1 GLU L 125    10021  17937  18401   7506   4386   4562       O  
ATOM   2476  OE2 GLU L 125      74.502  16.925  22.163  1.00127.83           O  
ANISOU 2476  OE2 GLU L 125    11677  17431  19461   8103   5965   4144       O  
ATOM   2477  N   GLU L 126      71.699  22.066  21.426  1.00 94.55           N  
ANISOU 2477  N   GLU L 126     8091  13961  13872   4195   2601   1845       N  
ATOM   2478  CA  GLU L 126      70.629  22.191  20.442  1.00 90.33           C  
ANISOU 2478  CA  GLU L 126     8324  12840  13158   3744   2683   1185       C  
ATOM   2479  C   GLU L 126      70.827  23.419  19.551  1.00 88.67           C  
ANISOU 2479  C   GLU L 126     7989  12951  12750   3161   2391   1010       C  
ATOM   2480  O   GLU L 126      70.523  23.391  18.355  1.00 88.55           O  
ANISOU 2480  O   GLU L 126     8381  12678  12586   2939   2702    667       O  
ATOM   2481  CB  GLU L 126      69.254  22.257  21.119  1.00 84.46           C  
ANISOU 2481  CB  GLU L 126     8055  11741  12295   3441   2248    852       C  
ATOM   2482  CG  GLU L 126      68.093  22.117  20.131  1.00 81.86           C  
ANISOU 2482  CG  GLU L 126     8459  10900  11745   3035   2409    272       C  
ATOM   2483  CD  GLU L 126      66.695  22.379  20.736  1.00 77.25           C  
ANISOU 2483  CD  GLU L 126     8224  10120  11008   2682   1920      3       C  
ATOM   2484  OE1 GLU L 126      66.584  23.079  21.770  1.00 74.54           O  
ANISOU 2484  OE1 GLU L 126     7596  10037  10689   2608   1363    163       O  
ATOM   2485  OE2 GLU L 126      65.695  21.906  20.143  1.00 75.95           O  
ANISOU 2485  OE2 GLU L 126     8616   9587  10654   2425   2117   -379       O  
ATOM   2486  N   LEU L 127      71.325  24.503  20.135  1.00 87.77           N  
ANISOU 2486  N   LEU L 127     7346  13408  12594   2850   1815   1246       N  
ATOM   2487  CA  LEU L 127      71.514  25.716  19.370  1.00 86.40           C  
ANISOU 2487  CA  LEU L 127     7096  13470  12262   2280   1566   1125       C  
ATOM   2488  C   LEU L 127      72.478  25.459  18.210  1.00 91.67           C  
ANISOU 2488  C   LEU L 127     7546  14331  12954   2460   2126   1261       C  
ATOM   2489  O   LEU L 127      72.268  25.951  17.099  1.00 91.12           O  
ANISOU 2489  O   LEU L 127     7739  14165  12717   2101   2213   1012       O  
ATOM   2490  CB  LEU L 127      71.977  26.864  20.270  1.00 85.98           C  
ANISOU 2490  CB  LEU L 127     6573  13946  12150   1850    953   1333       C  
ATOM   2491  CG  LEU L 127      70.883  27.516  21.129  1.00 81.17           C  
ANISOU 2491  CG  LEU L 127     6338  13060  11443   1480    427   1056       C  
ATOM   2492  CD1 LEU L 127      71.469  28.617  22.022  1.00 82.74           C  
ANISOU 2492  CD1 LEU L 127     6145  13759  11532    967    -59   1201       C  
ATOM   2493  CD2 LEU L 127      69.742  28.065  20.264  1.00 76.32           C  
ANISOU 2493  CD2 LEU L 127     6342  11932  10724   1168    393    661       C  
ATOM   2494  N   GLN L 128      73.515  24.663  18.455  1.00 97.20           N  
ANISOU 2494  N   GLN L 128     7752  15328  13852   3059   2551   1704       N  
ATOM   2495  CA  GLN L 128      74.483  24.343  17.404  1.00102.88           C  
ANISOU 2495  CA  GLN L 128     8232  16238  14620   3335   3193   1876       C  
ATOM   2496  C   GLN L 128      73.932  23.420  16.320  1.00103.44           C  
ANISOU 2496  C   GLN L 128     9052  15607  14642   3530   3926   1435       C  
ATOM   2497  O   GLN L 128      74.501  23.308  15.240  1.00107.56           O  
ANISOU 2497  O   GLN L 128     9571  16194  15102   3584   4462   1400       O  
ATOM   2498  CB  GLN L 128      75.785  23.790  17.982  1.00110.22           C  
ANISOU 2498  CB  GLN L 128     8324  17771  15785   3995   3494   2592       C  
ATOM   2499  CG  GLN L 128      76.950  24.785  17.932  1.00114.10           C  
ANISOU 2499  CG  GLN L 128     7947  19216  16188   3649   3184   3018       C  
ATOM   2500  CD  GLN L 128      78.113  24.326  18.782  1.00121.98           C  
ANISOU 2500  CD  GLN L 128     7966  21035  17345   4219   3285   3839       C  
ATOM   2501  OE1 GLN L 128      77.917  23.895  19.924  1.00122.47           O  
ANISOU 2501  OE1 GLN L 128     7876  21180  17476   4495   3055   4099       O  
ATOM   2502  NE2 GLN L 128      79.332  24.397  18.232  1.00128.56           N  
ANISOU 2502  NE2 GLN L 128     8073  22558  18215   4416   3642   4318       N  
ATOM   2503  N   ALA L 129      72.813  22.773  16.605  1.00100.11           N  
ANISOU 2503  N   ALA L 129     9291  14550  14196   3552   3962   1072       N  
ATOM   2504  CA  ALA L 129      72.136  21.956  15.604  1.00101.20           C  
ANISOU 2504  CA  ALA L 129    10235  14046  14170   3495   4596    550       C  
ATOM   2505  C   ALA L 129      71.012  22.741  14.928  1.00 95.95           C  
ANISOU 2505  C   ALA L 129    10027  13319  13110   2688   4128     62       C  
ATOM   2506  O   ALA L 129      70.092  22.160  14.354  1.00 95.69           O  
ANISOU 2506  O   ALA L 129    10677  12851  12829   2431   4405   -407       O  
ATOM   2507  CB  ALA L 129      71.579  20.706  16.238  1.00102.31           C  
ANISOU 2507  CB  ALA L 129    10850  13546  14478   3923   4998    457       C  
ATOM   2508  N   ASN L 130      71.088  24.064  15.024  1.00 92.49           N  
ANISOU 2508  N   ASN L 130     9198  13345  12597   2273   3444    218       N  
ATOM   2509  CA  ASN L 130      70.129  24.944  14.385  1.00 88.50           C  
ANISOU 2509  CA  ASN L 130     9006  12857  11763   1617   3023    -60       C  
ATOM   2510  C   ASN L 130      68.675  24.737  14.775  1.00 84.27           C  
ANISOU 2510  C   ASN L 130     8966  11968  11085   1400   2728   -359       C  
ATOM   2511  O   ASN L 130      67.774  24.910  13.957  1.00 83.07           O  
ANISOU 2511  O   ASN L 130     9188  11795  10580    951   2676   -625       O  
ATOM   2512  CB  ASN L 130      70.280  24.926  12.874  1.00 92.16           C  
ANISOU 2512  CB  ASN L 130     9695  13413  11907   1335   3467   -266       C  
ATOM   2513  CG  ASN L 130      70.973  26.155  12.362  1.00 93.48           C  
ANISOU 2513  CG  ASN L 130     9421  14075  12024   1040   3202      8       C  
ATOM   2514  OD1 ASN L 130      70.328  27.161  12.078  1.00 90.53           O  
ANISOU 2514  OD1 ASN L 130     9126  13812  11459    568   2733      9       O  
ATOM   2515  ND2 ASN L 130      72.305  26.108  12.288  1.00 97.74           N  
ANISOU 2515  ND2 ASN L 130     9455  14929  12752   1339   3520    311       N  
ATOM   2516  N   LYS L 131      68.451  24.388  16.034  1.00 82.25           N  
ANISOU 2516  N   LYS L 131     8649  11537  11066   1699   2520   -259       N  
ATOM   2517  CA  LYS L 131      67.108  24.318  16.577  1.00 77.96           C  
ANISOU 2517  CA  LYS L 131     8469  10737  10416   1504   2176   -470       C  
ATOM   2518  C   LYS L 131      67.082  24.967  17.938  1.00 74.94           C  
ANISOU 2518  C   LYS L 131     7758  10471  10244   1603   1606   -227       C  
ATOM   2519  O   LYS L 131      68.138  25.190  18.539  1.00 76.84           O  
ANISOU 2519  O   LYS L 131     7513  10988  10693   1834   1536     90       O  
ATOM   2520  CB  LYS L 131      66.664  22.876  16.717  1.00 80.06           C  
ANISOU 2520  CB  LYS L 131     9200  10530  10687   1732   2681   -711       C  
ATOM   2521  CG  LYS L 131      65.643  22.458  15.702  1.00 80.98           C  
ANISOU 2521  CG  LYS L 131     9902  10485  10384   1232   2908  -1156       C  
ATOM   2522  CD  LYS L 131      66.295  22.191  14.348  1.00 86.90           C  
ANISOU 2522  CD  LYS L 131    10808  11292  10920   1097   3506  -1330       C  
ATOM   2523  CE  LYS L 131      65.365  21.382  13.442  1.00 90.04           C  
ANISOU 2523  CE  LYS L 131    11894  11483  10834    561   3912  -1852       C  
ATOM   2524  NZ  LYS L 131      63.955  21.878  13.597  1.00 86.06           N  
ANISOU 2524  NZ  LYS L 131    11460  11218  10020     41   3273  -1920       N  
ATOM   2525  N   ALA L 132      65.881  25.236  18.436  1.00 70.66           N  
ANISOU 2525  N   ALA L 132     7461   9780   9604   1401   1227   -365       N  
ATOM   2526  CA  ALA L 132      65.737  25.862  19.733  1.00 68.54           C  
ANISOU 2526  CA  ALA L 132     6986   9578   9477   1439    741   -213       C  
ATOM   2527  C   ALA L 132      64.377  25.585  20.377  1.00 66.00           C  
ANISOU 2527  C   ALA L 132     6997   9002   9077   1399    543   -383       C  
ATOM   2528  O   ALA L 132      63.330  25.930  19.833  1.00 64.50           O  
ANISOU 2528  O   ALA L 132     7052   8775   8679   1113    427   -522       O  
ATOM   2529  CB  ALA L 132      65.987  27.366  19.629  1.00 67.25           C  
ANISOU 2529  CB  ALA L 132     6613   9644   9295   1101    373    -95       C  
ATOM   2530  N   THR L 133      64.402  24.972  21.550  1.00 65.60           N  
ANISOU 2530  N   THR L 133     6893   8861   9170   1691    503   -303       N  
ATOM   2531  CA  THR L 133      63.188  24.656  22.269  1.00 62.70           C  
ANISOU 2531  CA  THR L 133     6800   8286   8737   1671    338   -432       C  
ATOM   2532  C   THR L 133      63.287  25.159  23.698  1.00 61.90           C  
ANISOU 2532  C   THR L 133     6470   8317   8732   1761    -46   -277       C  
ATOM   2533  O   THR L 133      64.302  24.928  24.361  1.00 64.39           O  
ANISOU 2533  O   THR L 133     6452   8842   9172   1992    -35    -38       O  
ATOM   2534  CB  THR L 133      63.017  23.146  22.354  1.00 64.80           C  
ANISOU 2534  CB  THR L 133     7343   8237   9042   1922    778   -510       C  
ATOM   2535  OG1 THR L 133      63.326  22.552  21.089  1.00 67.39           O  
ANISOU 2535  OG1 THR L 133     7890   8430   9285   1857   1283   -671       O  
ATOM   2536  CG2 THR L 133      61.598  22.787  22.780  1.00 62.13           C  
ANISOU 2536  CG2 THR L 133     7341   7709   8555   1752    654   -694       C  
ATOM   2537  N   LEU L 134      62.245  25.845  24.165  1.00 58.86           N  
ANISOU 2537  N   LEU L 134     6240   7872   8253   1572   -354   -383       N  
ATOM   2538  CA  LEU L 134      62.142  26.258  25.557  1.00 57.78           C  
ANISOU 2538  CA  LEU L 134     6009   7813   8132   1596   -655   -328       C  
ATOM   2539  C   LEU L 134      61.263  25.242  26.246  1.00 56.86           C  
ANISOU 2539  C   LEU L 134     6094   7525   7986   1783   -597   -371       C  
ATOM   2540  O   LEU L 134      60.217  24.860  25.728  1.00 56.28           O  
ANISOU 2540  O   LEU L 134     6294   7273   7816   1702   -491   -516       O  
ATOM   2541  CB  LEU L 134      61.514  27.643  25.675  1.00 56.85           C  
ANISOU 2541  CB  LEU L 134     6008   7641   7953   1325   -900   -420       C  
ATOM   2542  CG  LEU L 134      62.418  28.877  25.610  1.00 58.82           C  
ANISOU 2542  CG  LEU L 134     6104   8014   8232   1055  -1014   -378       C  
ATOM   2543  CD1 LEU L 134      63.313  28.814  24.395  1.00 60.52           C  
ANISOU 2543  CD1 LEU L 134     6140   8362   8491   1011   -835   -280       C  
ATOM   2544  CD2 LEU L 134      61.561  30.125  25.572  1.00 57.90           C  
ANISOU 2544  CD2 LEU L 134     6260   7640   8098    875  -1079   -457       C  
ATOM   2545  N   VAL L 135      61.684  24.791  27.413  1.00 58.00           N  
ANISOU 2545  N   VAL L 135     6071   7794   8171   1985   -669   -209       N  
ATOM   2546  CA  VAL L 135      60.928  23.786  28.133  1.00 57.51           C  
ANISOU 2546  CA  VAL L 135     6199   7562   8092   2173   -585   -195       C  
ATOM   2547  C   VAL L 135      60.388  24.364  29.427  1.00 56.54           C  
ANISOU 2547  C   VAL L 135     6058   7578   7845   2082   -919   -214       C  
ATOM   2548  O   VAL L 135      61.151  24.781  30.307  1.00 58.58           O  
ANISOU 2548  O   VAL L 135     6045   8164   8048   2052  -1127    -74       O  
ATOM   2549  CB  VAL L 135      61.803  22.571  28.457  1.00 60.77           C  
ANISOU 2549  CB  VAL L 135     6461   7978   8651   2580   -290    107       C  
ATOM   2550  CG1 VAL L 135      60.962  21.480  29.108  1.00 61.17           C  
ANISOU 2550  CG1 VAL L 135     6795   7748   8699   2749   -125    131       C  
ATOM   2551  CG2 VAL L 135      62.465  22.049  27.204  1.00 62.60           C  
ANISOU 2551  CG2 VAL L 135     6735   8038   9011   2706    147    110       C  
ATOM   2552  N   CYS L 136      59.069  24.395  29.540  1.00 54.09           N  
ANISOU 2552  N   CYS L 136     6021   7087   7444   1992   -953   -383       N  
ATOM   2553  CA  CYS L 136      58.437  24.942  30.723  1.00 53.98           C  
ANISOU 2553  CA  CYS L 136     6047   7161   7303   1929  -1181   -434       C  
ATOM   2554  C   CYS L 136      57.736  23.827  31.484  1.00 54.35           C  
ANISOU 2554  C   CYS L 136     6210   7140   7299   2092  -1101   -358       C  
ATOM   2555  O   CYS L 136      56.718  23.314  31.012  1.00 53.30           O  
ANISOU 2555  O   CYS L 136     6290   6822   7138   2046   -961   -447       O  
ATOM   2556  CB  CYS L 136      57.439  25.999  30.310  1.00 52.16           C  
ANISOU 2556  CB  CYS L 136     5984   6811   7022   1762  -1235   -602       C  
ATOM   2557  SG  CYS L 136      56.701  26.888  31.665  1.00 53.02           S  
ANISOU 2557  SG  CYS L 136     6216   6934   6994   1712  -1373   -711       S  
ATOM   2558  N   LEU L 137      58.290  23.446  32.642  1.00 56.25           N  
ANISOU 2558  N   LEU L 137     6287   7597   7488   2231  -1190   -158       N  
ATOM   2559  CA  LEU L 137      57.767  22.332  33.461  1.00 56.85           C  
ANISOU 2559  CA  LEU L 137     6460   7616   7526   2419  -1088      3       C  
ATOM   2560  C   LEU L 137      56.864  22.774  34.630  1.00 56.74           C  
ANISOU 2560  C   LEU L 137     6522   7747   7288   2301  -1289    -91       C  
ATOM   2561  O   LEU L 137      57.320  23.409  35.593  1.00 58.35           O  
ANISOU 2561  O   LEU L 137     6571   8286   7313   2202  -1513    -67       O  
ATOM   2562  CB  LEU L 137      58.918  21.483  33.984  1.00 59.67           C  
ANISOU 2562  CB  LEU L 137     6548   8163   7959   2734   -997    421       C  
ATOM   2563  CG  LEU L 137      59.825  21.019  32.852  1.00 61.23           C  
ANISOU 2563  CG  LEU L 137     6675   8191   8397   2929   -693    536       C  
ATOM   2564  CD1 LEU L 137      61.031  20.216  33.341  1.00 65.84           C  
ANISOU 2564  CD1 LEU L 137     6902   9016   9098   3369   -532   1083       C  
ATOM   2565  CD2 LEU L 137      59.001  20.214  31.896  1.00 60.66           C  
ANISOU 2565  CD2 LEU L 137     7045   7576   8429   2901   -313    320       C  
ATOM   2566  N   ILE L 138      55.585  22.420  34.543  1.00 54.80           N  
ANISOU 2566  N   ILE L 138     6511   7302   7007   2260  -1183   -202       N  
ATOM   2567  CA  ILE L 138      54.600  22.836  35.529  1.00 54.06           C  
ANISOU 2567  CA  ILE L 138     6493   7333   6716   2187  -1295   -289       C  
ATOM   2568  C   ILE L 138      54.163  21.679  36.408  1.00 55.80           C  
ANISOU 2568  C   ILE L 138     6774   7571   6855   2299  -1207    -86       C  
ATOM   2569  O   ILE L 138      53.811  20.629  35.893  1.00 57.09           O  
ANISOU 2569  O   ILE L 138     7088   7482   7123   2325   -975    -14       O  
ATOM   2570  CB  ILE L 138      53.404  23.304  34.785  1.00 52.17           C  
ANISOU 2570  CB  ILE L 138     6375   6973   6476   2073  -1228   -460       C  
ATOM   2571  CG1 ILE L 138      53.854  24.119  33.581  1.00 51.19           C  
ANISOU 2571  CG1 ILE L 138     6207   6763   6479   1999  -1234   -557       C  
ATOM   2572  CG2 ILE L 138      52.476  24.118  35.691  1.00 52.97           C  
ANISOU 2572  CG2 ILE L 138     6521   7194   6410   2067  -1280   -553       C  
ATOM   2573  CD1 ILE L 138      52.686  24.477  32.655  1.00 50.92           C  
ANISOU 2573  CD1 ILE L 138     6202   6725   6420   1910  -1163   -588       C  
ATOM   2574  N   SER L 139      54.161  21.848  37.727  1.00 57.35           N  
ANISOU 2574  N   SER L 139     6901   8054   6834   2310  -1351     -6       N  
ATOM   2575  CA  SER L 139      53.926  20.683  38.613  1.00 59.18           C  
ANISOU 2575  CA  SER L 139     7159   8338   6988   2449  -1261    290       C  
ATOM   2576  C   SER L 139      53.275  20.948  39.971  1.00 60.17           C  
ANISOU 2576  C   SER L 139     7294   8774   6795   2370  -1381    282       C  
ATOM   2577  O   SER L 139      53.254  22.072  40.467  1.00 60.26           O  
ANISOU 2577  O   SER L 139     7291   9005   6600   2208  -1532     44       O  
ATOM   2578  CB  SER L 139      55.237  19.938  38.849  1.00 61.66           C  
ANISOU 2578  CB  SER L 139     7260   8777   7391   2704  -1231    707       C  
ATOM   2579  OG  SER L 139      56.244  20.889  39.075  1.00 62.26           O  
ANISOU 2579  OG  SER L 139     7056   9258   7341   2604  -1496    687       O  
ATOM   2580  N   ASP L 140      52.773  19.882  40.584  1.00 61.76           N  
ANISOU 2580  N   ASP L 140     7568   8956   6942   2463  -1253    539       N  
ATOM   2581  CA  ASP L 140      52.247  19.968  41.944  1.00 63.64           C  
ANISOU 2581  CA  ASP L 140     7795   9545   6841   2402  -1342    600       C  
ATOM   2582  C   ASP L 140      51.028  20.883  42.073  1.00 62.07           C  
ANISOU 2582  C   ASP L 140     7724   9365   6495   2235  -1322    228       C  
ATOM   2583  O   ASP L 140      50.802  21.444  43.141  1.00 64.46           O  
ANISOU 2583  O   ASP L 140     8037   9976   6478   2146  -1388    131       O  
ATOM   2584  CB  ASP L 140      53.328  20.463  42.907  1.00 66.61           C  
ANISOU 2584  CB  ASP L 140     7933  10449   6925   2353  -1600    729       C  
ATOM   2585  CG  ASP L 140      54.272  19.375  43.335  1.00 70.61           C  
ANISOU 2585  CG  ASP L 140     8206  11172   7453   2612  -1599   1328       C  
ATOM   2586  OD1 ASP L 140      53.898  18.189  43.238  1.00 71.28           O  
ANISOU 2586  OD1 ASP L 140     8420  10930   7734   2841  -1337   1634       O  
ATOM   2587  OD2 ASP L 140      55.385  19.717  43.794  1.00 74.19           O  
ANISOU 2587  OD2 ASP L 140     8337  12150   7704   2569  -1831   1530       O  
ATOM   2588  N   PHE L 141      50.238  21.039  41.015  1.00 59.09           N  
ANISOU 2588  N   PHE L 141     7425   8711   6315   2198  -1194     57       N  
ATOM   2589  CA  PHE L 141      49.066  21.911  41.109  1.00 58.93           C  
ANISOU 2589  CA  PHE L 141     7438   8766   6187   2155  -1118   -158       C  
ATOM   2590  C   PHE L 141      47.745  21.160  41.287  1.00 59.66           C  
ANISOU 2590  C   PHE L 141     7529   8939   6200   2101   -965    -22       C  
ATOM   2591  O   PHE L 141      47.640  19.976  40.943  1.00 60.36           O  
ANISOU 2591  O   PHE L 141     7670   8892   6372   2003   -886    157       O  
ATOM   2592  CB  PHE L 141      48.993  22.900  39.927  1.00 57.09           C  
ANISOU 2592  CB  PHE L 141     7186   8355   6152   2167  -1094   -352       C  
ATOM   2593  CG  PHE L 141      48.947  22.255  38.563  1.00 55.34           C  
ANISOU 2593  CG  PHE L 141     6926   7954   6145   2091  -1057   -276       C  
ATOM   2594  CD1 PHE L 141      50.112  21.924  37.900  1.00 54.53           C  
ANISOU 2594  CD1 PHE L 141     6839   7663   6218   2089  -1106   -260       C  
ATOM   2595  CD2 PHE L 141      47.748  22.025  37.933  1.00 55.21           C  
ANISOU 2595  CD2 PHE L 141     6840   8029   6107   1979   -951   -219       C  
ATOM   2596  CE1 PHE L 141      50.077  21.343  36.652  1.00 53.80           C  
ANISOU 2596  CE1 PHE L 141     6784   7388   6269   1970  -1004   -256       C  
ATOM   2597  CE2 PHE L 141      47.711  21.455  36.673  1.00 54.88           C  
ANISOU 2597  CE2 PHE L 141     6800   7894   6158   1773   -909   -205       C  
ATOM   2598  CZ  PHE L 141      48.880  21.119  36.032  1.00 53.84           C  
ANISOU 2598  CZ  PHE L 141     6775   7487   6195   1766   -913   -260       C  
ATOM   2599  N   TYR L 142      46.760  21.842  41.868  1.00 59.90           N  
ANISOU 2599  N   TYR L 142     7527   9177   6055   2145   -867   -105       N  
ATOM   2600  CA  TYR L 142      45.408  21.303  42.015  1.00 61.14           C  
ANISOU 2600  CA  TYR L 142     7590   9533   6106   2074   -719     48       C  
ATOM   2601  C   TYR L 142      44.486  22.478  42.243  1.00 62.29           C  
ANISOU 2601  C   TYR L 142     7638   9863   6168   2259   -552    -46       C  
ATOM   2602  O   TYR L 142      44.811  23.368  43.023  1.00 62.97           O  
ANISOU 2602  O   TYR L 142     7865   9923   6136   2390   -487   -244       O  
ATOM   2603  CB  TYR L 142      45.278  20.302  43.185  1.00 63.08           C  
ANISOU 2603  CB  TYR L 142     7904   9927   6135   1998   -692    243       C  
ATOM   2604  CG  TYR L 142      43.883  19.727  43.333  1.00 64.66           C  
ANISOU 2604  CG  TYR L 142     7995  10365   6207   1847   -528    408       C  
ATOM   2605  CD1 TYR L 142      42.964  20.305  44.175  1.00 66.17           C  
ANISOU 2605  CD1 TYR L 142     8076  10895   6171   1957   -392    403       C  
ATOM   2606  CD2 TYR L 142      43.476  18.632  42.576  1.00 65.24           C  
ANISOU 2606  CD2 TYR L 142     8087  10337   6364   1542   -465    548       C  
ATOM   2607  CE1 TYR L 142      41.679  19.797  44.289  1.00 68.27           C  
ANISOU 2607  CE1 TYR L 142     8157  11479   6304   1805   -242    604       C  
ATOM   2608  CE2 TYR L 142      42.199  18.113  42.681  1.00 66.88           C  
ANISOU 2608  CE2 TYR L 142     8160  10849   6404   1279   -329    701       C  
ATOM   2609  CZ  TYR L 142      41.302  18.701  43.540  1.00 68.56           C  
ANISOU 2609  CZ  TYR L 142     8166  11483   6399   1430   -242    762       C  
ATOM   2610  OH  TYR L 142      40.029  18.185  43.635  1.00 70.88           O  
ANISOU 2610  OH  TYR L 142     8245  12176   6509   1153   -109    965       O  
ATOM   2611  N   PRO L 143      43.332  22.494  41.554  1.00 62.96           N  
ANISOU 2611  N   PRO L 143     7477  10157   6287   2253   -438    118       N  
ATOM   2612  CA  PRO L 143      42.884  21.480  40.566  1.00 63.07           C  
ANISOU 2612  CA  PRO L 143     7347  10277   6338   1924   -500    294       C  
ATOM   2613  C   PRO L 143      43.697  21.392  39.276  1.00 60.49           C  
ANISOU 2613  C   PRO L 143     7085   9680   6217   1792   -629    204       C  
ATOM   2614  O   PRO L 143      44.405  22.324  38.928  1.00 59.65           O  
ANISOU 2614  O   PRO L 143     7023   9377   6265   2003   -679     71       O  
ATOM   2615  CB  PRO L 143      41.441  21.902  40.232  1.00 65.06           C  
ANISOU 2615  CB  PRO L 143     7207  11023   6488   1965   -359    527       C  
ATOM   2616  CG  PRO L 143      41.267  23.270  40.826  1.00 65.79           C  
ANISOU 2616  CG  PRO L 143     7282  11100   6616   2461   -158    478       C  
ATOM   2617  CD  PRO L 143      42.251  23.422  41.922  1.00 65.19           C  
ANISOU 2617  CD  PRO L 143     7591  10691   6488   2535   -176    186       C  
ATOM   2618  N   GLY L 144      43.538  20.293  38.550  1.00 60.70           N  
ANISOU 2618  N   GLY L 144     7149   9695   6221   1392   -630    258       N  
ATOM   2619  CA  GLY L 144      44.356  20.023  37.382  1.00 59.00           C  
ANISOU 2619  CA  GLY L 144     7070   9188   6158   1223   -680    136       C  
ATOM   2620  C   GLY L 144      43.895  20.766  36.156  1.00 59.20           C  
ANISOU 2620  C   GLY L 144     6825   9499   6169   1147   -734    179       C  
ATOM   2621  O   GLY L 144      43.365  20.179  35.203  1.00 61.36           O  
ANISOU 2621  O   GLY L 144     7021  10004   6290    687   -719    217       O  
ATOM   2622  N   ALA L 145      44.086  22.076  36.197  1.00 58.51           N  
ANISOU 2622  N   ALA L 145     6612   9414   6204   1559   -768    189       N  
ATOM   2623  CA  ALA L 145      43.768  22.965  35.071  1.00 58.73           C  
ANISOU 2623  CA  ALA L 145     6371   9681   6265   1623   -793    329       C  
ATOM   2624  C   ALA L 145      44.644  24.241  35.126  1.00 57.45           C  
ANISOU 2624  C   ALA L 145     6330   9153   6345   2045   -778    219       C  
ATOM   2625  O   ALA L 145      44.643  24.985  36.110  1.00 58.34           O  
ANISOU 2625  O   ALA L 145     6538   9124   6506   2374   -660    162       O  
ATOM   2626  CB  ALA L 145      42.293  23.318  35.056  1.00 60.38           C  
ANISOU 2626  CB  ALA L 145     6134  10518   6291   1681   -711    689       C  
ATOM   2627  N   VAL L 146      45.441  24.440  34.089  1.00 56.15           N  
ANISOU 2627  N   VAL L 146     6219   8815   6301   1957   -863    147       N  
ATOM   2628  CA  VAL L 146      46.201  25.656  33.920  1.00 55.85           C  
ANISOU 2628  CA  VAL L 146     6277   8469   6473   2246   -832     76       C  
ATOM   2629  C   VAL L 146      46.032  26.135  32.511  1.00 56.76           C  
ANISOU 2629  C   VAL L 146     6174   8779   6613   2203   -853    290       C  
ATOM   2630  O   VAL L 146      45.761  25.374  31.587  1.00 57.79           O  
ANISOU 2630  O   VAL L 146     6160   9221   6576   1838   -946    367       O  
ATOM   2631  CB  VAL L 146      47.727  25.449  34.102  1.00 53.44           C  
ANISOU 2631  CB  VAL L 146     6257   7751   6296   2166   -938   -217       C  
ATOM   2632  CG1 VAL L 146      48.059  25.062  35.533  1.00 53.62           C  
ANISOU 2632  CG1 VAL L 146     6452   7674   6248   2207   -952   -359       C  
ATOM   2633  CG2 VAL L 146      48.251  24.408  33.101  1.00 52.24           C  
ANISOU 2633  CG2 VAL L 146     6126   7584   6138   1852  -1014   -258       C  
ATOM   2634  N   THR L 147      46.234  27.421  32.352  1.00 57.42           N  
ANISOU 2634  N   THR L 147     6279   8659   6879   2535   -731    377       N  
ATOM   2635  CA  THR L 147      46.293  28.026  31.051  1.00 58.37           C  
ANISOU 2635  CA  THR L 147     6225   8901   7053   2549   -739    620       C  
ATOM   2636  C   THR L 147      47.706  28.568  30.940  1.00 57.54           C  
ANISOU 2636  C   THR L 147     6438   8263   7162   2544   -754    335       C  
ATOM   2637  O   THR L 147      48.206  29.198  31.891  1.00 58.42           O  
ANISOU 2637  O   THR L 147     6831   7965   7401   2704   -639    113       O  
ATOM   2638  CB  THR L 147      45.297  29.182  30.964  1.00 62.83           C  
ANISOU 2638  CB  THR L 147     6544   9635   7695   3023   -485   1081       C  
ATOM   2639  OG1 THR L 147      43.973  28.672  30.703  1.00 65.83           O  
ANISOU 2639  OG1 THR L 147     6442  10754   7817   2961   -522   1490       O  
ATOM   2640  CG2 THR L 147      45.712  30.160  29.890  1.00 64.17           C  
ANISOU 2640  CG2 THR L 147     6677   9680   8023   3170   -415   1319       C  
ATOM   2641  N   VAL L 148      48.360  28.285  29.809  1.00 56.69           N  
ANISOU 2641  N   VAL L 148     6289   8212   7039   2285   -884    319       N  
ATOM   2642  CA  VAL L 148      49.764  28.622  29.609  1.00 54.41           C  
ANISOU 2642  CA  VAL L 148     6226   7528   6921   2211   -920     77       C  
ATOM   2643  C   VAL L 148      49.911  29.679  28.543  1.00 55.94           C  
ANISOU 2643  C   VAL L 148     6345   7689   7221   2304   -840    321       C  
ATOM   2644  O   VAL L 148      49.333  29.564  27.467  1.00 56.42           O  
ANISOU 2644  O   VAL L 148     6138   8163   7136   2220   -877    624       O  
ATOM   2645  CB  VAL L 148      50.558  27.416  29.152  1.00 52.19           C  
ANISOU 2645  CB  VAL L 148     5986   7281   6563   1882  -1049   -130       C  
ATOM   2646  CG1 VAL L 148      51.965  27.834  28.803  1.00 50.74           C  
ANISOU 2646  CG1 VAL L 148     5914   6821   6545   1837  -1069   -276       C  
ATOM   2647  CG2 VAL L 148      50.549  26.369  30.243  1.00 51.34           C  
ANISOU 2647  CG2 VAL L 148     5989   7121   6394   1840  -1078   -305       C  
ATOM   2648  N   ALA L 149      50.715  30.695  28.841  1.00 56.59           N  
ANISOU 2648  N   ALA L 149     6671   7317   7514   2409   -724    198       N  
ATOM   2649  CA  ALA L 149      50.954  31.790  27.900  1.00 58.25           C  
ANISOU 2649  CA  ALA L 149     6884   7380   7868   2503   -587    445       C  
ATOM   2650  C   ALA L 149      52.458  32.104  27.794  1.00 58.06           C  
ANISOU 2650  C   ALA L 149     7077   7019   7963   2247   -635    150       C  
ATOM   2651  O   ALA L 149      53.157  32.277  28.820  1.00 57.73           O  
ANISOU 2651  O   ALA L 149     7278   6692   7965   2135   -629   -187       O  
ATOM   2652  CB  ALA L 149      50.191  33.022  28.339  1.00 61.43           C  
ANISOU 2652  CB  ALA L 149     7413   7488   8440   2930   -232    696       C  
ATOM   2653  N   TRP L 150      52.955  32.187  26.562  1.00 57.55           N  
ANISOU 2653  N   TRP L 150     6887   7079   7898   2106   -685    300       N  
ATOM   2654  CA  TRP L 150      54.355  32.488  26.354  1.00 57.29           C  
ANISOU 2654  CA  TRP L 150     6978   6823   7965   1854   -717     90       C  
ATOM   2655  C   TRP L 150      54.523  33.928  25.930  1.00 60.75           C  
ANISOU 2655  C   TRP L 150     7592   6898   8590   1925   -476    290       C  
ATOM   2656  O   TRP L 150      53.640  34.482  25.295  1.00 63.74           O  
ANISOU 2656  O   TRP L 150     7883   7332   9005   2198   -315    718       O  
ATOM   2657  CB  TRP L 150      54.924  31.583  25.284  1.00 55.62           C  
ANISOU 2657  CB  TRP L 150     6559   6948   7628   1631   -862     86       C  
ATOM   2658  CG  TRP L 150      55.136  30.154  25.704  1.00 53.86           C  
ANISOU 2658  CG  TRP L 150     6282   6897   7287   1531   -986   -159       C  
ATOM   2659  CD1 TRP L 150      54.232  29.117  25.615  1.00 53.25           C  
ANISOU 2659  CD1 TRP L 150     6128   7082   7023   1513  -1017   -140       C  
ATOM   2660  CD2 TRP L 150      56.346  29.582  26.231  1.00 52.49           C  
ANISOU 2660  CD2 TRP L 150     6120   6655   7168   1432  -1045   -395       C  
ATOM   2661  NE1 TRP L 150      54.810  27.942  26.062  1.00 51.92           N  
ANISOU 2661  NE1 TRP L 150     6013   6877   6836   1440  -1032   -372       N  
ATOM   2662  CE2 TRP L 150      56.106  28.200  26.432  1.00 51.56           C  
ANISOU 2662  CE2 TRP L 150     5979   6665   6948   1448  -1052   -480       C  
ATOM   2663  CE3 TRP L 150      57.595  30.104  26.561  1.00 53.60           C  
ANISOU 2663  CE3 TRP L 150     6257   6691   7416   1312  -1076   -492       C  
ATOM   2664  CZ2 TRP L 150      57.082  27.336  26.941  1.00 51.94           C  
ANISOU 2664  CZ2 TRP L 150     5992   6695   7047   1476  -1045   -584       C  
ATOM   2665  CZ3 TRP L 150      58.575  29.237  27.075  1.00 53.66           C  
ANISOU 2665  CZ3 TRP L 150     6133   6834   7420   1290  -1141   -583       C  
ATOM   2666  CH2 TRP L 150      58.309  27.871  27.264  1.00 52.59           C  
ANISOU 2666  CH2 TRP L 150     5968   6782   7232   1435  -1106   -591       C  
ATOM   2667  N   LYS L 151      55.653  34.528  26.285  1.00 61.62           N  
ANISOU 2667  N   LYS L 151     7934   6677   8802   1660   -429     31       N  
ATOM   2668  CA  LYS L 151      55.942  35.900  25.926  1.00 65.11           C  
ANISOU 2668  CA  LYS L 151     8646   6662   9431   1627   -137    167       C  
ATOM   2669  C   LYS L 151      57.361  36.023  25.378  1.00 65.48           C  
ANISOU 2669  C   LYS L 151     8650   6748   9480   1194   -245     37       C  
ATOM   2670  O   LYS L 151      58.301  35.448  25.917  1.00 63.48           O  
ANISOU 2670  O   LYS L 151     8306   6688   9126    888   -459   -280       O  
ATOM   2671  CB  LYS L 151      55.810  36.797  27.158  1.00 68.75           C  
ANISOU 2671  CB  LYS L 151     9584   6554   9985   1613    164    -93       C  
ATOM   2672  CG  LYS L 151      54.413  36.838  27.797  1.00 69.95           C  
ANISOU 2672  CG  LYS L 151     9809   6607  10162   2095    380     49       C  
ATOM   2673  CD  LYS L 151      53.467  37.784  27.033  1.00 74.84           C  
ANISOU 2673  CD  LYS L 151    10464   6973  10997   2600    789    632       C  
ATOM   2674  CE  LYS L 151      51.992  37.465  27.288  1.00 75.18           C  
ANISOU 2674  CE  LYS L 151    10264   7290  11009   3145    885    979       C  
ATOM   2675  NZ  LYS L 151      51.664  37.619  28.737  1.00 76.93           N  
ANISOU 2675  NZ  LYS L 151    10855   7147  11227   3215   1126    593       N  
ATOM   2676  N   ALA L 152      57.523  36.767  24.293  1.00 68.10           N  
ANISOU 2676  N   ALA L 152     8995   6964   9916   1189    -85    353       N  
ATOM   2677  CA  ALA L 152      58.851  37.192  23.885  1.00 69.19           C  
ANISOU 2677  CA  ALA L 152     9164   7042  10084    747    -93    244       C  
ATOM   2678  C   ALA L 152      58.889  38.668  24.218  1.00 74.13           C  
ANISOU 2678  C   ALA L 152    10304   6956  10908    634    312    247       C  
ATOM   2679  O   ALA L 152      58.061  39.403  23.732  1.00 77.20           O  
ANISOU 2679  O   ALA L 152    10852   7021  11459   1004    629    652       O  
ATOM   2680  CB  ALA L 152      59.045  36.977  22.415  1.00 68.57           C  
ANISOU 2680  CB  ALA L 152     8784   7318   9952    763   -152    584       C  
ATOM   2681  N   ASP L 153      59.784  39.087  25.102  1.00 76.18           N  
ANISOU 2681  N   ASP L 153    10837   6981  11127    120    346   -183       N  
ATOM   2682  CA  ASP L 153      59.866  40.485  25.467  1.00 83.17           C  
ANISOU 2682  CA  ASP L 153    12347   7092  12163   -125    820   -287       C  
ATOM   2683  C   ASP L 153      58.525  41.058  25.927  1.00 86.04           C  
ANISOU 2683  C   ASP L 153    13117   6870  12703    425   1266   -143       C  
ATOM   2684  O   ASP L 153      58.282  42.266  25.773  1.00 92.35           O  
ANISOU 2684  O   ASP L 153    14439   6909  13740    508   1828     22       O  
ATOM   2685  CB  ASP L 153      60.316  41.316  24.254  1.00 86.73           C  
ANISOU 2685  CB  ASP L 153    12869   7303  12783   -238   1046     78       C  
ATOM   2686  CG  ASP L 153      61.818  41.313  24.054  1.00 88.02           C  
ANISOU 2686  CG  ASP L 153    12863   7773  12805   -967    829   -148       C  
ATOM   2687  OD1 ASP L 153      62.528  40.769  24.920  1.00 87.50           O  
ANISOU 2687  OD1 ASP L 153    12633   8101  12513  -1390    531   -559       O  
ATOM   2688  OD2 ASP L 153      62.294  41.869  23.042  1.00 90.36           O  
ANISOU 2688  OD2 ASP L 153    13152   7981  13201  -1116    967    141       O  
ATOM   2689  N   SER L 154      57.633  40.221  26.444  1.00 81.98           N  
ANISOU 2689  N   SER L 154    12372   6677  12099    844   1088   -144       N  
ATOM   2690  CA  SER L 154      56.276  40.710  26.775  1.00 85.17           C  
ANISOU 2690  CA  SER L 154    13036   6647  12677   1471   1532    111       C  
ATOM   2691  C   SER L 154      55.310  40.916  25.583  1.00 85.44           C  
ANISOU 2691  C   SER L 154    12777   6794  12894   2139   1692    898       C  
ATOM   2692  O   SER L 154      54.300  41.585  25.732  1.00 88.75           O  
ANISOU 2692  O   SER L 154    13408   6797  13517   2703   2181   1255       O  
ATOM   2693  CB  SER L 154      56.325  41.983  27.650  1.00 92.20           C  
ANISOU 2693  CB  SER L 154    14750   6578  13703   1281   2180   -211       C  
ATOM   2694  OG  SER L 154      56.446  43.171  26.881  1.00 97.13           O  
ANISOU 2694  OG  SER L 154    15758   6529  14619   1346   2700    130       O  
ATOM   2695  N   SER L 155      55.623  40.337  24.423  1.00 82.71           N  
ANISOU 2695  N   SER L 155    11923   7064  12440   2071   1311   1192       N  
ATOM   2696  CA  SER L 155      54.666  40.194  23.314  1.00 82.81           C  
ANISOU 2696  CA  SER L 155    11481   7542  12441   2583   1288   1926       C  
ATOM   2697  C   SER L 155      54.181  38.749  23.270  1.00 77.42           C  
ANISOU 2697  C   SER L 155    10258   7710  11448   2597    782   1857       C  
ATOM   2698  O   SER L 155      54.989  37.826  23.422  1.00 73.45           O  
ANISOU 2698  O   SER L 155     9635   7507  10766   2166    406   1389       O  
ATOM   2699  CB  SER L 155      55.328  40.503  21.980  1.00 83.79           C  
ANISOU 2699  CB  SER L 155    11443   7837  12556   2387   1234   2274       C  
ATOM   2700  OG  SER L 155      56.035  41.721  22.028  1.00 88.79           O  
ANISOU 2700  OG  SER L 155    12616   7672  13449   2185   1665   2229       O  
ATOM   2701  N   PRO L 156      52.872  38.530  23.050  1.00 78.39           N  
ANISOU 2701  N   PRO L 156    10042   8243  11498   3076    809   2358       N  
ATOM   2702  CA  PRO L 156      52.399  37.152  23.129  1.00 73.82           C  
ANISOU 2702  CA  PRO L 156     9049   8398  10602   2964    380   2209       C  
ATOM   2703  C   PRO L 156      52.979  36.326  21.992  1.00 70.79           C  
ANISOU 2703  C   PRO L 156     8343   8617   9938   2548     15   2187       C  
ATOM   2704  O   PRO L 156      53.259  36.852  20.931  1.00 73.36           O  
ANISOU 2704  O   PRO L 156     8577   9041  10254   2509     78   2553       O  
ATOM   2705  CB  PRO L 156      50.871  37.282  22.988  1.00 77.12           C  
ANISOU 2705  CB  PRO L 156     9115   9215  10970   3506    525   2866       C  
ATOM   2706  CG  PRO L 156      50.573  38.750  22.970  1.00 83.42           C  
ANISOU 2706  CG  PRO L 156    10183   9383  12128   4029   1098   3367       C  
ATOM   2707  CD  PRO L 156      51.826  39.435  22.556  1.00 84.34           C  
ANISOU 2707  CD  PRO L 156    10688   8946  12413   3695   1209   3166       C  
ATOM   2708  N   VAL L 157      53.166  35.039  22.238  1.00 66.60           N  
ANISOU 2708  N   VAL L 157     7688   8438   9180   2248   -299   1758       N  
ATOM   2709  CA  VAL L 157      53.717  34.112  21.253  1.00 65.45           C  
ANISOU 2709  CA  VAL L 157     7335   8778   8756   1846   -539   1632       C  
ATOM   2710  C   VAL L 157      52.706  33.052  20.821  1.00 65.36           C  
ANISOU 2710  C   VAL L 157     6996   9480   8360   1728   -722   1755       C  
ATOM   2711  O   VAL L 157      52.453  32.095  21.557  1.00 62.80           O  
ANISOU 2711  O   VAL L 157     6707   9202   7954   1643   -826   1417       O  
ATOM   2712  CB  VAL L 157      54.898  33.340  21.834  1.00 61.77           C  
ANISOU 2712  CB  VAL L 157     7041   8094   8333   1555   -658   1021       C  
ATOM   2713  CG1 VAL L 157      55.634  32.670  20.727  1.00 61.06           C  
ANISOU 2713  CG1 VAL L 157     6821   8337   8041   1225   -735    935       C  
ATOM   2714  CG2 VAL L 157      55.824  34.268  22.593  1.00 63.19           C  
ANISOU 2714  CG2 VAL L 157     7524   7678   8809   1541   -528    817       C  
ATOM   2715  N   LYS L 158      52.172  33.199  19.615  1.00 69.07           N  
ANISOU 2715  N   LYS L 158     7151  10547   8547   1645   -758   2241       N  
ATOM   2716  CA  LYS L 158      51.135  32.297  19.130  1.00 70.60           C  
ANISOU 2716  CA  LYS L 158     7002  11552   8270   1390   -932   2399       C  
ATOM   2717  C   LYS L 158      51.678  30.956  18.627  1.00 69.29           C  
ANISOU 2717  C   LYS L 158     6944  11619   7767    790  -1044   1861       C  
ATOM   2718  O   LYS L 158      51.227  29.889  19.067  1.00 68.55           O  
ANISOU 2718  O   LYS L 158     6889  11669   7487    560  -1110   1552       O  
ATOM   2719  CB  LYS L 158      50.355  32.969  18.017  1.00 75.35           C  
ANISOU 2719  CB  LYS L 158     7166  12862   8602   1461   -941   3188       C  
ATOM   2720  CG  LYS L 158      48.870  32.851  18.234  1.00 79.56           C  
ANISOU 2720  CG  LYS L 158     7262  14060   8907   1629  -1010   3680       C  
ATOM   2721  CD  LYS L 158      48.477  33.158  19.700  1.00 77.88           C  
ANISOU 2721  CD  LYS L 158     7231  13234   9127   2164   -839   3578       C  
ATOM   2722  CE  LYS L 158      46.954  33.139  19.869  1.00 81.90           C  
ANISOU 2722  CE  LYS L 158     7212  14484   9420   2409   -857   4190       C  
ATOM   2723  NZ  LYS L 158      46.231  33.723  18.652  1.00 88.14           N  
ANISOU 2723  NZ  LYS L 158     7391  16207   9890   2501   -889   5143       N  
ATOM   2724  N   ALA L 159      52.671  31.022  17.741  1.00 68.86           N  
ANISOU 2724  N   ALA L 159     6982  11525   7655    554   -993   1745       N  
ATOM   2725  CA  ALA L 159      53.136  29.866  17.007  1.00 67.77           C  
ANISOU 2725  CA  ALA L 159     6962  11635   7154      7   -972   1317       C  
ATOM   2726  C   ALA L 159      54.235  29.072  17.710  1.00 64.36           C  
ANISOU 2726  C   ALA L 159     6887  10566   6999     17   -843    696       C  
ATOM   2727  O   ALA L 159      55.112  29.622  18.402  1.00 62.36           O  
ANISOU 2727  O   ALA L 159     6746   9767   7180    335   -804    611       O  
ATOM   2728  CB  ALA L 159      53.612  30.303  15.656  1.00 70.10           C  
ANISOU 2728  CB  ALA L 159     7148  12286   7201   -236   -929   1545       C  
ATOM   2729  N   GLY L 160      54.208  27.770  17.462  1.00 64.45           N  
ANISOU 2729  N   GLY L 160     7074  10696   6718   -378   -737    296       N  
ATOM   2730  CA  GLY L 160      55.262  26.891  17.913  1.00 62.85           C  
ANISOU 2730  CA  GLY L 160     7181   9959   6742   -331   -519   -184       C  
ATOM   2731  C   GLY L 160      55.146  26.481  19.368  1.00 60.79           C  
ANISOU 2731  C   GLY L 160     7027   9275   6794    -16   -558   -334       C  
ATOM   2732  O   GLY L 160      56.132  25.980  19.959  1.00 59.89           O  
ANISOU 2732  O   GLY L 160     7070   8725   6959    184   -409   -573       O  
ATOM   2733  N   VAL L 161      53.973  26.722  19.971  1.00 59.60           N  
ANISOU 2733  N   VAL L 161     6742   9312   6591     63   -745   -129       N  
ATOM   2734  CA  VAL L 161      53.773  26.238  21.324  1.00 57.42           C  
ANISOU 2734  CA  VAL L 161     6581   8704   6532    297   -766   -280       C  
ATOM   2735  C   VAL L 161      52.955  24.969  21.277  1.00 59.44           C  
ANISOU 2735  C   VAL L 161     6980   9140   6463    -90   -674   -481       C  
ATOM   2736  O   VAL L 161      52.142  24.741  20.374  1.00 62.34           O  
ANISOU 2736  O   VAL L 161     7258  10042   6385   -555   -694   -411       O  
ATOM   2737  CB  VAL L 161      53.171  27.241  22.326  1.00 55.75           C  
ANISOU 2737  CB  VAL L 161     6215   8425   6542    688   -937    -12       C  
ATOM   2738  CG1 VAL L 161      53.092  28.612  21.751  1.00 57.38           C  
ANISOU 2738  CG1 VAL L 161     6235   8758   6811    846   -984    371       C  
ATOM   2739  CG2 VAL L 161      51.819  26.775  22.774  1.00 56.83           C  
ANISOU 2739  CG2 VAL L 161     6257   8866   6468    610  -1006     84       C  
ATOM   2740  N   GLU L 162      53.196  24.130  22.270  1.00 58.17           N  
ANISOU 2740  N   GLU L 162     7044   8565   6492     52   -561   -710       N  
ATOM   2741  CA  GLU L 162      52.766  22.765  22.216  1.00 59.77           C  
ANISOU 2741  CA  GLU L 162     7539   8711   6459   -335   -334   -983       C  
ATOM   2742  C   GLU L 162      52.645  22.362  23.678  1.00 57.70           C  
ANISOU 2742  C   GLU L 162     7354   8108   6461     -2   -355   -989       C  
ATOM   2743  O   GLU L 162      53.632  22.322  24.408  1.00 55.77           O  
ANISOU 2743  O   GLU L 162     7167   7461   6562    410   -295  -1008       O  
ATOM   2744  CB  GLU L 162      53.851  21.970  21.502  1.00 61.87           C  
ANISOU 2744  CB  GLU L 162     8141   8624   6742   -462     63  -1290       C  
ATOM   2745  CG  GLU L 162      53.381  20.718  20.846  1.00 67.05           C  
ANISOU 2745  CG  GLU L 162     9203   9266   7008  -1085    420  -1632       C  
ATOM   2746  CD  GLU L 162      52.751  20.973  19.499  1.00 70.52           C  
ANISOU 2746  CD  GLU L 162     9545  10367   6882  -1745    347  -1648       C  
ATOM   2747  OE1 GLU L 162      53.441  21.496  18.586  1.00 71.44           O  
ANISOU 2747  OE1 GLU L 162     9584  10611   6948  -1748    387  -1624       O  
ATOM   2748  OE2 GLU L 162      51.563  20.629  19.346  1.00 72.42           O  
ANISOU 2748  OE2 GLU L 162     9752  11081   6682  -2308    247  -1656       O  
ATOM   2749  N   THR L 163      51.421  22.145  24.132  1.00 58.17           N  
ANISOU 2749  N   THR L 163     7340   8439   6323   -184   -469   -908       N  
ATOM   2750  CA  THR L 163      51.189  21.961  25.553  1.00 56.51           C  
ANISOU 2750  CA  THR L 163     7144   8005   6323    142   -530   -854       C  
ATOM   2751  C   THR L 163      50.505  20.629  25.837  1.00 58.94           C  
ANISOU 2751  C   THR L 163     7730   8230   6433   -237   -323  -1019       C  
ATOM   2752  O   THR L 163      49.674  20.171  25.052  1.00 62.77           O  
ANISOU 2752  O   THR L 163     8258   9075   6517   -841   -263  -1102       O  
ATOM   2753  CB  THR L 163      50.365  23.143  26.123  1.00 55.12           C  
ANISOU 2753  CB  THR L 163     6603   8167   6172    413   -820   -544       C  
ATOM   2754  OG1 THR L 163      51.062  24.366  25.868  1.00 53.56           O  
ANISOU 2754  OG1 THR L 163     6264   7904   6182    723   -919   -419       O  
ATOM   2755  CG2 THR L 163      50.166  23.004  27.615  1.00 53.18           C  
ANISOU 2755  CG2 THR L 163     6396   7716   6094    723   -858   -526       C  
ATOM   2756  N   THR L 164      50.876  19.974  26.930  1.00 58.13           N  
ANISOU 2756  N   THR L 164     7830   7686   6573     49   -192  -1051       N  
ATOM   2757  CA  THR L 164      50.170  18.751  27.302  1.00 60.98           C  
ANISOU 2757  CA  THR L 164     8490   7906   6774   -302     40  -1163       C  
ATOM   2758  C   THR L 164      48.914  19.059  28.096  1.00 60.16           C  
ANISOU 2758  C   THR L 164     8106   8236   6516   -352   -222   -965       C  
ATOM   2759  O   THR L 164      48.797  20.098  28.733  1.00 57.89           O  
ANISOU 2759  O   THR L 164     7485   8151   6359     72   -499   -750       O  
ATOM   2760  CB  THR L 164      51.027  17.781  28.147  1.00 61.62           C  
ANISOU 2760  CB  THR L 164     8914   7328   7170     50    365  -1178       C  
ATOM   2761  OG1 THR L 164      51.233  18.324  29.469  1.00 58.75           O  
ANISOU 2761  OG1 THR L 164     8289   7007   7029    589     97   -925       O  
ATOM   2762  CG2 THR L 164      52.331  17.483  27.447  1.00 62.36           C  
ANISOU 2762  CG2 THR L 164     9222   7005   7468    238    693  -1288       C  
ATOM   2763  N   THR L 165      47.963  18.143  28.050  1.00 63.52           N  
ANISOU 2763  N   THR L 165     8698   8795   6643   -911    -77  -1052       N  
ATOM   2764  CA  THR L 165      46.886  18.156  29.029  1.00 64.02           C  
ANISOU 2764  CA  THR L 165     8542   9178   6604   -913   -231   -851       C  
ATOM   2765  C   THR L 165      47.539  17.732  30.351  1.00 62.48           C  
ANISOU 2765  C   THR L 165     8564   8421   6753   -400   -118   -805       C  
ATOM   2766  O   THR L 165      48.641  17.147  30.336  1.00 63.30           O  
ANISOU 2766  O   THR L 165     9006   7943   7102   -195    144   -908       O  
ATOM   2767  CB  THR L 165      45.764  17.184  28.629  1.00 67.93           C  
ANISOU 2767  CB  THR L 165     9171   9987   6651  -1764    -81   -960       C  
ATOM   2768  OG1 THR L 165      46.162  15.852  28.943  1.00 70.18           O  
ANISOU 2768  OG1 THR L 165    10075   9560   7032  -1967    355  -1201       O  
ATOM   2769  CG2 THR L 165      45.514  17.264  27.135  1.00 71.09           C  
ANISOU 2769  CG2 THR L 165     9509  10857   6646  -2417    -93  -1092       C  
ATOM   2770  N   PRO L 166      46.909  18.082  31.489  1.00 61.06           N  
ANISOU 2770  N   PRO L 166     8146   8474   6579   -147   -298   -597       N  
ATOM   2771  CA  PRO L 166      47.396  17.732  32.834  1.00 60.07           C  
ANISOU 2771  CA  PRO L 166     8156   7995   6672    281   -243   -491       C  
ATOM   2772  C   PRO L 166      47.191  16.261  33.204  1.00 63.60           C  
ANISOU 2772  C   PRO L 166     9020   8064   7081    -13    107   -512       C  
ATOM   2773  O   PRO L 166      46.171  15.688  32.855  1.00 66.10           O  
ANISOU 2773  O   PRO L 166     9422   8578   7116   -613    216   -587       O  
ATOM   2774  CB  PRO L 166      46.513  18.574  33.744  1.00 58.61           C  
ANISOU 2774  CB  PRO L 166     7606   8276   6386    487   -488   -308       C  
ATOM   2775  CG  PRO L 166      46.012  19.663  32.882  1.00 58.17           C  
ANISOU 2775  CG  PRO L 166     7202   8672   6228    448   -666   -262       C  
ATOM   2776  CD  PRO L 166      45.861  19.107  31.540  1.00 60.22           C  
ANISOU 2776  CD  PRO L 166     7556   9025   6298   -110   -569   -388       C  
ATOM   2777  N   SER L 167      48.130  15.668  33.935  1.00 64.07           N  
ANISOU 2777  N   SER L 167     9314   7629   7402    389    297   -392       N  
ATOM   2778  CA  SER L 167      47.958  14.300  34.381  1.00 68.34           C  
ANISOU 2778  CA  SER L 167    10287   7718   7960    210    703   -322       C  
ATOM   2779  C   SER L 167      48.227  14.165  35.872  1.00 68.04           C  
ANISOU 2779  C   SER L 167    10156   7656   8039    706    636     30       C  
ATOM   2780  O   SER L 167      49.172  14.745  36.389  1.00 65.91           O  
ANISOU 2780  O   SER L 167     9653   7462   7929   1242    440    201       O  
ATOM   2781  CB  SER L 167      48.824  13.332  33.546  1.00 72.42           C  
ANISOU 2781  CB  SER L 167    11322   7525   8669    150   1230   -460       C  
ATOM   2782  OG  SER L 167      50.157  13.804  33.371  1.00 71.49           O  
ANISOU 2782  OG  SER L 167    11057   7268   8838    732   1188   -365       O  
ATOM   2783  N   LYS L 168      47.366  13.420  36.561  1.00 71.05           N  
ANISOU 2783  N   LYS L 168    10697   8019   8279    449    785    147       N  
ATOM   2784  CA  LYS L 168      47.588  13.062  37.967  1.00 72.25           C  
ANISOU 2784  CA  LYS L 168    10827   8132   8493    855    799    530       C  
ATOM   2785  C   LYS L 168      49.006  12.582  38.277  1.00 74.08           C  
ANISOU 2785  C   LYS L 168    11179   7926   9042   1448   1015    847       C  
ATOM   2786  O   LYS L 168      49.523  11.693  37.615  1.00 77.93           O  
ANISOU 2786  O   LYS L 168    12082   7780   9750   1450   1498    844       O  
ATOM   2787  CB  LYS L 168      46.619  11.966  38.393  1.00 76.31           C  
ANISOU 2787  CB  LYS L 168    11667   8459   8866    419   1116    621       C  
ATOM   2788  CG  LYS L 168      45.376  12.461  39.094  1.00 75.35           C  
ANISOU 2788  CG  LYS L 168    11204   9001   8425    182    819    650       C  
ATOM   2789  CD  LYS L 168      44.748  11.325  39.897  1.00 80.21           C  
ANISOU 2789  CD  LYS L 168    12119   9407   8950    -77   1137    889       C  
ATOM   2790  CE  LYS L 168      43.359  11.705  40.428  1.00 80.38           C  
ANISOU 2790  CE  LYS L 168    11793  10131   8618   -427    916    902       C  
ATOM   2791  NZ  LYS L 168      42.802  10.697  41.386  1.00 84.10           N  
ANISOU 2791  NZ  LYS L 168    12501  10467   8985   -633   1189   1190       N  
ATOM   2792  N   GLN L 169      49.616  13.159  39.304  1.00 72.66           N  
ANISOU 2792  N   GLN L 169    10628   8127   8851   1931    699   1146       N  
ATOM   2793  CA  GLN L 169      50.907  12.696  39.784  1.00 75.96           C  
ANISOU 2793  CA  GLN L 169    11002   8364   9496   2508    852   1612       C  
ATOM   2794  C   GLN L 169      50.707  11.593  40.817  1.00 80.74           C  
ANISOU 2794  C   GLN L 169    11809   8764  10104   2660   1152   2102       C  
ATOM   2795  O   GLN L 169      49.582  11.360  41.239  1.00 81.05           O  
ANISOU 2795  O   GLN L 169    11980   8879   9934   2284   1158   2020       O  
ATOM   2796  CB  GLN L 169      51.668  13.851  40.410  1.00 73.37           C  
ANISOU 2796  CB  GLN L 169    10143   8688   9047   2811    340   1716       C  
ATOM   2797  CG  GLN L 169      51.964  14.988  39.462  1.00 69.25           C  
ANISOU 2797  CG  GLN L 169     9438   8326   8548   2696     77   1298       C  
ATOM   2798  CD  GLN L 169      52.564  16.145  40.206  1.00 68.15           C  
ANISOU 2798  CD  GLN L 169     8871   8800   8221   2836   -383   1336       C  
ATOM   2799  OE1 GLN L 169      52.547  16.148  41.437  1.00 70.10           O  
ANISOU 2799  OE1 GLN L 169     8965   9432   8238   2922   -540   1597       O  
ATOM   2800  NE2 GLN L 169      53.101  17.133  39.486  1.00 64.91           N  
ANISOU 2800  NE2 GLN L 169     8298   8502   7864   2792   -579   1069       N  
ATOM   2801  N   SER L 170      51.780  10.919  41.229  1.00 84.91           N  
ANISOU 2801  N   SER L 170    12321   9078  10861   3231   1420   2680       N  
ATOM   2802  CA  SER L 170      51.643   9.862  42.238  1.00 90.40           C  
ANISOU 2802  CA  SER L 170    13195   9576  11576   3452   1743   3271       C  
ATOM   2803  C   SER L 170      50.972  10.377  43.528  1.00 88.85           C  
ANISOU 2803  C   SER L 170    12667  10134  10957   3310   1267   3385       C  
ATOM   2804  O   SER L 170      50.320   9.622  44.247  1.00 92.04           O  
ANISOU 2804  O   SER L 170    13288  10412  11271   3215   1485   3667       O  
ATOM   2805  CB  SER L 170      52.995   9.194  42.524  1.00 96.08           C  
ANISOU 2805  CB  SER L 170    13796  10107  12601   4224   2078   4032       C  
ATOM   2806  OG  SER L 170      54.059  10.058  42.158  1.00 94.26           O  
ANISOU 2806  OG  SER L 170    13077  10328  12408   4505   1740   4015       O  
ATOM   2807  N   ASN L 171      51.091  11.677  43.784  1.00 84.28           N  
ANISOU 2807  N   ASN L 171    11624  10293  10106   3245    675   3122       N  
ATOM   2808  CA  ASN L 171      50.511  12.292  44.986  1.00 83.36           C  
ANISOU 2808  CA  ASN L 171    11235  10890   9548   3096    280   3141       C  
ATOM   2809  C   ASN L 171      49.147  12.973  44.801  1.00 79.49           C  
ANISOU 2809  C   ASN L 171    10809  10554   8839   2587    124   2550       C  
ATOM   2810  O   ASN L 171      48.670  13.670  45.698  1.00 78.33           O  
ANISOU 2810  O   ASN L 171    10450  10980   8332   2487   -156   2470       O  
ATOM   2811  CB  ASN L 171      51.480  13.315  45.563  1.00 82.87           C  
ANISOU 2811  CB  ASN L 171    10676  11565   9246   3288   -192   3228       C  
ATOM   2812  CG  ASN L 171      52.119  14.155  44.495  1.00 80.05           C  
ANISOU 2812  CG  ASN L 171    10205  11139   9070   3274   -344   2824       C  
ATOM   2813  OD1 ASN L 171      51.585  15.217  44.103  1.00 75.65           O  
ANISOU 2813  OD1 ASN L 171     9634  10711   8399   2962   -573   2246       O  
ATOM   2814  ND2 ASN L 171      53.254  13.663  43.966  1.00 82.24           N  
ANISOU 2814  ND2 ASN L 171    10409  11178   9662   3654   -150   3172       N  
ATOM   2815  N   ASN L 172      48.541  12.803  43.627  1.00 77.95           N  
ANISOU 2815  N   ASN L 172    10879   9910   8828   2267    328   2161       N  
ATOM   2816  CA  ASN L 172      47.195  13.338  43.343  1.00 75.24           C  
ANISOU 2816  CA  ASN L 172    10509   9795   8283   1806    222   1738       C  
ATOM   2817  C   ASN L 172      47.099  14.834  43.082  1.00 71.18           C  
ANISOU 2817  C   ASN L 172     9674   9722   7650   1811   -150   1352       C  
ATOM   2818  O   ASN L 172      46.001  15.389  43.004  1.00 69.75           O  
ANISOU 2818  O   ASN L 172     9377   9829   7297   1571   -219   1126       O  
ATOM   2819  CB  ASN L 172      46.193  12.925  44.417  1.00 77.58           C  
ANISOU 2819  CB  ASN L 172    10817  10357   8304   1631    283   1941       C  
ATOM   2820  CG  ASN L 172      46.000  11.432  44.467  1.00 82.86           C  
ANISOU 2820  CG  ASN L 172    11904  10474   9106   1480    745   2260       C  
ATOM   2821  OD1 ASN L 172      46.620  10.744  45.283  1.00 86.69           O  
ANISOU 2821  OD1 ASN L 172    12468  10830   9641   1819    896   2769       O  
ATOM   2822  ND2 ASN L 172      45.179  10.907  43.554  1.00 83.80           N  
ANISOU 2822  ND2 ASN L 172    12309  10262   9268    942   1010   1990       N  
ATOM   2823  N   LYS L 173      48.242  15.494  42.951  1.00 69.61           N  
ANISOU 2823  N   LYS L 173     9322   9581   7546   2094   -346   1323       N  
ATOM   2824  CA  LYS L 173      48.261  16.822  42.345  1.00 65.85           C  
ANISOU 2824  CA  LYS L 173     8669   9290   7062   2059   -580    932       C  
ATOM   2825  C   LYS L 173      48.533  16.643  40.842  1.00 64.13           C  
ANISOU 2825  C   LYS L 173     8571   8668   7127   1957   -455    754       C  
ATOM   2826  O   LYS L 173      48.682  15.514  40.376  1.00 66.56           O  
ANISOU 2826  O   LYS L 173     9140   8547   7602   1890   -157    879       O  
ATOM   2827  CB  LYS L 173      49.301  17.692  43.042  1.00 65.92           C  
ANISOU 2827  CB  LYS L 173     8473   9627   6946   2273   -849    951       C  
ATOM   2828  CG  LYS L 173      48.864  18.068  44.440  1.00 67.79           C  
ANISOU 2828  CG  LYS L 173     8632  10331   6794   2242   -956    992       C  
ATOM   2829  CD  LYS L 173      50.016  18.212  45.412  1.00 70.90           C  
ANISOU 2829  CD  LYS L 173     8856  11127   6956   2350  -1164   1229       C  
ATOM   2830  CE  LYS L 173      50.274  19.681  45.731  1.00 70.49           C  
ANISOU 2830  CE  LYS L 173     8743  11396   6645   2188  -1367    820       C  
ATOM   2831  NZ  LYS L 173      50.722  19.886  47.145  1.00 74.03           N  
ANISOU 2831  NZ  LYS L 173     9080  12462   6588   2060  -1540    952       N  
ATOM   2832  N   TYR L 174      48.586  17.720  40.075  1.00 60.99           N  
ANISOU 2832  N   TYR L 174     8038   8366   6770   1925   -617    466       N  
ATOM   2833  CA  TYR L 174      48.713  17.567  38.619  1.00 60.23           C  
ANISOU 2833  CA  TYR L 174     8043   7980   6860   1759   -501    295       C  
ATOM   2834  C   TYR L 174      50.009  18.116  38.038  1.00 59.22           C  
ANISOU 2834  C   TYR L 174     7835   7741   6923   1972   -597    236       C  
ATOM   2835  O   TYR L 174      50.621  19.015  38.620  1.00 58.88           O  
ANISOU 2835  O   TYR L 174     7603   7939   6831   2154   -827    233       O  
ATOM   2836  CB  TYR L 174      47.525  18.198  37.897  1.00 58.50           C  
ANISOU 2836  CB  TYR L 174     7701   8012   6514   1473   -557     97       C  
ATOM   2837  CG  TYR L 174      46.237  17.415  38.012  1.00 61.16           C  
ANISOU 2837  CG  TYR L 174     8094   8482   6660   1105   -406    162       C  
ATOM   2838  CD1 TYR L 174      45.484  17.451  39.174  1.00 62.13           C  
ANISOU 2838  CD1 TYR L 174     8109   8898   6599   1159   -432    302       C  
ATOM   2839  CD2 TYR L 174      45.771  16.635  36.952  1.00 63.16           C  
ANISOU 2839  CD2 TYR L 174     8518   8614   6865    619   -217     63       C  
ATOM   2840  CE1 TYR L 174      44.301  16.735  39.280  1.00 64.87           C  
ANISOU 2840  CE1 TYR L 174     8463   9431   6754    772   -292    389       C  
ATOM   2841  CE2 TYR L 174      44.593  15.912  37.052  1.00 65.89           C  
ANISOU 2841  CE2 TYR L 174     8904   9154   6978    144    -83    113       C  
ATOM   2842  CZ  TYR L 174      43.859  15.971  38.216  1.00 66.81           C  
ANISOU 2842  CZ  TYR L 174     8856   9581   6948    239   -131    299       C  
ATOM   2843  OH  TYR L 174      42.689  15.256  38.325  1.00 70.16           O  
ANISOU 2843  OH  TYR L 174     9276  10258   7125   -274      3    378       O  
ATOM   2844  N   ALA L 175      50.410  17.578  36.888  1.00 59.22           N  
ANISOU 2844  N   ALA L 175     8000   7397   7101   1881   -388    163       N  
ATOM   2845  CA  ALA L 175      51.582  18.066  36.199  1.00 58.02           C  
ANISOU 2845  CA  ALA L 175     7752   7166   7129   2056   -439    114       C  
ATOM   2846  C   ALA L 175      51.270  18.411  34.749  1.00 56.92           C  
ANISOU 2846  C   ALA L 175     7666   6959   7002   1770   -393   -161       C  
ATOM   2847  O   ALA L 175      50.344  17.863  34.147  1.00 58.13           O  
ANISOU 2847  O   ALA L 175     7995   7055   7036   1398   -230   -280       O  
ATOM   2848  CB  ALA L 175      52.691  17.058  36.271  1.00 60.82           C  
ANISOU 2848  CB  ALA L 175     8214   7199   7698   2350   -163    389       C  
ATOM   2849  N   ALA L 176      52.046  19.327  34.187  1.00 54.93           N  
ANISOU 2849  N   ALA L 176     7244   6783   6843   1878   -542   -241       N  
ATOM   2850  CA  ALA L 176      52.003  19.538  32.770  1.00 54.62           C  
ANISOU 2850  CA  ALA L 176     7253   6684   6815   1645   -466   -429       C  
ATOM   2851  C   ALA L 176      53.238  20.234  32.237  1.00 54.04           C  
ANISOU 2851  C   ALA L 176     7033   6594   6905   1827   -539   -441       C  
ATOM   2852  O   ALA L 176      54.021  20.811  32.983  1.00 54.05           O  
ANISOU 2852  O   ALA L 176     6841   6724   6969   2064   -721   -330       O  
ATOM   2853  CB  ALA L 176      50.778  20.282  32.395  1.00 54.12           C  
ANISOU 2853  CB  ALA L 176     7059   6951   6555   1393   -627   -512       C  
ATOM   2854  N   SER L 177      53.397  20.167  30.923  1.00 54.44           N  
ANISOU 2854  N   SER L 177     7172   6546   6966   1634   -389   -583       N  
ATOM   2855  CA  SER L 177      54.552  20.711  30.281  1.00 54.12           C  
ANISOU 2855  CA  SER L 177     7003   6490   7072   1766   -401   -586       C  
ATOM   2856  C   SER L 177      54.089  21.455  29.050  1.00 53.34           C  
ANISOU 2856  C   SER L 177     6864   6558   6847   1474   -472   -730       C  
ATOM   2857  O   SER L 177      53.040  21.143  28.489  1.00 53.13           O  
ANISOU 2857  O   SER L 177     6941   6641   6605   1135   -414   -818       O  
ATOM   2858  CB  SER L 177      55.535  19.593  29.910  1.00 57.00           C  
ANISOU 2858  CB  SER L 177     7540   6507   7609   1934      3   -527       C  
ATOM   2859  OG  SER L 177      54.850  18.452  29.406  1.00 59.49           O  
ANISOU 2859  OG  SER L 177     8260   6511   7831   1659    382   -683       O  
ATOM   2860  N   SER L 178      54.892  22.434  28.642  1.00 52.51           N  
ANISOU 2860  N   SER L 178     6575   6535   6841   1567   -600   -708       N  
ATOM   2861  CA  SER L 178      54.654  23.211  27.445  1.00 52.01           C  
ANISOU 2861  CA  SER L 178     6442   6638   6681   1353   -651   -752       C  
ATOM   2862  C   SER L 178      56.020  23.518  26.826  1.00 52.72           C  
ANISOU 2862  C   SER L 178     6450   6656   6927   1443   -578   -750       C  
ATOM   2863  O   SER L 178      56.950  23.927  27.542  1.00 53.57           O  
ANISOU 2863  O   SER L 178     6403   6756   7195   1659   -684   -661       O  
ATOM   2864  CB  SER L 178      53.950  24.495  27.855  1.00 50.81           C  
ANISOU 2864  CB  SER L 178     6128   6675   6504   1419   -901   -646       C  
ATOM   2865  OG  SER L 178      53.861  25.414  26.796  1.00 51.64           O  
ANISOU 2865  OG  SER L 178     6125   6928   6568   1319   -940   -567       O  
ATOM   2866  N   TYR L 179      56.144  23.272  25.521  1.00 53.84           N  
ANISOU 2866  N   TYR L 179     6676   6815   6965   1221   -387   -842       N  
ATOM   2867  CA  TYR L 179      57.387  23.481  24.758  1.00 54.90           C  
ANISOU 2867  CA  TYR L 179     6731   6916   7214   1279   -252   -838       C  
ATOM   2868  C   TYR L 179      57.194  24.569  23.686  1.00 55.43           C  
ANISOU 2868  C   TYR L 179     6679   7230   7151   1053   -383   -796       C  
ATOM   2869  O   TYR L 179      56.221  24.526  22.911  1.00 55.41           O  
ANISOU 2869  O   TYR L 179     6739   7441   6875    751   -383   -819       O  
ATOM   2870  CB  TYR L 179      57.829  22.187  24.073  1.00 57.32           C  
ANISOU 2870  CB  TYR L 179     7299   6981   7498   1232    215   -987       C  
ATOM   2871  CG  TYR L 179      58.069  21.019  25.009  1.00 59.37           C  
ANISOU 2871  CG  TYR L 179     7719   6914   7927   1523    470   -939       C  
ATOM   2872  CD1 TYR L 179      59.354  20.668  25.407  1.00 61.13           C  
ANISOU 2872  CD1 TYR L 179     7787   7016   8421   1963    668   -729       C  
ATOM   2873  CD2 TYR L 179      57.015  20.257  25.485  1.00 59.32           C  
ANISOU 2873  CD2 TYR L 179     7976   6767   7797   1368    535  -1028       C  
ATOM   2874  CE1 TYR L 179      59.577  19.598  26.251  1.00 62.88           C  
ANISOU 2874  CE1 TYR L 179     8120   6963   8809   2309    941   -558       C  
ATOM   2875  CE2 TYR L 179      57.237  19.194  26.328  1.00 60.96           C  
ANISOU 2875  CE2 TYR L 179     8356   6633   8173   1653    812   -923       C  
ATOM   2876  CZ  TYR L 179      58.512  18.865  26.699  1.00 62.93           C  
ANISOU 2876  CZ  TYR L 179     8458   6740   8711   2154   1026   -665       C  
ATOM   2877  OH  TYR L 179      58.686  17.799  27.548  1.00 66.46           O  
ANISOU 2877  OH  TYR L 179     9053   6870   9331   2502   1332   -445       O  
ATOM   2878  N   LEU L 180      58.106  25.549  23.638  1.00 54.98           N  
ANISOU 2878  N   LEU L 180     6430   7205   7255   1157   -493   -686       N  
ATOM   2879  CA  LEU L 180      58.046  26.599  22.614  1.00 54.58           C  
ANISOU 2879  CA  LEU L 180     6287   7330   7119    981   -563   -578       C  
ATOM   2880  C   LEU L 180      59.200  26.395  21.666  1.00 56.52           C  
ANISOU 2880  C   LEU L 180     6489   7604   7383    917   -343   -617       C  
ATOM   2881  O   LEU L 180      60.344  26.431  22.086  1.00 58.04           O  
ANISOU 2881  O   LEU L 180     6540   7732   7780   1085   -307   -582       O  
ATOM   2882  CB  LEU L 180      58.154  27.989  23.246  1.00 53.93           C  
ANISOU 2882  CB  LEU L 180     6103   7186   7203   1080   -777   -433       C  
ATOM   2883  CG  LEU L 180      58.249  29.155  22.252  1.00 54.86           C  
ANISOU 2883  CG  LEU L 180     6155   7383   7304    957   -781   -244       C  
ATOM   2884  CD1 LEU L 180      56.949  29.265  21.460  1.00 56.23           C  
ANISOU 2884  CD1 LEU L 180     6313   7815   7237    874   -795    -52       C  
ATOM   2885  CD2 LEU L 180      58.523  30.447  22.947  1.00 54.72           C  
ANISOU 2885  CD2 LEU L 180     6167   7141   7484   1011   -863   -167       C  
ATOM   2886  N   SER L 181      58.902  26.143  20.393  1.00 58.46           N  
ANISOU 2886  N   SER L 181     6823   8025   7365    643   -182   -671       N  
ATOM   2887  CA  SER L 181      59.931  25.969  19.373  1.00 60.12           C  
ANISOU 2887  CA  SER L 181     7018   8284   7540    558     90   -726       C  
ATOM   2888  C   SER L 181      60.303  27.290  18.724  1.00 60.80           C  
ANISOU 2888  C   SER L 181     6899   8566   7635    461    -61   -498       C  
ATOM   2889  O   SER L 181      59.440  28.053  18.314  1.00 60.85           O  
ANISOU 2889  O   SER L 181     6870   8769   7482    316   -240   -311       O  
ATOM   2890  CB  SER L 181      59.444  25.010  18.312  1.00 62.37           C  
ANISOU 2890  CB  SER L 181     7572   8672   7453    208    396   -959       C  
ATOM   2891  OG  SER L 181      59.557  23.686  18.777  1.00 64.14           O  
ANISOU 2891  OG  SER L 181     8072   8554   7746    318    731  -1197       O  
ATOM   2892  N   LEU L 182      61.596  27.573  18.632  1.00 62.06           N  
ANISOU 2892  N   LEU L 182     6895   8700   7983    555     37   -447       N  
ATOM   2893  CA  LEU L 182      62.034  28.835  18.038  1.00 62.67           C  
ANISOU 2893  CA  LEU L 182     6814   8914   8085    412    -66   -226       C  
ATOM   2894  C   LEU L 182      63.115  28.576  17.017  1.00 64.99           C  
ANISOU 2894  C   LEU L 182     7010   9370   8312    322    232   -247       C  
ATOM   2895  O   LEU L 182      63.706  27.505  16.982  1.00 67.26           O  
ANISOU 2895  O   LEU L 182     7327   9604   8626    467    543   -411       O  
ATOM   2896  CB  LEU L 182      62.601  29.770  19.113  1.00 61.90           C  
ANISOU 2896  CB  LEU L 182     6578   8665   8278    502   -282   -118       C  
ATOM   2897  CG  LEU L 182      61.747  30.253  20.281  1.00 59.78           C  
ANISOU 2897  CG  LEU L 182     6424   8183   8106    597   -519   -116       C  
ATOM   2898  CD1 LEU L 182      62.581  31.160  21.191  1.00 60.60           C  
ANISOU 2898  CD1 LEU L 182     6446   8178   8402    512   -644    -97       C  
ATOM   2899  CD2 LEU L 182      60.549  30.983  19.758  1.00 59.54           C  
ANISOU 2899  CD2 LEU L 182     6514   8148   7960    555   -575     73       C  
ATOM   2900  N   THR L 183      63.344  29.578  16.188  1.00 65.84           N  
ANISOU 2900  N   THR L 183     7020   9650   8346    116    191    -41       N  
ATOM   2901  CA  THR L 183      64.562  29.736  15.415  1.00 69.13           C  
ANISOU 2901  CA  THR L 183     7257  10241   8769     27    415     22       C  
ATOM   2902  C   THR L 183      65.724  30.198  16.319  1.00 69.71           C  
ANISOU 2902  C   THR L 183     7046  10271   9169    131    324    122       C  
ATOM   2903  O   THR L 183      65.524  31.021  17.223  1.00 68.68           O  
ANISOU 2903  O   THR L 183     6918   9982   9196     88     40    196       O  
ATOM   2904  CB  THR L 183      64.320  30.829  14.371  1.00 70.53           C  
ANISOU 2904  CB  THR L 183     7419  10616   8764   -255    350    290       C  
ATOM   2905  OG1 THR L 183      63.943  30.230  13.131  1.00 72.46           O  
ANISOU 2905  OG1 THR L 183     7777  11165   8590   -468    567    211       O  
ATOM   2906  CG2 THR L 183      65.559  31.682  14.175  1.00 73.27           C  
ANISOU 2906  CG2 THR L 183     7534  11023   9283   -366    396    476       C  
ATOM   2907  N   PRO L 184      66.946  29.689  16.082  1.00 72.35           N  
ANISOU 2907  N   PRO L 184     7124  10795   9569    233    594    139       N  
ATOM   2908  CA  PRO L 184      68.035  30.230  16.900  1.00 73.55           C  
ANISOU 2908  CA  PRO L 184     6899  11103   9942    213    446    312       C  
ATOM   2909  C   PRO L 184      68.101  31.763  16.839  1.00 74.30           C  
ANISOU 2909  C   PRO L 184     6999  11176  10057   -201    202    460       C  
ATOM   2910  O   PRO L 184      68.269  32.406  17.887  1.00 74.78           O  
ANISOU 2910  O   PRO L 184     7008  11169  10235   -355    -48    473       O  
ATOM   2911  CB  PRO L 184      69.293  29.605  16.290  1.00 77.40           C  
ANISOU 2911  CB  PRO L 184     7045  11914  10448    370    836    420       C  
ATOM   2912  CG  PRO L 184      68.817  28.361  15.632  1.00 77.96           C  
ANISOU 2912  CG  PRO L 184     7421  11810  10390    624   1249    198       C  
ATOM   2913  CD  PRO L 184      67.396  28.610  15.185  1.00 75.24           C  
ANISOU 2913  CD  PRO L 184     7520  11263   9806    366   1077     17       C  
ATOM   2914  N   GLU L 185      67.941  32.351  15.649  1.00 75.25           N  
ANISOU 2914  N   GLU L 185     7228  11329  10037   -414    312    570       N  
ATOM   2915  CA  GLU L 185      67.976  33.820  15.523  1.00 76.66           C  
ANISOU 2915  CA  GLU L 185     7487  11372  10268   -775    182    768       C  
ATOM   2916  C   GLU L 185      66.812  34.532  16.259  1.00 74.80           C  
ANISOU 2916  C   GLU L 185     7611  10688  10123   -757    -27    758       C  
ATOM   2917  O   GLU L 185      66.963  35.666  16.720  1.00 76.83           O  
ANISOU 2917  O   GLU L 185     8002  10675  10514  -1020    -87    832       O  
ATOM   2918  CB  GLU L 185      68.132  34.267  14.055  1.00 78.67           C  
ANISOU 2918  CB  GLU L 185     7737  11809  10344   -971    381    985       C  
ATOM   2919  CG  GLU L 185      66.895  34.204  13.219  1.00 77.79           C  
ANISOU 2919  CG  GLU L 185     7885  11678   9995   -898    399   1071       C  
ATOM   2920  CD  GLU L 185      67.134  34.609  11.766  1.00 81.69           C  
ANISOU 2920  CD  GLU L 185     8324  12480  10236  -1131    587   1330       C  
ATOM   2921  OE1 GLU L 185      66.193  34.478  10.942  1.00 82.56           O  
ANISOU 2921  OE1 GLU L 185     8559  12776  10036  -1143    599   1451       O  
ATOM   2922  OE2 GLU L 185      68.248  35.065  11.439  1.00 83.95           O  
ANISOU 2922  OE2 GLU L 185     8407  12906  10585  -1346    714   1445       O  
ATOM   2923  N   GLN L 186      65.684  33.841  16.413  1.00 71.75           N  
ANISOU 2923  N   GLN L 186     7396  10209   9655   -468    -81    654       N  
ATOM   2924  CA  GLN L 186      64.553  34.375  17.155  1.00 70.41           C  
ANISOU 2924  CA  GLN L 186     7506   9676   9572   -357   -226    672       C  
ATOM   2925  C   GLN L 186      64.900  34.370  18.620  1.00 69.69           C  
ANISOU 2925  C   GLN L 186     7420   9416   9644   -371   -371    450       C  
ATOM   2926  O   GLN L 186      64.633  35.335  19.348  1.00 71.16           O  
ANISOU 2926  O   GLN L 186     7846   9241   9950   -494   -412    440       O  
ATOM   2927  CB  GLN L 186      63.294  33.528  16.943  1.00 68.08           C  
ANISOU 2927  CB  GLN L 186     7303   9470   9095   -105   -258    636       C  
ATOM   2928  CG  GLN L 186      62.583  33.724  15.614  1.00 69.98           C  
ANISOU 2928  CG  GLN L 186     7552   9967   9070   -165   -184    922       C  
ATOM   2929  CD  GLN L 186      61.472  32.706  15.417  1.00 69.70           C  
ANISOU 2929  CD  GLN L 186     7549  10181   8752    -82   -227    828       C  
ATOM   2930  OE1 GLN L 186      61.719  31.499  15.356  1.00 69.51           O  
ANISOU 2930  OE1 GLN L 186     7532  10283   8597   -112   -127    509       O  
ATOM   2931  NE2 GLN L 186      60.237  33.185  15.334  1.00 70.38           N  
ANISOU 2931  NE2 GLN L 186     7660  10339   8743     15   -329   1133       N  
ATOM   2932  N   TRP L 187      65.479  33.265  19.059  1.00 68.52           N  
ANISOU 2932  N   TRP L 187     7029   9528   9476   -240   -398    290       N  
ATOM   2933  CA  TRP L 187      65.932  33.158  20.435  1.00 68.88           C  
ANISOU 2933  CA  TRP L 187     6971   9600   9599   -278   -563    156       C  
ATOM   2934  C   TRP L 187      66.851  34.324  20.784  1.00 72.22           C  
ANISOU 2934  C   TRP L 187     7337  10045  10060   -767   -620    188       C  
ATOM   2935  O   TRP L 187      66.552  35.077  21.703  1.00 73.21           O  
ANISOU 2935  O   TRP L 187     7723   9888  10205   -988   -710     56       O  
ATOM   2936  CB  TRP L 187      66.588  31.788  20.686  1.00 68.32           C  
ANISOU 2936  CB  TRP L 187     6563   9878   9518      2   -510    141       C  
ATOM   2937  CG  TRP L 187      67.285  31.644  22.015  1.00 70.14           C  
ANISOU 2937  CG  TRP L 187     6523  10360   9766    -53   -697    146       C  
ATOM   2938  CD1 TRP L 187      68.601  31.293  22.220  1.00 73.71           C  
ANISOU 2938  CD1 TRP L 187     6455  11336  10215    -76   -682    341       C  
ATOM   2939  CD2 TRP L 187      66.718  31.832  23.321  1.00 69.27           C  
ANISOU 2939  CD2 TRP L 187     6585  10109   9624   -105   -921      5       C  
ATOM   2940  NE1 TRP L 187      68.883  31.266  23.563  1.00 74.91           N  
ANISOU 2940  NE1 TRP L 187     6414  11753  10297   -182   -929    363       N  
ATOM   2941  CE2 TRP L 187      67.750  31.596  24.262  1.00 72.39           C  
ANISOU 2941  CE2 TRP L 187     6551  11006   9946   -228  -1072    117       C  
ATOM   2942  CE3 TRP L 187      65.447  32.191  23.789  1.00 66.72           C  
ANISOU 2942  CE3 TRP L 187     6700   9350   9299    -59   -987   -168       C  
ATOM   2943  CZ2 TRP L 187      67.544  31.718  25.644  1.00 72.67           C  
ANISOU 2943  CZ2 TRP L 187     6631  11122   9857   -381  -1308     12       C  
ATOM   2944  CZ3 TRP L 187      65.248  32.313  25.154  1.00 66.69           C  
ANISOU 2944  CZ3 TRP L 187     6775   9344   9222   -158  -1166   -302       C  
ATOM   2945  CH2 TRP L 187      66.289  32.077  26.066  1.00 69.62           C  
ANISOU 2945  CH2 TRP L 187     6760  10220   9472   -352  -1335   -237       C  
ATOM   2946  N   LYS L 188      67.914  34.520  20.004  1.00 74.98           N  
ANISOU 2946  N   LYS L 188     7396  10702  10390   -993   -515    341       N  
ATOM   2947  CA  LYS L 188      68.869  35.588  20.285  1.00 79.59           C  
ANISOU 2947  CA  LYS L 188     7896  11381  10962  -1585   -557    371       C  
ATOM   2948  C   LYS L 188      68.316  36.979  20.055  1.00 81.17           C  
ANISOU 2948  C   LYS L 188     8616  10989  11236  -1899   -441    372       C  
ATOM   2949  O   LYS L 188      68.850  37.938  20.591  1.00 85.93           O  
ANISOU 2949  O   LYS L 188     9357  11470  11822  -2469   -438    280       O  
ATOM   2950  CB  LYS L 188      70.153  35.458  19.464  1.00 82.90           C  
ANISOU 2950  CB  LYS L 188     7825  12336  11338  -1757   -445    586       C  
ATOM   2951  CG  LYS L 188      70.485  34.067  18.950  1.00 82.64           C  
ANISOU 2951  CG  LYS L 188     7404  12700  11294  -1231   -302    690       C  
ATOM   2952  CD  LYS L 188      71.199  33.191  19.982  1.00 84.10           C  
ANISOU 2952  CD  LYS L 188     7109  13372  11471  -1043   -413    758       C  
ATOM   2953  CE  LYS L 188      72.372  33.918  20.659  1.00 89.71           C  
ANISOU 2953  CE  LYS L 188     7385  14623  12075  -1642   -607    892       C  
ATOM   2954  NZ  LYS L 188      73.158  32.994  21.530  1.00 92.09           N  
ANISOU 2954  NZ  LYS L 188     7053  15612  12324  -1397   -705   1129       N  
ATOM   2955  N   SER L 189      67.271  37.103  19.252  1.00 78.86           N  
ANISOU 2955  N   SER L 189     8610  10351  11002  -1561   -305    509       N  
ATOM   2956  CA  SER L 189      66.820  38.417  18.823  1.00 81.98           C  
ANISOU 2956  CA  SER L 189     9438  10203  11505  -1737    -98    681       C  
ATOM   2957  C   SER L 189      65.925  39.102  19.848  1.00 82.67           C  
ANISOU 2957  C   SER L 189    10036   9665  11710  -1700    -30    528       C  
ATOM   2958  O   SER L 189      65.671  40.303  19.763  1.00 86.78           O  
ANISOU 2958  O   SER L 189    11005   9597  12370  -1872    244    641       O  
ATOM   2959  CB  SER L 189      66.077  38.301  17.506  1.00 81.06           C  
ANISOU 2959  CB  SER L 189     9325  10123  11351  -1378     22   1020       C  
ATOM   2960  OG  SER L 189      64.746  37.867  17.748  1.00 78.78           O  
ANISOU 2960  OG  SER L 189     9182   9697  11053   -911    -33   1031       O  
ATOM   2961  N   HIS L 190      65.424  38.335  20.802  1.00 79.40           N  
ANISOU 2961  N   HIS L 190     9588   9332  11250  -1442   -210    292       N  
ATOM   2962  CA  HIS L 190      64.650  38.918  21.864  1.00 80.30           C  
ANISOU 2962  CA  HIS L 190    10169   8905  11437  -1422   -113    101       C  
ATOM   2963  C   HIS L 190      65.510  39.052  23.082  1.00 83.15           C  
ANISOU 2963  C   HIS L 190    10540   9391  11662  -1983   -240   -274       C  
ATOM   2964  O   HIS L 190      66.564  38.449  23.170  1.00 83.54           O  
ANISOU 2964  O   HIS L 190    10107  10071  11565  -2233   -470   -308       O  
ATOM   2965  CB  HIS L 190      63.440  38.065  22.151  1.00 75.97           C  
ANISOU 2965  CB  HIS L 190     9591   8397  10878   -827   -214    110       C  
ATOM   2966  CG  HIS L 190      62.488  38.016  21.010  1.00 74.94           C  
ANISOU 2966  CG  HIS L 190     9429   8259  10787   -384   -108    507       C  
ATOM   2967  ND1 HIS L 190      61.588  39.027  20.749  1.00 77.83           N  
ANISOU 2967  ND1 HIS L 190    10138   8125  11309   -154    185    816       N  
ATOM   2968  CD2 HIS L 190      62.343  37.111  20.018  1.00 72.41           C  
ANISOU 2968  CD2 HIS L 190     8762   8425  10326   -179   -222    681       C  
ATOM   2969  CE1 HIS L 190      60.904  38.728  19.660  1.00 76.72           C  
ANISOU 2969  CE1 HIS L 190     9769   8293  11089    175    171   1226       C  
ATOM   2970  NE2 HIS L 190      61.343  37.570  19.197  1.00 73.39           N  
ANISOU 2970  NE2 HIS L 190     8963   8465  10456    100    -79   1096       N  
ATOM   2971  N   ARG L 191      65.064  39.860  24.023  1.00 85.94           N  
ANISOU 2971  N   ARG L 191    11432   9188  12032  -2194    -52   -527       N  
ATOM   2972  CA  ARG L 191      65.831  40.068  25.209  1.00 89.18           C  
ANISOU 2972  CA  ARG L 191    11899   9779  12206  -2870   -166   -916       C  
ATOM   2973  C   ARG L 191      65.569  38.989  26.249  1.00 85.83           C  
ANISOU 2973  C   ARG L 191    11201   9810  11601  -2624   -483  -1082       C  
ATOM   2974  O   ARG L 191      66.411  38.698  27.091  1.00 87.62           O  
ANISOU 2974  O   ARG L 191    11139  10604  11548  -3098   -739  -1253       O  
ATOM   2975  CB  ARG L 191      65.501  41.420  25.761  1.00 94.92           C  
ANISOU 2975  CB  ARG L 191    13429   9657  12979  -3294    267  -1185       C  
ATOM   2976  CG  ARG L 191      66.642  41.888  26.483  1.00101.13           C  
ANISOU 2976  CG  ARG L 191    14254  10711  13460  -4293    194  -1532       C  
ATOM   2977  CD  ARG L 191      67.008  43.195  25.981  1.00108.50           C  
ANISOU 2977  CD  ARG L 191    15722  10998  14505  -4862    629  -1553       C  
ATOM   2978  NE  ARG L 191      66.307  44.123  26.765  1.00113.61           N  
ANISOU 2978  NE  ARG L 191    17260  10718  15190  -5045   1119  -1910       N  
ATOM   2979  CZ  ARG L 191      66.280  45.451  26.660  1.00120.74           C  
ANISOU 2979  CZ  ARG L 191    18989  10653  16233  -5496   1737  -2043       C  
ATOM   2980  NH1 ARG L 191      65.575  45.989  27.560  1.00123.98           N  
ANISOU 2980  NH1 ARG L 191    20143  10329  16636  -5533   2166  -2413       N  
ATOM   2981  NH2 ARG L 191      67.021  46.349  25.871  1.00125.59           N  
ANISOU 2981  NH2 ARG L 191    19828  10946  16944  -6075   2022  -1910       N  
ATOM   2982  N   SER L 192      64.395  38.385  26.171  1.00 81.06           N  
ANISOU 2982  N   SER L 192    10643   9028  11129  -1902   -469   -971       N  
ATOM   2983  CA  SER L 192      64.027  37.330  27.085  1.00 77.70           C  
ANISOU 2983  CA  SER L 192     9999   8961  10562  -1618   -722  -1080       C  
ATOM   2984  C   SER L 192      62.721  36.715  26.611  1.00 73.19           C  
ANISOU 2984  C   SER L 192     9448   8203  10156   -870   -665   -880       C  
ATOM   2985  O   SER L 192      61.980  37.321  25.843  1.00 73.25           O  
ANISOU 2985  O   SER L 192     9704   7779  10347   -611   -412   -680       O  
ATOM   2986  CB  SER L 192      63.859  37.882  28.502  1.00 80.76           C  
ANISOU 2986  CB  SER L 192    10800   9138  10746  -2026   -659  -1475       C  
ATOM   2987  OG  SER L 192      62.701  38.693  28.589  1.00 81.72           O  
ANISOU 2987  OG  SER L 192    11550   8456  11045  -1768   -255  -1551       O  
ATOM   2988  N   TYR L 193      62.469  35.494  27.067  1.00 69.70           N  
ANISOU 2988  N   TYR L 193     8712   8150   9623   -556   -895   -882       N  
ATOM   2989  CA  TYR L 193      61.201  34.812  26.868  1.00 65.94           C  
ANISOU 2989  CA  TYR L 193     8255   7585   9214      9   -870   -757       C  
ATOM   2990  C   TYR L 193      60.680  34.399  28.218  1.00 65.21           C  
ANISOU 2990  C   TYR L 193     8261   7523   8991     87   -958   -961       C  
ATOM   2991  O   TYR L 193      61.454  34.254  29.156  1.00 66.75           O  
ANISOU 2991  O   TYR L 193     8354   8002   9005   -241  -1121  -1134       O  
ATOM   2992  CB  TYR L 193      61.383  33.567  26.022  1.00 62.95           C  
ANISOU 2992  CB  TYR L 193     7475   7612   8829    268   -993   -577       C  
ATOM   2993  CG  TYR L 193      61.381  33.804  24.527  1.00 63.17           C  
ANISOU 2993  CG  TYR L 193     7443   7625   8932    319   -866   -343       C  
ATOM   2994  CD1 TYR L 193      60.219  33.622  23.777  1.00 61.53           C  
ANISOU 2994  CD1 TYR L 193     7285   7375   8717    619   -788   -152       C  
ATOM   2995  CD2 TYR L 193      62.540  34.208  23.857  1.00 65.45           C  
ANISOU 2995  CD2 TYR L 193     7579   8046   9243     19   -835   -278       C  
ATOM   2996  CE1 TYR L 193      60.206  33.834  22.404  1.00 62.15           C  
ANISOU 2996  CE1 TYR L 193     7278   7562   8775    609   -694     98       C  
ATOM   2997  CE2 TYR L 193      62.536  34.424  22.481  1.00 66.13           C  
ANISOU 2997  CE2 TYR L 193     7611   8163   9352     46   -709    -48       C  
ATOM   2998  CZ  TYR L 193      61.363  34.234  21.761  1.00 64.58           C  
ANISOU 2998  CZ  TYR L 193     7482   7941   9113    336   -646    138       C  
ATOM   2999  OH  TYR L 193      61.358  34.443  20.397  1.00 65.33           O  
ANISOU 2999  OH  TYR L 193     7493   8185   9143    305   -544    399       O  
ATOM   3000  N   SER L 194      59.375  34.176  28.303  1.00 63.16           N  
ANISOU 3000  N   SER L 194     8139   7079   8780    499   -864   -892       N  
ATOM   3001  CA  SER L 194      58.732  33.939  29.581  1.00 63.11           C  
ANISOU 3001  CA  SER L 194     8284   7045   8650    583   -881  -1075       C  
ATOM   3002  C   SER L 194      57.639  32.889  29.469  1.00 60.09           C  
ANISOU 3002  C   SER L 194     7741   6826   8266   1027   -940   -913       C  
ATOM   3003  O   SER L 194      56.922  32.822  28.470  1.00 58.55           O  
ANISOU 3003  O   SER L 194     7473   6614   8161   1274   -859   -669       O  
ATOM   3004  CB  SER L 194      58.144  35.243  30.116  1.00 66.61           C  
ANISOU 3004  CB  SER L 194     9241   6927   9140    525   -537  -1229       C  
ATOM   3005  OG  SER L 194      59.142  36.015  30.742  1.00 71.38           O  
ANISOU 3005  OG  SER L 194    10081   7431   9609    -71   -497  -1539       O  
ATOM   3006  N   CYS L 195      57.503  32.083  30.509  1.00 58.41           N  
ANISOU 3006  N   CYS L 195     7463   6826   7903   1064  -1080  -1027       N  
ATOM   3007  CA  CYS L 195      56.449  31.114  30.549  1.00 55.89           C  
ANISOU 3007  CA  CYS L 195     7047   6632   7556   1387  -1104   -907       C  
ATOM   3008  C   CYS L 195      55.517  31.541  31.642  1.00 57.30           C  
ANISOU 3008  C   CYS L 195     7470   6646   7656   1494   -975  -1021       C  
ATOM   3009  O   CYS L 195      55.912  31.606  32.803  1.00 58.80           O  
ANISOU 3009  O   CYS L 195     7769   6891   7681   1296  -1031  -1240       O  
ATOM   3010  CB  CYS L 195      57.017  29.731  30.863  1.00 54.89           C  
ANISOU 3010  CB  CYS L 195     6673   6839   7344   1395  -1292   -884       C  
ATOM   3011  SG  CYS L 195      55.801  28.428  30.721  1.00 52.29           S  
ANISOU 3011  SG  CYS L 195     6292   6602   6972   1657  -1264   -763       S  
ATOM   3012  N   GLN L 196      54.276  31.821  31.272  1.00 57.51           N  
ANISOU 3012  N   GLN L 196     7542   6549   7759   1800   -788   -836       N  
ATOM   3013  CA  GLN L 196      53.286  32.290  32.223  1.00 59.27           C  
ANISOU 3013  CA  GLN L 196     7983   6597   7938   1998   -564   -891       C  
ATOM   3014  C   GLN L 196      52.153  31.303  32.462  1.00 57.83           C  
ANISOU 3014  C   GLN L 196     7588   6729   7656   2238   -626   -727       C  
ATOM   3015  O   GLN L 196      51.282  31.090  31.604  1.00 57.37           O  
ANISOU 3015  O   GLN L 196     7304   6861   7634   2436   -598   -411       O  
ATOM   3016  CB  GLN L 196      52.709  33.599  31.745  1.00 62.37           C  
ANISOU 3016  CB  GLN L 196     8592   6580   8525   2237   -180   -718       C  
ATOM   3017  CG  GLN L 196      53.710  34.718  31.667  1.00 65.95           C  
ANISOU 3017  CG  GLN L 196     9388   6597   9074   1939    -10   -920       C  
ATOM   3018  CD  GLN L 196      53.039  36.046  31.297  1.00 71.29           C  
ANISOU 3018  CD  GLN L 196    10377   6718   9990   2264    511   -697       C  
ATOM   3019  OE1 GLN L 196      51.823  36.105  31.061  1.00 72.31           O  
ANISOU 3019  OE1 GLN L 196    10365   6898  10214   2779    716   -311       O  
ATOM   3020  NE2 GLN L 196      53.828  37.112  31.244  1.00 74.61           N  
ANISOU 3020  NE2 GLN L 196    11210   6630  10509   1966    764   -886       N  
ATOM   3021  N   VAL L 197      52.146  30.729  33.654  1.00 57.41           N  
ANISOU 3021  N   VAL L 197     7589   6796   7427   2164   -710   -916       N  
ATOM   3022  CA  VAL L 197      51.154  29.747  33.967  1.00 55.94           C  
ANISOU 3022  CA  VAL L 197     7228   6896   7130   2316   -759   -776       C  
ATOM   3023  C   VAL L 197      50.078  30.376  34.828  1.00 58.52           C  
ANISOU 3023  C   VAL L 197     7704   7125   7404   2564   -471   -775       C  
ATOM   3024  O   VAL L 197      50.373  30.905  35.894  1.00 61.66           O  
ANISOU 3024  O   VAL L 197     8399   7336   7694   2469   -345  -1058       O  
ATOM   3025  CB  VAL L 197      51.802  28.558  34.682  1.00 54.36           C  
ANISOU 3025  CB  VAL L 197     6961   6914   6779   2132  -1000   -882       C  
ATOM   3026  CG1 VAL L 197      50.771  27.490  34.945  1.00 54.04           C  
ANISOU 3026  CG1 VAL L 197     6791   7110   6633   2228  -1011   -732       C  
ATOM   3027  CG2 VAL L 197      52.934  27.986  33.843  1.00 52.35           C  
ANISOU 3027  CG2 VAL L 197     6568   6707   6615   1980  -1171   -849       C  
ATOM   3028  N   THR L 198      48.829  30.336  34.371  1.00 59.25           N  
ANISOU 3028  N   THR L 198     7578   7402   7533   2855   -336   -444       N  
ATOM   3029  CA  THR L 198      47.714  30.830  35.192  1.00 62.11           C  
ANISOU 3029  CA  THR L 198     8005   7738   7854   3181     -1   -363       C  
ATOM   3030  C   THR L 198      46.933  29.687  35.773  1.00 60.80           C  
ANISOU 3030  C   THR L 198     7611   8009   7481   3149   -135   -280       C  
ATOM   3031  O   THR L 198      46.587  28.763  35.060  1.00 59.80           O  
ANISOU 3031  O   THR L 198     7172   8253   7298   3018   -350    -67       O  
ATOM   3032  CB  THR L 198      46.778  31.698  34.358  1.00 65.80           C  
ANISOU 3032  CB  THR L 198     8296   8200   8506   3614    311     88       C  
ATOM   3033  OG1 THR L 198      47.509  32.837  33.886  1.00 67.51           O  
ANISOU 3033  OG1 THR L 198     8808   7902   8939   3653    514     25       O  
ATOM   3034  CG2 THR L 198      45.546  32.165  35.162  1.00 69.25           C  
ANISOU 3034  CG2 THR L 198     8728   8653   8930   4068    743    272       C  
ATOM   3035  N   HIS L 199      46.674  29.738  37.069  1.00 62.65           N  
ANISOU 3035  N   HIS L 199     8043   8198   7565   3196     20   -475       N  
ATOM   3036  CA  HIS L 199      45.984  28.652  37.743  1.00 62.30           C  
ANISOU 3036  CA  HIS L 199     7815   8549   7308   3134    -87   -396       C  
ATOM   3037  C   HIS L 199      45.019  29.240  38.758  1.00 66.35           C  
ANISOU 3037  C   HIS L 199     8426   9059   7723   3443    311   -390       C  
ATOM   3038  O   HIS L 199      45.382  30.137  39.510  1.00 68.50           O  
ANISOU 3038  O   HIS L 199     9103   8957   7965   3487    587   -701       O  
ATOM   3039  CB  HIS L 199      46.998  27.757  38.440  1.00 60.13           C  
ANISOU 3039  CB  HIS L 199     7676   8296   6872   2783   -385   -650       C  
ATOM   3040  CG  HIS L 199      46.380  26.686  39.272  1.00 60.62           C  
ANISOU 3040  CG  HIS L 199     7634   8680   6718   2717   -443   -560       C  
ATOM   3041  ND1 HIS L 199      46.154  26.836  40.622  1.00 62.73           N  
ANISOU 3041  ND1 HIS L 199     8074   9010   6752   2741   -302   -708       N  
ATOM   3042  CD2 HIS L 199      45.944  25.444  38.949  1.00 59.47           C  
ANISOU 3042  CD2 HIS L 199     7275   8792   6528   2571   -587   -350       C  
ATOM   3043  CE1 HIS L 199      45.610  25.731  41.100  1.00 62.80           C  
ANISOU 3043  CE1 HIS L 199     7935   9323   6603   2660   -385   -541       C  
ATOM   3044  NE2 HIS L 199      45.469  24.871  40.106  1.00 60.90           N  
ANISOU 3044  NE2 HIS L 199     7483   9169   6487   2543   -542   -331       N  
ATOM   3045  N   GLU L 200      43.789  28.736  38.775  1.00 67.57           N  
ANISOU 3045  N   GLU L 200     8223   9652   7797   3606    382    -50       N  
ATOM   3046  CA  GLU L 200      42.749  29.284  39.635  1.00 71.75           C  
ANISOU 3046  CA  GLU L 200     8761  10246   8255   3987    830     46       C  
ATOM   3047  C   GLU L 200      42.810  30.804  39.675  1.00 76.29           C  
ANISOU 3047  C   GLU L 200     9682  10270   9035   4389   1350    -41       C  
ATOM   3048  O   GLU L 200      42.808  31.413  40.749  1.00 79.40           O  
ANISOU 3048  O   GLU L 200    10503  10342   9324   4483   1745   -364       O  
ATOM   3049  CB  GLU L 200      42.859  28.731  41.045  1.00 72.24           C  
ANISOU 3049  CB  GLU L 200     9052  10377   8018   3774    810   -261       C  
ATOM   3050  CG  GLU L 200      42.524  27.273  41.143  1.00 70.13           C  
ANISOU 3050  CG  GLU L 200     8479  10596   7571   3475    466    -83       C  
ATOM   3051  CD  GLU L 200      41.081  27.025  40.810  1.00 72.60           C  
ANISOU 3051  CD  GLU L 200     8301  11427   7856   3671    612    382       C  
ATOM   3052  OE1 GLU L 200      40.213  27.390  41.636  1.00 75.69           O  
ANISOU 3052  OE1 GLU L 200     8645  11975   8139   3971    982    472       O  
ATOM   3053  OE2 GLU L 200      40.826  26.468  39.717  1.00 71.64           O  
ANISOU 3053  OE2 GLU L 200     7827  11612   7782   3482    373    661       O  
ATOM   3054  N   GLY L 201      42.855  31.416  38.493  1.00 77.03           N  
ANISOU 3054  N   GLY L 201     9635  10233   9401   4601   1403    250       N  
ATOM   3055  CA  GLY L 201      42.768  32.871  38.363  1.00 81.55           C  
ANISOU 3055  CA  GLY L 201    10524  10224  10238   5071   2000    312       C  
ATOM   3056  C   GLY L 201      43.991  33.571  38.913  1.00 81.85           C  
ANISOU 3056  C   GLY L 201    11281   9549  10269   4744   2127   -329       C  
ATOM   3057  O   GLY L 201      43.945  34.737  39.259  1.00 86.98           O  
ANISOU 3057  O   GLY L 201    12423   9576  11050   5007   2750   -482       O  
ATOM   3058  N   SER L 202      45.102  32.856  38.966  1.00 77.46           N  
ANISOU 3058  N   SER L 202    10785   9099   9548   4144   1572   -679       N  
ATOM   3059  CA  SER L 202      46.282  33.346  39.643  1.00 78.47           C  
ANISOU 3059  CA  SER L 202    11479   8801   9535   3684   1592  -1271       C  
ATOM   3060  C   SER L 202      47.489  32.887  38.852  1.00 74.24           C  
ANISOU 3060  C   SER L 202    10795   8368   9043   3259   1041  -1321       C  
ATOM   3061  O   SER L 202      47.576  31.708  38.454  1.00 70.22           O  
ANISOU 3061  O   SER L 202     9860   8335   8487   3140    562  -1123       O  
ATOM   3062  CB  SER L 202      46.322  32.783  41.063  1.00 79.27           C  
ANISOU 3062  CB  SER L 202    11737   9158   9223   3384   1515  -1623       C  
ATOM   3063  OG  SER L 202      47.130  33.587  41.894  1.00 83.66           O  
ANISOU 3063  OG  SER L 202    12905   9327   9556   2968   1746  -2193       O  
ATOM   3064  N   THR L 203      48.422  33.806  38.615  1.00 75.88           N  
ANISOU 3064  N   THR L 203    11383   8107   9340   3014   1167  -1588       N  
ATOM   3065  CA  THR L 203      49.491  33.569  37.634  1.00 72.00           C  
ANISOU 3065  CA  THR L 203    10707   7688   8963   2719    748  -1539       C  
ATOM   3066  C   THR L 203      50.870  33.459  38.250  1.00 71.50           C  
ANISOU 3066  C   THR L 203    10823   7709   8636   2079    453  -1965       C  
ATOM   3067  O   THR L 203      51.266  34.294  39.051  1.00 76.26           O  
ANISOU 3067  O   THR L 203    11912   8015   9050   1745    724  -2384       O  
ATOM   3068  CB  THR L 203      49.551  34.719  36.601  1.00 74.77           C  
ANISOU 3068  CB  THR L 203    11232   7524   9652   2923   1088  -1369       C  
ATOM   3069  OG1 THR L 203      48.452  34.612  35.696  1.00 74.27           O  
ANISOU 3069  OG1 THR L 203    10766   7645   9808   3482   1185   -789       O  
ATOM   3070  CG2 THR L 203      50.850  34.672  35.802  1.00 72.68           C  
ANISOU 3070  CG2 THR L 203    10896   7278   9443   2503    728  -1443       C  
ATOM   3071  N   VAL L 204      51.608  32.436  37.854  1.00 67.27           N  
ANISOU 3071  N   VAL L 204     9892   7605   8064   1888    -61  -1836       N  
ATOM   3072  CA  VAL L 204      53.031  32.341  38.204  1.00 68.49           C  
ANISOU 3072  CA  VAL L 204    10050   7968   8005   1339   -368  -2071       C  
ATOM   3073  C   VAL L 204      53.905  32.259  36.959  1.00 66.02           C  
ANISOU 3073  C   VAL L 204     9491   7667   7927   1265   -587  -1895       C  
ATOM   3074  O   VAL L 204      53.650  31.455  36.034  1.00 62.33           O  
ANISOU 3074  O   VAL L 204     8682   7347   7652   1548   -744  -1574       O  
ATOM   3075  CB  VAL L 204      53.368  31.168  39.188  1.00 67.65           C  
ANISOU 3075  CB  VAL L 204     9684   8453   7566   1168   -730  -2043       C  
ATOM   3076  CG1 VAL L 204      52.439  29.981  38.986  1.00 64.14           C  
ANISOU 3076  CG1 VAL L 204     8932   8207   7230   1591   -824  -1700       C  
ATOM   3077  CG2 VAL L 204      54.827  30.751  39.049  1.00 67.17           C  
ANISOU 3077  CG2 VAL L 204     9338   8778   7408    805  -1117  -1984       C  
ATOM   3078  N   GLU L 205      54.943  33.091  36.969  1.00 69.00           N  
ANISOU 3078  N   GLU L 205    10069   7914   8234    807   -567  -2138       N  
ATOM   3079  CA  GLU L 205      55.733  33.389  35.784  1.00 68.16           C  
ANISOU 3079  CA  GLU L 205     9831   7710   8358    708   -645  -2012       C  
ATOM   3080  C   GLU L 205      57.220  33.122  35.980  1.00 69.29           C  
ANISOU 3080  C   GLU L 205     9722   8314   8290    190   -994  -2079       C  
ATOM   3081  O   GLU L 205      57.807  33.516  36.981  1.00 73.61           O  
ANISOU 3081  O   GLU L 205    10426   9057   8486   -336  -1035  -2367       O  
ATOM   3082  CB  GLU L 205      55.482  34.844  35.342  1.00 71.66           C  
ANISOU 3082  CB  GLU L 205    10754   7475   9000    691   -178  -2133       C  
ATOM   3083  CG  GLU L 205      56.721  35.656  34.940  1.00 75.11           C  
ANISOU 3083  CG  GLU L 205    11335   7771   9433    137   -176  -2300       C  
ATOM   3084  CD  GLU L 205      56.365  36.943  34.193  1.00 79.18           C  
ANISOU 3084  CD  GLU L 205    12294   7533  10258    270    334  -2258       C  
ATOM   3085  OE1 GLU L 205      56.487  38.055  34.767  1.00 84.45           O  
ANISOU 3085  OE1 GLU L 205    13576   7664  10847    -97    764  -2623       O  
ATOM   3086  OE2 GLU L 205      55.942  36.834  33.020  1.00 76.99           O  
ANISOU 3086  OE2 GLU L 205    11773   7197  10283    731    347  -1837       O  
ATOM   3087  N   LYS L 206      57.821  32.437  35.018  1.00 66.14           N  
ANISOU 3087  N   LYS L 206     8908   8156   8068    321  -1221  -1789       N  
ATOM   3088  CA  LYS L 206      59.264  32.233  35.011  1.00 68.01           C  
ANISOU 3088  CA  LYS L 206     8807   8868   8165    -72  -1496  -1734       C  
ATOM   3089  C   LYS L 206      59.826  32.704  33.677  1.00 67.53           C  
ANISOU 3089  C   LYS L 206     8676   8614   8369   -112  -1430  -1627       C  
ATOM   3090  O   LYS L 206      59.133  32.675  32.658  1.00 64.71           O  
ANISOU 3090  O   LYS L 206     8368   7928   8292    276  -1278  -1475       O  
ATOM   3091  CB  LYS L 206      59.619  30.766  35.259  1.00 65.76           C  
ANISOU 3091  CB  LYS L 206     8030   9135   7821    187  -1772  -1413       C  
ATOM   3092  CG  LYS L 206      59.463  30.340  36.696  1.00 68.03           C  
ANISOU 3092  CG  LYS L 206     8294   9800   7753     81  -1905  -1452       C  
ATOM   3093  CD  LYS L 206      60.707  30.705  37.496  1.00 73.67           C  
ANISOU 3093  CD  LYS L 206     8793  11138   8060   -545  -2139  -1500       C  
ATOM   3094  CE  LYS L 206      60.512  30.503  38.988  1.00 76.76           C  
ANISOU 3094  CE  LYS L 206     9218  11966   7982   -783  -2261  -1583       C  
ATOM   3095  NZ  LYS L 206      60.097  29.119  39.319  1.00 74.34           N  
ANISOU 3095  NZ  LYS L 206     8621  11892   7734   -226  -2361  -1182       N  
ATOM   3096  N   THR L 207      61.073  33.155  33.682  1.00 70.26           N  
ANISOU 3096  N   THR L 207     8873   9245   8576   -632  -1550  -1679       N  
ATOM   3097  CA  THR L 207      61.612  33.808  32.508  1.00 70.80           C  
ANISOU 3097  CA  THR L 207     8943   9097   8859   -764  -1441  -1615       C  
ATOM   3098  C   THR L 207      63.104  33.539  32.278  1.00 73.50           C  
ANISOU 3098  C   THR L 207     8768  10070   9090  -1109  -1686  -1440       C  
ATOM   3099  O   THR L 207      63.900  33.470  33.224  1.00 77.56           O  
ANISOU 3099  O   THR L 207     9041  11170   9260  -1557  -1908  -1473       O  
ATOM   3100  CB  THR L 207      61.251  35.332  32.455  1.00 74.10           C  
ANISOU 3100  CB  THR L 207     9993   8829   9334  -1083  -1072  -1908       C  
ATOM   3101  OG1 THR L 207      62.426  36.092  32.185  1.00 77.70           O  
ANISOU 3101  OG1 THR L 207    10434   9387   9701  -1728  -1082  -1997       O  
ATOM   3102  CG2 THR L 207      60.586  35.819  33.755  1.00 76.92           C  
ANISOU 3102  CG2 THR L 207    10837   8936   9454  -1272   -886  -2275       C  
ATOM   3103  N   VAL L 208      63.480  33.363  31.012  1.00 71.84           N  
ANISOU 3103  N   VAL L 208     8332   9831   9132   -900  -1638  -1207       N  
ATOM   3104  CA  VAL L 208      64.877  33.067  30.663  1.00 73.95           C  
ANISOU 3104  CA  VAL L 208     8047  10712   9339  -1120  -1801   -969       C  
ATOM   3105  C   VAL L 208      65.445  33.990  29.593  1.00 75.59           C  
ANISOU 3105  C   VAL L 208     8318  10724   9677  -1439  -1656   -969       C  
ATOM   3106  O   VAL L 208      64.713  34.519  28.759  1.00 73.87           O  
ANISOU 3106  O   VAL L 208     8477   9902   9686  -1254  -1421  -1011       O  
ATOM   3107  CB  VAL L 208      65.016  31.652  30.143  1.00 70.98           C  
ANISOU 3107  CB  VAL L 208     7234  10608   9126   -497  -1825   -616       C  
ATOM   3108  CG1 VAL L 208      64.710  30.682  31.251  1.00 70.22           C  
ANISOU 3108  CG1 VAL L 208     7000  10790   8889   -229  -1962   -520       C  
ATOM   3109  CG2 VAL L 208      64.080  31.441  28.963  1.00 66.33           C  
ANISOU 3109  CG2 VAL L 208     6913   9473   8818    -55  -1596   -613       C  
ATOM   3110  N   ALA L 209      66.761  34.156  29.600  1.00 80.08           N  
ANISOU 3110  N   ALA L 209     8456  11887  10084  -1910  -1796   -847       N  
ATOM   3111  CA  ALA L 209      67.418  35.023  28.624  1.00 82.35           C  
ANISOU 3111  CA  ALA L 209     8763  12062  10464  -2292  -1661   -822       C  
ATOM   3112  C   ALA L 209      68.551  34.303  27.886  1.00 82.96           C  
ANISOU 3112  C   ALA L 209     8129  12803  10591  -2136  -1733   -424       C  
ATOM   3113  O   ALA L 209      69.095  33.322  28.375  1.00 83.58           O  
ANISOU 3113  O   ALA L 209     7655  13535  10568  -1896  -1899   -155       O  
ATOM   3114  CB  ALA L 209      67.930  36.300  29.306  1.00 88.53           C  
ANISOU 3114  CB  ALA L 209     9838  12836  10963  -3253  -1656  -1137       C  
ATOM   3115  N   PRO L 210      68.872  34.768  26.678  1.00 83.25           N  
ANISOU 3115  N   PRO L 210     8179  12655  10798  -2200  -1551   -334       N  
ATOM   3116  CA  PRO L 210      69.969  34.238  25.864  1.00 84.77           C  
ANISOU 3116  CA  PRO L 210     7741  13428  11038  -2080  -1524     24       C  
ATOM   3117  C   PRO L 210      71.320  34.525  26.507  1.00 91.77           C  
ANISOU 3117  C   PRO L 210     8050  15190  11630  -2736  -1742    180       C  
ATOM   3118  O   PRO L 210      71.451  35.515  27.237  1.00 95.56           O  
ANISOU 3118  O   PRO L 210     8782  15672  11855  -3528  -1856    -90       O  
ATOM   3119  CB  PRO L 210      69.841  35.025  24.562  1.00 84.37           C  
ANISOU 3119  CB  PRO L 210     7997  12897  11164  -2189  -1277      4       C  
ATOM   3120  CG  PRO L 210      68.385  35.468  24.527  1.00 80.45           C  
ANISOU 3120  CG  PRO L 210     8215  11553  10798  -1970  -1151   -233       C  
ATOM   3121  CD  PRO L 210      68.032  35.734  25.947  1.00 81.53           C  
ANISOU 3121  CD  PRO L 210     8598  11612  10766  -2237  -1297   -503       C  
ATOM   3122  N   THR L 211      72.319  33.678  26.240  1.00 94.49           N  
ANISOU 3122  N   THR L 211     7625  16300  11977  -2442  -1757    625       N  
ATOM   3123  CA  THR L 211      73.691  33.880  26.764  1.00101.82           C  
ANISOU 3123  CA  THR L 211     7801  18299  12589  -3039  -1980    926       C  
ATOM   3124  C   THR L 211      73.820  35.115  27.659  1.00106.62           C  
ANISOU 3124  C   THR L 211     8701  19003  12808  -4155  -2205    561       C  
ATOM   3125  O   THR L 211      74.910  35.440  28.138  1.00114.12           O  
ANISOU 3125  O   THR L 211     9071  20905  13385  -4891  -2428    747       O  
ATOM   3126  CB  THR L 211      74.780  33.925  25.628  1.00105.13           C  
ANISOU 3126  CB  THR L 211     7669  19171  13106  -3061  -1797   1284       C  
ATOM   3127  OG1 THR L 211      75.755  34.936  25.921  1.00111.89           O  
ANISOU 3127  OG1 THR L 211     8218  20674  13622  -4113  -1989   1300       O  
ATOM   3128  CG2 THR L 211      74.160  34.244  24.275  1.00100.65           C  
ANISOU 3128  CG2 THR L 211     7676  17715  12851  -2808  -1464   1080       C  
TER    3129      THR L 211                                                      
ATOM   3130  N   PRO A  34       8.939  41.917  26.646  1.00 82.54           N  
ANISOU 3130  N   PRO A  34    12541   8825   9998   1212    -39  -1685       N  
ATOM   3131  CA  PRO A  34       8.003  40.804  26.503  1.00 80.29           C  
ANISOU 3131  CA  PRO A  34    12155   8896   9454   1289    287  -1384       C  
ATOM   3132  C   PRO A  34       6.537  41.252  26.703  1.00 82.11           C  
ANISOU 3132  C   PRO A  34    12425   9112   9662   1530    855  -1368       C  
ATOM   3133  O   PRO A  34       6.247  42.056  27.598  1.00 86.18           O  
ANISOU 3133  O   PRO A  34    13339   9403  10004   1681   1020  -1666       O  
ATOM   3134  CB  PRO A  34       8.445  39.816  27.603  1.00 81.46           C  
ANISOU 3134  CB  PRO A  34    12742   9185   9023   1277     68  -1492       C  
ATOM   3135  CG  PRO A  34       9.804  40.253  28.021  1.00 83.83           C  
ANISOU 3135  CG  PRO A  34    13216   9266   9371   1162   -536  -1804       C  
ATOM   3136  CD  PRO A  34       9.833  41.736  27.801  1.00 86.17           C  
ANISOU 3136  CD  PRO A  34    13447   9208  10087   1168   -495  -2032       C  
ATOM   3137  N   PHE A  35       5.628  40.708  25.881  1.00 79.65           N  
ANISOU 3137  N   PHE A  35    11687   9018   9557   1573   1135  -1054       N  
ATOM   3138  CA  PHE A  35       4.247  41.214  25.769  1.00 81.11           C  
ANISOU 3138  CA  PHE A  35    11690   9159   9968   1806   1615  -1013       C  
ATOM   3139  C   PHE A  35       3.254  40.172  25.250  1.00 79.16           C  
ANISOU 3139  C   PHE A  35    11022   9202   9852   1822   1862   -742       C  
ATOM   3140  O   PHE A  35       2.144  40.520  24.870  1.00 80.80           O  
ANISOU 3140  O   PHE A  35    10894   9389  10416   2003   2150   -676       O  
ATOM   3141  CB  PHE A  35       4.240  42.389  24.804  1.00 81.09           C  
ANISOU 3141  CB  PHE A  35    11426   8931  10454   1887   1531   -959       C  
ATOM   3142  CG  PHE A  35       4.749  42.031  23.437  1.00 77.12           C  
ANISOU 3142  CG  PHE A  35    10554   8551  10198   1752   1229   -658       C  
ATOM   3143  CD1 PHE A  35       4.673  42.941  22.380  1.00 77.74           C  
ANISOU 3143  CD1 PHE A  35    10434   8437  10665   1859   1189   -503       C  
ATOM   3144  CD2 PHE A  35       5.293  40.772  23.207  1.00 73.74           C  
ANISOU 3144  CD2 PHE A  35    10039   8399   9578   1546   1022   -517       C  
ATOM   3145  CE1 PHE A  35       5.159  42.600  21.112  1.00 75.29           C  
ANISOU 3145  CE1 PHE A  35     9905   8217  10486   1764    968   -216       C  
ATOM   3146  CE2 PHE A  35       5.772  40.406  21.957  1.00 71.27           C  
ANISOU 3146  CE2 PHE A  35     9453   8182   9446   1436    802   -262       C  
ATOM   3147  CZ  PHE A  35       5.708  41.311  20.900  1.00 72.30           C  
ANISOU 3147  CZ  PHE A  35     9443   8129   9900   1546    786   -111       C  
ATOM   3148  N   LEU A  36       3.663  38.909  25.194  1.00 76.24           N  
ANISOU 3148  N   LEU A  36    10629   9072   9267   1638   1714   -601       N  
ATOM   3149  CA  LEU A  36       2.776  37.843  24.742  1.00 75.06           C  
ANISOU 3149  CA  LEU A  36    10083   9156   9281   1610   1928   -389       C  
ATOM   3150  C   LEU A  36       2.553  36.802  25.844  1.00 77.02           C  
ANISOU 3150  C   LEU A  36    10648   9480   9137   1565   2262   -403       C  
ATOM   3151  O   LEU A  36       3.504  36.413  26.519  1.00 77.36           O  
ANISOU 3151  O   LEU A  36    11154   9519   8720   1480   2050   -460       O  
ATOM   3152  CB  LEU A  36       3.380  37.158  23.524  1.00 70.64           C  
ANISOU 3152  CB  LEU A  36     9203   8777   8861   1431   1516   -174       C  
ATOM   3153  CG  LEU A  36       2.400  36.638  22.462  1.00 69.86           C  
ANISOU 3153  CG  LEU A  36     8552   8845   9148   1459   1551      2       C  
ATOM   3154  CD1 LEU A  36       2.935  35.347  21.865  1.00 66.50           C  
ANISOU 3154  CD1 LEU A  36     8012   8623   8631   1239   1311    154       C  
ATOM   3155  CD2 LEU A  36       0.996  36.425  23.011  1.00 73.35           C  
ANISOU 3155  CD2 LEU A  36     8769   9289   9813   1581   2043    -49       C  
ATOM   3156  N   LYS A  37       1.310  36.363  26.032  1.00 78.98           N  
ANISOU 3156  N   LYS A  37    10650   9759   9599   1638   2786   -347       N  
ATOM   3157  CA  LYS A  37       1.013  35.302  26.997  1.00 81.37           C  
ANISOU 3157  CA  LYS A  37    11254  10084   9580   1592   3229   -299       C  
ATOM   3158  C   LYS A  37       0.675  33.986  26.307  1.00 79.55           C  
ANISOU 3158  C   LYS A  37    10554  10035   9636   1402   3239    -80       C  
ATOM   3159  O   LYS A  37      -0.170  33.944  25.414  1.00 79.50           O  
ANISOU 3159  O   LYS A  37     9898  10092  10218   1399   3267    -30       O  
ATOM   3160  CB  LYS A  37      -0.131  35.691  27.931  1.00 87.42           C  
ANISOU 3160  CB  LYS A  37    12158  10664  10392   1795   3996   -415       C  
ATOM   3161  CG  LYS A  37       0.279  35.831  29.385  1.00 91.66           C  
ANISOU 3161  CG  LYS A  37    13608  11038  10179   1911   4261   -565       C  
ATOM   3162  CD  LYS A  37      -0.932  35.928  30.296  1.00 98.08           C  
ANISOU 3162  CD  LYS A  37    14587  11655  11023   2099   5202   -627       C  
ATOM   3163  CE  LYS A  37      -0.522  35.920  31.760  1.00102.79           C  
ANISOU 3163  CE  LYS A  37    16251  12086  10718   2244   5487   -755       C  
ATOM   3164  NZ  LYS A  37      -1.536  36.599  32.597  1.00109.37           N  
ANISOU 3164  NZ  LYS A  37    17350  12654  11553   2500   6354   -925       N  
ATOM   3165  N   CYS A  38       1.331  32.909  26.722  1.00 78.47           N  
ANISOU 3165  N   CYS A  38    10756   9958   9100   1262   3175     32       N  
ATOM   3166  CA  CYS A  38       1.058  31.602  26.149  1.00 76.90           C  
ANISOU 3166  CA  CYS A  38    10175   9879   9164   1069   3216    216       C  
ATOM   3167  C   CYS A  38       0.676  30.557  27.209  1.00 80.76           C  
ANISOU 3167  C   CYS A  38    11031  10261   9393   1037   3823    326       C  
ATOM   3168  O   CYS A  38       1.118  30.633  28.358  1.00 83.57           O  
ANISOU 3168  O   CYS A  38    12128  10504   9121   1156   3986    304       O  
ATOM   3169  CB  CYS A  38       2.274  31.108  25.355  1.00 72.15           C  
ANISOU 3169  CB  CYS A  38     9549   9421   8443    909   2553    306       C  
ATOM   3170  SG  CYS A  38       2.962  32.248  24.130  1.00 67.37           S  
ANISOU 3170  SG  CYS A  38     8670   8875   8053    935   1926    238       S  
ATOM   3171  N   TYR A  39      -0.136  29.583  26.801  1.00 81.38           N  
ANISOU 3171  N   TYR A  39    10621  10346   9955    885   4139    439       N  
ATOM   3172  CA  TYR A  39      -0.442  28.409  27.613  1.00 84.91           C  
ANISOU 3172  CA  TYR A  39    11360  10651  10253    805   4733    602       C  
ATOM   3173  C   TYR A  39       0.827  27.601  27.648  1.00 81.97           C  
ANISOU 3173  C   TYR A  39    11425  10349   9369    718   4252    743       C  
ATOM   3174  O   TYR A  39       1.597  27.651  26.700  1.00 77.58           O  
ANISOU 3174  O   TYR A  39    10613   9962   8901    631   3573    720       O  
ATOM   3175  CB  TYR A  39      -1.505  27.573  26.901  1.00 86.35           C  
ANISOU 3175  CB  TYR A  39    10755  10806  11249    605   5033    643       C  
ATOM   3176  CG  TYR A  39      -2.703  27.180  27.746  1.00 93.51           C  
ANISOU 3176  CG  TYR A  39    11608  11446  12476    607   6041    686       C  
ATOM   3177  CD1 TYR A  39      -3.640  28.140  28.146  1.00 97.44           C  
ANISOU 3177  CD1 TYR A  39    11930  11819  13272    791   6557    542       C  
ATOM   3178  CD2 TYR A  39      -2.930  25.839  28.101  1.00 96.42           C  
ANISOU 3178  CD2 TYR A  39    12059  11638  12937    423   6543    876       C  
ATOM   3179  CE1 TYR A  39      -4.745  27.789  28.903  1.00104.68           C  
ANISOU 3179  CE1 TYR A  39    12755  12450  14570    793   7586    580       C  
ATOM   3180  CE2 TYR A  39      -4.046  25.472  28.867  1.00103.11           C  
ANISOU 3180  CE2 TYR A  39    12839  12176  14162    406   7592    935       C  
ATOM   3181  CZ  TYR A  39      -4.943  26.452  29.265  1.00107.63           C  
ANISOU 3181  CZ  TYR A  39    13226  12635  15033    590   8127    783       C  
ATOM   3182  OH  TYR A  39      -6.048  26.116  30.031  1.00115.72           O  
ANISOU 3182  OH  TYR A  39    14160  13312  16497    579   9272    839       O  
ATOM   3183  N   CYS A  40       1.071  26.847  28.712  1.00 85.12           N  
ANISOU 3183  N   CYS A  40    12501  10596   9243    765   4608    902       N  
ATOM   3184  CA  CYS A  40       2.177  25.891  28.658  1.00 82.80           C  
ANISOU 3184  CA  CYS A  40    12512  10344   8606    690   4154   1065       C  
ATOM   3185  C   CYS A  40       1.960  24.620  29.444  1.00 86.88           C  
ANISOU 3185  C   CYS A  40    13471  10645   8895    668   4724   1325       C  
ATOM   3186  O   CYS A  40       1.197  24.592  30.406  1.00 92.97           O  
ANISOU 3186  O   CYS A  40    14639  11204   9481    776   5501   1395       O  
ATOM   3187  CB  CYS A  40       3.522  26.528  29.009  1.00 81.04           C  
ANISOU 3187  CB  CYS A  40    12822  10195   7773    848   3453    971       C  
ATOM   3188  SG  CYS A  40       3.726  26.979  30.687  1.00 88.56           S  
ANISOU 3188  SG  CYS A  40    14861  10966   7821   1159   3693    930       S  
ATOM   3189  N   SER A  41       2.634  23.563  29.007  1.00 84.44           N  
ANISOU 3189  N   SER A  41    13109  10355   8619    536   4390   1481       N  
ATOM   3190  CA  SER A  41       2.571  22.268  29.678  1.00 88.82           C  
ANISOU 3190  CA  SER A  41    14117  10665   8964    520   4868   1770       C  
ATOM   3191  C   SER A  41       3.739  21.407  29.230  1.00 85.56           C  
ANISOU 3191  C   SER A  41    13760  10305   8443    468   4228   1891       C  
ATOM   3192  O   SER A  41       4.345  21.657  28.183  1.00 79.81           O  
ANISOU 3192  O   SER A  41    12527   9790   8007    364   3571   1746       O  
ATOM   3193  CB  SER A  41       1.249  21.544  29.382  1.00 91.60           C  
ANISOU 3193  CB  SER A  41    13908  10834  10061    283   5659   1834       C  
ATOM   3194  OG  SER A  41       1.133  21.280  27.994  1.00 87.50           O  
ANISOU 3194  OG  SER A  41    12504  10472  10270     25   5242   1698       O  
ATOM   3195  N   GLY A  42       4.040  20.378  30.017  1.00 89.42           N  
ANISOU 3195  N   GLY A  42    14888  10563   8524    560   4473   2175       N  
ATOM   3196  CA  GLY A  42       5.178  19.517  29.728  1.00 87.54           C  
ANISOU 3196  CA  GLY A  42    14762  10322   8175    568   3895   2312       C  
ATOM   3197  C   GLY A  42       6.444  20.134  30.283  1.00 87.60           C  
ANISOU 3197  C   GLY A  42    15324  10437   7523    855   3133   2248       C  
ATOM   3198  O   GLY A  42       7.056  19.586  31.198  1.00 91.78           O  
ANISOU 3198  O   GLY A  42    16620  10802   7450   1099   3020   2456       O  
ATOM   3199  N   HIS A  43       6.823  21.298  29.755  1.00 83.86           N  
ANISOU 3199  N   HIS A  43    14478  10206   7181    841   2598   1953       N  
ATOM   3200  CA  HIS A  43       7.964  22.033  30.302  1.00 84.55           C  
ANISOU 3200  CA  HIS A  43    15006  10358   6760   1082   1870   1815       C  
ATOM   3201  C   HIS A  43       7.721  23.547  30.473  1.00 84.23           C  
ANISOU 3201  C   HIS A  43    14953  10429   6621   1145   1786   1509       C  
ATOM   3202  O   HIS A  43       8.056  24.352  29.583  1.00 80.31           O  
ANISOU 3202  O   HIS A  43    13871  10096   6547   1022   1376   1291       O  
ATOM   3203  CB  HIS A  43       9.211  21.758  29.453  1.00 80.79           C  
ANISOU 3203  CB  HIS A  43    14102   9982   6613   1013   1108   1772       C  
ATOM   3204  CG  HIS A  43      10.502  21.984  30.185  1.00 84.14           C  
ANISOU 3204  CG  HIS A  43    15020  10369   6581   1280    349   1707       C  
ATOM   3205  ND1 HIS A  43      10.731  21.522  31.473  1.00 90.63           N  
ANISOU 3205  ND1 HIS A  43    16754  11014   6668   1590    300   1872       N  
ATOM   3206  CD2 HIS A  43      11.635  22.626  29.809  1.00 81.69           C  
ANISOU 3206  CD2 HIS A  43    14409  10147   6484   1293   -413   1482       C  
ATOM   3207  CE1 HIS A  43      11.956  21.860  31.849  1.00 91.99           C  
ANISOU 3207  CE1 HIS A  43    17138  11190   6626   1795   -566   1721       C  
ATOM   3208  NE2 HIS A  43      12.523  22.533  30.858  1.00 87.33           N  
ANISOU 3208  NE2 HIS A  43    15771  10748   6664   1597   -984   1474       N  
ATOM   3209  N   CYS A  44       7.134  23.926  31.607  1.00 89.04           N  
ANISOU 3209  N   CYS A  44    16250  10911   6668   1348   2230   1503       N  
ATOM   3210  CA  CYS A  44       6.879  25.333  31.895  1.00 90.00           C  
ANISOU 3210  CA  CYS A  44    16461  11082   6655   1441   2206   1200       C  
ATOM   3211  C   CYS A  44       8.044  25.928  32.692  1.00 92.64           C  
ANISOU 3211  C   CYS A  44    17441  11391   6367   1693   1427   1001       C  
ATOM   3212  O   CYS A  44       8.513  25.307  33.653  1.00 97.75           O  
ANISOU 3212  O   CYS A  44    18890  11907   6342   1933   1271   1139       O  
ATOM   3213  CB  CYS A  44       5.555  25.505  32.673  1.00 95.22           C  
ANISOU 3213  CB  CYS A  44    17502  11585   7091   1534   3182   1247       C  
ATOM   3214  SG  CYS A  44       4.033  25.216  31.692  1.00 93.59           S  
ANISOU 3214  SG  CYS A  44    16320  11392   7849   1229   4027   1328       S  
ATOM   3215  N   PRO A  45       8.521  27.127  32.294  1.00 90.07           N  
ANISOU 3215  N   PRO A  45    16778  11158   6284   1649    906    669       N  
ATOM   3216  CA  PRO A  45       9.463  27.901  33.114  1.00 94.04           C  
ANISOU 3216  CA  PRO A  45    17856  11592   6281   1869    198    376       C  
ATOM   3217  C   PRO A  45       8.897  28.133  34.498  1.00101.16           C  
ANISOU 3217  C   PRO A  45    19798  12331   6307   2171    605    325       C  
ATOM   3218  O   PRO A  45       7.719  28.476  34.652  1.00102.56           O  
ANISOU 3218  O   PRO A  45    20026  12457   6484   2168   1439    336       O  
ATOM   3219  CB  PRO A  45       9.555  29.262  32.396  1.00 90.78           C  
ANISOU 3219  CB  PRO A  45    16844  11239   6409   1719    -37     46       C  
ATOM   3220  CG  PRO A  45       8.563  29.214  31.262  1.00 85.72           C  
ANISOU 3220  CG  PRO A  45    15411  10712   6445   1480    571    197       C  
ATOM   3221  CD  PRO A  45       8.294  27.759  30.986  1.00 84.62           C  
ANISOU 3221  CD  PRO A  45    15146  10612   6393   1391    890    557       C  
ATOM   3222  N   ASP A  46       9.738  27.979  35.502  1.00106.60           N  
ANISOU 3222  N   ASP A  46    21329  12916   6257   2456      7    249       N  
ATOM   3223  CA  ASP A  46       9.254  28.077  36.856  1.00114.50           C  
ANISOU 3223  CA  ASP A  46    23498  13737   6271   2794    399    230       C  
ATOM   3224  C   ASP A  46       8.975  29.508  37.278  1.00117.37           C  
ANISOU 3224  C   ASP A  46    24123  14035   6436   2881    423   -213       C  
ATOM   3225  O   ASP A  46       8.894  29.807  38.478  1.00125.27           O  
ANISOU 3225  O   ASP A  46    26218  14870   6510   3211    475   -366       O  
ATOM   3226  CB  ASP A  46      10.187  27.343  37.813  1.00120.61           C  
ANISOU 3226  CB  ASP A  46    25207  14403   6216   3132   -271    328       C  
ATOM   3227  CG  ASP A  46      10.286  25.876  37.478  1.00119.10           C  
ANISOU 3227  CG  ASP A  46    24847  14209   6195   3080   -102    813       C  
ATOM   3228  OD1 ASP A  46       9.925  25.512  36.328  1.00112.65           O  
ANISOU 3228  OD1 ASP A  46    23025  13514   6262   2728    261    973       O  
ATOM   3229  OD2 ASP A  46      10.706  25.087  38.342  1.00124.85           O  
ANISOU 3229  OD2 ASP A  46    26472  14795   6171   3404   -336   1028       O  
ATOM   3230  N   ASP A  47       8.823  30.403  36.301  1.00111.71           N  
ANISOU 3230  N   ASP A  47    22475  13419   6550   2611    399   -421       N  
ATOM   3231  CA  ASP A  47       8.158  31.667  36.609  1.00114.16           C  
ANISOU 3231  CA  ASP A  47    22958  13626   6790   2677    777   -753       C  
ATOM   3232  C   ASP A  47       6.755  31.645  36.042  1.00111.54           C  
ANISOU 3232  C   ASP A  47    22069  13323   6987   2530   1860   -544       C  
ATOM   3233  O   ASP A  47       6.279  32.606  35.440  1.00108.96           O  
ANISOU 3233  O   ASP A  47    21156  13008   7237   2414   2047   -727       O  
ATOM   3234  CB  ASP A  47       8.948  32.923  36.231  1.00112.50           C  
ANISOU 3234  CB  ASP A  47    22359  13399   6988   2578    -11  -1208       C  
ATOM   3235  CG  ASP A  47       9.160  33.070  34.780  1.00104.77           C  
ANISOU 3235  CG  ASP A  47    20189  12567   7050   2235   -180  -1127       C  
ATOM   3236  OD1 ASP A  47       8.827  34.134  34.203  1.00103.01           O  
ANISOU 3236  OD1 ASP A  47    19477  12308   7353   2119    -36  -1320       O  
ATOM   3237  OD2 ASP A  47       9.712  32.122  34.230  1.00101.23           O  
ANISOU 3237  OD2 ASP A  47    19356  12245   6862   2110   -474   -870       O  
ATOM   3238  N   ALA A  48       6.100  30.512  36.269  1.00113.07           N  
ANISOU 3238  N   ALA A  48    22460  13491   7009   2553   2560   -154       N  
ATOM   3239  CA  ALA A  48       4.745  30.295  35.824  1.00111.62           C  
ANISOU 3239  CA  ALA A  48    21735  13294   7382   2416   3595     49       C  
ATOM   3240  C   ALA A  48       3.748  30.597  36.936  1.00119.27           C  
ANISOU 3240  C   ALA A  48    23504  14020   7794   2674   4573      9       C  
ATOM   3241  O   ALA A  48       3.843  30.046  38.045  1.00126.11           O  
ANISOU 3241  O   ALA A  48    25444  14718   7754   2931   4825    138       O  
ATOM   3242  CB  ALA A  48       4.580  28.844  35.352  1.00109.04           C  
ANISOU 3242  CB  ALA A  48    21051  13021   7357   2239   3857    477       C  
ATOM   3243  N   ILE A  49       2.826  31.512  36.656  1.00118.98           N  
ANISOU 3243  N   ILE A  49    23002  13937   8268   2644   5119   -172       N  
ATOM   3244  CA  ILE A  49       1.502  31.386  37.226  1.00124.68           C  
ANISOU 3244  CA  ILE A  49    23944  14442   8988   2755   6383    -55       C  
ATOM   3245  C   ILE A  49       0.965  30.327  36.279  1.00120.16           C  
ANISOU 3245  C   ILE A  49    22412  13972   9270   2449   6698    293       C  
ATOM   3246  O   ILE A  49       1.092  30.465  35.066  1.00113.39           O  
ANISOU 3246  O   ILE A  49    20544  13330   9210   2202   6182    261       O  
ATOM   3247  CB  ILE A  49       0.712  32.707  37.192  1.00126.19           C  
ANISOU 3247  CB  ILE A  49    23861  14528   9556   2844   6819   -378       C  
ATOM   3248  CG1 ILE A  49      -0.697  32.522  37.794  1.00132.93           C  
ANISOU 3248  CG1 ILE A  49    24866  15115  10525   2964   8240   -253       C  
ATOM   3249  CG2 ILE A  49       0.745  33.339  35.803  1.00118.21           C  
ANISOU 3249  CG2 ILE A  49    21625  13726   9562   2600   6257   -490       C  
ATOM   3250  CD1 ILE A  49      -1.717  31.872  36.929  1.00130.31           C  
ANISOU 3250  CD1 ILE A  49    23404  14814  11292   2704   8854      2       C  
ATOM   3251  N   ASN A  50       0.444  29.240  36.834  1.00124.86           N  
ANISOU 3251  N   ASN A  50    23397  14388   9656   2471   7503    622       N  
ATOM   3252  CA  ASN A  50       0.492  27.948  36.138  1.00121.17           C  
ANISOU 3252  CA  ASN A  50    22364  13997   9678   2200   7454    959       C  
ATOM   3253  C   ASN A  50      -0.107  27.881  34.741  1.00114.61           C  
ANISOU 3253  C   ASN A  50    20139  13333  10074   1862   7408    947       C  
ATOM   3254  O   ASN A  50      -1.223  28.344  34.490  1.00115.73           O  
ANISOU 3254  O   ASN A  50    19677  13399  10896   1818   8052    849       O  
ATOM   3255  CB  ASN A  50      -0.001  26.796  37.040  1.00128.77           C  
ANISOU 3255  CB  ASN A  50    24051  14654  10222   2286   8430   1332       C  
ATOM   3256  CG  ASN A  50      -1.485  26.901  37.375  1.00134.78           C  
ANISOU 3256  CG  ASN A  50    24614  15134  11462   2285   9811   1371       C  
ATOM   3257  OD1 ASN A  50      -1.976  26.235  38.291  1.00141.96           O  
ANISOU 3257  OD1 ASN A  50    26264  15713  11959   2412  10812   1636       O  
ATOM   3258  ND2 ASN A  50      -2.209  27.742  36.629  1.00132.23           N  
ANISOU 3258  ND2 ASN A  50    23285  14908  12050   2161   9900   1117       N  
ATOM   3259  N   ASN A  51       0.668  27.301  33.837  1.00108.49           N  
ANISOU 3259  N   ASN A  51    18886  12773   9564   1653   6605   1033       N  
ATOM   3260  CA  ASN A  51       0.262  27.168  32.455  1.00102.98           C  
ANISOU 3260  CA  ASN A  51    16995  12246   9885   1359   6397   1009       C  
ATOM   3261  C   ASN A  51       0.218  28.519  31.766  1.00 99.32           C  
ANISOU 3261  C   ASN A  51    15994  11946   9797   1385   5947    706       C  
ATOM   3262  O   ASN A  51      -0.621  28.771  30.904  1.00 98.22           O  
ANISOU 3262  O   ASN A  51    14977  11860  10483   1264   6092    638       O  
ATOM   3263  CB  ASN A  51      -1.073  26.430  32.379  1.00106.67           C  
ANISOU 3263  CB  ASN A  51    16958  12519  11053   1203   7385   1161       C  
ATOM   3264  CG  ASN A  51      -1.078  25.170  33.232  1.00111.36           C  
ANISOU 3264  CG  ASN A  51    18238  12853  11220   1211   8005   1492       C  
ATOM   3265  OD1 ASN A  51      -0.597  24.114  32.818  1.00109.17           O  
ANISOU 3265  OD1 ASN A  51    17848  12602  11030   1041   7702   1685       O  
ATOM   3266  ND2 ASN A  51      -1.599  25.286  34.437  1.00118.54           N  
ANISOU 3266  ND2 ASN A  51    19931  13479  11631   1433   8907   1568       N  
ATOM   3267  N   THR A  52       1.131  29.396  32.157  1.00 98.33           N  
ANISOU 3267  N   THR A  52    16413  11868   9082   1558   5370    516       N  
ATOM   3268  CA  THR A  52       1.297  30.646  31.447  1.00 94.91           C  
ANISOU 3268  CA  THR A  52    15517  11549   8994   1567   4865    257       C  
ATOM   3269  C   THR A  52       2.734  31.094  31.550  1.00 92.65           C  
ANISOU 3269  C   THR A  52    15657  11338   8208   1615   3959    115       C  
ATOM   3270  O   THR A  52       3.301  31.121  32.638  1.00 96.92           O  
ANISOU 3270  O   THR A  52    17080  11768   7975   1798   3861     46       O  
ATOM   3271  CB  THR A  52       0.419  31.745  32.013  1.00 99.35           C  
ANISOU 3271  CB  THR A  52    16217  11941   9591   1775   5453     45       C  
ATOM   3272  OG1 THR A  52      -0.327  31.227  33.109  1.00106.51           O  
ANISOU 3272  OG1 THR A  52    17688  12622  10157   1902   6399    155       O  
ATOM   3273  CG2 THR A  52      -0.525  32.244  30.955  1.00 97.55           C  
ANISOU 3273  CG2 THR A  52    14979  11770  10318   1697   5588     -6       C  
ATOM   3274  N   CYS A  53       3.327  31.411  30.408  1.00 86.66           N  
ANISOU 3274  N   CYS A  53    14279  10741   7906   1460   3297     69       N  
ATOM   3275  CA  CYS A  53       4.625  32.050  30.372  1.00 84.84           C  
ANISOU 3275  CA  CYS A  53    14261  10531   7444   1476   2491   -114       C  
ATOM   3276  C   CYS A  53       4.465  33.325  29.569  1.00 82.54           C  
ANISOU 3276  C   CYS A  53    13460  10235   7666   1459   2328   -298       C  
ATOM   3277  O   CYS A  53       3.632  33.396  28.679  1.00 80.49           O  
ANISOU 3277  O   CYS A  53    12555  10044   7983   1393   2581   -207       O  
ATOM   3278  CB  CYS A  53       5.681  31.130  29.735  1.00 80.82           C  
ANISOU 3278  CB  CYS A  53    13531  10157   7020   1304   1896     49       C  
ATOM   3279  SG  CYS A  53       5.246  30.283  28.168  1.00 75.09           S  
ANISOU 3279  SG  CYS A  53    11870   9614   7048   1042   1962    292       S  
ATOM   3280  N   ILE A  54       5.229  34.349  29.903  1.00 83.79           N  
ANISOU 3280  N   ILE A  54    13928  10279   7631   1537   1897   -566       N  
ATOM   3281  CA  ILE A  54       5.229  35.551  29.086  1.00 81.92           C  
ANISOU 3281  CA  ILE A  54    13239   9983   7903   1513   1718   -706       C  
ATOM   3282  C   ILE A  54       6.391  35.433  28.125  1.00 77.46           C  
ANISOU 3282  C   ILE A  54    12300   9496   7634   1318   1065   -645       C  
ATOM   3283  O   ILE A  54       7.442  34.909  28.485  1.00 77.45           O  
ANISOU 3283  O   ILE A  54    12558   9508   7363   1262    617   -669       O  
ATOM   3284  CB  ILE A  54       5.349  36.848  29.936  1.00 86.53           C  
ANISOU 3284  CB  ILE A  54    14329  10319   8231   1689   1692  -1069       C  
ATOM   3285  CG1 ILE A  54       6.395  36.679  31.039  1.00 90.04           C  
ANISOU 3285  CG1 ILE A  54    15527  10679   8005   1748   1229  -1275       C  
ATOM   3286  CG2 ILE A  54       4.004  37.210  30.572  1.00 90.81           C  
ANISOU 3286  CG2 ILE A  54    15066  10747   8692   1898   2485  -1128       C  
ATOM   3287  CD1 ILE A  54       6.473  37.849  31.999  1.00 95.50           C  
ANISOU 3287  CD1 ILE A  54    16833  11105   8347   1933   1189  -1691       C  
ATOM   3288  N   THR A  55       6.192  35.859  26.883  1.00 74.12           N  
ANISOU 3288  N   THR A  55    11277   9112   7773   1238   1033   -547       N  
ATOM   3289  CA  THR A  55       7.312  35.951  25.961  1.00 70.70           C  
ANISOU 3289  CA  THR A  55    10548   8680   7635   1074    530   -504       C  
ATOM   3290  C   THR A  55       7.174  37.112  24.986  1.00 70.11           C  
ANISOU 3290  C   THR A  55    10124   8479   8034   1089    527   -514       C  
ATOM   3291  O   THR A  55       6.108  37.732  24.853  1.00 71.10           O  
ANISOU 3291  O   THR A  55    10136   8561   8317   1237    870   -514       O  
ATOM   3292  CB  THR A  55       7.507  34.687  25.177  1.00 66.75           C  
ANISOU 3292  CB  THR A  55     9728   8389   7244    926    453   -238       C  
ATOM   3293  OG1 THR A  55       8.776  34.736  24.523  1.00 64.77           O  
ANISOU 3293  OG1 THR A  55     9302   8090   7218    785     12   -231       O  
ATOM   3294  CG2 THR A  55       6.436  34.572  24.145  1.00 64.83           C  
ANISOU 3294  CG2 THR A  55     9019   8266   7346    932    743    -60       C  
ATOM   3295  N   ASN A  56       8.280  37.396  24.312  1.00 68.62           N  
ANISOU 3295  N   ASN A  56     9772   8197   8106    952    164   -509       N  
ATOM   3296  CA  ASN A  56       8.325  38.417  23.281  1.00 68.08           C  
ANISOU 3296  CA  ASN A  56     9434   7961   8472    958    180   -452       C  
ATOM   3297  C   ASN A  56       8.327  37.765  21.905  1.00 64.39           C  
ANISOU 3297  C   ASN A  56     8595   7659   8211    882    179   -144       C  
ATOM   3298  O   ASN A  56       8.295  38.458  20.884  1.00 63.78           O  
ANISOU 3298  O   ASN A  56     8351   7463   8420    923    223    -18       O  
ATOM   3299  CB  ASN A  56       9.576  39.293  23.453  1.00 70.07           C  
ANISOU 3299  CB  ASN A  56     9777   7903   8944    848   -127   -669       C  
ATOM   3300  CG  ASN A  56      10.870  38.467  23.660  1.00 69.88           C  
ANISOU 3300  CG  ASN A  56     9733   7917   8903    663   -525   -714       C  
ATOM   3301  OD1 ASN A  56      10.867  37.224  23.674  1.00 67.25           O  
ANISOU 3301  OD1 ASN A  56     9370   7837   8345    630   -562   -559       O  
ATOM   3302  ND2 ASN A  56      11.977  39.176  23.865  1.00 72.39           N  
ANISOU 3302  ND2 ASN A  56    10042   7940   9523    550   -834   -950       N  
ATOM   3303  N   GLY A  57       8.355  36.430  21.892  1.00 62.28           N  
ANISOU 3303  N   GLY A  57     8267   7635   7762    794    141    -26       N  
ATOM   3304  CA  GLY A  57       8.484  35.647  20.653  1.00 59.29           C  
ANISOU 3304  CA  GLY A  57     7607   7405   7515    708    103    213       C  
ATOM   3305  C   GLY A  57       7.163  35.104  20.125  1.00 58.78           C  
ANISOU 3305  C   GLY A  57     7336   7548   7450    797    293    347       C  
ATOM   3306  O   GLY A  57       6.326  35.865  19.628  1.00 59.81           O  
ANISOU 3306  O   GLY A  57     7344   7637   7743    957    390    380       O  
ATOM   3307  N   HIS A  58       6.971  33.792  20.216  1.00 57.33           N  
ANISOU 3307  N   HIS A  58     7087   7554   7141    703    319    412       N  
ATOM   3308  CA  HIS A  58       5.716  33.174  19.803  1.00 57.44           C  
ANISOU 3308  CA  HIS A  58     6841   7731   7252    747    474    481       C  
ATOM   3309  C   HIS A  58       5.229  32.158  20.806  1.00 58.39           C  
ANISOU 3309  C   HIS A  58     7028   7929   7229    684    709    454       C  
ATOM   3310  O   HIS A  58       5.945  31.747  21.714  1.00 58.47           O  
ANISOU 3310  O   HIS A  58     7347   7899   6968    623    696    426       O  
ATOM   3311  CB  HIS A  58       5.882  32.460  18.475  1.00 55.37           C  
ANISOU 3311  CB  HIS A  58     6382   7581   7077    672    294    614       C  
ATOM   3312  CG  HIS A  58       5.999  33.376  17.308  1.00 55.78           C  
ANISOU 3312  CG  HIS A  58     6402   7555   7237    792    154    696       C  
ATOM   3313  ND1 HIS A  58       7.101  34.175  17.097  1.00 55.51           N  
ANISOU 3313  ND1 HIS A  58     6548   7331   7214    777    104    729       N  
ATOM   3314  CD2 HIS A  58       5.156  33.608  16.277  1.00 57.14           C  
ANISOU 3314  CD2 HIS A  58     6413   7780   7517    947     51    762       C  
ATOM   3315  CE1 HIS A  58       6.917  34.885  15.997  1.00 56.89           C  
ANISOU 3315  CE1 HIS A  58     6730   7426   7459    923     60    850       C  
ATOM   3316  NE2 HIS A  58       5.745  34.559  15.481  1.00 57.73           N  
ANISOU 3316  NE2 HIS A  58     6661   7694   7582   1051    -19    873       N  
ATOM   3317  N   CYS A  59       3.994  31.741  20.627  1.00 59.89           N  
ANISOU 3317  N   CYS A  59     6926   8199   7630    712    921    466       N  
ATOM   3318  CA  CYS A  59       3.467  30.611  21.372  1.00 61.74           C  
ANISOU 3318  CA  CYS A  59     7169   8464   7826    617   1234    484       C  
ATOM   3319  C   CYS A  59       3.606  29.381  20.498  1.00 59.61           C  
ANISOU 3319  C   CYS A  59     6676   8300   7673    445   1068    571       C  
ATOM   3320  O   CYS A  59       3.552  29.497  19.269  1.00 58.89           O  
ANISOU 3320  O   CYS A  59     6336   8282   7759    453    785    580       O  
ATOM   3321  CB  CYS A  59       1.984  30.811  21.690  1.00 64.98           C  
ANISOU 3321  CB  CYS A  59     7289   8839   8560    716   1639    417       C  
ATOM   3322  SG  CYS A  59       1.633  32.277  22.614  1.00 67.78           S  
ANISOU 3322  SG  CYS A  59     7878   9035   8839    953   1911    284       S  
ATOM   3323  N   PHE A  60       3.744  28.215  21.116  1.00 59.27           N  
ANISOU 3323  N   PHE A  60     6774   8237   7508    316   1256    634       N  
ATOM   3324  CA  PHE A  60       3.837  26.987  20.356  1.00 58.21           C  
ANISOU 3324  CA  PHE A  60     6445   8156   7516    147   1143    689       C  
ATOM   3325  C   PHE A  60       3.137  25.829  21.056  1.00 60.77           C  
ANISOU 3325  C   PHE A  60     6738   8396   7956     27   1566    734       C  
ATOM   3326  O   PHE A  60       2.954  25.828  22.269  1.00 62.62           O  
ANISOU 3326  O   PHE A  60     7277   8523   7991     81   1951    780       O  
ATOM   3327  CB  PHE A  60       5.315  26.617  20.091  1.00 55.61           C  
ANISOU 3327  CB  PHE A  60     6370   7828   6932     88    833    765       C  
ATOM   3328  CG  PHE A  60       6.003  25.980  21.270  1.00 56.01           C  
ANISOU 3328  CG  PHE A  60     6821   7784   6675     73    942    849       C  
ATOM   3329  CD1 PHE A  60       5.825  24.630  21.555  1.00 57.37           C  
ANISOU 3329  CD1 PHE A  60     7037   7895   6865    -38   1151    948       C  
ATOM   3330  CD2 PHE A  60       6.780  26.744  22.122  1.00 56.74           C  
ANISOU 3330  CD2 PHE A  60     7276   7819   6465    192    812    819       C  
ATOM   3331  CE1 PHE A  60       6.422  24.049  22.665  1.00 59.24           C  
ANISOU 3331  CE1 PHE A  60     7724   8020   6765      7   1235   1064       C  
ATOM   3332  CE2 PHE A  60       7.389  26.177  23.230  1.00 59.13           C  
ANISOU 3332  CE2 PHE A  60     8012   8030   6423    236    814    885       C  
ATOM   3333  CZ  PHE A  60       7.211  24.817  23.505  1.00 59.89           C  
ANISOU 3333  CZ  PHE A  60     8202   8072   6481    163   1030   1034       C  
ATOM   3334  N   ALA A  61       2.734  24.850  20.260  1.00 61.39           N  
ANISOU 3334  N   ALA A  61     6483   8489   8355   -131   1516    711       N  
ATOM   3335  CA  ALA A  61       2.329  23.536  20.742  1.00 64.23           C  
ANISOU 3335  CA  ALA A  61     6821   8710   8874   -301   1889    772       C  
ATOM   3336  C   ALA A  61       3.092  22.553  19.870  1.00 62.17           C  
ANISOU 3336  C   ALA A  61     6554   8465   8603   -438   1569    789       C  
ATOM   3337  O   ALA A  61       3.378  22.843  18.703  1.00 61.14           O  
ANISOU 3337  O   ALA A  61     6265   8456   8509   -421   1146    697       O  
ATOM   3338  CB  ALA A  61       0.835  23.334  20.585  1.00 67.60           C  
ANISOU 3338  CB  ALA A  61     6706   9070   9908   -384   2186    646       C  
ATOM   3339  N   ILE A  62       3.438  21.405  20.428  1.00 62.76           N  
ANISOU 3339  N   ILE A  62     6858   8387   8600   -544   1800    918       N  
ATOM   3340  CA  ILE A  62       4.237  20.434  19.713  1.00 60.70           C  
ANISOU 3340  CA  ILE A  62     6636   8096   8332   -651   1553    936       C  
ATOM   3341  C   ILE A  62       3.745  19.015  20.024  1.00 63.87           C  
ANISOU 3341  C   ILE A  62     6989   8264   9013   -841   1933    991       C  
ATOM   3342  O   ILE A  62       3.182  18.766  21.092  1.00 67.03           O  
ANISOU 3342  O   ILE A  62     7531   8501   9436   -852   2436   1113       O  
ATOM   3343  CB  ILE A  62       5.725  20.622  20.073  1.00 58.04           C  
ANISOU 3343  CB  ILE A  62     6732   7774   7546   -520   1316   1074       C  
ATOM   3344  CG1 ILE A  62       6.627  19.852  19.132  1.00 55.93           C  
ANISOU 3344  CG1 ILE A  62     6438   7484   7328   -589   1049   1063       C  
ATOM   3345  CG2 ILE A  62       6.007  20.226  21.500  1.00 59.99           C  
ANISOU 3345  CG2 ILE A  62     7438   7866   7489   -440   1595   1268       C  
ATOM   3346  CD1 ILE A  62       8.063  19.940  19.558  1.00 54.20           C  
ANISOU 3346  CD1 ILE A  62     6539   7231   6824   -461    840   1187       C  
ATOM   3347  N   ILE A  63       3.878  18.114  19.055  1.00 63.24           N  
ANISOU 3347  N   ILE A  63     6723   8136   9171   -993   1744    886       N  
ATOM   3348  CA  ILE A  63       3.668  16.689  19.281  1.00 65.75           C  
ANISOU 3348  CA  ILE A  63     7049   8175   9756  -1181   2069    942       C  
ATOM   3349  C   ILE A  63       4.911  15.936  18.801  1.00 64.02           C  
ANISOU 3349  C   ILE A  63     7082   7901   9342  -1169   1812   1000       C  
ATOM   3350  O   ILE A  63       5.503  16.288  17.774  1.00 61.81           O  
ANISOU 3350  O   ILE A  63     6741   7782   8962  -1119   1395    869       O  
ATOM   3351  CB  ILE A  63       2.431  16.169  18.546  1.00 68.84           C  
ANISOU 3351  CB  ILE A  63     6883   8475  10799  -1416   2122    676       C  
ATOM   3352  CG1 ILE A  63       2.164  14.710  18.901  1.00 72.78           C  
ANISOU 3352  CG1 ILE A  63     7387   8609  11658  -1641   2555    736       C  
ATOM   3353  CG2 ILE A  63       2.629  16.272  17.069  1.00 67.19           C  
ANISOU 3353  CG2 ILE A  63     6468   8432  10630  -1428   1537    412       C  
ATOM   3354  CD1 ILE A  63       0.806  14.193  18.466  1.00 77.01           C  
ANISOU 3354  CD1 ILE A  63     7307   8968  12984  -1910   2711    458       C  
ATOM   3355  N   GLU A  64       5.357  14.944  19.563  1.00 65.20           N  
ANISOU 3355  N   GLU A  64     7554   7797   9420  -1178   2093   1220       N  
ATOM   3356  CA  GLU A  64       6.432  14.094  19.074  1.00 64.25           C  
ANISOU 3356  CA  GLU A  64     7595   7566   9249  -1166   1895   1256       C  
ATOM   3357  C   GLU A  64       6.287  12.664  19.541  1.00 67.88           C  
ANISOU 3357  C   GLU A  64     8204   7649   9939  -1287   2289   1399       C  
ATOM   3358  O   GLU A  64       5.712  12.401  20.592  1.00 71.40           O  
ANISOU 3358  O   GLU A  64     8830   7904  10392  -1300   2750   1595       O  
ATOM   3359  CB  GLU A  64       7.811  14.661  19.402  1.00 61.73           C  
ANISOU 3359  CB  GLU A  64     7599   7364   8493   -913   1589   1412       C  
ATOM   3360  CG  GLU A  64       7.999  15.146  20.818  1.00 63.71           C  
ANISOU 3360  CG  GLU A  64     8241   7604   8360   -721   1703   1647       C  
ATOM   3361  CD  GLU A  64       9.278  15.988  20.987  1.00 61.90           C  
ANISOU 3361  CD  GLU A  64     8186   7525   7806   -494   1256   1683       C  
ATOM   3362  OE1 GLU A  64       9.240  16.992  21.737  1.00 61.68           O  
ANISOU 3362  OE1 GLU A  64     8334   7615   7485   -361   1191   1704       O  
ATOM   3363  OE2 GLU A  64      10.322  15.651  20.375  1.00 60.83           O  
ANISOU 3363  OE2 GLU A  64     7993   7358   7763   -454    990   1665       O  
ATOM   3364  N   GLU A  65       6.753  11.722  18.735  1.00 67.83           N  
ANISOU 3364  N   GLU A  65     8148   7490  10137  -1375   2174   1298       N  
ATOM   3365  CA  GLU A  65       6.677  10.338  19.155  1.00 71.56           C  
ANISOU 3365  CA  GLU A  65     8783   7546  10861  -1482   2559   1443       C  
ATOM   3366  C   GLU A  65       8.073   9.784  19.268  1.00 70.17           C  
ANISOU 3366  C   GLU A  65     8959   7246  10455  -1274   2390   1638       C  
ATOM   3367  O   GLU A  65       8.913  10.066  18.431  1.00 68.26           O  
ANISOU 3367  O   GLU A  65     8635   7167  10134  -1188   2013   1499       O  
ATOM   3368  CB  GLU A  65       5.778   9.514  18.229  1.00 74.04           C  
ANISOU 3368  CB  GLU A  65     8696   7666  11771  -1804   2658   1119       C  
ATOM   3369  CG  GLU A  65       6.466   8.775  17.099  1.00 73.64           C  
ANISOU 3369  CG  GLU A  65     8627   7519  11832  -1846   2385    904       C  
ATOM   3370  CD  GLU A  65       5.533   7.786  16.415  1.00 77.63           C  
ANISOU 3370  CD  GLU A  65     8818   7731  12947  -2176   2513    576       C  
ATOM   3371  OE1 GLU A  65       4.438   7.524  16.952  1.00 81.06           O  
ANISOU 3371  OE1 GLU A  65     9027   7967  13803  -2384   2890    575       O  
ATOM   3372  OE2 GLU A  65       5.896   7.267  15.343  1.00 78.00           O  
ANISOU 3372  OE2 GLU A  65     8841   7715  13081  -2231   2259    297       O  
ATOM   3373  N   ASP A  66       8.348   9.071  20.347  1.00 72.88           N  
ANISOU 3373  N   ASP A  66     9716   7292  10683  -1153   2680   1982       N  
ATOM   3374  CA  ASP A  66       9.699   8.594  20.585  1.00 73.42           C  
ANISOU 3374  CA  ASP A  66    10106   7231  10558   -889   2453   2193       C  
ATOM   3375  C   ASP A  66       9.958   7.266  19.897  1.00 75.10           C  
ANISOU 3375  C   ASP A  66    10261   7091  11183  -1001   2576   2122       C  
ATOM   3376  O   ASP A  66       9.205   6.882  19.023  1.00 75.47           O  
ANISOU 3376  O   ASP A  66     9986   7067  11622  -1291   2705   1824       O  
ATOM   3377  CB  ASP A  66      10.040   8.537  22.080  1.00 76.55           C  
ANISOU 3377  CB  ASP A  66    11076   7484  10523   -605   2563   2610       C  
ATOM   3378  CG  ASP A  66       9.163   7.592  22.854  1.00 81.64           C  
ANISOU 3378  CG  ASP A  66    12015   7718  11285   -708   3209   2854       C  
ATOM   3379  OD1 ASP A  66       8.908   6.446  22.409  1.00 84.29           O  
ANISOU 3379  OD1 ASP A  66    12247   7698  12082   -900   3504   2823       O  
ATOM   3380  OD2 ASP A  66       8.769   8.003  23.952  1.00 84.02           O  
ANISOU 3380  OD2 ASP A  66    12704   8016  11204   -581   3455   3084       O  
ATOM   3381  N   ASP A  67      11.014   6.566  20.298  1.00 76.64           N  
ANISOU 3381  N   ASP A  67    10768   7040  11310   -753   2500   2373       N  
ATOM   3382  CA  ASP A  67      11.459   5.416  19.545  1.00 78.10           C  
ANISOU 3382  CA  ASP A  67    10889   6900  11888   -807   2569   2274       C  
ATOM   3383  C   ASP A  67      10.581   4.187  19.722  1.00 83.22           C  
ANISOU 3383  C   ASP A  67    11630   7071  12921  -1043   3106   2329       C  
ATOM   3384  O   ASP A  67      10.674   3.239  18.940  1.00 84.97           O  
ANISOU 3384  O   ASP A  67    11738   7000  13548  -1178   3206   2139       O  
ATOM   3385  CB  ASP A  67      12.940   5.157  19.777  1.00 78.47           C  
ANISOU 3385  CB  ASP A  67    11129   6845  11842   -440   2265   2480       C  
ATOM   3386  CG  ASP A  67      13.801   6.236  19.159  1.00 74.69           C  
ANISOU 3386  CG  ASP A  67    10375   6758  11247   -317   1806   2289       C  
ATOM   3387  OD1 ASP A  67      13.410   6.753  18.089  1.00 71.33           O  
ANISOU 3387  OD1 ASP A  67     9631   6567  10903   -532   1778   1947       O  
ATOM   3388  OD2 ASP A  67      14.844   6.593  19.750  1.00 75.09           O  
ANISOU 3388  OD2 ASP A  67    10535   6860  11136     -1   1464   2478       O  
ATOM   3389  N   GLN A  68       9.720   4.213  20.737  1.00 85.94           N  
ANISOU 3389  N   GLN A  68    12186   7299  13167  -1099   3499   2570       N  
ATOM   3390  CA  GLN A  68       8.573   3.315  20.781  1.00 90.53           C  
ANISOU 3390  CA  GLN A  68    12687   7464  14246  -1434   4092   2532       C  
ATOM   3391  C   GLN A  68       7.370   4.183  20.438  1.00 89.53           C  
ANISOU 3391  C   GLN A  68    12095   7644  14279  -1724   4139   2216       C  
ATOM   3392  O   GLN A  68       7.484   5.407  20.400  1.00 85.18           O  
ANISOU 3392  O   GLN A  68    11439   7572  13355  -1604   3782   2141       O  
ATOM   3393  CB  GLN A  68       8.415   2.652  22.153  1.00 95.95           C  
ANISOU 3393  CB  GLN A  68    13959   7712  14787  -1289   4641   3054       C  
ATOM   3394  CG  GLN A  68       9.236   3.295  23.275  1.00 95.95           C  
ANISOU 3394  CG  GLN A  68    14524   7901  14031   -824   4384   3462       C  
ATOM   3395  CD  GLN A  68      10.703   2.836  23.276  1.00 96.10           C  
ANISOU 3395  CD  GLN A  68    14809   7822  13883   -446   3919   3638       C  
ATOM   3396  OE1 GLN A  68      11.476   3.164  22.374  1.00 91.96           O  
ANISOU 3396  OE1 GLN A  68    13922   7561  13458   -406   3414   3359       O  
ATOM   3397  NE2 GLN A  68      11.085   2.080  24.301  1.00101.17           N  
ANISOU 3397  NE2 GLN A  68    16098   8054  14289   -142   4114   4117       N  
ATOM   3398  N   GLY A  69       6.218   3.563  20.187  1.00 93.78           N  
ANISOU 3398  N   GLY A  69    12317   7876  15437  -2100   4563   2018       N  
ATOM   3399  CA  GLY A  69       5.055   4.303  19.668  1.00 93.08           C  
ANISOU 3399  CA  GLY A  69    11654   8050  15662  -2378   4508   1636       C  
ATOM   3400  C   GLY A  69       4.557   5.458  20.521  1.00 91.64           C  
ANISOU 3400  C   GLY A  69    11508   8170  15141  -2262   4645   1813       C  
ATOM   3401  O   GLY A  69       3.541   6.076  20.204  1.00 91.87           O  
ANISOU 3401  O   GLY A  69    11043   8376  15488  -2459   4648   1533       O  
ATOM   3402  N   GLU A  70       5.281   5.762  21.593  1.00 90.63           N  
ANISOU 3402  N   GLU A  70    11973   8090  14374  -1917   4714   2251       N  
ATOM   3403  CA  GLU A  70       4.792   6.709  22.584  1.00 91.10           C  
ANISOU 3403  CA  GLU A  70    12213   8327  14072  -1789   4969   2447       C  
ATOM   3404  C   GLU A  70       4.816   8.154  22.091  1.00 85.87           C  
ANISOU 3404  C   GLU A  70    11235   8242  13151  -1709   4421   2181       C  
ATOM   3405  O   GLU A  70       5.850   8.649  21.642  1.00 81.05           O  
ANISOU 3405  O   GLU A  70    10694   7931  12170  -1510   3820   2124       O  
ATOM   3406  CB  GLU A  70       5.571   6.571  23.897  1.00 93.18           C  
ANISOU 3406  CB  GLU A  70    13310   8441  13655  -1409   5137   2965       C  
ATOM   3407  CG  GLU A  70       4.723   6.881  25.104  1.00 97.94           C  
ANISOU 3407  CG  GLU A  70    14259   8899  14055  -1364   5823   3234       C  
ATOM   3408  CD  GLU A  70       3.409   6.085  25.081  1.00104.39           C  
ANISOU 3408  CD  GLU A  70    14727   9257  15679  -1760   6652   3183       C  
ATOM   3409  OE1 GLU A  70       3.456   4.840  24.907  1.00107.12           O  
ANISOU 3409  OE1 GLU A  70    15118   9137  16445  -1910   6932   3268       O  
ATOM   3410  OE2 GLU A  70       2.324   6.702  25.223  1.00106.20           O  
ANISOU 3410  OE2 GLU A  70    14590   9556  16203  -1927   7035   3039       O  
ATOM   3411  N   THR A  71       3.674   8.828  22.180  1.00 87.18           N  
ANISOU 3411  N   THR A  71    11035   8517  13572  -1858   4672   2028       N  
ATOM   3412  CA  THR A  71       3.574  10.224  21.748  1.00 83.09           C  
ANISOU 3412  CA  THR A  71    10225   8493  12851  -1770   4208   1796       C  
ATOM   3413  C   THR A  71       3.376  11.141  22.954  1.00 83.82           C  
ANISOU 3413  C   THR A  71    10684   8690  12473  -1549   4505   2036       C  
ATOM   3414  O   THR A  71       2.561  10.854  23.817  1.00 88.99           O  
ANISOU 3414  O   THR A  71    11468   9059  13286  -1614   5215   2209       O  
ATOM   3415  CB  THR A  71       2.400  10.429  20.758  1.00 83.86           C  
ANISOU 3415  CB  THR A  71     9551   8669  13642  -2064   4122   1363       C  
ATOM   3416  OG1 THR A  71       1.164  10.269  21.451  1.00 89.44           O  
ANISOU 3416  OG1 THR A  71    10038   9106  14841  -2238   4823   1406       O  
ATOM   3417  CG2 THR A  71       2.450   9.410  19.619  1.00 84.36           C  
ANISOU 3417  CG2 THR A  71     9318   8558  14178  -2301   3871   1075       C  
ATOM   3418  N   THR A  72       4.138  12.226  23.023  1.00 79.82           N  
ANISOU 3418  N   THR A  72    10374   8551  11400  -1289   4008   2036       N  
ATOM   3419  CA  THR A  72       4.007  13.195  24.115  1.00 80.90           C  
ANISOU 3419  CA  THR A  72    10897   8800  11042  -1062   4204   2193       C  
ATOM   3420  C   THR A  72       3.702  14.613  23.610  1.00 77.76           C  
ANISOU 3420  C   THR A  72    10107   8793  10646  -1027   3849   1917       C  
ATOM   3421  O   THR A  72       4.287  15.072  22.616  1.00 73.13           O  
ANISOU 3421  O   THR A  72     9258   8471  10060  -1016   3234   1720       O  
ATOM   3422  CB  THR A  72       5.284  13.250  24.972  1.00 80.06           C  
ANISOU 3422  CB  THR A  72    11535   8701  10184   -722   3926   2473       C  
ATOM   3423  OG1 THR A  72       6.421  13.393  24.123  1.00 75.69           O  
ANISOU 3423  OG1 THR A  72    10825   8359   9574   -658   3206   2344       O  
ATOM   3424  CG2 THR A  72       5.448  11.980  25.783  1.00 85.31           C  
ANISOU 3424  CG2 THR A  72    12752   8934  10727   -662   4373   2832       C  
ATOM   3425  N   LEU A  73       2.786  15.305  24.288  1.00 80.29           N  
ANISOU 3425  N   LEU A  73    10416   9111  10978   -993   4292   1918       N  
ATOM   3426  CA  LEU A  73       2.468  16.685  23.925  1.00 77.41           C  
ANISOU 3426  CA  LEU A  73     9731   9068  10616   -916   4003   1688       C  
ATOM   3427  C   LEU A  73       3.222  17.678  24.792  1.00 76.21           C  
ANISOU 3427  C   LEU A  73    10165   9062   9728   -609   3819   1796       C  
ATOM   3428  O   LEU A  73       3.576  17.379  25.944  1.00 78.80           O  
ANISOU 3428  O   LEU A  73    11173   9215   9552   -441   4098   2047       O  
ATOM   3429  CB  LEU A  73       0.973  16.981  24.055  1.00 81.45           C  
ANISOU 3429  CB  LEU A  73     9769   9485  11692  -1043   4559   1560       C  
ATOM   3430  CG  LEU A  73      -0.078  16.218  23.250  1.00 84.27           C  
ANISOU 3430  CG  LEU A  73     9384   9677  12958  -1363   4739   1352       C  
ATOM   3431  CD1 LEU A  73       0.547  15.527  22.045  1.00 80.87           C  
ANISOU 3431  CD1 LEU A  73     8745   9316  12664  -1501   4121   1205       C  
ATOM   3432  CD2 LEU A  73      -0.820  15.219  24.158  1.00 91.22           C  
ANISOU 3432  CD2 LEU A  73    10375  10100  14183  -1518   5670   1551       C  
ATOM   3433  N   ALA A  74       3.440  18.870  24.237  1.00 72.76           N  
ANISOU 3433  N   ALA A  74     9497   8917   9229   -525   3337   1596       N  
ATOM   3434  CA  ALA A  74       3.971  19.993  25.006  1.00 72.33           C  
ANISOU 3434  CA  ALA A  74     9894   8980   8607   -268   3167   1608       C  
ATOM   3435  C   ALA A  74       3.562  21.315  24.389  1.00 69.65           C  
ANISOU 3435  C   ALA A  74     9138   8863   8462   -237   2936   1370       C  
ATOM   3436  O   ALA A  74       3.330  21.394  23.201  1.00 67.00           O  
ANISOU 3436  O   ALA A  74     8257   8652   8546   -360   2655   1218       O  
ATOM   3437  CB  ALA A  74       5.496  19.902  25.140  1.00 69.92           C  
ANISOU 3437  CB  ALA A  74    10004   8724   7837   -123   2596   1694       C  
ATOM   3438  N   SER A  75       3.434  22.335  25.225  1.00 71.42           N  
ANISOU 3438  N   SER A  75     9679   9104   8354    -47   3073   1338       N  
ATOM   3439  CA  SER A  75       3.248  23.697  24.758  1.00 69.64           C  
ANISOU 3439  CA  SER A  75     9175   9049   8237     37   2816   1137       C  
ATOM   3440  C   SER A  75       3.928  24.708  25.692  1.00 70.13           C  
ANISOU 3440  C   SER A  75     9812   9115   7720    267   2664   1100       C  
ATOM   3441  O   SER A  75       4.261  24.392  26.835  1.00 72.75           O  
ANISOU 3441  O   SER A  75    10783   9316   7544    391   2845   1214       O  
ATOM   3442  CB  SER A  75       1.768  24.015  24.565  1.00 71.73           C  
ANISOU 3442  CB  SER A  75     8930   9281   9044    -10   3266   1026       C  
ATOM   3443  OG  SER A  75       1.012  23.467  25.597  1.00 76.51           O  
ANISOU 3443  OG  SER A  75     9758   9659   9652    -16   4012   1139       O  
ATOM   3444  N   GLY A  76       4.151  25.914  25.181  1.00 67.74           N  
ANISOU 3444  N   GLY A  76     9317   8936   7486    336   2302    932       N  
ATOM   3445  CA  GLY A  76       4.892  26.925  25.911  1.00 68.46           C  
ANISOU 3445  CA  GLY A  76     9877   9005   7128    517   2052    829       C  
ATOM   3446  C   GLY A  76       5.353  28.075  25.038  1.00 65.35           C  
ANISOU 3446  C   GLY A  76     9181   8707   6944    528   1594    676       C  
ATOM   3447  O   GLY A  76       4.802  28.337  23.978  1.00 63.04           O  
ANISOU 3447  O   GLY A  76     8372   8497   7081    465   1570    649       O  
ATOM   3448  N   CYS A  77       6.386  28.759  25.500  1.00 65.74           N  
ANISOU 3448  N   CYS A  77     9578   8710   6691    621   1212    572       N  
ATOM   3449  CA  CYS A  77       6.861  29.971  24.856  1.00 63.53           C  
ANISOU 3449  CA  CYS A  77     9090   8432   6615    636    871    426       C  
ATOM   3450  C   CYS A  77       8.107  29.680  24.035  1.00 60.87           C  
ANISOU 3450  C   CYS A  77     8563   8124   6442    519    399    470       C  
ATOM   3451  O   CYS A  77       9.007  28.966  24.467  1.00 61.51           O  
ANISOU 3451  O   CYS A  77     8861   8174   6338    505    157    514       O  
ATOM   3452  CB  CYS A  77       7.141  31.059  25.903  1.00 66.27           C  
ANISOU 3452  CB  CYS A  77     9897   8643   6642    795    792    216       C  
ATOM   3453  SG  CYS A  77       5.655  31.677  26.765  1.00 70.20           S  
ANISOU 3453  SG  CYS A  77    10608   9056   7009    970   1454    124       S  
ATOM   3454  N   MET A  78       8.133  30.206  22.819  1.00 58.70           N  
ANISOU 3454  N   MET A  78     7892   7884   6525    460    300    475       N  
ATOM   3455  CA  MET A  78       9.292  30.116  21.971  1.00 55.85           C  
ANISOU 3455  CA  MET A  78     7358   7500   6363    363    -22    510       C  
ATOM   3456  C   MET A  78       9.882  31.509  22.024  1.00 56.62           C  
ANISOU 3456  C   MET A  78     7496   7442   6576    409   -204    357       C  
ATOM   3457  O   MET A  78       9.235  32.471  21.630  1.00 56.62           O  
ANISOU 3457  O   MET A  78     7399   7408   6705    476    -63    325       O  
ATOM   3458  CB  MET A  78       8.852  29.760  20.561  1.00 53.88           C  
ANISOU 3458  CB  MET A  78     6751   7353   6368    292     63    628       C  
ATOM   3459  CG  MET A  78       9.920  29.883  19.477  1.00 53.35           C  
ANISOU 3459  CG  MET A  78     6534   7224   6513    222   -125    675       C  
ATOM   3460  SD  MET A  78       9.308  29.282  17.842  1.00 54.17           S  
ANISOU 3460  SD  MET A  78     6394   7452   6737    188    -40    795       S  
ATOM   3461  CE  MET A  78       8.208  27.972  18.331  1.00 51.98           C  
ANISOU 3461  CE  MET A  78     6056   7310   6383    131    117    802       C  
ATOM   3462  N   LYS A  79      11.085  31.631  22.562  1.00 57.35           N  
ANISOU 3462  N   LYS A  79     7721   7405   6664    384   -535    245       N  
ATOM   3463  CA  LYS A  79      11.676  32.944  22.738  1.00 59.42           C  
ANISOU 3463  CA  LYS A  79     8010   7459   7106    396   -721     45       C  
ATOM   3464  C   LYS A  79      11.997  33.680  21.423  1.00 57.92           C  
ANISOU 3464  C   LYS A  79     7489   7156   7363    319   -641    118       C  
ATOM   3465  O   LYS A  79      12.277  33.047  20.403  1.00 56.53           O  
ANISOU 3465  O   LYS A  79     7088   7040   7350    241   -573    295       O  
ATOM   3466  CB  LYS A  79      12.902  32.855  23.654  1.00 62.10           C  
ANISOU 3466  CB  LYS A  79     8521   7663   7411    386  -1183   -142       C  
ATOM   3467  CG  LYS A  79      14.111  32.162  23.087  1.00 60.63           C  
ANISOU 3467  CG  LYS A  79     8031   7430   7574    270  -1429    -70       C  
ATOM   3468  CD  LYS A  79      15.298  32.460  23.964  1.00 63.95           C  
ANISOU 3468  CD  LYS A  79     8525   7655   8120    281  -1974   -334       C  
ATOM   3469  CE  LYS A  79      16.483  31.666  23.540  1.00 63.57           C  
ANISOU 3469  CE  LYS A  79     8134   7543   8475    201  -2222   -271       C  
ATOM   3470  NZ  LYS A  79      17.643  32.016  24.353  1.00 68.09           N  
ANISOU 3470  NZ  LYS A  79     8679   7900   9294    220  -2838   -568       N  
ATOM   3471  N   TYR A  80      11.934  35.007  21.441  1.00 58.80           N  
ANISOU 3471  N   TYR A  80     7631   7070   7640    359   -607    -10       N  
ATOM   3472  CA  TYR A  80      12.246  35.786  20.255  1.00 58.69           C  
ANISOU 3472  CA  TYR A  80     7401   6881   8019    314   -472     94       C  
ATOM   3473  C   TYR A  80      13.694  35.564  19.833  1.00 59.25           C  
ANISOU 3473  C   TYR A  80     7256   6779   8479    147   -619     93       C  
ATOM   3474  O   TYR A  80      14.599  35.699  20.638  1.00 61.66           O  
ANISOU 3474  O   TYR A  80     7551   6929   8948     75   -931   -132       O  
ATOM   3475  CB  TYR A  80      12.009  37.255  20.541  1.00 61.79           C  
ANISOU 3475  CB  TYR A  80     7904   7020   8554    387   -412    -64       C  
ATOM   3476  CG  TYR A  80      12.403  38.184  19.427  1.00 62.69           C  
ANISOU 3476  CG  TYR A  80     7876   6860   9084    356   -231     60       C  
ATOM   3477  CD1 TYR A  80      11.681  38.222  18.243  1.00 61.30           C  
ANISOU 3477  CD1 TYR A  80     7666   6764   8861    472     23    342       C  
ATOM   3478  CD2 TYR A  80      13.470  39.064  19.570  1.00 65.37           C  
ANISOU 3478  CD2 TYR A  80     8145   6820   9873    225   -315   -112       C  
ATOM   3479  CE1 TYR A  80      12.021  39.093  17.230  1.00 62.58           C  
ANISOU 3479  CE1 TYR A  80     7822   6638   9318    489    235    502       C  
ATOM   3480  CE2 TYR A  80      13.812  39.946  18.556  1.00 66.53           C  
ANISOU 3480  CE2 TYR A  80     8206   6647  10424    196    -37     39       C  
ATOM   3481  CZ  TYR A  80      13.083  39.953  17.393  1.00 65.28           C  
ANISOU 3481  CZ  TYR A  80     8112   6578  10114    345    261    371       C  
ATOM   3482  OH  TYR A  80      13.420  40.811  16.376  1.00 67.73           O  
ANISOU 3482  OH  TYR A  80     8452   6541  10739    359    577    570       O  
ATOM   3483  N   GLU A  81      13.922  35.223  18.569  1.00 57.84           N  
ANISOU 3483  N   GLU A  81     6906   6603   8467    101   -400    323       N  
ATOM   3484  CA  GLU A  81      15.254  34.811  18.133  1.00 58.39           C  
ANISOU 3484  CA  GLU A  81     6735   6511   8938    -46   -432    342       C  
ATOM   3485  C   GLU A  81      15.968  35.827  17.285  1.00 60.77           C  
ANISOU 3485  C   GLU A  81     6900   6446   9745   -124   -169    394       C  
ATOM   3486  O   GLU A  81      16.939  35.511  16.598  1.00 61.65           O  
ANISOU 3486  O   GLU A  81     6797   6394  10233   -232     -4    477       O  
ATOM   3487  CB  GLU A  81      15.204  33.482  17.392  1.00 56.47           C  
ANISOU 3487  CB  GLU A  81     6438   6486   8530    -51   -314    543       C  
ATOM   3488  CG  GLU A  81      15.100  32.295  18.324  1.00 56.02           C  
ANISOU 3488  CG  GLU A  81     6434   6655   8194    -40   -583    480       C  
ATOM   3489  CD  GLU A  81      14.790  31.006  17.624  1.00 53.60           C  
ANISOU 3489  CD  GLU A  81     6111   6551   7703    -40   -439    658       C  
ATOM   3490  OE1 GLU A  81      15.633  30.084  17.692  1.00 53.86           O  
ANISOU 3490  OE1 GLU A  81     6020   6556   7890    -94   -539    665       O  
ATOM   3491  OE2 GLU A  81      13.702  30.920  17.027  1.00 52.35           O  
ANISOU 3491  OE2 GLU A  81     6049   6557   7284     24   -261    765       O  
ATOM   3492  N   GLY A  82      15.512  37.061  17.339  1.00 62.46           N  
ANISOU 3492  N   GLY A  82     7241   6480  10010    -65    -68    351       N  
ATOM   3493  CA  GLY A  82      16.128  38.103  16.540  1.00 65.32           C  
ANISOU 3493  CA  GLY A  82     7528   6425  10866   -133    260    434       C  
ATOM   3494  C   GLY A  82      15.769  37.951  15.079  1.00 64.22           C  
ANISOU 3494  C   GLY A  82     7539   6316  10548    -25    685    799       C  
ATOM   3495  O   GLY A  82      14.608  37.783  14.723  1.00 62.36           O  
ANISOU 3495  O   GLY A  82     7528   6345   9822    167    692    944       O  
ATOM   3496  N   SER A  83      16.777  38.008  14.227  1.00 66.60           N  
ANISOU 3496  N   SER A  83     7723   6318  11264   -135   1039    931       N  
ATOM   3497  CA  SER A  83      16.558  37.902  12.794  1.00 67.01           C  
ANISOU 3497  CA  SER A  83     8040   6341  11081     -5   1482   1278       C  
ATOM   3498  C   SER A  83      16.081  36.486  12.460  1.00 63.66           C  
ANISOU 3498  C   SER A  83     7691   6353  10143     71   1343   1349       C  
ATOM   3499  O   SER A  83      15.256  36.284  11.575  1.00 63.35           O  
ANISOU 3499  O   SER A  83     7966   6481   9622    262   1433   1550       O  
ATOM   3500  CB  SER A  83      17.842  38.243  12.021  1.00 70.66           C  
ANISOU 3500  CB  SER A  83     8379   6325  12142   -151   2012   1397       C  
ATOM   3501  OG  SER A  83      18.580  37.077  11.724  1.00 69.40           O  
ANISOU 3501  OG  SER A  83     8028   6258  12084   -244   2099   1403       O  
ATOM   3502  N   ASP A  84      16.592  35.501  13.185  1.00 62.11           N  
ANISOU 3502  N   ASP A  84     7219   6318  10063    -65   1079   1169       N  
ATOM   3503  CA  ASP A  84      16.242  34.108  12.905  1.00 59.64           C  
ANISOU 3503  CA  ASP A  84     6956   6349   9354    -23    983   1220       C  
ATOM   3504  C   ASP A  84      14.850  33.777  13.367  1.00 57.34           C  
ANISOU 3504  C   ASP A  84     6808   6436   8544    103    671   1180       C  
ATOM   3505  O   ASP A  84      14.401  34.268  14.402  1.00 57.47           O  
ANISOU 3505  O   ASP A  84     6790   6503   8545    114    433   1029       O  
ATOM   3506  CB  ASP A  84      17.196  33.160  13.612  1.00 59.16           C  
ANISOU 3506  CB  ASP A  84     6570   6305   9602   -173    786   1060       C  
ATOM   3507  CG  ASP A  84      18.557  33.142  12.989  1.00 62.21           C  
ANISOU 3507  CG  ASP A  84     6723   6341  10574   -290   1147   1104       C  
ATOM   3508  OD1 ASP A  84      18.997  32.069  12.566  1.00 62.84           O  
ANISOU 3508  OD1 ASP A  84     6730   6474  10671   -303   1265   1151       O  
ATOM   3509  OD2 ASP A  84      19.194  34.199  12.897  1.00 66.31           O  
ANISOU 3509  OD2 ASP A  84     7114   6488  11592   -372   1366   1088       O  
ATOM   3510  N   PHE A  85      14.171  32.930  12.604  1.00 56.29           N  
ANISOU 3510  N   PHE A  85     6830   6538   8018    195    691   1288       N  
ATOM   3511  CA  PHE A  85      12.911  32.362  13.045  1.00 53.55           C  
ANISOU 3511  CA  PHE A  85     6501   6526   7318    269    419   1220       C  
ATOM   3512  C   PHE A  85      12.594  31.148  12.239  1.00 52.76           C  
ANISOU 3512  C   PHE A  85     6478   6612   6956    285    420   1269       C  
ATOM   3513  O   PHE A  85      12.786  31.130  11.029  1.00 54.63           O  
ANISOU 3513  O   PHE A  85     6929   6765   7064    362    612   1395       O  
ATOM   3514  CB  PHE A  85      11.745  33.337  12.890  1.00 54.46           C  
ANISOU 3514  CB  PHE A  85     6748   6680   7263    458    366   1263       C  
ATOM   3515  CG  PHE A  85      10.411  32.724  13.220  1.00 53.27           C  
ANISOU 3515  CG  PHE A  85     6527   6836   6877    529    147   1186       C  
ATOM   3516  CD1 PHE A  85       9.908  32.797  14.507  1.00 52.74           C  
ANISOU 3516  CD1 PHE A  85     6333   6855   6850    501     50   1040       C  
ATOM   3517  CD2 PHE A  85       9.670  32.056  12.245  1.00 53.64           C  
ANISOU 3517  CD2 PHE A  85     6643   7052   6687    624     57   1238       C  
ATOM   3518  CE1 PHE A  85       8.670  32.242  14.810  1.00 53.25           C  
ANISOU 3518  CE1 PHE A  85     6288   7144   6801    552    -38    977       C  
ATOM   3519  CE2 PHE A  85       8.435  31.474  12.549  1.00 53.66           C  
ANISOU 3519  CE2 PHE A  85     6478   7289   6622    657   -136   1132       C  
ATOM   3520  CZ  PHE A  85       7.934  31.567  13.825  1.00 53.22           C  
ANISOU 3520  CZ  PHE A  85     6242   7293   6688    612   -135   1018       C  
ATOM   3521  N   GLN A  86      11.973  30.184  12.896  1.00 51.70           N  
ANISOU 3521  N   GLN A  86     6228   6711   6705    233    221   1164       N  
ATOM   3522  CA  GLN A  86      11.775  28.896  12.298  1.00 51.60           C  
ANISOU 3522  CA  GLN A  86     6243   6831   6533    199    204   1154       C  
ATOM   3523  C   GLN A  86      10.700  28.176  13.055  1.00 50.61           C  
ANISOU 3523  C   GLN A  86     5985   6921   6323    163     22   1050       C  
ATOM   3524  O   GLN A  86      10.861  27.929  14.222  1.00 51.48           O  
ANISOU 3524  O   GLN A  86     5998   7042   6520     85    -13   1000       O  
ATOM   3525  CB  GLN A  86      13.080  28.128  12.439  1.00 51.46           C  
ANISOU 3525  CB  GLN A  86     6138   6681   6733     69    326   1152       C  
ATOM   3526  CG  GLN A  86      13.149  26.782  11.791  1.00 51.45           C  
ANISOU 3526  CG  GLN A  86     6188   6734   6627     28    380   1134       C  
ATOM   3527  CD  GLN A  86      14.483  26.144  12.066  1.00 52.18           C  
ANISOU 3527  CD  GLN A  86     6138   6657   7032    -65    502   1135       C  
ATOM   3528  OE1 GLN A  86      15.507  26.525  11.495  1.00 55.30           O  
ANISOU 3528  OE1 GLN A  86     6525   6829   7658    -62    761   1195       O  
ATOM   3529  NE2 GLN A  86      14.493  25.196  12.960  1.00 50.92           N  
ANISOU 3529  NE2 GLN A  86     5854   6563   6929   -132    342   1082       N  
ATOM   3530  N   CYS A  87       9.602  27.838  12.401  1.00 51.44           N  
ANISOU 3530  N   CYS A  87     6098   7169   6278    230    -92   1010       N  
ATOM   3531  CA  CYS A  87       8.555  27.030  13.049  1.00 51.44           C  
ANISOU 3531  CA  CYS A  87     5900   7319   6324    159   -186    900       C  
ATOM   3532  C   CYS A  87       8.235  25.772  12.238  1.00 52.42           C  
ANISOU 3532  C   CYS A  87     6017   7501   6398     88   -266    813       C  
ATOM   3533  O   CYS A  87       8.549  24.638  12.664  1.00 52.16           O  
ANISOU 3533  O   CYS A  87     5932   7442   6444    -63   -183    782       O  
ATOM   3534  CB  CYS A  87       7.251  27.815  13.225  1.00 52.67           C  
ANISOU 3534  CB  CYS A  87     5917   7564   6530    288   -289    851       C  
ATOM   3535  SG  CYS A  87       5.957  26.908  14.148  1.00 53.45           S  
ANISOU 3535  SG  CYS A  87     5698   7770   6839    177   -246    719       S  
ATOM   3536  N   LYS A  88       7.607  25.960  11.077  1.00 53.42           N  
ANISOU 3536  N   LYS A  88     6232   7682   6384    216   -458    763       N  
ATOM   3537  CA  LYS A  88       7.392  24.835  10.198  1.00 55.07           C  
ANISOU 3537  CA  LYS A  88     6505   7914   6506    162   -588    627       C  
ATOM   3538  C   LYS A  88       8.648  24.341   9.434  1.00 55.38           C  
ANISOU 3538  C   LYS A  88     6860   7820   6362    144   -398    681       C  
ATOM   3539  O   LYS A  88       8.745  23.167   9.117  1.00 56.35           O  
ANISOU 3539  O   LYS A  88     7011   7912   6487     37   -395    560       O  
ATOM   3540  CB  LYS A  88       6.290  25.152   9.217  1.00 58.46           C  
ANISOU 3540  CB  LYS A  88     6965   8436   6813    339   -958    511       C  
ATOM   3541  CG  LYS A  88       4.945  24.560   9.559  1.00 60.68           C  
ANISOU 3541  CG  LYS A  88     6828   8813   7416    251  -1191    297       C  
ATOM   3542  CD  LYS A  88       4.013  24.819   8.348  1.00 66.54           C  
ANISOU 3542  CD  LYS A  88     7632   9627   8025    469  -1699    141       C  
ATOM   3543  CE  LYS A  88       2.618  24.118   8.454  1.00 70.23           C  
ANISOU 3543  CE  LYS A  88     7588  10151   8945    370  -2024   -154       C  
ATOM   3544  NZ  LYS A  88       2.037  24.184   9.850  1.00 69.25           N  
ANISOU 3544  NZ  LYS A  88     6966  10021   9325    220  -1714   -127       N  
ATOM   3545  N   ASP A  89       9.591  25.229   9.120  1.00 54.87           N  
ANISOU 3545  N   ASP A  89     7017   7635   6196    246   -193    850       N  
ATOM   3546  CA  ASP A  89      10.649  24.896   8.171  1.00 55.72           C  
ANISOU 3546  CA  ASP A  89     7442   7581   6148    275     61    900       C  
ATOM   3547  C   ASP A  89      11.929  24.494   8.857  1.00 54.47           C  
ANISOU 3547  C   ASP A  89     7124   7272   6299    130    360    965       C  
ATOM   3548  O   ASP A  89      12.899  25.278   8.887  1.00 55.10           O  
ANISOU 3548  O   ASP A  89     7225   7184   6527    156    614   1102       O  
ATOM   3549  CB  ASP A  89      10.947  26.073   7.230  1.00 57.99           C  
ANISOU 3549  CB  ASP A  89     8105   7750   6177    489    204   1065       C  
ATOM   3550  CG  ASP A  89       9.803  26.371   6.290  1.00 61.47           C  
ANISOU 3550  CG  ASP A  89     8823   8306   6225    712   -155   1008       C  
ATOM   3551  OD1 ASP A  89       8.936  25.489   6.095  1.00 62.61           O  
ANISOU 3551  OD1 ASP A  89     8888   8597   6303    680   -503    788       O  
ATOM   3552  OD2 ASP A  89       9.771  27.492   5.746  1.00 64.05           O  
ANISOU 3552  OD2 ASP A  89     9444   8548   6342    929   -114   1178       O  
ATOM   3553  N   SER A  90      11.950  23.270   9.372  1.00 53.26           N  
ANISOU 3553  N   SER A  90     6801   7140   6296    -13    324    864       N  
ATOM   3554  CA  SER A  90      13.121  22.766  10.064  1.00 51.57           C  
ANISOU 3554  CA  SER A  90     6422   6777   6395   -107    513    921       C  
ATOM   3555  C   SER A  90      13.542  21.425   9.451  1.00 52.86           C  
ANISOU 3555  C   SER A  90     6687   6829   6570   -151    660    832       C  
ATOM   3556  O   SER A  90      13.374  20.362  10.047  1.00 52.76           O  
ANISOU 3556  O   SER A  90     6542   6814   6692   -252    587    771       O  
ATOM   3557  CB  SER A  90      12.818  22.651  11.551  1.00 49.27           C  
ANISOU 3557  CB  SER A  90     5874   6568   6278   -192    339    931       C  
ATOM   3558  OG  SER A  90      12.374  23.907  12.049  1.00 48.15           O  
ANISOU 3558  OG  SER A  90     5688   6509   6099   -135    233    974       O  
ATOM   3559  N   PRO A  91      14.117  21.480   8.248  1.00 54.95           N  
ANISOU 3559  N   PRO A  91     7237   6957   6686    -59    925    834       N  
ATOM   3560  CA  PRO A  91      14.399  20.270   7.505  1.00 56.11           C  
ANISOU 3560  CA  PRO A  91     7568   6982   6771    -70   1088    706       C  
ATOM   3561  C   PRO A  91      15.294  19.299   8.276  1.00 55.57           C  
ANISOU 3561  C   PRO A  91     7220   6755   7138   -159   1221    726       C  
ATOM   3562  O   PRO A  91      15.388  18.135   7.878  1.00 57.02           O  
ANISOU 3562  O   PRO A  91     7506   6826   7332   -186   1320    602       O  
ATOM   3563  CB  PRO A  91      15.141  20.782   6.266  1.00 58.91           C  
ANISOU 3563  CB  PRO A  91     8303   7158   6924     78   1492    769       C  
ATOM   3564  CG  PRO A  91      15.012  22.257   6.283  1.00 58.67           C  
ANISOU 3564  CG  PRO A  91     8311   7173   6808    163   1480    934       C  
ATOM   3565  CD  PRO A  91      14.771  22.664   7.663  1.00 55.93           C  
ANISOU 3565  CD  PRO A  91     7522   6954   6773     55   1198    980       C  
ATOM   3566  N   LYS A  92      15.966  19.773   9.332  1.00 54.11           N  
ANISOU 3566  N   LYS A  92     6716   6534   7310   -180   1192    862       N  
ATOM   3567  CA  LYS A  92      16.920  18.941  10.081  1.00 54.58           C  
ANISOU 3567  CA  LYS A  92     6517   6421   7799   -200   1237    900       C  
ATOM   3568  C   LYS A  92      16.260  18.234  11.239  1.00 53.10           C  
ANISOU 3568  C   LYS A  92     6226   6335   7614   -270    930    906       C  
ATOM   3569  O   LYS A  92      16.804  17.288  11.783  1.00 54.36           O  
ANISOU 3569  O   LYS A  92     6281   6347   8025   -259    928    941       O  
ATOM   3570  CB  LYS A  92      18.123  19.754  10.583  1.00 55.21           C  
ANISOU 3570  CB  LYS A  92     6305   6355   8316   -159   1304   1007       C  
ATOM   3571  CG  LYS A  92      19.147  20.153   9.513  1.00 57.59           C  
ANISOU 3571  CG  LYS A  92     6627   6410   8845   -101   1792   1029       C  
ATOM   3572  CD  LYS A  92      20.231  21.061  10.062  1.00 58.26           C  
ANISOU 3572  CD  LYS A  92     6323   6322   9492   -104   1826   1096       C  
ATOM   3573  CE  LYS A  92      20.933  20.414  11.231  1.00 59.58           C  
ANISOU 3573  CE  LYS A  92     6101   6410  10128    -91   1502   1082       C  
ATOM   3574  NZ  LYS A  92      22.236  21.056  11.532  1.00 62.73           N  
ANISOU 3574  NZ  LYS A  92     6040   6548  11247    -83   1553   1079       N  
ATOM   3575  N   ALA A  93      15.084  18.716  11.618  1.00 51.64           N  
ANISOU 3575  N   ALA A  93     6084   6370   7166   -320    711    890       N  
ATOM   3576  CA  ALA A  93      14.292  18.115  12.666  1.00 50.99           C  
ANISOU 3576  CA  ALA A  93     5954   6359   7060   -392    540    907       C  
ATOM   3577  C   ALA A  93      13.800  16.729  12.287  1.00 52.48           C  
ANISOU 3577  C   ALA A  93     6222   6452   7267   -482    623    800       C  
ATOM   3578  O   ALA A  93      13.528  16.447  11.130  1.00 54.02           O  
ANISOU 3578  O   ALA A  93     6549   6631   7346   -505    694    640       O  
ATOM   3579  CB  ALA A  93      13.120  18.996  12.968  1.00 49.94           C  
ANISOU 3579  CB  ALA A  93     5815   6444   6715   -418    390    887       C  
ATOM   3580  N   GLN A  94      13.673  15.878  13.293  1.00 53.31           N  
ANISOU 3580  N   GLN A  94     6295   6463   7497   -523    609    886       N  
ATOM   3581  CA  GLN A  94      13.153  14.520  13.159  1.00 54.68           C  
ANISOU 3581  CA  GLN A  94     6522   6480   7772   -636    718    803       C  
ATOM   3582  C   GLN A  94      11.801  14.520  12.473  1.00 55.32           C  
ANISOU 3582  C   GLN A  94     6590   6680   7751   -778    658    584       C  
ATOM   3583  O   GLN A  94      11.062  15.498  12.549  1.00 54.28           O  
ANISOU 3583  O   GLN A  94     6381   6761   7481   -777    523    565       O  
ATOM   3584  CB  GLN A  94      13.020  13.922  14.564  1.00 55.32           C  
ANISOU 3584  CB  GLN A  94     6627   6452   7940   -637    737    998       C  
ATOM   3585  CG  GLN A  94      13.331  14.989  15.624  1.00 54.49           C  
ANISOU 3585  CG  GLN A  94     6523   6486   7693   -512    570   1166       C  
ATOM   3586  CD  GLN A  94      12.313  15.029  16.705  1.00 55.72           C  
ANISOU 3586  CD  GLN A  94     6768   6694   7711   -558    619   1260       C  
ATOM   3587  OE1 GLN A  94      12.615  14.828  17.868  1.00 57.82           O  
ANISOU 3587  OE1 GLN A  94     7213   6867   7887   -449    594   1451       O  
ATOM   3588  NE2 GLN A  94      11.079  15.255  16.325  1.00 57.25           N  
ANISOU 3588  NE2 GLN A  94     6854   7006   7893   -702    700   1121       N  
ATOM   3589  N   LEU A  95      11.463  13.405  11.823  1.00 57.80           N  
ANISOU 3589  N   LEU A  95     6954   6826   8179   -891    726    393       N  
ATOM   3590  CA  LEU A  95      10.204  13.328  11.088  1.00 59.44           C  
ANISOU 3590  CA  LEU A  95     7108   7115   8362  -1024    566    113       C  
ATOM   3591  C   LEU A  95       8.987  13.244  11.987  1.00 60.39           C  
ANISOU 3591  C   LEU A  95     6986   7262   8695  -1176    563    128       C  
ATOM   3592  O   LEU A  95       8.000  13.911  11.728  1.00 60.30           O  
ANISOU 3592  O   LEU A  95     6814   7432   8667  -1206    366     -7       O  
ATOM   3593  CB  LEU A  95      10.217  12.173  10.109  1.00 62.40           C  
ANISOU 3593  CB  LEU A  95     7623   7268   8817  -1109    599   -161       C  
ATOM   3594  CG  LEU A  95      10.805  12.429   8.722  1.00 64.31           C  
ANISOU 3594  CG  LEU A  95     8164   7531   8738   -970    558   -333       C  
ATOM   3595  CD1 LEU A  95      11.696  13.682   8.645  1.00 61.23           C  
ANISOU 3595  CD1 LEU A  95     7860   7298   8107   -766    629   -106       C  
ATOM   3596  CD2 LEU A  95      11.563  11.184   8.251  1.00 66.32           C  
ANISOU 3596  CD2 LEU A  95     8613   7464   9122   -979    804   -450       C  
ATOM   3597  N   ARG A  96       9.069  12.430  13.042  1.00 61.27           N  
ANISOU 3597  N   ARG A  96     7090   7165   9025  -1247    812    309       N  
ATOM   3598  CA  ARG A  96       7.946  12.203  13.958  1.00 62.28           C  
ANISOU 3598  CA  ARG A  96     7036   7230   9397  -1399    977    356       C  
ATOM   3599  C   ARG A  96       7.851  13.315  15.004  1.00 60.53           C  
ANISOU 3599  C   ARG A  96     6817   7207   8976  -1274   1012    593       C  
ATOM   3600  O   ARG A  96       7.968  13.091  16.205  1.00 60.86           O  
ANISOU 3600  O   ARG A  96     6999   7131   8994  -1237   1251    848       O  
ATOM   3601  CB  ARG A  96       8.104  10.845  14.614  1.00 64.46           C  
ANISOU 3601  CB  ARG A  96     7420   7140   9934  -1497   1301    487       C  
ATOM   3602  CG  ARG A  96       8.264   9.727  13.600  1.00 67.07           C  
ANISOU 3602  CG  ARG A  96     7778   7226  10479  -1615   1286    225       C  
ATOM   3603  CD  ARG A  96       6.967   8.933  13.396  1.00 71.11           C  
ANISOU 3603  CD  ARG A  96     8032   7526  11461  -1914   1373    -49       C  
ATOM   3604  NE  ARG A  96       6.021   9.586  12.510  1.00 71.64           N  
ANISOU 3604  NE  ARG A  96     7829   7825  11566  -1993   1011   -402       N  
ATOM   3605  CZ  ARG A  96       4.706   9.445  12.594  1.00 74.79           C  
ANISOU 3605  CZ  ARG A  96     7843   8154  12420  -2215   1010   -609       C  
ATOM   3606  NH1 ARG A  96       4.170   8.695  13.552  1.00 77.62           N  
ANISOU 3606  NH1 ARG A  96     8062   8199  13230  -2406   1464   -472       N  
ATOM   3607  NH2 ARG A  96       3.921  10.093  11.742  1.00 75.90           N  
ANISOU 3607  NH2 ARG A  96     7734   8516  12588  -2225    567   -938       N  
ATOM   3608  N   ARG A  97       7.647  14.528  14.514  1.00 58.91           N  
ANISOU 3608  N   ARG A  97     6518   7278   8588  -1184    767    503       N  
ATOM   3609  CA  ARG A  97       7.552  15.734  15.332  1.00 57.19           C  
ANISOU 3609  CA  ARG A  97     6305   7245   8179  -1055    763    661       C  
ATOM   3610  C   ARG A  97       6.779  16.759  14.501  1.00 56.35           C  
ANISOU 3610  C   ARG A  97     5996   7365   8051  -1023    509    467       C  
ATOM   3611  O   ARG A  97       7.051  16.939  13.340  1.00 55.69           O  
ANISOU 3611  O   ARG A  97     5961   7351   7849   -972    271    325       O  
ATOM   3612  CB  ARG A  97       8.966  16.265  15.630  1.00 54.55           C  
ANISOU 3612  CB  ARG A  97     6207   6948   7572   -866    674    847       C  
ATOM   3613  CG  ARG A  97       9.047  17.714  16.025  1.00 52.47           C  
ANISOU 3613  CG  ARG A  97     5955   6881   7101   -727    554    909       C  
ATOM   3614  CD  ARG A  97      10.472  18.137  16.324  1.00 51.06           C  
ANISOU 3614  CD  ARG A  97     5932   6677   6792   -579    436   1039       C  
ATOM   3615  NE  ARG A  97      10.576  19.586  16.571  1.00 50.54           N  
ANISOU 3615  NE  ARG A  97     5864   6757   6584   -472    306   1047       N  
ATOM   3616  CZ  ARG A  97      10.349  20.540  15.656  1.00 49.46           C  
ANISOU 3616  CZ  ARG A  97     5635   6742   6416   -443    216    951       C  
ATOM   3617  NH1 ARG A  97       9.974  20.230  14.425  1.00 49.42           N  
ANISOU 3617  NH1 ARG A  97     5574   6762   6442   -490    193    829       N  
ATOM   3618  NH2 ARG A  97      10.447  21.817  15.981  1.00 49.17           N  
ANISOU 3618  NH2 ARG A  97     5611   6779   6293   -348    135    970       N  
ATOM   3619  N   THR A  98       5.785  17.400  15.077  1.00 57.83           N  
ANISOU 3619  N   THR A  98     5986   7638   8349  -1025    578    465       N  
ATOM   3620  CA  THR A  98       5.071  18.442  14.362  1.00 58.07           C  
ANISOU 3620  CA  THR A  98     5819   7864   8379   -936    301    311       C  
ATOM   3621  C   THR A  98       4.863  19.572  15.354  1.00 57.39           C  
ANISOU 3621  C   THR A  98     5733   7873   8198   -810    440    460       C  
ATOM   3622  O   THR A  98       4.377  19.335  16.461  1.00 59.56           O  
ANISOU 3622  O   THR A  98     5969   8053   8609   -869    781    549       O  
ATOM   3623  CB  THR A  98       3.699  17.951  13.850  1.00 62.31           C  
ANISOU 3623  CB  THR A  98     5955   8362   9359  -1083    191     37       C  
ATOM   3624  OG1 THR A  98       3.883  16.895  12.892  1.00 64.16           O  
ANISOU 3624  OG1 THR A  98     6236   8482   9659  -1202     17   -163       O  
ATOM   3625  CG2 THR A  98       2.924  19.110  13.200  1.00 62.74           C  
ANISOU 3625  CG2 THR A  98     5799   8613   9426   -924   -166   -100       C  
ATOM   3626  N   ILE A  99       5.263  20.788  14.992  1.00 55.50           N  
ANISOU 3626  N   ILE A  99     5597   7780   7711   -629    232    494       N  
ATOM   3627  CA  ILE A  99       5.136  21.921  15.897  1.00 54.74           C  
ANISOU 3627  CA  ILE A  99     5538   7742   7517   -501    346    597       C  
ATOM   3628  C   ILE A  99       4.378  23.024  15.197  1.00 55.85           C  
ANISOU 3628  C   ILE A  99     5488   8010   7723   -360    116    493       C  
ATOM   3629  O   ILE A  99       4.507  23.177  13.995  1.00 56.25           O  
ANISOU 3629  O   ILE A  99     5568   8118   7685   -294   -186    418       O  
ATOM   3630  CB  ILE A  99       6.509  22.421  16.290  1.00 52.62           C  
ANISOU 3630  CB  ILE A  99     5595   7458   6942   -406    319    749       C  
ATOM   3631  CG1 ILE A  99       6.404  23.563  17.289  1.00 52.94           C  
ANISOU 3631  CG1 ILE A  99     5726   7524   6866   -281    409    803       C  
ATOM   3632  CG2 ILE A  99       7.305  22.852  15.068  1.00 50.31           C  
ANISOU 3632  CG2 ILE A  99     5388   7201   6526   -333     81    731       C  
ATOM   3633  CD1 ILE A  99       7.796  24.038  17.764  1.00 50.91           C  
ANISOU 3633  CD1 ILE A  99     5746   7213   6386   -207    306    895       C  
ATOM   3634  N   GLU A 100       3.549  23.770  15.916  1.00 57.13           N  
ANISOU 3634  N   GLU A 100     5489   8191   8028   -283    268    488       N  
ATOM   3635  CA  GLU A 100       2.820  24.876  15.279  1.00 58.50           C  
ANISOU 3635  CA  GLU A 100     5470   8457   8303    -99     28    406       C  
ATOM   3636  C   GLU A 100       3.011  26.126  16.116  1.00 57.54           C  
ANISOU 3636  C   GLU A 100     5502   8324   8038     57    192    505       C  
ATOM   3637  O   GLU A 100       3.192  26.034  17.328  1.00 57.75           O  
ANISOU 3637  O   GLU A 100     5677   8279   7987     12    521    569       O  
ATOM   3638  CB  GLU A 100       1.326  24.547  15.073  1.00 62.23           C  
ANISOU 3638  CB  GLU A 100     5432   8927   9286   -138    -16    216       C  
ATOM   3639  CG  GLU A 100       1.048  23.727  13.805  1.00 64.29           C  
ANISOU 3639  CG  GLU A 100     5539   9214   9672   -212   -428     27       C  
ATOM   3640  CD  GLU A 100      -0.386  23.171  13.723  1.00 70.09           C  
ANISOU 3640  CD  GLU A 100     5677   9893  11063   -317   -489   -219       C  
ATOM   3641  OE1 GLU A 100      -1.348  23.926  13.983  1.00 72.86           O  
ANISOU 3641  OE1 GLU A 100     5659  10252  11771   -186   -475   -276       O  
ATOM   3642  OE2 GLU A 100      -0.565  21.979  13.381  1.00 71.73           O  
ANISOU 3642  OE2 GLU A 100     5740  10013  11502   -533   -550   -379       O  
ATOM   3643  N   CYS A 101       3.025  27.285  15.470  1.00 57.26           N  
ANISOU 3643  N   CYS A 101     5506   8326   7925    257    -40    517       N  
ATOM   3644  CA  CYS A 101       3.255  28.538  16.173  1.00 56.92           C  
ANISOU 3644  CA  CYS A 101     5624   8226   7776    403     95    579       C  
ATOM   3645  C   CYS A 101       2.168  29.543  15.855  1.00 59.91           C  
ANISOU 3645  C   CYS A 101     5750   8612   8401    625     -3    520       C  
ATOM   3646  O   CYS A 101       1.464  29.405  14.852  1.00 61.39           O  
ANISOU 3646  O   CYS A 101     5695   8864   8765    706   -309    453       O  
ATOM   3647  CB  CYS A 101       4.613  29.103  15.793  1.00 54.38           C  
ANISOU 3647  CB  CYS A 101     5650   7851   7161    435    -27    687       C  
ATOM   3648  SG  CYS A 101       5.926  27.874  15.958  1.00 53.26           S  
ANISOU 3648  SG  CYS A 101     5712   7682   6844    218     12    745       S  
ATOM   3649  N   CYS A 102       2.012  30.534  16.732  1.00 60.81           N  
ANISOU 3649  N   CYS A 102     5930   8642   8535    745    228    522       N  
ATOM   3650  CA  CYS A 102       1.056  31.629  16.529  1.00 63.79           C  
ANISOU 3650  CA  CYS A 102     6083   8977   9176   1000    175    480       C  
ATOM   3651  C   CYS A 102       1.389  32.736  17.516  1.00 63.91           C  
ANISOU 3651  C   CYS A 102     6360   8850   9072   1101    447    485       C  
ATOM   3652  O   CYS A 102       2.068  32.478  18.516  1.00 62.69           O  
ANISOU 3652  O   CYS A 102     6491   8653   8676    966    679    476       O  
ATOM   3653  CB  CYS A 102      -0.386  31.168  16.732  1.00 67.22           C  
ANISOU 3653  CB  CYS A 102     5989   9434  10116   1011    300    343       C  
ATOM   3654  SG  CYS A 102      -0.678  30.458  18.324  1.00 67.98           S  
ANISOU 3654  SG  CYS A 102     6083   9450  10299    822    957    299       S  
ATOM   3655  N   ARG A 103       0.898  33.954  17.264  1.00 65.80           N  
ANISOU 3655  N   ARG A 103     6532   8992   9475   1359    388    483       N  
ATOM   3656  CA  ARG A 103       1.399  35.107  18.010  1.00 65.75           C  
ANISOU 3656  CA  ARG A 103     6843   8805   9336   1452    579    466       C  
ATOM   3657  C   ARG A 103       0.339  35.970  18.655  1.00 69.34           C  
ANISOU 3657  C   ARG A 103     7121   9133  10093   1677    859    359       C  
ATOM   3658  O   ARG A 103       0.519  37.172  18.795  1.00 70.51           O  
ANISOU 3658  O   ARG A 103     7457   9094  10238   1847    896    347       O  
ATOM   3659  CB  ARG A 103       2.315  35.975  17.138  1.00 64.85           C  
ANISOU 3659  CB  ARG A 103     6997   8574   9069   1534    321    594       C  
ATOM   3660  CG  ARG A 103       3.556  36.456  17.871  1.00 63.74           C  
ANISOU 3660  CG  ARG A 103     7238   8272   8710   1407    431    556       C  
ATOM   3661  CD  ARG A 103       4.447  37.389  17.041  1.00 63.58           C  
ANISOU 3661  CD  ARG A 103     7431   8051   8674   1462    292    681       C  
ATOM   3662  NE  ARG A 103       5.733  37.633  17.708  1.00 62.34           N  
ANISOU 3662  NE  ARG A 103     7528   7734   8426   1276    337    598       N  
ATOM   3663  CZ  ARG A 103       6.631  38.527  17.306  1.00 62.68           C  
ANISOU 3663  CZ  ARG A 103     7735   7512   8568   1265    324    652       C  
ATOM   3664  NH1 ARG A 103       6.393  39.285  16.236  1.00 63.93           N  
ANISOU 3664  NH1 ARG A 103     7929   7529   8831   1455    322    839       N  
ATOM   3665  NH2 ARG A 103       7.766  38.664  17.978  1.00 61.86           N  
ANISOU 3665  NH2 ARG A 103     7763   7254   8486   1076    305    517       N  
ATOM   3666  N   THR A 104      -0.749  35.349  19.085  1.00 72.37           N  
ANISOU 3666  N   THR A 104     7133   9575  10790   1669   1114    270       N  
ATOM   3667  CA  THR A 104      -1.848  36.062  19.728  1.00 76.72           C  
ANISOU 3667  CA  THR A 104     7443   9983  11726   1888   1484    154       C  
ATOM   3668  C   THR A 104      -1.961  35.596  21.174  1.00 78.03           C  
ANISOU 3668  C   THR A 104     7811  10085  11751   1762   2092     55       C  
ATOM   3669  O   THR A 104      -1.727  34.427  21.479  1.00 76.73           O  
ANISOU 3669  O   THR A 104     7712  10019  11422   1525   2207     90       O  
ATOM   3670  CB  THR A 104      -3.174  35.753  19.018  1.00 80.36           C  
ANISOU 3670  CB  THR A 104     7212  10506  12817   2013   1345    113       C  
ATOM   3671  OG1 THR A 104      -3.131  36.285  17.695  1.00 80.12           O  
ANISOU 3671  OG1 THR A 104     7105  10510  12825   2213    743    211       O  
ATOM   3672  CG2 THR A 104      -4.378  36.335  19.786  1.00 86.17           C  
ANISOU 3672  CG2 THR A 104     7588  11065  14087   2226   1842    -23       C  
ATOM   3673  N   ASN A 105      -2.335  36.503  22.065  1.00 81.16           N  
ANISOU 3673  N   ASN A 105     8365  10286  12187   1947   2510    -61       N  
ATOM   3674  CA  ASN A 105      -2.554  36.113  23.442  1.00 83.61           C  
ANISOU 3674  CA  ASN A 105     8963  10502  12304   1888   3155   -150       C  
ATOM   3675  C   ASN A 105      -3.283  34.776  23.593  1.00 85.03           C  
ANISOU 3675  C   ASN A 105     8782  10758  12769   1711   3493   -107       C  
ATOM   3676  O   ASN A 105      -4.432  34.606  23.159  1.00 88.08           O  
ANISOU 3676  O   ASN A 105     8488  11129  13850   1771   3613   -144       O  
ATOM   3677  CB  ASN A 105      -3.258  37.225  24.230  1.00 88.92           C  
ANISOU 3677  CB  ASN A 105     9710  10927  13150   2163   3658   -311       C  
ATOM   3678  CG  ASN A 105      -2.305  37.976  25.155  1.00 88.62           C  
ANISOU 3678  CG  ASN A 105    10459  10738  12475   2202   3718   -433       C  
ATOM   3679  OD1 ASN A 105      -2.649  38.312  26.293  1.00 92.46           O  
ANISOU 3679  OD1 ASN A 105    11308  11038  12785   2326   4292   -585       O  
ATOM   3680  ND2 ASN A 105      -1.089  38.210  24.677  1.00 84.42           N  
ANISOU 3680  ND2 ASN A 105    10204  10263  11610   2094   3134   -388       N  
ATOM   3681  N   LEU A 106      -2.578  33.835  24.213  1.00 83.16           N  
ANISOU 3681  N   LEU A 106     8994  10568  12034   1498   3618    -35       N  
ATOM   3682  CA  LEU A 106      -3.089  32.508  24.520  1.00 84.98           C  
ANISOU 3682  CA  LEU A 106     9040  10803  12446   1303   4022     34       C  
ATOM   3683  C   LEU A 106      -3.460  31.680  23.294  1.00 83.59           C  
ANISOU 3683  C   LEU A 106     8192  10774  12795   1140   3615     73       C  
ATOM   3684  O   LEU A 106      -4.164  30.694  23.405  1.00 86.48           O  
ANISOU 3684  O   LEU A 106     8203  11087  13567    982   3966     80       O  
ATOM   3685  CB  LEU A 106      -4.267  32.597  25.486  1.00 91.72           C  
ANISOU 3685  CB  LEU A 106     9769  11432  13650   1414   4906    -42       C  
ATOM   3686  CG  LEU A 106      -3.990  32.311  26.969  1.00 94.74           C  
ANISOU 3686  CG  LEU A 106    10957  11649  13391   1425   5583     -7       C  
ATOM   3687  CD1 LEU A 106      -2.985  33.297  27.554  1.00 93.19           C  
ANISOU 3687  CD1 LEU A 106    11547  11430  12432   1588   5326    -96       C  
ATOM   3688  CD2 LEU A 106      -5.303  32.273  27.796  1.00102.07           C  
ANISOU 3688  CD2 LEU A 106    11685  12312  14785   1523   6614    -58       C  
ATOM   3689  N   CYS A 107      -2.944  32.045  22.130  1.00 80.10           N  
ANISOU 3689  N   CYS A 107     7631  10484  12319   1172   2892     92       N  
ATOM   3690  CA  CYS A 107      -3.398  31.423  20.889  1.00 79.82           C  
ANISOU 3690  CA  CYS A 107     7007  10573  12746   1087   2438     76       C  
ATOM   3691  C   CYS A 107      -3.185  29.923  20.807  1.00 78.60           C  
ANISOU 3691  C   CYS A 107     6819  10471  12575    781   2466    124       C  
ATOM   3692  O   CYS A 107      -3.788  29.262  19.967  1.00 80.15           O  
ANISOU 3692  O   CYS A 107     6483  10716  13256    683   2204     45       O  
ATOM   3693  CB  CYS A 107      -2.776  32.106  19.668  1.00 76.55           C  
ANISOU 3693  CB  CYS A 107     6660  10283  12142   1214   1710    120       C  
ATOM   3694  SG  CYS A 107      -1.011  32.026  19.586  1.00 70.36           S  
ANISOU 3694  SG  CYS A 107     6579   9572  10583   1082   1423    258       S  
ATOM   3695  N   ASN A 108      -2.349  29.375  21.677  1.00 76.61           N  
ANISOU 3695  N   ASN A 108     7140  10184  11786    648   2746    235       N  
ATOM   3696  CA  ASN A 108      -1.957  27.989  21.504  1.00 75.22           C  
ANISOU 3696  CA  ASN A 108     7004  10035  11540    386   2701    311       C  
ATOM   3697  C   ASN A 108      -2.852  26.966  22.185  1.00 79.75           C  
ANISOU 3697  C   ASN A 108     7341  10428  12532    218   3359    315       C  
ATOM   3698  O   ASN A 108      -2.672  25.771  21.975  1.00 79.45           O  
ANISOU 3698  O   ASN A 108     7264  10364  12560     -9   3348    365       O  
ATOM   3699  CB  ASN A 108      -0.489  27.770  21.863  1.00 71.34           C  
ANISOU 3699  CB  ASN A 108     7198   9589  10319    337   2521    448       C  
ATOM   3700  CG  ASN A 108      -0.189  28.128  23.293  1.00 73.16           C  
ANISOU 3700  CG  ASN A 108     8022   9692  10081    441   2970    499       C  
ATOM   3701  OD1 ASN A 108      -1.060  28.629  24.015  1.00 76.96           O  
ANISOU 3701  OD1 ASN A 108     8466  10047  10728    562   3486    438       O  
ATOM   3702  ND2 ASN A 108       1.046  27.865  23.724  1.00 70.47           N  
ANISOU 3702  ND2 ASN A 108     8252   9366   9157    417   2768    594       N  
ATOM   3703  N   GLN A 109      -3.817  27.421  22.981  1.00 84.99           N  
ANISOU 3703  N   GLN A 109     7843  10926  13524    327   3989    263       N  
ATOM   3704  CA  GLN A 109      -4.822  26.524  23.543  1.00 90.37           C  
ANISOU 3704  CA  GLN A 109     8184  11372  14778    164   4725    260       C  
ATOM   3705  C   GLN A 109      -5.603  25.900  22.406  1.00 92.23           C  
ANISOU 3705  C   GLN A 109     7548  11629  15866     -9   4364     93       C  
ATOM   3706  O   GLN A 109      -5.834  24.694  22.393  1.00 93.71           O  
ANISOU 3706  O   GLN A 109     7539  11681  16385   -276   4592    104       O  
ATOM   3707  CB  GLN A 109      -5.786  27.285  24.440  1.00 96.13           C  
ANISOU 3707  CB  GLN A 109     8802  11902  15821    349   5480    201       C  
ATOM   3708  CG  GLN A 109      -7.037  26.484  24.794  1.00103.39           C  
ANISOU 3708  CG  GLN A 109     9122  12535  17626    179   6275    158       C  
ATOM   3709  CD  GLN A 109      -8.248  27.378  24.987  1.00109.22           C  
ANISOU 3709  CD  GLN A 109     9258  13124  19117    378   6720    -11       C  
ATOM   3710  OE1 GLN A 109      -9.351  26.908  25.306  1.00115.59           O  
ANISOU 3710  OE1 GLN A 109     9470  13653  20794    267   7446    -76       O  
ATOM   3711  NE2 GLN A 109      -8.050  28.683  24.783  1.00107.12           N  
ANISOU 3711  NE2 GLN A 109     9105  13001  18595    675   6315    -86       N  
ATOM   3712  N   TYR A 110      -6.004  26.743  21.453  1.00 92.40           N  
ANISOU 3712  N   TYR A 110     7084  11794  16230    165   3766    -73       N  
ATOM   3713  CA  TYR A 110      -6.673  26.298  20.227  1.00 94.51           C  
ANISOU 3713  CA  TYR A 110     6587  12117  17207     71   3180   -281       C  
ATOM   3714  C   TYR A 110      -5.694  25.620  19.269  1.00 89.68           C  
ANISOU 3714  C   TYR A 110     6267  11689  16120    -69   2479   -256       C  
ATOM   3715  O   TYR A 110      -5.711  25.911  18.075  1.00 89.20           O  
ANISOU 3715  O   TYR A 110     5987  11790  16116     37   1708   -381       O  
ATOM   3716  CB  TYR A 110      -7.240  27.492  19.450  1.00 95.63           C  
ANISOU 3716  CB  TYR A 110     6295  12367  17675    386   2628   -426       C  
ATOM   3717  CG  TYR A 110      -8.268  28.331  20.156  1.00101.12           C  
ANISOU 3717  CG  TYR A 110     6587  12883  18950    595   3194   -496       C  
ATOM   3718  CD1 TYR A 110      -7.890  29.267  21.119  1.00 99.96           C  
ANISOU 3718  CD1 TYR A 110     7018  12685  18279    794   3684   -364       C  
ATOM   3719  CD2 TYR A 110      -9.616  28.242  19.812  1.00107.92           C  
ANISOU 3719  CD2 TYR A 110     6464  13609  20933    617   3188   -731       C  
ATOM   3720  CE1 TYR A 110      -8.836  30.065  21.756  1.00105.19           C  
ANISOU 3720  CE1 TYR A 110     7342  13153  19471   1013   4255   -448       C  
ATOM   3721  CE2 TYR A 110     -10.570  29.029  20.440  1.00113.40           C  
ANISOU 3721  CE2 TYR A 110     6729  14108  22251    834   3752   -803       C  
ATOM   3722  CZ  TYR A 110     -10.174  29.941  21.412  1.00111.94           C  
ANISOU 3722  CZ  TYR A 110     7186  13867  21477   1038   4321   -653       C  
ATOM   3723  OH  TYR A 110     -11.120  30.722  22.046  1.00117.60           O  
ANISOU 3723  OH  TYR A 110     7515  14359  22808   1272   4949   -741       O  
ATOM   3724  N   LEU A 111      -4.845  24.725  19.753  1.00 86.66           N  
ANISOU 3724  N   LEU A 111     6409  11261  15256   -271   2739    -92       N  
ATOM   3725  CA  LEU A 111      -3.787  24.238  18.875  1.00 81.58           C  
ANISOU 3725  CA  LEU A 111     6100  10780  14117   -350   2120    -59       C  
ATOM   3726  C   LEU A 111      -3.471  22.767  19.085  1.00 81.78           C  
ANISOU 3726  C   LEU A 111     6254  10660  14160   -653   2372     -3       C  
ATOM   3727  O   LEU A 111      -3.196  22.330  20.199  1.00 82.02           O  
ANISOU 3727  O   LEU A 111     6676  10530  13957   -724   2995    191       O  
ATOM   3728  CB  LEU A 111      -2.545  25.120  18.963  1.00 75.79           C  
ANISOU 3728  CB  LEU A 111     6042  10206  12550   -156   1884    114       C  
ATOM   3729  CG  LEU A 111      -1.992  25.507  17.595  1.00 73.07           C  
ANISOU 3729  CG  LEU A 111     5741  10054  11967    -50   1109     61       C  
ATOM   3730  CD1 LEU A 111      -3.089  25.895  16.627  1.00 76.41           C  
ANISOU 3730  CD1 LEU A 111     5561  10525  12947     77    673   -152       C  
ATOM   3731  CD2 LEU A 111      -0.971  26.623  17.727  1.00 69.50           C  
ANISOU 3731  CD2 LEU A 111     5816   9688  10905    151    980    209       C  
ATOM   3732  N   GLN A 112      -3.445  22.039  17.970  1.00 81.87           N  
ANISOU 3732  N   GLN A 112     6022  10715  14372   -794   1843   -170       N  
ATOM   3733  CA  GLN A 112      -3.723  20.616  17.934  1.00 84.15           C  
ANISOU 3733  CA  GLN A 112     6091  10786  15096  -1110   2053   -253       C  
ATOM   3734  C   GLN A 112      -2.843  19.908  16.927  1.00 80.86           C  
ANISOU 3734  C   GLN A 112     5934  10456  14332  -1198   1489   -313       C  
ATOM   3735  O   GLN A 112      -3.347  19.177  16.083  1.00 83.91           O  
ANISOU 3735  O   GLN A 112     5918  10772  15193  -1365   1155   -584       O  
ATOM   3736  CB  GLN A 112      -5.134  20.466  17.409  1.00 90.28           C  
ANISOU 3736  CB  GLN A 112     5985  11454  16865  -1209   1919   -582       C  
ATOM   3737  CG  GLN A 112      -6.161  19.947  18.349  1.00 96.71           C  
ANISOU 3737  CG  GLN A 112     6339  11933  18473  -1407   2746   -597       C  
ATOM   3738  CD  GLN A 112      -7.400  19.506  17.564  1.00103.66           C  
ANISOU 3738  CD  GLN A 112     6250  12673  20463  -1580   2427  -1005       C  
ATOM   3739  OE1 GLN A 112      -7.292  19.168  16.382  1.00103.80           O  
ANISOU 3739  OE1 GLN A 112     6127  12805  20508  -1621   1610  -1260       O  
ATOM   3740  NE2 GLN A 112      -8.567  19.523  18.200  1.00109.31           N  
ANISOU 3740  NE2 GLN A 112     6303  13122  22106  -1666   3053  -1093       N  
ATOM   3741  N   PRO A 113      -1.535  20.114  16.995  1.00 75.25           N  
ANISOU 3741  N   PRO A 113     5875   9873  12843  -1085   1379    -96       N  
ATOM   3742  CA  PRO A 113      -0.678  19.614  15.916  1.00 72.71           C  
ANISOU 3742  CA  PRO A 113     5793   9637  12197  -1115    861   -166       C  
ATOM   3743  C   PRO A 113      -0.781  18.094  15.731  1.00 74.74           C  
ANISOU 3743  C   PRO A 113     5935   9660  12804  -1409    980   -282       C  
ATOM   3744  O   PRO A 113      -0.827  17.370  16.725  1.00 75.92           O  
ANISOU 3744  O   PRO A 113     6164   9576  13106  -1560   1573   -122       O  
ATOM   3745  CB  PRO A 113       0.737  20.007  16.384  1.00 67.85           C  
ANISOU 3745  CB  PRO A 113     5824   9107  10848   -974    934    121       C  
ATOM   3746  CG  PRO A 113       0.626  20.063  17.886  1.00 69.12           C  
ANISOU 3746  CG  PRO A 113     6156   9138  10969   -974   1557    334       C  
ATOM   3747  CD  PRO A 113      -0.775  20.549  18.176  1.00 72.87           C  
ANISOU 3747  CD  PRO A 113     6121   9567  11998   -966   1803    205       C  
ATOM   3748  N   THR A 114      -0.797  17.620  14.481  1.00 75.44           N  
ANISOU 3748  N   THR A 114     5909   9778  12976  -1469    440   -553       N  
ATOM   3749  CA  THR A 114      -0.822  16.168  14.207  1.00 78.38           C  
ANISOU 3749  CA  THR A 114     6210   9895  13677  -1751    508   -711       C  
ATOM   3750  C   THR A 114       0.459  15.640  13.541  1.00 75.34           C  
ANISOU 3750  C   THR A 114     6361   9533  12732  -1719    284   -669       C  
ATOM   3751  O   THR A 114       0.977  16.240  12.595  1.00 73.65           O  
ANISOU 3751  O   THR A 114     6387   9532  12065  -1524   -188   -733       O  
ATOM   3752  CB  THR A 114      -2.004  15.742  13.297  1.00 84.29           C  
ANISOU 3752  CB  THR A 114     6341  10554  15129  -1907     74  -1171       C  
ATOM   3753  OG1 THR A 114      -1.620  15.880  11.922  1.00 83.23           O  
ANISOU 3753  OG1 THR A 114     6431  10598  14594  -1767   -663  -1400       O  
ATOM   3754  CG2 THR A 114      -3.280  16.562  13.578  1.00 87.97           C  
ANISOU 3754  CG2 THR A 114     6175  11063  16188  -1845     73  -1286       C  
ATOM   3755  N   LEU A 115       0.951  14.502  14.023  1.00 74.95           N  
ANISOU 3755  N   LEU A 115     6510   9224  12745  -1894    672   -554       N  
ATOM   3756  CA  LEU A 115       2.041  13.807  13.365  1.00 72.61           C  
ANISOU 3756  CA  LEU A 115     6621   8873  12096  -1886    513   -567       C  
ATOM   3757  C   LEU A 115       1.619  13.453  11.945  1.00 76.18           C  
ANISOU 3757  C   LEU A 115     6922   9330  12692  -1950    -42  -1011       C  
ATOM   3758  O   LEU A 115       0.455  13.126  11.703  1.00 81.51           O  
ANISOU 3758  O   LEU A 115     7108   9893  13968  -2128   -198  -1326       O  
ATOM   3759  CB  LEU A 115       2.362  12.520  14.123  1.00 73.72           C  
ANISOU 3759  CB  LEU A 115     6902   8656  12452  -2074   1021   -409       C  
ATOM   3760  CG  LEU A 115       3.061  12.691  15.466  1.00 71.55           C  
ANISOU 3760  CG  LEU A 115     6983   8345  11856  -1947   1485     44       C  
ATOM   3761  CD1 LEU A 115       3.094  11.377  16.218  1.00 74.65           C  
ANISOU 3761  CD1 LEU A 115     7503   8327  12533  -2119   1998    206       C  
ATOM   3762  CD2 LEU A 115       4.481  13.249  15.258  1.00 66.80           C  
ANISOU 3762  CD2 LEU A 115     6814   7946  10620  -1690   1242    220       C  
ATOM   3763  N   PRO A 116       2.560  13.507  10.992  1.00 74.53           N  
ANISOU 3763  N   PRO A 116     7140   9223  11953  -1796   -343  -1060       N  
ATOM   3764  CA  PRO A 116       2.256  13.040   9.634  1.00 78.13           C  
ANISOU 3764  CA  PRO A 116     7622   9644  12418  -1830   -858  -1498       C  
ATOM   3765  C   PRO A 116       1.851  11.557   9.661  1.00 82.45           C  
ANISOU 3765  C   PRO A 116     7969   9815  13543  -2156   -711  -1759       C  
ATOM   3766  O   PRO A 116       2.107  10.882  10.664  1.00 82.04           O  
ANISOU 3766  O   PRO A 116     7904   9527  13740  -2305   -149  -1510       O  
ATOM   3767  CB  PRO A 116       3.571  13.244   8.880  1.00 75.02           C  
ANISOU 3767  CB  PRO A 116     7838   9346  11322  -1607   -926  -1396       C  
ATOM   3768  CG  PRO A 116       4.624  13.431   9.950  1.00 70.54           C  
ANISOU 3768  CG  PRO A 116     7454   8769  10579  -1543   -413   -937       C  
ATOM   3769  CD  PRO A 116       3.927  14.033  11.117  1.00 69.81           C  
ANISOU 3769  CD  PRO A 116     7020   8752  10753  -1576   -210   -738       C  
ATOM   3770  N   PRO A 117       1.211  11.054   8.583  1.00 87.30           N  
ANISOU 3770  N   PRO A 117     8459  10342  14369  -2254  -1228  -2263       N  
ATOM   3771  CA  PRO A 117       0.634   9.705   8.650  1.00 92.35           C  
ANISOU 3771  CA  PRO A 117     8794  10573  15721  -2610  -1106  -2571       C  
ATOM   3772  C   PRO A 117       1.561   8.493   8.393  1.00 92.65           C  
ANISOU 3772  C   PRO A 117     9268  10301  15633  -2707   -853  -2613       C  
ATOM   3773  O   PRO A 117       1.238   7.404   8.851  1.00 95.92           O  
ANISOU 3773  O   PRO A 117     9457  10318  16670  -3004   -512  -2695       O  
ATOM   3774  CB  PRO A 117      -0.516   9.744   7.614  1.00 98.83           C  
ANISOU 3774  CB  PRO A 117     9243  11419  16889  -2668  -1882  -3165       C  
ATOM   3775  CG  PRO A 117      -0.537  11.178   7.057  1.00 96.93           C  
ANISOU 3775  CG  PRO A 117     9166  11621  16041  -2288  -2391  -3093       C  
ATOM   3776  CD  PRO A 117       0.815  11.763   7.356  1.00 89.62           C  
ANISOU 3776  CD  PRO A 117     8841  10879  14330  -2041  -1978  -2585       C  
ATOM   3777  N   VAL A 118       2.690   8.642   7.695  1.00 90.44           N  
ANISOU 3777  N   VAL A 118     9591  10144  14628  -2462   -944  -2550       N  
ATOM   3778  CA  VAL A 118       3.452   7.441   7.205  1.00 92.45           C  
ANISOU 3778  CA  VAL A 118    10234  10067  14827  -2535   -781  -2714       C  
ATOM   3779  C   VAL A 118       2.628   6.540   6.254  1.00 98.53           C  
ANISOU 3779  C   VAL A 118    10882  10572  15981  -2761  -1239  -3375       C  
ATOM   3780  O   VAL A 118       1.552   6.038   6.607  1.00101.30           O  
ANISOU 3780  O   VAL A 118    10673  10696  17119  -3070  -1279  -3610       O  
ATOM   3781  CB  VAL A 118       4.069   6.542   8.346  1.00 90.48           C  
ANISOU 3781  CB  VAL A 118    10000   9477  14901  -2666    -64  -2334       C  
ATOM   3782  CG1 VAL A 118       4.655   5.262   7.768  1.00 92.92           C  
ANISOU 3782  CG1 VAL A 118    10630   9389  15285  -2750     61  -2576       C  
ATOM   3783  CG2 VAL A 118       5.145   7.289   9.101  1.00 85.31           C  
ANISOU 3783  CG2 VAL A 118     9595   9044  13776  -2398    267  -1767       C  
TER    3784      VAL A 118                                                      
ATOM   3785  N   GLN I   1      -8.924 -11.551  27.797  1.00 86.44           N  
ANISOU 3785  N   GLN I   1     8855  17046   6941  -2007  -1597  -2958       N  
ATOM   3786  CA  GLN I   1      -8.134 -11.722  29.053  1.00 81.84           C  
ANISOU 3786  CA  GLN I   1     8526  15663   6906  -1806  -1380  -2895       C  
ATOM   3787  C   GLN I   1      -7.556 -10.391  29.516  1.00 76.66           C  
ANISOU 3787  C   GLN I   1     7935  14853   6338  -1405  -1385  -2333       C  
ATOM   3788  O   GLN I   1      -7.435  -9.460  28.734  1.00 77.92           O  
ANISOU 3788  O   GLN I   1     8008  15435   6164  -1275  -1483  -2044       O  
ATOM   3789  CB  GLN I   1      -7.004 -12.749  28.869  1.00 84.26           C  
ANISOU 3789  CB  GLN I   1     9078  15589   7347  -1931  -1110  -3350       C  
ATOM   3790  CG  GLN I   1      -7.451 -14.231  28.822  1.00 89.44           C  
ANISOU 3790  CG  GLN I   1     9722  16103   8159  -2311   -998  -3945       C  
ATOM   3791  CD  GLN I   1      -8.102 -14.733  30.125  1.00 89.51           C  
ANISOU 3791  CD  GLN I   1     9711  15632   8667  -2322   -969  -3901       C  
ATOM   3792  OE1 GLN I   1      -7.753 -14.286  31.260  1.00 86.17           O  
ANISOU 3792  OE1 GLN I   1     9392  14765   8583  -2040   -923  -3530       O  
ATOM   3793  NE2 GLN I   1      -9.060 -15.667  29.972  1.00 91.75           N  
ANISOU 3793  NE2 GLN I   1     9851  16026   8984  -2668   -989  -4291       N  
ATOM   3794  N   VAL I   2      -7.223 -10.294  30.792  1.00 69.92           N  
ANISOU 3794  N   VAL I   2     7221  13414   5933  -1223  -1273  -2173       N  
ATOM   3795  CA  VAL I   2      -6.583  -9.108  31.317  1.00 66.10           C  
ANISOU 3795  CA  VAL I   2     6817  12722   5576   -884  -1239  -1722       C  
ATOM   3796  C   VAL I   2      -5.182  -8.960  30.720  1.00 65.61           C  
ANISOU 3796  C   VAL I   2     6938  12588   5402   -793  -1099  -1755       C  
ATOM   3797  O   VAL I   2      -4.489  -9.955  30.505  1.00 66.36           O  
ANISOU 3797  O   VAL I   2     7176  12490   5547   -940   -948  -2135       O  
ATOM   3798  CB  VAL I   2      -6.501  -9.222  32.846  1.00 62.69           C  
ANISOU 3798  CB  VAL I   2     6498  11707   5614   -778  -1138  -1634       C  
ATOM   3799  CG1 VAL I   2      -5.568  -8.179  33.465  1.00 59.23           C  
ANISOU 3799  CG1 VAL I   2     6191  10976   5338   -482  -1051  -1287       C  
ATOM   3800  CG2 VAL I   2      -7.895  -9.132  33.431  1.00 63.06           C  
ANISOU 3800  CG2 VAL I   2     6346  11853   5759   -825  -1263  -1525       C  
ATOM   3801  N   GLN I   3      -4.798  -7.720  30.415  1.00 64.81           N  
ANISOU 3801  N   GLN I   3     6811  12641   5171   -553  -1129  -1355       N  
ATOM   3802  CA  GLN I   3      -3.474  -7.390  29.901  1.00 64.10           C  
ANISOU 3802  CA  GLN I   3     6874  12485   4996   -435   -992  -1310       C  
ATOM   3803  C   GLN I   3      -2.907  -6.158  30.606  1.00 61.01           C  
ANISOU 3803  C   GLN I   3     6535  11805   4841   -129   -938   -870       C  
ATOM   3804  O   GLN I   3      -3.592  -5.155  30.752  1.00 61.77           O  
ANISOU 3804  O   GLN I   3     6482  12046   4942     17  -1036   -504       O  
ATOM   3805  CB  GLN I   3      -3.535  -7.146  28.393  1.00 68.01           C  
ANISOU 3805  CB  GLN I   3     7254  13614   4973   -512  -1069  -1304       C  
ATOM   3806  CG  GLN I   3      -3.122  -8.353  27.544  1.00 71.85           C  
ANISOU 3806  CG  GLN I   3     7826  14241   5235   -791   -968  -1843       C  
ATOM   3807  CD  GLN I   3      -2.537  -7.955  26.170  1.00 75.86           C  
ANISOU 3807  CD  GLN I   3     8315  15247   5262   -798   -944  -1804       C  
ATOM   3808  OE1 GLN I   3      -1.655  -7.078  26.072  1.00 74.27           O  
ANISOU 3808  OE1 GLN I   3     8183  14956   5079   -560   -859  -1476       O  
ATOM   3809  NE2 GLN I   3      -3.038  -8.603  25.102  1.00 80.21           N  
ANISOU 3809  NE2 GLN I   3     8761  16347   5367  -1092  -1011  -2150       N  
ATOM   3810  N   LEU I   4      -1.662  -6.234  31.061  1.00 58.08           N  
ANISOU 3810  N   LEU I   4     6360  11015   4694    -40   -770   -911       N  
ATOM   3811  CA  LEU I   4      -0.985  -5.056  31.615  1.00 55.14           C  
ANISOU 3811  CA  LEU I   4     6036  10396   4518    211   -702   -546       C  
ATOM   3812  C   LEU I   4       0.389  -4.945  30.959  1.00 55.78           C  
ANISOU 3812  C   LEU I   4     6238  10438   4517    272   -558   -563       C  
ATOM   3813  O   LEU I   4       1.156  -5.890  30.997  1.00 55.92           O  
ANISOU 3813  O   LEU I   4     6385  10243   4620    178   -442   -861       O  
ATOM   3814  CB  LEU I   4      -0.843  -5.186  33.131  1.00 52.16           C  
ANISOU 3814  CB  LEU I   4     5753   9516   4548    253   -647   -550       C  
ATOM   3815  CG  LEU I   4      -2.124  -5.327  33.977  1.00 52.10           C  
ANISOU 3815  CG  LEU I   4     5644   9477   4674    197   -747   -539       C  
ATOM   3816  CD1 LEU I   4      -1.850  -5.984  35.298  1.00 49.11           C  
ANISOU 3816  CD1 LEU I   4     5385   8659   4616    154   -675   -667       C  
ATOM   3817  CD2 LEU I   4      -2.820  -4.003  34.186  1.00 51.41           C  
ANISOU 3817  CD2 LEU I   4     5415   9495   4624    368   -800   -167       C  
ATOM   3818  N   VAL I   5       0.690  -3.831  30.298  1.00 56.87           N  
ANISOU 3818  N   VAL I   5     6316  10787   4504    428   -545   -236       N  
ATOM   3819  CA  VAL I   5       2.045  -3.665  29.762  1.00 57.07           C  
ANISOU 3819  CA  VAL I   5     6451  10743   4489    495   -387   -227       C  
ATOM   3820  C   VAL I   5       2.737  -2.385  30.214  1.00 55.31           C  
ANISOU 3820  C   VAL I   5     6243  10273   4500    718   -299    146       C  
ATOM   3821  O   VAL I   5       2.291  -1.278  29.873  1.00 57.30           O  
ANISOU 3821  O   VAL I   5     6366  10722   4684    851   -336    514       O  
ATOM   3822  CB  VAL I   5       2.136  -3.888  28.222  1.00 60.69           C  
ANISOU 3822  CB  VAL I   5     6861  11722   4477    400   -381   -316       C  
ATOM   3823  CG1 VAL I   5       0.762  -3.796  27.560  1.00 63.82           C  
ANISOU 3823  CG1 VAL I   5     7058  12663   4527    310   -582   -238       C  
ATOM   3824  CG2 VAL I   5       3.172  -2.969  27.585  1.00 60.99           C  
ANISOU 3824  CG2 VAL I   5     6919  11818   4436    563   -251    -33       C  
ATOM   3825  N   GLU I   6       3.798  -2.567  31.012  1.00 52.00           N  
ANISOU 3825  N   GLU I   6     5960   9417   4379    747   -177     53       N  
ATOM   3826  CA  GLU I   6       4.617  -1.481  31.573  1.00 50.08           C  
ANISOU 3826  CA  GLU I   6     5742   8887   4398    908    -75    318       C  
ATOM   3827  C   GLU I   6       5.515  -0.878  30.536  1.00 51.75           C  
ANISOU 3827  C   GLU I   6     5948   9253   4463    996     45    491       C  
ATOM   3828  O   GLU I   6       5.880  -1.545  29.584  1.00 54.91           O  
ANISOU 3828  O   GLU I   6     6378   9882   4604    919     88    318       O  
ATOM   3829  CB  GLU I   6       5.529  -2.016  32.676  1.00 47.59           C  
ANISOU 3829  CB  GLU I   6     5548   8139   4395    875     -4    144       C  
ATOM   3830  CG  GLU I   6       4.829  -2.680  33.849  1.00 46.67           C  
ANISOU 3830  CG  GLU I   6     5451   7831   4451    785    -95    -10       C  
ATOM   3831  CD  GLU I   6       4.638  -4.173  33.647  1.00 47.57           C  
ANISOU 3831  CD  GLU I   6     5607   7974   4492    630   -113   -341       C  
ATOM   3832  OE1 GLU I   6       4.749  -4.626  32.501  1.00 49.59           O  
ANISOU 3832  OE1 GLU I   6     5861   8472   4507    573    -77   -481       O  
ATOM   3833  OE2 GLU I   6       4.358  -4.894  34.631  1.00 46.62           O  
ANISOU 3833  OE2 GLU I   6     5517   7637   4560    554   -146   -467       O  
ATOM   3834  N   SER I   7       5.903   0.370  30.724  1.00 51.01           N  
ANISOU 3834  N   SER I   7     5816   9019   4548   1146    127    812       N  
ATOM   3835  CA  SER I   7       6.874   0.990  29.808  1.00 53.19           C  
ANISOU 3835  CA  SER I   7     6082   9393   4733   1235    272   1007       C  
ATOM   3836  C   SER I   7       7.466   2.198  30.456  1.00 51.98           C  
ANISOU 3836  C   SER I   7     5914   8903   4933   1359    391   1265       C  
ATOM   3837  O   SER I   7       6.915   2.697  31.429  1.00 50.93           O  
ANISOU 3837  O   SER I   7     5754   8547   5050   1385    357   1324       O  
ATOM   3838  CB  SER I   7       6.241   1.430  28.481  1.00 56.59           C  
ANISOU 3838  CB  SER I   7     6384  10333   4784   1283    233   1262       C  
ATOM   3839  OG  SER I   7       5.369   2.550  28.665  1.00 56.76           O  
ANISOU 3839  OG  SER I   7     6262  10381   4923   1417    192   1644       O  
ATOM   3840  N   GLY I   8       8.566   2.685  29.893  1.00 53.07           N  
ANISOU 3840  N   GLY I   8     6060   9011   5093   1423    550   1402       N  
ATOM   3841  CA  GLY I   8       9.230   3.872  30.414  1.00 52.02           C  
ANISOU 3841  CA  GLY I   8     5900   8552   5313   1517    693   1630       C  
ATOM   3842  C   GLY I   8      10.509   3.563  31.149  1.00 50.57           C  
ANISOU 3842  C   GLY I   8     5803   8036   5374   1451    774   1424       C  
ATOM   3843  O   GLY I   8      11.234   4.473  31.522  1.00 51.62           O  
ANISOU 3843  O   GLY I   8     5910   7917   5786   1490    904   1563       O  
ATOM   3844  N   GLY I   9      10.796   2.283  31.364  1.00 49.66           N  
ANISOU 3844  N   GLY I   9     5773   7916   5180   1346    708   1104       N  
ATOM   3845  CA  GLY I   9      12.059   1.894  31.994  1.00 49.07           C  
ANISOU 3845  CA  GLY I   9     5744   7569   5332   1297    778    953       C  
ATOM   3846  C   GLY I   9      13.262   2.431  31.235  1.00 50.61           C  
ANISOU 3846  C   GLY I   9     5907   7763   5561   1360    965   1104       C  
ATOM   3847  O   GLY I   9      13.119   2.918  30.117  1.00 53.08           O  
ANISOU 3847  O   GLY I   9     6181   8321   5666   1434   1043   1303       O  
ATOM   3848  N   GLY I  10      14.457   2.341  31.824  1.00 49.56           N  
ANISOU 3848  N   GLY I  10     5769   7382   5679   1328   1037   1035       N  
ATOM   3849  CA  GLY I  10      15.663   2.829  31.143  1.00 50.90           C  
ANISOU 3849  CA  GLY I  10     5891   7533   5914   1379   1229   1174       C  
ATOM   3850  C   GLY I  10      16.731   3.314  32.103  1.00 50.95           C  
ANISOU 3850  C   GLY I  10     5841   7235   6285   1335   1279   1188       C  
ATOM   3851  O   GLY I  10      16.545   3.258  33.330  1.00 50.20           O  
ANISOU 3851  O   GLY I  10     5746   6968   6360   1254   1158   1081       O  
ATOM   3852  N   LEU I  11      17.845   3.800  31.552  1.00 51.75           N  
ANISOU 3852  N   LEU I  11     5877   7297   6486   1370   1459   1318       N  
ATOM   3853  CA  LEU I  11      18.988   4.191  32.367  1.00 51.27           C  
ANISOU 3853  CA  LEU I  11     5731   6988   6760   1304   1510   1316       C  
ATOM   3854  C   LEU I  11      18.921   5.630  32.859  1.00 51.70           C  
ANISOU 3854  C   LEU I  11     5726   6860   7057   1275   1571   1473       C  
ATOM   3855  O   LEU I  11      18.610   6.542  32.097  1.00 54.21           O  
ANISOU 3855  O   LEU I  11     6025   7217   7356   1360   1702   1708       O  
ATOM   3856  CB  LEU I  11      20.280   4.005  31.571  1.00 53.88           C  
ANISOU 3856  CB  LEU I  11     5998   7345   7127   1343   1695   1367       C  
ATOM   3857  CG  LEU I  11      21.429   3.267  32.272  1.00 53.96           C  
ANISOU 3857  CG  LEU I  11     5928   7218   7357   1281   1678   1230       C  
ATOM   3858  CD1 LEU I  11      22.494   2.963  31.221  1.00 56.33           C  
ANISOU 3858  CD1 LEU I  11     6173   7587   7644   1351   1895   1277       C  
ATOM   3859  CD2 LEU I  11      22.023   3.993  33.524  1.00 52.27           C  
ANISOU 3859  CD2 LEU I  11     5601   6795   7464   1161   1615   1247       C  
ATOM   3860  N   VAL I  12      19.270   5.828  34.126  1.00 50.66           N  
ANISOU 3860  N   VAL I  12     5548   6534   7166   1146   1495   1349       N  
ATOM   3861  CA  VAL I  12      19.148   7.115  34.799  1.00 50.58           C  
ANISOU 3861  CA  VAL I  12     5486   6317   7414   1069   1562   1398       C  
ATOM   3862  C   VAL I  12      20.268   7.300  35.813  1.00 51.06           C  
ANISOU 3862  C   VAL I  12     5442   6229   7730    897   1551   1267       C  
ATOM   3863  O   VAL I  12      20.699   6.337  36.437  1.00 51.59           O  
ANISOU 3863  O   VAL I  12     5489   6363   7750    829   1399   1123       O  
ATOM   3864  CB  VAL I  12      17.877   7.151  35.588  1.00 48.69           C  
ANISOU 3864  CB  VAL I  12     5317   6059   7125   1034   1428   1293       C  
ATOM   3865  CG1 VAL I  12      17.479   8.548  35.785  1.00 51.12           C  
ANISOU 3865  CG1 VAL I  12     5584   6167   7673   1022   1578   1397       C  
ATOM   3866  CG2 VAL I  12      16.831   6.442  34.825  1.00 48.89           C  
ANISOU 3866  CG2 VAL I  12     5430   6304   6842   1159   1343   1338       C  
ATOM   3867  N   GLN I  13      20.735   8.528  35.988  1.00 52.46           N  
ANISOU 3867  N   GLN I  13     5532   6213   8188    819   1713   1327       N  
ATOM   3868  CA  GLN I  13      21.733   8.793  36.980  1.00 52.46           C  
ANISOU 3868  CA  GLN I  13     5410   6109   8411    614   1692   1176       C  
ATOM   3869  C   GLN I  13      21.048   8.993  38.322  1.00 51.39           C  
ANISOU 3869  C   GLN I  13     5304   5923   8300    447   1563    948       C  
ATOM   3870  O   GLN I  13      19.910   9.421  38.385  1.00 51.27           O  
ANISOU 3870  O   GLN I  13     5377   5841   8263    493   1592    947       O  
ATOM   3871  CB  GLN I  13      22.575  10.002  36.574  1.00 55.12           C  
ANISOU 3871  CB  GLN I  13     5630   6255   9059    568   1946   1301       C  
ATOM   3872  CG  GLN I  13      23.682   9.675  35.575  1.00 56.34           C  
ANISOU 3872  CG  GLN I  13     5705   6487   9217    661   2057   1470       C  
ATOM   3873  CD  GLN I  13      24.507  10.902  35.271  1.00 60.62           C  
ANISOU 3873  CD  GLN I  13     6115   6821  10097    593   2316   1595       C  
ATOM   3874  OE1 GLN I  13      25.384  10.897  34.397  1.00 63.01           O  
ANISOU 3874  OE1 GLN I  13     6341   7154  10448    666   2466   1767       O  
ATOM   3875  NE2 GLN I  13      24.222  11.982  35.985  1.00 62.56           N  
ANISOU 3875  NE2 GLN I  13     6330   6836  10603    443   2401   1500       N  
ATOM   3876  N   PRO I  14      21.733   8.633  39.409  1.00 51.69           N  
ANISOU 3876  N   PRO I  14     5252   6026   8362    252   1415    767       N  
ATOM   3877  CA  PRO I  14      21.222   8.918  40.746  1.00 51.04           C  
ANISOU 3877  CA  PRO I  14     5178   5934   8280     47   1314    528       C  
ATOM   3878  C   PRO I  14      20.793  10.359  40.845  1.00 52.58           C  
ANISOU 3878  C   PRO I  14     5379   5873   8727    -31   1542    467       C  
ATOM   3879  O   PRO I  14      21.557  11.257  40.511  1.00 54.32           O  
ANISOU 3879  O   PRO I  14     5499   5923   9216    -90   1741    513       O  
ATOM   3880  CB  PRO I  14      22.446   8.720  41.631  1.00 51.95           C  
ANISOU 3880  CB  PRO I  14     5122   6164   8452   -177   1197    410       C  
ATOM   3881  CG  PRO I  14      23.306   7.765  40.865  1.00 52.19           C  
ANISOU 3881  CG  PRO I  14     5087   6307   8435    -25   1153    599       C  
ATOM   3882  CD  PRO I  14      23.093   8.061  39.426  1.00 52.03           C  
ANISOU 3882  CD  PRO I  14     5149   6169   8452    202   1361    795       C  
ATOM   3883  N   GLY I  15      19.576  10.577  41.308  1.00 52.19           N  
ANISOU 3883  N   GLY I  15     5432   5772   8627    -29   1538    366       N  
ATOM   3884  CA  GLY I  15      19.097  11.923  41.526  1.00 53.20           C  
ANISOU 3884  CA  GLY I  15     5553   5616   9043   -104   1785    284       C  
ATOM   3885  C   GLY I  15      18.334  12.423  40.333  1.00 53.43           C  
ANISOU 3885  C   GLY I  15     5633   5497   9170    166   1972    584       C  
ATOM   3886  O   GLY I  15      17.847  13.561  40.337  1.00 56.02           O  
ANISOU 3886  O   GLY I  15     5941   5546   9796    166   2219    600       O  
ATOM   3887  N   GLY I  16      18.263  11.594  39.297  1.00 51.48           N  
ANISOU 3887  N   GLY I  16     5434   5441   8687    388   1873    829       N  
ATOM   3888  CA  GLY I  16      17.405  11.873  38.154  1.00 52.43           C  
ANISOU 3888  CA  GLY I  16     5593   5545   8783    644   1985   1136       C  
ATOM   3889  C   GLY I  16      15.985  11.365  38.373  1.00 51.75           C  
ANISOU 3889  C   GLY I  16     5602   5578   8481    733   1843   1107       C  
ATOM   3890  O   GLY I  16      15.678  10.770  39.401  1.00 50.16           O  
ANISOU 3890  O   GLY I  16     5449   5456   8153    603   1670    851       O  
ATOM   3891  N   SER I  17      15.106  11.586  37.405  1.00 52.52           N  
ANISOU 3891  N   SER I  17     5709   5720   8528    952   1910   1392       N  
ATOM   3892  CA  SER I  17      13.753  11.064  37.517  1.00 51.38           C  
ANISOU 3892  CA  SER I  17     5626   5721   8174   1038   1765   1385       C  
ATOM   3893  C   SER I  17      13.259  10.450  36.241  1.00 51.27           C  
ANISOU 3893  C   SER I  17     5629   5996   7857   1241   1676   1647       C  
ATOM   3894  O   SER I  17      13.745  10.748  35.166  1.00 53.01           O  
ANISOU 3894  O   SER I  17     5803   6274   8066   1353   1788   1907       O  
ATOM   3895  CB  SER I  17      12.770  12.125  37.991  1.00 52.83           C  
ANISOU 3895  CB  SER I  17     5767   5658   8646   1059   1940   1407       C  
ATOM   3896  OG  SER I  17      12.995  13.325  37.332  1.00 54.74           O  
ANISOU 3896  OG  SER I  17     5912   5670   9217   1160   2222   1681       O  
ATOM   3897  N   LEU I  18      12.254   9.602  36.388  1.00 50.13           N  
ANISOU 3897  N   LEU I  18     5543   6050   7455   1267   1480   1565       N  
ATOM   3898  CA  LEU I  18      11.759   8.755  35.332  1.00 49.67           C  
ANISOU 3898  CA  LEU I  18     5507   6324   7041   1392   1346   1700       C  
ATOM   3899  C   LEU I  18      10.288   8.631  35.544  1.00 50.34           C  
ANISOU 3899  C   LEU I  18     5585   6503   7040   1444   1247   1715       C  
ATOM   3900  O   LEU I  18       9.822   8.691  36.678  1.00 49.46           O  
ANISOU 3900  O   LEU I  18     5496   6238   7060   1348   1220   1515       O  
ATOM   3901  CB  LEU I  18      12.290   7.358  35.553  1.00 48.06           C  
ANISOU 3901  CB  LEU I  18     5391   6272   6597   1291   1160   1444       C  
ATOM   3902  CG  LEU I  18      13.179   6.730  34.522  1.00 48.19           C  
ANISOU 3902  CG  LEU I  18     5421   6465   6424   1334   1170   1496       C  
ATOM   3903  CD1 LEU I  18      12.896   5.262  34.578  1.00 46.23           C  
ANISOU 3903  CD1 LEU I  18     5250   6404   5911   1286    981   1278       C  
ATOM   3904  CD2 LEU I  18      12.789   7.314  33.183  1.00 51.31           C  
ANISOU 3904  CD2 LEU I  18     5758   7043   6695   1494   1274   1824       C  
ATOM   3905  N   ARG I  19       9.531   8.390  34.487  1.00 51.75           N  
ANISOU 3905  N   ARG I  19     5722   6971   6969   1578   1182   1934       N  
ATOM   3906  CA  ARG I  19       8.121   8.088  34.699  1.00 51.14           C  
ANISOU 3906  CA  ARG I  19     5619   7030   6783   1608   1051   1925       C  
ATOM   3907  C   ARG I  19       7.598   6.798  34.078  1.00 50.90           C  
ANISOU 3907  C   ARG I  19     5626   7380   6335   1589    830   1834       C  
ATOM   3908  O   ARG I  19       7.532   6.691  32.853  1.00 52.97           O  
ANISOU 3908  O   ARG I  19     5839   7945   6344   1673    813   2033       O  
ATOM   3909  CB  ARG I  19       7.239   9.213  34.240  1.00 52.96           C  
ANISOU 3909  CB  ARG I  19     5700   7241   7182   1779   1182   2295       C  
ATOM   3910  CG  ARG I  19       5.838   8.862  34.563  1.00 53.95           C  
ANISOU 3910  CG  ARG I  19     5779   7499   7220   1797   1045   2264       C  
ATOM   3911  CD  ARG I  19       4.985  10.078  34.604  1.00 56.74           C  
ANISOU 3911  CD  ARG I  19     5972   7690   7896   1950   1219   2572       C  
ATOM   3912  NE  ARG I  19       4.397  10.355  33.307  1.00 60.02           N  
ANISOU 3912  NE  ARG I  19     6226   8436   8143   2135   1194   3018       N  
ATOM   3913  CZ  ARG I  19       3.159  10.818  33.156  1.00 63.43           C  
ANISOU 3913  CZ  ARG I  19     6479   8955   8666   2277   1200   3300       C  
ATOM   3914  NH1 ARG I  19       2.394  11.033  34.236  1.00 61.67           N  
ANISOU 3914  NH1 ARG I  19     6237   8477   8718   2252   1253   3140       N  
ATOM   3915  NH2 ARG I  19       2.686  11.065  31.929  1.00 65.90           N  
ANISOU 3915  NH2 ARG I  19     6615   9637   8786   2441   1157   3754       N  
ATOM   3916  N   LEU I  20       7.164   5.849  34.911  1.00 48.34           N  
ANISOU 3916  N   LEU I  20     5376   7056   5936   1469    676   1538       N  
ATOM   3917  CA  LEU I  20       6.624   4.605  34.376  1.00 47.89           C  
ANISOU 3917  CA  LEU I  20     5347   7314   5534   1425    493   1410       C  
ATOM   3918  C   LEU I  20       5.122   4.686  34.103  1.00 50.03           C  
ANISOU 3918  C   LEU I  20     5508   7808   5692   1484    396   1544       C  
ATOM   3919  O   LEU I  20       4.370   5.386  34.791  1.00 50.52           O  
ANISOU 3919  O   LEU I  20     5502   7714   5979   1527    441   1629       O  
ATOM   3920  CB  LEU I  20       6.917   3.423  35.280  1.00 45.04           C  
ANISOU 3920  CB  LEU I  20     5100   6854   5158   1272    387   1064       C  
ATOM   3921  CG  LEU I  20       8.348   3.313  35.819  1.00 44.16           C  
ANISOU 3921  CG  LEU I  20     5061   6517   5202   1205    459    942       C  
ATOM   3922  CD1 LEU I  20       8.560   2.019  36.614  1.00 40.95           C  
ANISOU 3922  CD1 LEU I  20     4731   6060   4767   1077    344    671       C  
ATOM   3923  CD2 LEU I  20       9.314   3.458  34.679  1.00 44.52           C  
ANISOU 3923  CD2 LEU I  20     5097   6658   5160   1272    560   1063       C  
ATOM   3924  N   SER I  21       4.699   3.967  33.073  1.00 50.95           N  
ANISOU 3924  N   SER I  21     5593   8308   5458   1473    274   1551       N  
ATOM   3925  CA  SER I  21       3.297   3.856  32.720  1.00 52.66           C  
ANISOU 3925  CA  SER I  21     5679   8819   5509   1497    142   1657       C  
ATOM   3926  C   SER I  21       2.976   2.383  32.583  1.00 52.14           C  
ANISOU 3926  C   SER I  21     5679   8967   5166   1330    -25   1320       C  
ATOM   3927  O   SER I  21       3.841   1.565  32.284  1.00 52.34           O  
ANISOU 3927  O   SER I  21     5819   9003   5064   1241    -13   1096       O  
ATOM   3928  CB  SER I  21       3.002   4.528  31.366  1.00 55.78           C  
ANISOU 3928  CB  SER I  21     5915   9586   5692   1631    153   2049       C  
ATOM   3929  OG  SER I  21       3.857   5.629  31.100  1.00 57.59           O  
ANISOU 3929  OG  SER I  21     6125   9638   6117   1763    351   2332       O  
ATOM   3930  N   CYS I  22       1.718   2.036  32.747  1.00 52.05           N  
ANISOU 3930  N   CYS I  22     5577   9120   5081   1286   -159   1286       N  
ATOM   3931  CA  CYS I  22       1.329   0.713  32.358  1.00 52.50           C  
ANISOU 3931  CA  CYS I  22     5660   9431   4858   1119   -301    992       C  
ATOM   3932  C   CYS I  22      -0.087   0.779  31.849  1.00 54.84           C  
ANISOU 3932  C   CYS I  22     5758  10114   4965   1118   -449   1135       C  
ATOM   3933  O   CYS I  22      -0.990   1.252  32.529  1.00 53.65           O  
ANISOU 3933  O   CYS I  22     5504   9870   5011   1177   -472   1266       O  
ATOM   3934  CB  CYS I  22       1.496  -0.289  33.501  1.00 50.64           C  
ANISOU 3934  CB  CYS I  22     5563   8883   4796    981   -315    642       C  
ATOM   3935  SG  CYS I  22      -0.003  -1.071  34.227  1.00 49.98           S  
ANISOU 3935  SG  CYS I  22     5407   8849   4733    854   -462    471       S  
ATOM   3936  N   ALA I  23      -0.259   0.327  30.618  1.00 57.19           N  
ANISOU 3936  N   ALA I  23     5987  10877   4866   1044   -541   1111       N  
ATOM   3937  CA  ALA I  23      -1.543   0.373  29.976  1.00 59.67           C  
ANISOU 3937  CA  ALA I  23     6077  11663   4934   1023   -709   1266       C  
ATOM   3938  C   ALA I  23      -2.280  -0.897  30.324  1.00 59.02           C  
ANISOU 3938  C   ALA I  23     6009  11638   4779    798   -838    865       C  
ATOM   3939  O   ALA I  23      -1.685  -1.955  30.280  1.00 59.49           O  
ANISOU 3939  O   ALA I  23     6227  11612   4763    634   -808    477       O  
ATOM   3940  CB  ALA I  23      -1.352   0.487  28.471  1.00 62.98           C  
ANISOU 3940  CB  ALA I  23     6400  12623   4905   1016   -752   1420       C  
ATOM   3941  N   ALA I  24      -3.556  -0.790  30.680  1.00 58.79           N  
ANISOU 3941  N   ALA I  24     5803  11724   4812    794   -956    966       N  
ATOM   3942  CA  ALA I  24      -4.385  -1.949  30.965  1.00 59.26           C  
ANISOU 3942  CA  ALA I  24     5838  11867   4813    570  -1079    615       C  
ATOM   3943  C   ALA I  24      -5.476  -2.157  29.921  1.00 64.34           C  
ANISOU 3943  C   ALA I  24     6226  13148   5071    456  -1281    670       C  
ATOM   3944  O   ALA I  24      -6.065  -1.207  29.411  1.00 67.31           O  
ANISOU 3944  O   ALA I  24     6371  13848   5354    606  -1354   1101       O  
ATOM   3945  CB  ALA I  24      -5.015  -1.805  32.298  1.00 57.12           C  
ANISOU 3945  CB  ALA I  24     5556  11230   4918    615  -1052    636       C  
ATOM   3946  N   SER I  25      -5.782  -3.407  29.622  1.00 65.66           N  
ANISOU 3946  N   SER I  25     6411  13503   5034    180  -1367    242       N  
ATOM   3947  CA  SER I  25      -6.923  -3.677  28.776  1.00 69.70           C  
ANISOU 3947  CA  SER I  25     6657  14635   5190     20  -1579    240       C  
ATOM   3948  C   SER I  25      -7.614  -4.960  29.210  1.00 70.10           C  
ANISOU 3948  C   SER I  25     6711  14624   5298   -264  -1640   -224       C  
ATOM   3949  O   SER I  25      -7.124  -5.677  30.086  1.00 66.56           O  
ANISOU 3949  O   SER I  25     6482  13659   5149   -325  -1505   -524       O  
ATOM   3950  CB  SER I  25      -6.509  -3.739  27.314  1.00 72.94           C  
ANISOU 3950  CB  SER I  25     7024  15610   5082    -74  -1632    216       C  
ATOM   3951  OG  SER I  25      -5.388  -4.576  27.140  1.00 72.19           O  
ANISOU 3951  OG  SER I  25     7196  15294   4940   -208  -1477   -214       O  
ATOM   3952  N   GLY I  26      -8.776  -5.217  28.623  1.00 73.03           N  
ANISOU 3952  N   GLY I  26     6814  15532   5403   -433  -1843   -245       N  
ATOM   3953  CA  GLY I  26      -9.489  -6.458  28.863  1.00 73.70           C  
ANISOU 3953  CA  GLY I  26     6866  15624   5512   -745  -1902   -705       C  
ATOM   3954  C   GLY I  26     -10.256  -6.560  30.163  1.00 70.97           C  
ANISOU 3954  C   GLY I  26     6483  14879   5604   -708  -1885   -668       C  
ATOM   3955  O   GLY I  26     -10.771  -7.622  30.504  1.00 71.55           O  
ANISOU 3955  O   GLY I  26     6553  14860   5775   -958  -1894  -1042       O  
ATOM   3956  N   PHE I  27     -10.312  -5.466  30.907  1.00 68.77           N  
ANISOU 3956  N   PHE I  27     6180  14343   5607   -405  -1830   -234       N  
ATOM   3957  CA  PHE I  27     -11.116  -5.423  32.115  1.00 67.09           C  
ANISOU 3957  CA  PHE I  27     5903  13813   5775   -358  -1801   -164       C  
ATOM   3958  C   PHE I  27     -11.532  -3.991  32.320  1.00 67.13           C  
ANISOU 3958  C   PHE I  27     5728  13856   5924    -47  -1799    381       C  
ATOM   3959  O   PHE I  27     -10.995  -3.091  31.690  1.00 67.25           O  
ANISOU 3959  O   PHE I  27     5727  14010   5815    143  -1782    689       O  
ATOM   3960  CB  PHE I  27     -10.348  -5.966  33.330  1.00 63.60           C  
ANISOU 3960  CB  PHE I  27     5768  12705   5690   -360  -1601   -401       C  
ATOM   3961  CG  PHE I  27      -9.215  -5.102  33.792  1.00 60.30           C  
ANISOU 3961  CG  PHE I  27     5556  11912   5442   -104  -1440   -187       C  
ATOM   3962  CD1 PHE I  27      -7.996  -5.140  33.155  1.00 60.19           C  
ANISOU 3962  CD1 PHE I  27     5721  11878   5271    -84  -1373   -267       C  
ATOM   3963  CD2 PHE I  27      -9.350  -4.285  34.901  1.00 58.55           C  
ANISOU 3963  CD2 PHE I  27     5347  11348   5549     92  -1334     58       C  
ATOM   3964  CE1 PHE I  27      -6.919  -4.352  33.609  1.00 57.91           C  
ANISOU 3964  CE1 PHE I  27     5608  11238   5159    131  -1222    -82       C  
ATOM   3965  CE2 PHE I  27      -8.269  -3.510  35.369  1.00 55.97           C  
ANISOU 3965  CE2 PHE I  27     5208  10672   5386    286  -1176    202       C  
ATOM   3966  CZ  PHE I  27      -7.060  -3.551  34.720  1.00 55.19           C  
ANISOU 3966  CZ  PHE I  27     5271  10561   5136    303  -1131    140       C  
ATOM   3967  N   THR I  28     -12.500  -3.760  33.185  1.00 66.79           N  
ANISOU 3967  N   THR I  28     5535  13675   6167     11  -1789    512       N  
ATOM   3968  CA  THR I  28     -12.902  -2.388  33.397  1.00 67.93           C  
ANISOU 3968  CA  THR I  28     5497  13802   6512    315  -1737   1017       C  
ATOM   3969  C   THR I  28     -12.027  -1.676  34.453  1.00 64.56           C  
ANISOU 3969  C   THR I  28     5324  12757   6447    526  -1482   1094       C  
ATOM   3970  O   THR I  28     -12.089  -1.940  35.646  1.00 62.39           O  
ANISOU 3970  O   THR I  28     5179  12074   6454    496  -1359    925       O  
ATOM   3971  CB  THR I  28     -14.437  -2.256  33.518  1.00 70.90           C  
ANISOU 3971  CB  THR I  28     5503  14460   6977    308  -1855   1208       C  
ATOM   3972  OG1 THR I  28     -14.777  -1.340  34.555  1.00 69.34           O  
ANISOU 3972  OG1 THR I  28     5260  13874   7211    550  -1670   1474       O  
ATOM   3973  CG2 THR I  28     -15.058  -3.608  33.793  1.00 71.79           C  
ANISOU 3973  CG2 THR I  28     5605  14626   7044    -19  -1948    771       C  
ATOM   3974  N   PHE I  29     -11.191  -0.779  33.960  1.00 64.59           N  
ANISOU 3974  N   PHE I  29     5388  12739   6414    719  -1406   1348       N  
ATOM   3975  CA  PHE I  29     -10.018  -0.281  34.668  1.00 61.33           C  
ANISOU 3975  CA  PHE I  29     5256  11811   6235    846  -1188   1325       C  
ATOM   3976  C   PHE I  29     -10.325   0.379  36.004  1.00 59.96           C  
ANISOU 3976  C   PHE I  29     5099  11192   6492    975   -997   1403       C  
ATOM   3977  O   PHE I  29      -9.583   0.172  36.992  1.00 57.29           O  
ANISOU 3977  O   PHE I  29     5018  10430   6319    931   -859   1171       O  
ATOM   3978  CB  PHE I  29      -9.250   0.685  33.739  1.00 62.68           C  
ANISOU 3978  CB  PHE I  29     5412  12108   6296   1035  -1144   1652       C  
ATOM   3979  CG  PHE I  29      -7.934   1.172  34.285  1.00 59.32           C  
ANISOU 3979  CG  PHE I  29     5259  11207   6073   1134   -935   1610       C  
ATOM   3980  CD1 PHE I  29      -6.862   0.306  34.442  1.00 56.97           C  
ANISOU 3980  CD1 PHE I  29     5241  10729   5676    981   -915   1244       C  
ATOM   3981  CD2 PHE I  29      -7.756   2.512  34.593  1.00 59.15           C  
ANISOU 3981  CD2 PHE I  29     5188  10925   6360   1375   -747   1945       C  
ATOM   3982  CE1 PHE I  29      -5.658   0.758  34.934  1.00 54.85           C  
ANISOU 3982  CE1 PHE I  29     5186  10069   5587   1061   -742   1222       C  
ATOM   3983  CE2 PHE I  29      -6.546   2.970  35.094  1.00 56.71           C  
ANISOU 3983  CE2 PHE I  29     5111  10202   6237   1432   -558   1879       C  
ATOM   3984  CZ  PHE I  29      -5.497   2.093  35.251  1.00 54.65           C  
ANISOU 3984  CZ  PHE I  29     5112   9812   5839   1272   -573   1527       C  
ATOM   3985  N   SER I  30     -11.401   1.165  36.051  1.00 60.90           N  
ANISOU 3985  N   SER I  30     4931  11419   6787   1127   -979   1728       N  
ATOM   3986  CA  SER I  30     -11.677   1.943  37.240  1.00 59.59           C  
ANISOU 3986  CA  SER I  30     4767  10831   7042   1264   -747   1805       C  
ATOM   3987  C   SER I  30     -12.512   1.161  38.239  1.00 59.20           C  
ANISOU 3987  C   SER I  30     4708  10686   7099   1104   -752   1547       C  
ATOM   3988  O   SER I  30     -13.102   1.725  39.168  1.00 58.84           O  
ANISOU 3988  O   SER I  30     4587  10398   7371   1195   -575   1614       O  
ATOM   3989  CB  SER I  30     -12.337   3.250  36.878  1.00 62.82           C  
ANISOU 3989  CB  SER I  30     4876  11315   7679   1536   -654   2294       C  
ATOM   3990  OG  SER I  30     -13.525   3.009  36.160  1.00 66.27           O  
ANISOU 3990  OG  SER I  30     4973  12240   7968   1522   -860   2499       O  
ATOM   3991  N   ASN I  31     -12.537  -0.152  38.063  1.00 58.50           N  
ANISOU 3991  N   ASN I  31     4698  10767   6762    856   -924   1237       N  
ATOM   3992  CA  ASN I  31     -13.171  -1.019  39.026  1.00 57.64           C  
ANISOU 3992  CA  ASN I  31     4614  10532   6755    682   -913    979       C  
ATOM   3993  C   ASN I  31     -12.151  -1.643  40.002  1.00 55.60           C  
ANISOU 3993  C   ASN I  31     4702   9879   6545    564   -801    666       C  
ATOM   3994  O   ASN I  31     -12.540  -2.216  41.030  1.00 54.98           O  
ANISOU 3994  O   ASN I  31     4674   9625   6592    448   -736    497       O  
ATOM   3995  CB  ASN I  31     -13.958  -2.115  38.311  1.00 59.73           C  
ANISOU 3995  CB  ASN I  31     4712  11202   6782    462  -1146    834       C  
ATOM   3996  CG  ASN I  31     -15.351  -1.664  37.867  1.00 63.56           C  
ANISOU 3996  CG  ASN I  31     4792  12059   7300    532  -1249   1123       C  
ATOM   3997  OD1 ASN I  31     -16.070  -2.428  37.238  1.00 65.71           O  
ANISOU 3997  OD1 ASN I  31     4878  12719   7372    346  -1450   1027       O  
ATOM   3998  ND2 ASN I  31     -15.735  -0.439  38.205  1.00 64.26           N  
ANISOU 3998  ND2 ASN I  31     4728  12025   7663    791  -1098   1467       N  
ATOM   3999  N   TYR I  32     -10.853  -1.545  39.697  1.00 53.75           N  
ANISOU 3999  N   TYR I  32     4686   9526   6211    595   -775    616       N  
ATOM   4000  CA  TYR I  32      -9.832  -2.263  40.479  1.00 50.75           C  
ANISOU 4000  CA  TYR I  32     4596   8839   5847    475   -707    350       C  
ATOM   4001  C   TYR I  32      -8.708  -1.365  41.048  1.00 49.22           C  
ANISOU 4001  C   TYR I  32     4585   8336   5781    604   -538    409       C  
ATOM   4002  O   TYR I  32      -8.309  -0.397  40.425  1.00 50.45           O  
ANISOU 4002  O   TYR I  32     4705   8521   5944    763   -496    607       O  
ATOM   4003  CB  TYR I  32      -9.192  -3.333  39.616  1.00 49.54           C  
ANISOU 4003  CB  TYR I  32     4545   8822   5455    328   -837    147       C  
ATOM   4004  CG  TYR I  32     -10.084  -4.463  39.180  1.00 51.42           C  
ANISOU 4004  CG  TYR I  32     4656   9307   5576    123   -980    -33       C  
ATOM   4005  CD1 TYR I  32     -10.852  -4.361  38.034  1.00 54.81           C  
ANISOU 4005  CD1 TYR I  32     4850  10171   5805    104  -1136     56       C  
ATOM   4006  CD2 TYR I  32     -10.089  -5.672  39.858  1.00 50.47           C  
ANISOU 4006  CD2 TYR I  32     4642   8999   5535    -69   -956   -294       C  
ATOM   4007  CE1 TYR I  32     -11.630  -5.417  37.589  1.00 56.33           C  
ANISOU 4007  CE1 TYR I  32     4916  10615   5872   -127  -1270   -159       C  
ATOM   4008  CE2 TYR I  32     -10.835  -6.731  39.423  1.00 52.66           C  
ANISOU 4008  CE2 TYR I  32     4806   9463   5738   -281  -1059   -495       C  
ATOM   4009  CZ  TYR I  32     -11.620  -6.599  38.290  1.00 55.65           C  
ANISOU 4009  CZ  TYR I  32     4951  10284   5909   -325  -1219   -454       C  
ATOM   4010  OH  TYR I  32     -12.386  -7.646  37.846  1.00 57.57           O  
ANISOU 4010  OH  TYR I  32     5064  10742   6069   -576  -1323   -697       O  
ATOM   4011  N   THR I  33      -8.169  -1.679  42.218  1.00 46.98           N  
ANISOU 4011  N   THR I  33     4483   7776   5592    523   -438    247       N  
ATOM   4012  CA  THR I  33      -6.946  -0.981  42.609  1.00 46.43           C  
ANISOU 4012  CA  THR I  33     4582   7474   5587    593   -316    257       C  
ATOM   4013  C   THR I  33      -5.739  -1.575  41.881  1.00 45.92           C  
ANISOU 4013  C   THR I  33     4660   7429   5360    554   -400    176       C  
ATOM   4014  O   THR I  33      -5.694  -2.781  41.636  1.00 46.37           O  
ANISOU 4014  O   THR I  33     4760   7555   5305    422   -502     21       O  
ATOM   4015  CB  THR I  33      -6.667  -0.990  44.120  1.00 44.72           C  
ANISOU 4015  CB  THR I  33     4493   7013   5487    511   -185    129       C  
ATOM   4016  OG1 THR I  33      -6.893  -2.278  44.638  1.00 46.66           O  
ANISOU 4016  OG1 THR I  33     4786   7272   5669    346   -260    -17       O  
ATOM   4017  CG2 THR I  33      -7.580  -0.141  44.831  1.00 44.83           C  
ANISOU 4017  CG2 THR I  33     4393   6962   5678    570    -34    189       C  
ATOM   4018  N   LEU I  34      -4.780  -0.728  41.513  1.00 44.60           N  
ANISOU 4018  N   LEU I  34     4554   7183   5210    667   -330    277       N  
ATOM   4019  CA  LEU I  34      -3.582  -1.216  40.855  1.00 44.11           C  
ANISOU 4019  CA  LEU I  34     4618   7125   5016    642   -378    208       C  
ATOM   4020  C   LEU I  34      -2.362  -1.028  41.750  1.00 42.74           C  
ANISOU 4020  C   LEU I  34     4606   6688   4944    620   -280    141       C  
ATOM   4021  O   LEU I  34      -2.338  -0.136  42.605  1.00 42.40           O  
ANISOU 4021  O   LEU I  34     4568   6489   5052    651   -158    176       O  
ATOM   4022  CB  LEU I  34      -3.384  -0.512  39.511  1.00 45.71           C  
ANISOU 4022  CB  LEU I  34     4740   7517   5112    775   -395    398       C  
ATOM   4023  CG  LEU I  34      -4.283  -0.992  38.366  1.00 48.22           C  
ANISOU 4023  CG  LEU I  34     4904   8205   5212    749   -545    434       C  
ATOM   4024  CD1 LEU I  34      -4.006  -2.423  38.016  1.00 47.03           C  
ANISOU 4024  CD1 LEU I  34     4842   8136   4893    571   -641    160       C  
ATOM   4025  CD2 LEU I  34      -5.722  -0.864  38.735  1.00 49.38           C  
ANISOU 4025  CD2 LEU I  34     4870   8453   5439    749   -581    506       C  
ATOM   4026  N   ASN I  35      -1.351  -1.872  41.572  1.00 41.38           N  
ANISOU 4026  N   ASN I  35     4549   6475   4700    553   -322     32       N  
ATOM   4027  CA  ASN I  35      -0.119  -1.672  42.328  1.00 40.02           C  
ANISOU 4027  CA  ASN I  35     4490   6105   4611    535   -251      4       C  
ATOM   4028  C   ASN I  35       1.102  -1.662  41.476  1.00 39.97           C  
ANISOU 4028  C   ASN I  35     4540   6091   4555    586   -242     27       C  
ATOM   4029  O   ASN I  35       1.120  -2.223  40.386  1.00 40.53           O  
ANISOU 4029  O   ASN I  35     4600   6300   4500    597   -294      0       O  
ATOM   4030  CB  ASN I  35       0.082  -2.760  43.377  1.00 39.25           C  
ANISOU 4030  CB  ASN I  35     4461   5916   4537    400   -285   -111       C  
ATOM   4031  CG  ASN I  35      -1.044  -2.833  44.340  1.00 38.73           C  
ANISOU 4031  CG  ASN I  35     4348   5858   4511    332   -275   -135       C  
ATOM   4032  OD1 ASN I  35      -0.893  -2.518  45.528  1.00 38.21           O  
ANISOU 4032  OD1 ASN I  35     4314   5713   4493    274   -214   -149       O  
ATOM   4033  ND2 ASN I  35      -2.204  -3.211  43.838  1.00 38.89           N  
ANISOU 4033  ND2 ASN I  35     4277   6004   4497    324   -329   -148       N  
ATOM   4034  N   TRP I  36       2.143  -1.054  42.013  1.00 38.97           N  
ANISOU 4034  N   TRP I  36     4468   5816   4523    595   -166     53       N  
ATOM   4035  CA  TRP I  36       3.489  -1.307  41.543  1.00 38.50           C  
ANISOU 4035  CA  TRP I  36     4466   5710   4453    610   -153     49       C  
ATOM   4036  C   TRP I  36       4.181  -2.229  42.526  1.00 37.73           C  
ANISOU 4036  C   TRP I  36     4421   5510   4406    505   -188    -30       C  
ATOM   4037  O   TRP I  36       4.149  -2.026  43.743  1.00 38.60           O  
ANISOU 4037  O   TRP I  36     4535   5563   4568    429   -183    -43       O  
ATOM   4038  CB  TRP I  36       4.264  -0.014  41.440  1.00 38.75           C  
ANISOU 4038  CB  TRP I  36     4490   5656   4578    682    -45    153       C  
ATOM   4039  CG  TRP I  36       3.780   0.829  40.364  1.00 40.53           C  
ANISOU 4039  CG  TRP I  36     4647   5978   4776    810      4    302       C  
ATOM   4040  CD1 TRP I  36       2.958   1.898  40.471  1.00 41.04           C  
ANISOU 4040  CD1 TRP I  36     4632   6019   4944    881     82    418       C  
ATOM   4041  CD2 TRP I  36       4.078   0.678  38.975  1.00 41.58           C  
ANISOU 4041  CD2 TRP I  36     4764   6268   4767    888     -7    382       C  
ATOM   4042  NE1 TRP I  36       2.710   2.425  39.223  1.00 43.02           N  
ANISOU 4042  NE1 TRP I  36     4800   6412   5132   1015    103    617       N  
ATOM   4043  CE2 TRP I  36       3.394   1.687  38.291  1.00 42.39           C  
ANISOU 4043  CE2 TRP I  36     4766   6472   4870   1009     41    589       C  
ATOM   4044  CE3 TRP I  36       4.843  -0.228  38.243  1.00 41.33           C  
ANISOU 4044  CE3 TRP I  36     4784   6310   4611    865    -36    300       C  
ATOM   4045  CZ2 TRP I  36       3.462   1.821  36.928  1.00 43.90           C  
ANISOU 4045  CZ2 TRP I  36     4905   6883   4892   1097     37    737       C  
ATOM   4046  CZ3 TRP I  36       4.903  -0.082  36.889  1.00 42.14           C  
ANISOU 4046  CZ3 TRP I  36     4851   6614   4545    940    -19    392       C  
ATOM   4047  CH2 TRP I  36       4.216   0.929  36.249  1.00 43.66           C  
ANISOU 4047  CH2 TRP I  36     4943   6955   4692   1049      4    617       C  
ATOM   4048  N   VAL I  37       4.756  -3.287  42.001  1.00 37.79           N  
ANISOU 4048  N   VAL I  37     4455   5509   4396    497   -212    -79       N  
ATOM   4049  CA  VAL I  37       5.687  -4.092  42.766  1.00 38.04           C  
ANISOU 4049  CA  VAL I  37     4504   5428   4520    440   -223    -79       C  
ATOM   4050  C   VAL I  37       7.019  -4.107  41.991  1.00 39.21           C  
ANISOU 4050  C   VAL I  37     4659   5531   4709    508   -165    -52       C  
ATOM   4051  O   VAL I  37       7.016  -4.052  40.739  1.00 39.82           O  
ANISOU 4051  O   VAL I  37     4746   5677   4707    573   -123    -87       O  
ATOM   4052  CB  VAL I  37       5.169  -5.505  42.944  1.00 37.73           C  
ANISOU 4052  CB  VAL I  37     4466   5354   4515    375   -258   -149       C  
ATOM   4053  CG1 VAL I  37       6.175  -6.326  43.742  1.00 38.13           C  
ANISOU 4053  CG1 VAL I  37     4504   5283   4702    344   -255    -73       C  
ATOM   4054  CG2 VAL I  37       3.854  -5.471  43.623  1.00 37.73           C  
ANISOU 4054  CG2 VAL I  37     4448   5410   4478    308   -301   -168       C  
ATOM   4055  N   ARG I  38       8.147  -4.144  42.702  1.00 38.66           N  
ANISOU 4055  N   ARG I  38     4566   5381   4741    487   -161     20       N  
ATOM   4056  CA  ARG I  38       9.437  -4.196  42.018  1.00 38.42           C  
ANISOU 4056  CA  ARG I  38     4518   5300   4780    554    -94     56       C  
ATOM   4057  C   ARG I  38      10.338  -5.304  42.507  1.00 38.82           C  
ANISOU 4057  C   ARG I  38     4519   5250   4980    541    -96    112       C  
ATOM   4058  O   ARG I  38      10.135  -5.900  43.552  1.00 38.78           O  
ANISOU 4058  O   ARG I  38     4484   5227   5025    476   -162    171       O  
ATOM   4059  CB  ARG I  38      10.165  -2.888  42.142  1.00 38.22           C  
ANISOU 4059  CB  ARG I  38     4467   5281   4776    565    -58    128       C  
ATOM   4060  CG  ARG I  38      10.743  -2.694  43.507  1.00 37.92           C  
ANISOU 4060  CG  ARG I  38     4373   5235   4799    463   -117    182       C  
ATOM   4061  CD  ARG I  38      11.213  -1.270  43.705  1.00 37.81           C  
ANISOU 4061  CD  ARG I  38     4333   5221   4811    428    -65    187       C  
ATOM   4062  NE  ARG I  38      11.649  -1.079  45.081  1.00 38.87           N  
ANISOU 4062  NE  ARG I  38     4408   5410   4950    281   -132    188       N  
ATOM   4063  CZ  ARG I  38      12.258   0.003  45.550  1.00 38.94           C  
ANISOU 4063  CZ  ARG I  38     4370   5427   4998    185    -93    151       C  
ATOM   4064  NH1 ARG I  38      12.517   1.012  44.748  1.00 38.81           N  
ANISOU 4064  NH1 ARG I  38     4360   5318   5068    244     30    142       N  
ATOM   4065  NH2 ARG I  38      12.623   0.059  46.827  1.00 39.36           N  
ANISOU 4065  NH2 ARG I  38     4358   5598   5001     17   -173    127       N  
ATOM   4066  N   GLN I  39      11.356  -5.575  41.720  1.00 39.87           N  
ANISOU 4066  N   GLN I  39     4629   5322   5199    615     -7    121       N  
ATOM   4067  CA  GLN I  39      12.309  -6.637  42.041  1.00 41.25           C  
ANISOU 4067  CA  GLN I  39     4725   5373   5577    638     28    206       C  
ATOM   4068  C   GLN I  39      13.744  -6.360  41.543  1.00 41.41           C  
ANISOU 4068  C   GLN I  39     4674   5354   5707    713    117    280       C  
ATOM   4069  O   GLN I  39      13.989  -6.340  40.345  1.00 42.33           O  
ANISOU 4069  O   GLN I  39     4828   5457   5800    780    240    184       O  
ATOM   4070  CB  GLN I  39      11.800  -7.935  41.445  1.00 42.29           C  
ANISOU 4070  CB  GLN I  39     4891   5391   5785    652    111     77       C  
ATOM   4071  CG  GLN I  39      12.664  -9.139  41.720  1.00 43.36           C  
ANISOU 4071  CG  GLN I  39     4934   5337   6204    696    196    174       C  
ATOM   4072  CD  GLN I  39      12.092 -10.366  41.073  1.00 44.51           C  
ANISOU 4072  CD  GLN I  39     5121   5329   6461    686    324    -12       C  
ATOM   4073  OE1 GLN I  39      11.932 -11.391  41.714  1.00 45.70           O  
ANISOU 4073  OE1 GLN I  39     5220   5322   6822    670    349     62       O  
ATOM   4074  NE2 GLN I  39      11.760 -10.257  39.788  1.00 45.44           N  
ANISOU 4074  NE2 GLN I  39     5323   5508   6432    682    415   -257       N  
ATOM   4075  N   ALA I  40      14.673  -6.132  42.464  1.00 41.21           N  
ANISOU 4075  N   ALA I  40     4532   5346   5782    687     54    451       N  
ATOM   4076  CA  ALA I  40      16.090  -5.941  42.103  1.00 42.33           C  
ANISOU 4076  CA  ALA I  40     4566   5454   6065    749    132    545       C  
ATOM   4077  C   ALA I  40      16.737  -7.222  41.547  1.00 44.18           C  
ANISOU 4077  C   ALA I  40     4737   5520   6531    856    274    569       C  
ATOM   4078  O   ALA I  40      16.463  -8.333  42.029  1.00 44.84           O  
ANISOU 4078  O   ALA I  40     4786   5500   6750    863    270    622       O  
ATOM   4079  CB  ALA I  40      16.866  -5.453  43.312  1.00 42.74           C  
ANISOU 4079  CB  ALA I  40     4475   5611   6154    664      5    719       C  
ATOM   4080  N   PRO I  41      17.632  -7.078  40.551  1.00 45.44           N  
ANISOU 4080  N   PRO I  41     4867   5630   6768    941    428    539       N  
ATOM   4081  CA  PRO I  41      18.250  -8.281  39.973  1.00 47.41           C  
ANISOU 4081  CA  PRO I  41     5054   5691   7269   1044    615    523       C  
ATOM   4082  C   PRO I  41      18.546  -9.327  41.037  1.00 48.88           C  
ANISOU 4082  C   PRO I  41     5093   5759   7721   1064    570    734       C  
ATOM   4083  O   PRO I  41      19.180  -9.019  42.034  1.00 49.47           O  
ANISOU 4083  O   PRO I  41     5018   5932   7848   1038    430    977       O  
ATOM   4084  CB  PRO I  41      19.546  -7.740  39.385  1.00 47.78           C  
ANISOU 4084  CB  PRO I  41     5001   5745   7407   1114    731    591       C  
ATOM   4085  CG  PRO I  41      19.184  -6.283  38.988  1.00 45.67           C  
ANISOU 4085  CG  PRO I  41     4839   5655   6857   1055    673    522       C  
ATOM   4086  CD  PRO I  41      18.194  -5.821  39.999  1.00 44.54           C  
ANISOU 4086  CD  PRO I  41     4754   5612   6559    945    464    538       C  
ATOM   4087  N   GLY I  42      18.039 -10.539  40.868  1.00 50.05           N  
ANISOU 4087  N   GLY I  42     5272   5717   8027   1093    682    652       N  
ATOM   4088  CA  GLY I  42      18.421 -11.630  41.764  1.00 51.59           C  
ANISOU 4088  CA  GLY I  42     5299   5753   8550   1146    693    908       C  
ATOM   4089  C   GLY I  42      17.896 -11.551  43.187  1.00 50.62           C  
ANISOU 4089  C   GLY I  42     5128   5776   8329   1057    454   1132       C  
ATOM   4090  O   GLY I  42      18.232 -12.390  44.030  1.00 51.61           O  
ANISOU 4090  O   GLY I  42     5087   5823   8699   1102    438   1421       O  
ATOM   4091  N   LYS I  43      17.068 -10.554  43.471  1.00 48.44           N  
ANISOU 4091  N   LYS I  43     4983   5718   7706    935    284   1020       N  
ATOM   4092  CA  LYS I  43      16.523 -10.418  44.810  1.00 47.82           C  
ANISOU 4092  CA  LYS I  43     4870   5807   7493    829     81   1188       C  
ATOM   4093  C   LYS I  43      15.038 -10.729  44.791  1.00 47.20           C  
ANISOU 4093  C   LYS I  43     4956   5690   7290    760     74   1005       C  
ATOM   4094  O   LYS I  43      14.550 -11.257  43.793  1.00 47.96           O  
ANISOU 4094  O   LYS I  43     5154   5617   7452    794    225    778       O  
ATOM   4095  CB  LYS I  43      16.802  -9.034  45.376  1.00 46.78           C  
ANISOU 4095  CB  LYS I  43     4721   5950   7102    723    -89   1211       C  
ATOM   4096  CG  LYS I  43      18.295  -8.729  45.533  1.00 48.42           C  
ANISOU 4096  CG  LYS I  43     4728   6232   7437    757   -107   1408       C  
ATOM   4097  CD  LYS I  43      18.939  -9.634  46.589  1.00 52.30           C  
ANISOU 4097  CD  LYS I  43     4982   6772   8118    783   -187   1781       C  
ATOM   4098  CE  LYS I  43      20.486  -9.628  46.522  1.00 54.84           C  
ANISOU 4098  CE  LYS I  43     5057   7121   8657    861   -165   2006       C  
ATOM   4099  NZ  LYS I  43      20.980  -8.225  46.294  1.00 54.66           N  
ANISOU 4099  NZ  LYS I  43     5052   7272   8445    761   -223   1854       N  
ATOM   4100  N   GLY I  44      14.335 -10.402  45.881  1.00 45.82           N  
ANISOU 4100  N   GLY I  44     4792   5692   6926    647    -91   1087       N  
ATOM   4101  CA  GLY I  44      12.932 -10.750  46.056  1.00 44.16           C  
ANISOU 4101  CA  GLY I  44     4698   5457   6623    576   -104    964       C  
ATOM   4102  C   GLY I  44      11.937  -9.709  45.582  1.00 42.47           C  
ANISOU 4102  C   GLY I  44     4646   5365   6127    508   -145    696       C  
ATOM   4103  O   GLY I  44      12.314  -8.689  45.013  1.00 41.64           O  
ANISOU 4103  O   GLY I  44     4578   5338   5905    524   -145    599       O  
ATOM   4104  N   LEU I  45      10.653  -9.982  45.784  1.00 41.66           N  
ANISOU 4104  N   LEU I  45     4621   5265   5945    439   -166    599       N  
ATOM   4105  CA  LEU I  45       9.626  -9.019  45.447  1.00 40.77           C  
ANISOU 4105  CA  LEU I  45     4621   5277   5592    386   -208    399       C  
ATOM   4106  C   LEU I  45       9.474  -7.941  46.554  1.00 41.15           C  
ANISOU 4106  C   LEU I  45     4659   5527   5450    295   -324    469       C  
ATOM   4107  O   LEU I  45       9.539  -8.241  47.772  1.00 41.77           O  
ANISOU 4107  O   LEU I  45     4666   5690   5513    222   -397    639       O  
ATOM   4108  CB  LEU I  45       8.303  -9.737  45.207  1.00 41.20           C  
ANISOU 4108  CB  LEU I  45     4734   5268   5652    340   -178    261       C  
ATOM   4109  CG  LEU I  45       8.278 -10.780  44.087  1.00 43.05           C  
ANISOU 4109  CG  LEU I  45     4988   5316   6052    377    -40    101       C  
ATOM   4110  CD1 LEU I  45       6.899 -11.435  44.058  1.00 42.18           C  
ANISOU 4110  CD1 LEU I  45     4910   5175   5940    284    -32    -39       C  
ATOM   4111  CD2 LEU I  45       8.680 -10.215  42.695  1.00 41.94           C  
ANISOU 4111  CD2 LEU I  45     4902   5222   5812    438     26    -79       C  
ATOM   4112  N   GLU I  46       9.299  -6.682  46.150  1.00 39.87           N  
ANISOU 4112  N   GLU I  46     4555   5449   5146    291   -325    343       N  
ATOM   4113  CA  GLU I  46       9.060  -5.604  47.127  1.00 39.50           C  
ANISOU 4113  CA  GLU I  46     4506   5554   4949    188   -382    337       C  
ATOM   4114  C   GLU I  46       7.886  -4.741  46.711  1.00 38.70           C  
ANISOU 4114  C   GLU I  46     4485   5472   4748    189   -344    179       C  
ATOM   4115  O   GLU I  46       7.940  -4.075  45.692  1.00 39.19           O  
ANISOU 4115  O   GLU I  46     4578   5500   4812    269   -286    113       O  
ATOM   4116  CB  GLU I  46      10.296  -4.719  47.278  1.00 39.51           C  
ANISOU 4116  CB  GLU I  46     4449   5613   4951    168   -390    376       C  
ATOM   4117  CG  GLU I  46      10.238  -3.729  48.403  1.00 39.85           C  
ANISOU 4117  CG  GLU I  46     4471   5812   4858     17   -430    332       C  
ATOM   4118  CD  GLU I  46      11.430  -2.784  48.388  1.00 41.15           C  
ANISOU 4118  CD  GLU I  46     4572   6014   5048    -25   -418    321       C  
ATOM   4119  OE1 GLU I  46      12.214  -2.850  47.427  1.00 40.56           O  
ANISOU 4119  OE1 GLU I  46     4478   5837   5098     86   -372    364       O  
ATOM   4120  OE2 GLU I  46      11.574  -1.954  49.325  1.00 43.57           O  
ANISOU 4120  OE2 GLU I  46     4845   6457   5251   -186   -437    245       O  
ATOM   4121  N   TRP I  47       6.821  -4.762  47.492  1.00 38.23           N  
ANISOU 4121  N   TRP I  47     4440   5477   4610    110   -366    148       N  
ATOM   4122  CA  TRP I  47       5.704  -3.876  47.246  1.00 37.49           C  
ANISOU 4122  CA  TRP I  47     4385   5405   4455    117   -318     30       C  
ATOM   4123  C   TRP I  47       6.129  -2.432  47.277  1.00 38.49           C  
ANISOU 4123  C   TRP I  47     4512   5538   4575    111   -253    -21       C  
ATOM   4124  O   TRP I  47       6.880  -2.034  48.170  1.00 39.74           O  
ANISOU 4124  O   TRP I  47     4641   5752   4705      8   -264    -18       O  
ATOM   4125  CB  TRP I  47       4.666  -4.038  48.314  1.00 37.63           C  
ANISOU 4125  CB  TRP I  47     4397   5497   4402     15   -328     12       C  
ATOM   4126  CG  TRP I  47       3.534  -3.167  48.088  1.00 38.10           C  
ANISOU 4126  CG  TRP I  47     4468   5564   4444     38   -261    -87       C  
ATOM   4127  CD1 TRP I  47       2.595  -3.291  47.122  1.00 37.96           C  
ANISOU 4127  CD1 TRP I  47     4444   5529   4450    123   -254   -115       C  
ATOM   4128  CD2 TRP I  47       3.184  -2.022  48.846  1.00 38.73           C  
ANISOU 4128  CD2 TRP I  47     4544   5678   4493    -27   -176   -169       C  
ATOM   4129  NE1 TRP I  47       1.669  -2.291  47.233  1.00 38.42           N  
ANISOU 4129  NE1 TRP I  47     4477   5607   4515    140   -178   -161       N  
ATOM   4130  CE2 TRP I  47       2.003  -1.505  48.298  1.00 39.02           C  
ANISOU 4130  CE2 TRP I  47     4562   5684   4579     52   -108   -209       C  
ATOM   4131  CE3 TRP I  47       3.745  -1.387  49.948  1.00 39.64           C  
ANISOU 4131  CE3 TRP I  47     4656   5859   4545   -159   -140   -229       C  
ATOM   4132  CZ2 TRP I  47       1.390  -0.368  48.801  1.00 40.01           C  
ANISOU 4132  CZ2 TRP I  47     4668   5788   4746     30     25   -293       C  
ATOM   4133  CZ3 TRP I  47       3.134  -0.258  50.453  1.00 40.24           C  
ANISOU 4133  CZ3 TRP I  47     4731   5924   4633   -214     -3   -368       C  
ATOM   4134  CH2 TRP I  47       1.967   0.231  49.892  1.00 40.91           C  
ANISOU 4134  CH2 TRP I  47     4799   5924   4819   -108     93   -394       C  
ATOM   4135  N   VAL I  48       5.616  -1.643  46.332  1.00 38.23           N  
ANISOU 4135  N   VAL I  48     4494   5459   4572    209   -181    -58       N  
ATOM   4136  CA  VAL I  48       5.999  -0.241  46.221  1.00 38.46           C  
ANISOU 4136  CA  VAL I  48     4515   5435   4665    223    -77    -85       C  
ATOM   4137  C   VAL I  48       4.840   0.717  46.502  1.00 39.52           C  
ANISOU 4137  C   VAL I  48     4637   5542   4836    224     27   -148       C  
ATOM   4138  O   VAL I  48       4.964   1.607  47.332  1.00 39.83           O  
ANISOU 4138  O   VAL I  48     4668   5544   4920    128    123   -243       O  
ATOM   4139  CB  VAL I  48       6.521   0.089  44.825  1.00 38.00           C  
ANISOU 4139  CB  VAL I  48     4453   5325   4659    363    -33    -12       C  
ATOM   4140  CG1 VAL I  48       6.772   1.569  44.715  1.00 38.15           C  
ANISOU 4140  CG1 VAL I  48     4450   5252   4793    383    106    -10       C  
ATOM   4141  CG2 VAL I  48       7.771  -0.721  44.513  1.00 37.50           C  
ANISOU 4141  CG2 VAL I  48     4388   5259   4601    371    -88     36       C  
ATOM   4142  N   SER I  49       3.716   0.537  45.810  1.00 39.60           N  
ANISOU 4142  N   SER I  49     4630   5578   4840    322     22   -106       N  
ATOM   4143  CA  SER I  49       2.616   1.481  45.949  1.00 40.79           C  
ANISOU 4143  CA  SER I  49     4733   5690   5075    361    139   -119       C  
ATOM   4144  C   SER I  49       1.263   0.963  45.447  1.00 40.23           C  
ANISOU 4144  C   SER I  49     4610   5712   4963    430     83    -67       C  
ATOM   4145  O   SER I  49       1.229   0.086  44.593  1.00 40.72           O  
ANISOU 4145  O   SER I  49     4672   5866   4933    470    -30    -24       O  
ATOM   4146  CB  SER I  49       2.977   2.791  45.219  1.00 41.24           C  
ANISOU 4146  CB  SER I  49     4755   5629   5286    472    281    -41       C  
ATOM   4147  OG  SER I  49       1.924   3.752  45.268  1.00 42.26           O  
ANISOU 4147  OG  SER I  49     4810   5681   5565    543    429    -10       O  
ATOM   4148  N   TYR I  50       0.164   1.532  45.954  1.00 40.46           N  
ANISOU 4148  N   TYR I  50     4579   5722   5072    434    179    -88       N  
ATOM   4149  CA  TYR I  50      -1.172   1.215  45.442  1.00 40.90           C  
ANISOU 4149  CA  TYR I  50     4541   5883   5116    505    134    -16       C  
ATOM   4150  C   TYR I  50      -1.982   2.491  45.202  1.00 42.65           C  
ANISOU 4150  C   TYR I  50     4645   6038   5524    634    294     87       C  
ATOM   4151  O   TYR I  50      -1.641   3.527  45.784  1.00 44.09           O  
ANISOU 4151  O   TYR I  50     4840   6048   5865    626    475     34       O  
ATOM   4152  CB  TYR I  50      -1.921   0.292  46.402  1.00 40.53           C  
ANISOU 4152  CB  TYR I  50     4500   5898   5001    377     84   -115       C  
ATOM   4153  CG  TYR I  50      -2.658   1.001  47.504  1.00 41.34           C  
ANISOU 4153  CG  TYR I  50     4567   5940   5201    328    244   -191       C  
ATOM   4154  CD1 TYR I  50      -3.935   1.478  47.311  1.00 42.38           C  
ANISOU 4154  CD1 TYR I  50     4568   6083   5450    416    326   -129       C  
ATOM   4155  CD2 TYR I  50      -2.088   1.185  48.741  1.00 41.59           C  
ANISOU 4155  CD2 TYR I  50     4676   5928   5197    183    322   -330       C  
ATOM   4156  CE1 TYR I  50      -4.616   2.143  48.317  1.00 43.13           C  
ANISOU 4156  CE1 TYR I  50     4623   6101   5663    376    516   -220       C  
ATOM   4157  CE2 TYR I  50      -2.788   1.843  49.767  1.00 42.50           C  
ANISOU 4157  CE2 TYR I  50     4762   6006   5379    115    503   -448       C  
ATOM   4158  CZ  TYR I  50      -4.041   2.318  49.543  1.00 42.76           C  
ANISOU 4158  CZ  TYR I  50     4677   6005   5564    217    614   -401       C  
ATOM   4159  OH  TYR I  50      -4.724   2.980  50.550  1.00 44.78           O  
ANISOU 4159  OH  TYR I  50     4898   6200   5915    154    834   -538       O  
ATOM   4160  N   THR I  51      -2.977   2.435  44.298  1.00 42.58           N  
ANISOU 4160  N   THR I  51     4504   6165   5510    750    236    241       N  
ATOM   4161  CA  THR I  51      -4.040   3.453  44.185  1.00 44.27           C  
ANISOU 4161  CA  THR I  51     4552   6340   5928    884    380    388       C  
ATOM   4162  C   THR I  51      -5.321   2.695  44.165  1.00 44.38           C  
ANISOU 4162  C   THR I  51     4453   6539   5871    861    270    402       C  
ATOM   4163  O   THR I  51      -5.467   1.814  43.336  1.00 44.72           O  
ANISOU 4163  O   THR I  51     4470   6795   5726    843     78    436       O  
ATOM   4164  CB  THR I  51      -4.146   4.102  42.794  1.00 45.95           C  
ANISOU 4164  CB  THR I  51     4632   6648   6181   1078    370    676       C  
ATOM   4165  OG1 THR I  51      -3.104   3.639  41.931  1.00 46.73           O  
ANISOU 4165  OG1 THR I  51     4823   6846   6085   1069    242    694       O  
ATOM   4166  CG2 THR I  51      -4.236   5.624  42.865  1.00 47.51           C  
ANISOU 4166  CG2 THR I  51     4732   6612   6707   1227    632    832       C  
ATOM   4167  N   SER I  52      -6.298   3.095  44.971  1.00 46.29           N  
ANISOU 4167  N   SER I  52     4604   6708   6277    863    410    376       N  
ATOM   4168  CA  SER I  52      -7.647   2.507  44.878  1.00 47.21           C  
ANISOU 4168  CA  SER I  52     4561   7008   6369    858    322    428       C  
ATOM   4169  C   SER I  52      -8.302   2.735  43.517  1.00 49.48           C  
ANISOU 4169  C   SER I  52     4637   7517   6645   1015    214    702       C  
ATOM   4170  O   SER I  52      -7.857   3.571  42.706  1.00 50.40           O  
ANISOU 4170  O   SER I  52     4707   7620   6822   1166    258    904       O  
ATOM   4171  CB  SER I  52      -8.554   3.046  45.965  1.00 47.78           C  
ANISOU 4171  CB  SER I  52     4553   6949   6653    853    536    368       C  
ATOM   4172  OG  SER I  52      -8.393   4.434  45.977  1.00 49.46           O  
ANISOU 4172  OG  SER I  52     4714   6948   7132    995    775    458       O  
ATOM   4173  N   SER I  53      -9.369   1.981  43.277  1.00 50.43           N  
ANISOU 4173  N   SER I  53     4612   7870   6679    967     73    722       N  
ATOM   4174  CA  SER I  53     -10.122   2.087  42.035  1.00 52.66           C  
ANISOU 4174  CA  SER I  53     4654   8458   6897   1077    -67    978       C  
ATOM   4175  C   SER I  53     -10.389   3.536  41.592  1.00 54.54           C  
ANISOU 4175  C   SER I  53     4702   8638   7382   1327     93   1317       C  
ATOM   4176  O   SER I  53     -10.216   3.869  40.424  1.00 56.13           O  
ANISOU 4176  O   SER I  53     4798   9043   7486   1444      0   1569       O  
ATOM   4177  CB  SER I  53     -11.432   1.309  42.158  1.00 53.78           C  
ANISOU 4177  CB  SER I  53     4617   8812   7005    981   -179    943       C  
ATOM   4178  OG  SER I  53     -12.169   1.729  43.296  1.00 53.71           O  
ANISOU 4178  OG  SER I  53     4545   8609   7254   1000     22    913       O  
ATOM   4179  N   SER I  54     -10.786   4.399  42.516  1.00 54.77           N  
ANISOU 4179  N   SER I  54     4682   8387   7740   1408    355   1328       N  
ATOM   4180  CA  SER I  54     -11.049   5.779  42.140  1.00 57.78           C  
ANISOU 4180  CA  SER I  54     4868   8644   8441   1656    559   1659       C  
ATOM   4181  C   SER I  54      -9.790   6.622  42.144  1.00 57.36           C  
ANISOU 4181  C   SER I  54     4987   8299   8507   1714    733   1652       C  
ATOM   4182  O   SER I  54      -9.788   7.745  41.662  1.00 59.89           O  
ANISOU 4182  O   SER I  54     5165   8496   9095   1921    904   1952       O  
ATOM   4183  CB  SER I  54     -12.071   6.426  43.069  1.00 59.99           C  
ANISOU 4183  CB  SER I  54     4991   8712   9091   1731    824   1671       C  
ATOM   4184  OG  SER I  54     -11.433   7.300  43.977  1.00 59.61           O  
ANISOU 4184  OG  SER I  54     5095   8243   9311   1734   1144   1498       O  
ATOM   4185  N   GLY I  55      -8.722   6.101  42.724  1.00 54.42           N  
ANISOU 4185  N   GLY I  55     4901   7805   7970   1530    705   1327       N  
ATOM   4186  CA  GLY I  55      -7.516   6.885  42.850  1.00 54.54           C  
ANISOU 4186  CA  GLY I  55     5068   7542   8111   1550    876   1279       C  
ATOM   4187  C   GLY I  55      -7.483   7.882  43.997  1.00 54.98           C  
ANISOU 4187  C   GLY I  55     5158   7206   8524   1541   1224   1118       C  
ATOM   4188  O   GLY I  55      -6.500   8.618  44.170  1.00 54.58           O  
ANISOU 4188  O   GLY I  55     5218   6902   8617   1530   1395   1045       O  
ATOM   4189  N   SER I  56      -8.539   7.920  44.796  1.00 55.73           N  
ANISOU 4189  N   SER I  56     5155   7251   8770   1526   1350   1033       N  
ATOM   4190  CA  SER I  56      -8.555   8.850  45.925  1.00 57.22           C  
ANISOU 4190  CA  SER I  56     5377   7079   9285   1489   1716    819       C  
ATOM   4191  C   SER I  56      -7.708   8.363  47.117  1.00 55.43           C  
ANISOU 4191  C   SER I  56     5419   6796   8847   1208   1721    382       C  
ATOM   4192  O   SER I  56      -7.343   9.161  47.974  1.00 56.06           O  
ANISOU 4192  O   SER I  56     5570   6606   9125   1124   2006    148       O  
ATOM   4193  CB  SER I  56      -9.991   9.152  46.371  1.00 59.21           C  
ANISOU 4193  CB  SER I  56     5409   7286   9802   1581   1901    882       C  
ATOM   4194  OG  SER I  56     -10.547   8.024  47.025  1.00 57.86           O  
ANISOU 4194  OG  SER I  56     5290   7334   9362   1409   1737    685       O  
ATOM   4195  N   LEU I  57      -7.442   7.054  47.178  1.00 53.05           N  
ANISOU 4195  N   LEU I  57     5243   6758   8154   1057   1417    282       N  
ATOM   4196  CA  LEU I  57      -6.619   6.443  48.220  1.00 50.84           C  
ANISOU 4196  CA  LEU I  57     5185   6495   7636    807   1368    -41       C  
ATOM   4197  C   LEU I  57      -5.353   5.994  47.542  1.00 49.75           C  
ANISOU 4197  C   LEU I  57     5177   6434   7292    779   1154      0       C  
ATOM   4198  O   LEU I  57      -5.367   5.624  46.373  1.00 49.80           O  
ANISOU 4198  O   LEU I  57     5125   6585   7213    899    968    225       O  
ATOM   4199  CB  LEU I  57      -7.301   5.221  48.835  1.00 49.91           C  
ANISOU 4199  CB  LEU I  57     5087   6592   7283    672   1212   -138       C  
ATOM   4200  CG  LEU I  57      -8.218   5.348  50.052  1.00 50.55           C  
ANISOU 4200  CG  LEU I  57     5128   6633   7445    577   1422   -317       C  
ATOM   4201  CD1 LEU I  57      -8.538   6.768  50.337  1.00 52.72           C  
ANISOU 4201  CD1 LEU I  57     5310   6634   8087    670   1787   -365       C  
ATOM   4202  CD2 LEU I  57      -9.457   4.516  49.816  1.00 50.23           C  
ANISOU 4202  CD2 LEU I  57     4943   6784   7360    617   1290   -182       C  
ATOM   4203  N   THR I  58      -4.256   5.984  48.293  1.00 49.41           N  
ANISOU 4203  N   THR I  58     5299   6328   7147    604   1178   -226       N  
ATOM   4204  CA  THR I  58      -2.938   5.948  47.707  1.00 46.59           C  
ANISOU 4204  CA  THR I  58     5037   5963   6703    597   1068   -189       C  
ATOM   4205  C   THR I  58      -1.971   5.609  48.849  1.00 45.93           C  
ANISOU 4205  C   THR I  58     5103   5906   6444    355   1046   -455       C  
ATOM   4206  O   THR I  58      -2.142   6.096  49.953  1.00 47.77           O  
ANISOU 4206  O   THR I  58     5355   6070   6727    218   1230   -676       O  
ATOM   4207  CB  THR I  58      -2.652   7.341  47.146  1.00 48.33           C  
ANISOU 4207  CB  THR I  58     5185   5937   7241    738   1298    -78       C  
ATOM   4208  OG1 THR I  58      -2.457   7.287  45.721  1.00 47.29           O  
ANISOU 4208  OG1 THR I  58     4991   5889   7090    921   1167    224       O  
ATOM   4209  CG2 THR I  58      -1.495   8.046  47.914  1.00 48.83           C  
ANISOU 4209  CG2 THR I  58     5356   5815   7384    570   1464   -329       C  
ATOM   4210  N   GLY I  59      -0.993   4.744  48.591  1.00 44.38           N  
ANISOU 4210  N   GLY I  59     4995   5836   6033    297    825   -428       N  
ATOM   4211  CA  GLY I  59      -0.107   4.231  49.636  1.00 43.00           C  
ANISOU 4211  CA  GLY I  59     4922   5755   5661     80    751   -603       C  
ATOM   4212  C   GLY I  59       1.276   3.847  49.116  1.00 41.88           C  
ANISOU 4212  C   GLY I  59     4836   5648   5430     71    599   -536       C  
ATOM   4213  O   GLY I  59       1.431   3.422  47.963  1.00 40.01           O  
ANISOU 4213  O   GLY I  59     4587   5428   5186    214    484   -362       O  
ATOM   4214  N   TYR I  60       2.275   3.979  49.982  1.00 41.71           N  
ANISOU 4214  N   TYR I  60     4859   5664   5325   -111    603   -683       N  
ATOM   4215  CA  TYR I  60       3.661   3.794  49.597  1.00 41.28           C  
ANISOU 4215  CA  TYR I  60     4827   5627   5231   -128    495   -627       C  
ATOM   4216  C   TYR I  60       4.480   3.037  50.632  1.00 42.23           C  
ANISOU 4216  C   TYR I  60     4967   5945   5132   -325    353   -686       C  
ATOM   4217  O   TYR I  60       4.187   3.061  51.819  1.00 44.65           O  
ANISOU 4217  O   TYR I  60     5278   6375   5313   -500    387   -829       O  
ATOM   4218  CB  TYR I  60       4.309   5.150  49.432  1.00 42.75           C  
ANISOU 4218  CB  TYR I  60     4993   5629   5622   -146    685   -716       C  
ATOM   4219  CG  TYR I  60       3.663   6.027  48.408  1.00 43.03           C  
ANISOU 4219  CG  TYR I  60     4979   5459   5913     61    849   -593       C  
ATOM   4220  CD1 TYR I  60       4.013   5.921  47.087  1.00 42.35           C  
ANISOU 4220  CD1 TYR I  60     4875   5348   5869    243    783   -367       C  
ATOM   4221  CD2 TYR I  60       2.712   6.967  48.765  1.00 44.75           C  
ANISOU 4221  CD2 TYR I  60     5151   5520   6332     77   1086   -685       C  
ATOM   4222  CE1 TYR I  60       3.459   6.724  46.133  1.00 43.14           C  
ANISOU 4222  CE1 TYR I  60     4905   5311   6177    436    920   -193       C  
ATOM   4223  CE2 TYR I  60       2.130   7.783  47.814  1.00 45.61           C  
ANISOU 4223  CE2 TYR I  60     5179   5444   6708    291   1241   -501       C  
ATOM   4224  CZ  TYR I  60       2.509   7.652  46.496  1.00 45.31           C  
ANISOU 4224  CZ  TYR I  60     5115   5425   6677    470   1143   -235       C  
ATOM   4225  OH  TYR I  60       1.933   8.430  45.522  1.00 47.01           O  
ANISOU 4225  OH  TYR I  60     5225   5514   7122    689   1277     11       O  
ATOM   4226  N   ALA I  61       5.556   2.407  50.176  1.00 42.17           N  
ANISOU 4226  N   ALA I  61     4956   5984   5081   -295    205   -559       N  
ATOM   4227  CA  ALA I  61       6.458   1.672  51.067  1.00 41.82           C  
ANISOU 4227  CA  ALA I  61     4888   6140   4861   -453     58   -537       C  
ATOM   4228  C   ALA I  61       7.336   2.710  51.704  1.00 43.39           C  
ANISOU 4228  C   ALA I  61     5052   6371   5062   -635    139   -711       C  
ATOM   4229  O   ALA I  61       7.650   3.708  51.060  1.00 43.82           O  
ANISOU 4229  O   ALA I  61     5103   6239   5308   -585    274   -773       O  
ATOM   4230  CB  ALA I  61       7.288   0.713  50.277  1.00 40.46           C  
ANISOU 4230  CB  ALA I  61     4699   5965   4710   -335    -86   -337       C  
ATOM   4231  N   ASP I  62       7.744   2.511  52.951  1.00 45.28           N  
ANISOU 4231  N   ASP I  62     5252   6861   5091   -862     65   -788       N  
ATOM   4232  CA  ASP I  62       8.654   3.497  53.536  1.00 47.31           C  
ANISOU 4232  CA  ASP I  62     5458   7187   5333  -1079    133   -995       C  
ATOM   4233  C   ASP I  62       9.841   3.841  52.638  1.00 47.03           C  
ANISOU 4233  C   ASP I  62     5373   7018   5476  -1005    119   -918       C  
ATOM   4234  O   ASP I  62      10.286   4.975  52.615  1.00 49.21           O  
ANISOU 4234  O   ASP I  62     5628   7180   5890  -1107    270  -1106       O  
ATOM   4235  CB  ASP I  62       9.137   3.095  54.929  1.00 49.44           C  
ANISOU 4235  CB  ASP I  62     5655   7841   5287  -1349     -1  -1041       C  
ATOM   4236  CG  ASP I  62       8.081   3.294  55.977  1.00 51.41           C  
ANISOU 4236  CG  ASP I  62     5948   8226   5359  -1506    105  -1241       C  
ATOM   4237  OD1 ASP I  62       7.059   3.951  55.641  1.00 52.21           O  
ANISOU 4237  OD1 ASP I  62     6124   8077   5639  -1417    317  -1387       O  
ATOM   4238  OD2 ASP I  62       8.248   2.766  57.102  1.00 51.78           O  
ANISOU 4238  OD2 ASP I  62     5941   8639   5092  -1704    -16  -1220       O  
ATOM   4239  N   SER I  63      10.356   2.875  51.893  1.00 45.57           N  
ANISOU 4239  N   SER I  63     5167   6831   5315   -835    -32   -653       N  
ATOM   4240  CA  SER I  63      11.522   3.125  51.057  1.00 44.74           C  
ANISOU 4240  CA  SER I  63     5006   6624   5369   -765    -35   -568       C  
ATOM   4241  C   SER I  63      11.297   4.090  49.889  1.00 44.84           C  
ANISOU 4241  C   SER I  63     5070   6333   5634   -608    160   -599       C  
ATOM   4242  O   SER I  63      12.276   4.514  49.247  1.00 46.74           O  
ANISOU 4242  O   SER I  63     5260   6481   6018   -577    201   -552       O  
ATOM   4243  CB  SER I  63      12.093   1.817  50.521  1.00 43.87           C  
ANISOU 4243  CB  SER I  63     4857   6566   5248   -611   -202   -292       C  
ATOM   4244  OG  SER I  63      11.102   1.115  49.791  1.00 42.44           O  
ANISOU 4244  OG  SER I  63     4766   6264   5094   -413   -196   -196       O  
ATOM   4245  N   VAL I  64      10.048   4.428  49.581  1.00 42.70           N  
ANISOU 4245  N   VAL I  64     4876   5919   5428   -500    283   -638       N  
ATOM   4246  CA  VAL I  64       9.797   5.327  48.457  1.00 42.73           C  
ANISOU 4246  CA  VAL I  64     4898   5667   5671   -331    463   -592       C  
ATOM   4247  C   VAL I  64       8.883   6.522  48.746  1.00 44.84           C  
ANISOU 4247  C   VAL I  64     5179   5754   6105   -363    703   -758       C  
ATOM   4248  O   VAL I  64       8.795   7.447  47.920  1.00 45.65           O  
ANISOU 4248  O   VAL I  64     5263   5625   6456   -237    886   -694       O  
ATOM   4249  CB  VAL I  64       9.230   4.603  47.232  1.00 40.63           C  
ANISOU 4249  CB  VAL I  64     4671   5370   5396    -76    400   -369       C  
ATOM   4250  CG1 VAL I  64       9.997   3.358  46.946  1.00 38.76           C  
ANISOU 4250  CG1 VAL I  64     4424   5263   5039    -37    214   -237       C  
ATOM   4251  CG2 VAL I  64       7.748   4.320  47.422  1.00 40.86           C  
ANISOU 4251  CG2 VAL I  64     4740   5422   5363    -21    402   -383       C  
ATOM   4252  N   LYS I  65       8.197   6.486  49.892  1.00 45.40           N  
ANISOU 4252  N   LYS I  65     5268   5926   6055   -520    721   -947       N  
ATOM   4253  CA  LYS I  65       7.264   7.534  50.306  1.00 47.07           C  
ANISOU 4253  CA  LYS I  65     5485   5963   6438   -561    979  -1139       C  
ATOM   4254  C   LYS I  65       7.936   8.860  50.066  1.00 48.96           C  
ANISOU 4254  C   LYS I  65     5680   5949   6973   -617   1215  -1255       C  
ATOM   4255  O   LYS I  65       9.037   9.070  50.535  1.00 50.73           O  
ANISOU 4255  O   LYS I  65     5871   6248   7157   -823   1189  -1399       O  
ATOM   4256  CB  LYS I  65       6.954   7.407  51.807  1.00 48.66           C  
ANISOU 4256  CB  LYS I  65     5700   6364   6424   -824    982  -1408       C  
ATOM   4257  CG  LYS I  65       5.509   7.653  52.179  1.00 50.13           C  
ANISOU 4257  CG  LYS I  65     5908   6474   6666   -784   1147  -1502       C  
ATOM   4258  CD  LYS I  65       5.293   7.962  53.684  1.00 53.91           C  
ANISOU 4258  CD  LYS I  65     6396   7106   6982  -1087   1262  -1855       C  
ATOM   4259  CE  LYS I  65       5.381   6.703  54.583  1.00 54.39           C  
ANISOU 4259  CE  LYS I  65     6472   7571   6622  -1228    997  -1808       C  
ATOM   4260  NZ  LYS I  65       4.321   5.616  54.304  1.00 52.95           N  
ANISOU 4260  NZ  LYS I  65     6315   7450   6354  -1036    867  -1563       N  
ATOM   4261  N   GLY I  66       7.309   9.745  49.313  1.00 49.41           N  
ANISOU 4261  N   GLY I  66     5715   5711   7346   -435   1447  -1164       N  
ATOM   4262  CA  GLY I  66       7.812  11.110  49.187  1.00 51.74           C  
ANISOU 4262  CA  GLY I  66     5959   5701   8000   -497   1741  -1285       C  
ATOM   4263  C   GLY I  66       8.663  11.362  47.955  1.00 52.74           C  
ANISOU 4263  C   GLY I  66     6046   5702   8293   -336   1742  -1017       C  
ATOM   4264  O   GLY I  66       8.850  12.498  47.544  1.00 54.87           O  
ANISOU 4264  O   GLY I  66     6260   5663   8926   -300   2015  -1001       O  
ATOM   4265  N   ARG I  67       9.196  10.298  47.363  1.00 50.74           N  
ANISOU 4265  N   ARG I  67     5814   5675   7792   -243   1464   -805       N  
ATOM   4266  CA  ARG I  67      10.071  10.429  46.230  1.00 49.20           C  
ANISOU 4266  CA  ARG I  67     5583   5410   7702   -109   1463   -569       C  
ATOM   4267  C   ARG I  67       9.344   9.912  45.014  1.00 47.46           C  
ANISOU 4267  C   ARG I  67     5377   5243   7414    189   1381   -235       C  
ATOM   4268  O   ARG I  67       9.622  10.320  43.895  1.00 47.69           O  
ANISOU 4268  O   ARG I  67     5366   5175   7578    358   1467     11       O  
ATOM   4269  CB  ARG I  67      11.299   9.574  46.450  1.00 49.11           C  
ANISOU 4269  CB  ARG I  67     5566   5630   7465   -236   1230   -595       C  
ATOM   4270  CG  ARG I  67      12.202  10.000  47.580  1.00 50.97           C  
ANISOU 4270  CG  ARG I  67     5750   5908   7709   -556   1256   -897       C  
ATOM   4271  CD  ARG I  67      13.555   9.221  47.528  1.00 49.62           C  
ANISOU 4271  CD  ARG I  67     5520   5957   7378   -626   1033   -817       C  
ATOM   4272  NE  ARG I  67      13.348   7.783  47.662  1.00 47.55           N  
ANISOU 4272  NE  ARG I  67     5295   5962   6811   -552    760   -689       N  
ATOM   4273  CZ  ARG I  67      13.712   6.887  46.753  1.00 45.96           C  
ANISOU 4273  CZ  ARG I  67     5097   5821   6544   -362    631   -442       C  
ATOM   4274  NH1 ARG I  67      14.357   7.285  45.666  1.00 45.11           N  
ANISOU 4274  NH1 ARG I  67     4957   5574   6607   -235    733   -293       N  
ATOM   4275  NH2 ARG I  67      13.462   5.589  46.952  1.00 44.42           N  
ANISOU 4275  NH2 ARG I  67     4930   5820   6127   -311    424   -354       N  
ATOM   4276  N   PHE I  68       8.457   8.954  45.234  1.00 45.73           N  
ANISOU 4276  N   PHE I  68     5204   5215   6954    232   1205   -227       N  
ATOM   4277  CA  PHE I  68       7.680   8.391  44.156  1.00 45.17           C  
ANISOU 4277  CA  PHE I  68     5134   5248   6779    468   1109     37       C  
ATOM   4278  C   PHE I  68       6.228   8.854  44.330  1.00 47.29           C  
ANISOU 4278  C   PHE I  68     5367   5437   7165    555   1228     59       C  
ATOM   4279  O   PHE I  68       5.731   8.975  45.461  1.00 47.74           O  
ANISOU 4279  O   PHE I  68     5440   5460   7239    413   1286   -172       O  
ATOM   4280  CB  PHE I  68       7.675   6.867  44.249  1.00 43.41           C  
ANISOU 4280  CB  PHE I  68     4972   5291   6232    444    830     22       C  
ATOM   4281  CG  PHE I  68       8.934   6.197  43.824  1.00 41.74           C  
ANISOU 4281  CG  PHE I  68     4774   5172   5913    428    709     70       C  
ATOM   4282  CD1 PHE I  68      10.097   6.925  43.593  1.00 43.71           C  
ANISOU 4282  CD1 PHE I  68     4983   5303   6322    391    821     86       C  
ATOM   4283  CD2 PHE I  68       8.978   4.805  43.730  1.00 40.22           C  
ANISOU 4283  CD2 PHE I  68     4621   5165   5495    438    503     87       C  
ATOM   4284  CE1 PHE I  68      11.307   6.275  43.211  1.00 42.95           C  
ANISOU 4284  CE1 PHE I  68     4876   5295   6146    381    720    139       C  
ATOM   4285  CE2 PHE I  68      10.151   4.147  43.367  1.00 41.21           C  
ANISOU 4285  CE2 PHE I  68     4742   5350   5567    435    422    132       C  
ATOM   4286  CZ  PHE I  68      11.332   4.881  43.098  1.00 41.66           C  
ANISOU 4286  CZ  PHE I  68     4749   5311   5769    413    525    164       C  
ATOM   4287  N   THR I  69       5.527   9.050  43.219  1.00 47.81           N  
ANISOU 4287  N   THR I  69     5368   5514   7285    784   1256    349       N  
ATOM   4288  CA  THR I  69       4.109   9.380  43.255  1.00 48.22           C  
ANISOU 4288  CA  THR I  69     5345   5530   7446    899   1342    435       C  
ATOM   4289  C   THR I  69       3.387   8.459  42.295  1.00 47.24           C  
ANISOU 4289  C   THR I  69     5192   5692   7067   1048   1123    654       C  
ATOM   4290  O   THR I  69       3.734   8.397  41.113  1.00 47.43           O  
ANISOU 4290  O   THR I  69     5184   5827   7009   1176   1070    891       O  
ATOM   4291  CB  THR I  69       3.895  10.838  42.832  1.00 51.06           C  
ANISOU 4291  CB  THR I  69     5587   5598   8215   1040   1651    624       C  
ATOM   4292  OG1 THR I  69       4.698  11.681  43.666  1.00 52.01           O  
ANISOU 4292  OG1 THR I  69     5737   5441   8584    862   1872    368       O  
ATOM   4293  CG2 THR I  69       2.412  11.262  42.920  1.00 52.04           C  
ANISOU 4293  CG2 THR I  69     5594   5658   8520   1178   1775    742       C  
ATOM   4294  N   ILE I  70       2.403   7.721  42.809  1.00 46.86           N  
ANISOU 4294  N   ILE I  70     5149   5781   6876   1008   1003    557       N  
ATOM   4295  CA  ILE I  70       1.541   6.892  41.972  1.00 45.61           C  
ANISOU 4295  CA  ILE I  70     4936   5895   6499   1116    812    723       C  
ATOM   4296  C   ILE I  70       0.402   7.785  41.538  1.00 47.53           C  
ANISOU 4296  C   ILE I  70     5009   6096   6956   1298    951    975       C  
ATOM   4297  O   ILE I  70       0.131   8.792  42.178  1.00 47.96           O  
ANISOU 4297  O   ILE I  70     5011   5885   7325   1313   1192    943       O  
ATOM   4298  CB  ILE I  70       0.984   5.694  42.740  1.00 43.88           C  
ANISOU 4298  CB  ILE I  70     4778   5822   6073    980    639    516       C  
ATOM   4299  CG1 ILE I  70       0.431   4.631  41.796  1.00 43.49           C  
ANISOU 4299  CG1 ILE I  70     4695   6060   5769   1032    422    617       C  
ATOM   4300  CG2 ILE I  70      -0.094   6.134  43.655  1.00 45.65           C  
ANISOU 4300  CG2 ILE I  70     4941   5948   6458    960    766    437       C  
ATOM   4301  CD1 ILE I  70       0.242   3.282  42.445  1.00 41.73           C  
ANISOU 4301  CD1 ILE I  70     4553   5943   5359    880    258    410       C  
ATOM   4302  N   SER I  71      -0.208   7.451  40.409  1.00 48.28           N  
ANISOU 4302  N   SER I  71     4998   6457   6889   1434    813   1232       N  
ATOM   4303  CA  SER I  71      -1.441   8.068  40.002  1.00 50.28           C  
ANISOU 4303  CA  SER I  71     5047   6761   7298   1608    884   1511       C  
ATOM   4304  C   SER I  71      -1.963   7.254  38.859  1.00 51.07           C  
ANISOU 4304  C   SER I  71     5061   7281   7063   1664    633   1691       C  
ATOM   4305  O   SER I  71      -1.261   6.388  38.355  1.00 49.65           O  
ANISOU 4305  O   SER I  71     4993   7284   6587   1578    468   1587       O  
ATOM   4306  CB  SER I  71      -1.211   9.493  39.561  1.00 52.69           C  
ANISOU 4306  CB  SER I  71     5237   6830   7953   1784   1147   1806       C  
ATOM   4307  OG  SER I  71      -0.416   9.549  38.398  1.00 53.66           O  
ANISOU 4307  OG  SER I  71     5358   7100   7929   1862   1090   2035       O  
ATOM   4308  N   ARG I  72      -3.211   7.510  38.471  1.00 53.05           N  
ANISOU 4308  N   ARG I  72     5097   7695   7364   1795    614   1944       N  
ATOM   4309  CA  ARG I  72      -3.849   6.743  37.417  1.00 53.87           C  
ANISOU 4309  CA  ARG I  72     5083   8262   7123   1812    361   2092       C  
ATOM   4310  C   ARG I  72      -4.717   7.660  36.603  1.00 57.55           C  
ANISOU 4310  C   ARG I  72     5261   8885   7720   2040    415   2572       C  
ATOM   4311  O   ARG I  72      -5.173   8.697  37.098  1.00 59.51           O  
ANISOU 4311  O   ARG I  72     5386   8846   8378   2179    649   2740       O  
ATOM   4312  CB  ARG I  72      -4.696   5.607  37.993  1.00 52.82           C  
ANISOU 4312  CB  ARG I  72     4964   8276   6829   1654    187   1823       C  
ATOM   4313  CG  ARG I  72      -5.716   6.038  39.006  1.00 53.09           C  
ANISOU 4313  CG  ARG I  72     4894   8117   7160   1684    322   1804       C  
ATOM   4314  CD  ARG I  72      -6.936   5.183  38.873  1.00 54.14           C  
ANISOU 4314  CD  ARG I  72     4885   8567   7120   1623    125   1787       C  
ATOM   4315  NE  ARG I  72      -6.860   3.999  39.704  1.00 51.91           N  
ANISOU 4315  NE  ARG I  72     4778   8250   6694   1398     26   1397       N  
ATOM   4316  CZ  ARG I  72      -7.266   2.796  39.337  1.00 51.28           C  
ANISOU 4316  CZ  ARG I  72     4688   8457   6340   1259   -198   1263       C  
ATOM   4317  NH1 ARG I  72      -7.737   2.600  38.131  1.00 53.00           N  
ANISOU 4317  NH1 ARG I  72     4735   9063   6339   1293   -366   1444       N  
ATOM   4318  NH2 ARG I  72      -7.162   1.783  40.174  1.00 50.27           N  
ANISOU 4318  NH2 ARG I  72     4712   8234   6154   1071   -243    948       N  
ATOM   4319  N   ASP I  73      -4.937   7.297  35.344  1.00 59.58           N  
ANISOU 4319  N   ASP I  73     5394   9608   7637   2079    214   2803       N  
ATOM   4320  CA  ASP I  73      -5.844   8.068  34.509  1.00 63.72           C  
ANISOU 4320  CA  ASP I  73     5598  10386   8229   2295    217   3322       C  
ATOM   4321  C   ASP I  73      -6.991   7.178  34.033  1.00 64.98           C  
ANISOU 4321  C   ASP I  73     5578  11059   8054   2215    -70   3331       C  
ATOM   4322  O   ASP I  73      -6.817   6.388  33.120  1.00 65.75           O  
ANISOU 4322  O   ASP I  73     5689  11593   7699   2101   -294   3275       O  
ATOM   4323  CB  ASP I  73      -5.099   8.700  33.327  1.00 65.65           C  
ANISOU 4323  CB  ASP I  73     5786  10791   8367   2432    259   3703       C  
ATOM   4324  CG  ASP I  73      -6.007   9.592  32.483  1.00 71.12           C  
ANISOU 4324  CG  ASP I  73     6113  11749   9160   2684    279   4333       C  
ATOM   4325  OD1 ASP I  73      -7.236   9.433  32.590  1.00 71.89           O  
ANISOU 4325  OD1 ASP I  73     5990  12051   9274   2714    172   4438       O  
ATOM   4326  OD2 ASP I  73      -5.506  10.459  31.719  1.00 73.80           O  
ANISOU 4326  OD2 ASP I  73     6361  12100   9581   2857    409   4757       O  
ATOM   4327  N   ASN I  74      -8.159   7.295  34.657  1.00 65.71           N  
ANISOU 4327  N   ASN I  74     5494  11101   8371   2256    -48   3374       N  
ATOM   4328  CA  ASN I  74      -9.283   6.435  34.285  1.00 67.14           C  
ANISOU 4328  CA  ASN I  74     5486  11761   8265   2154   -319   3357       C  
ATOM   4329  C   ASN I  74      -9.960   6.706  32.924  1.00 71.61           C  
ANISOU 4329  C   ASN I  74     5706  12921   8580   2276   -499   3855       C  
ATOM   4330  O   ASN I  74     -10.721   5.865  32.442  1.00 73.05           O  
ANISOU 4330  O   ASN I  74     5744  13593   8419   2131   -766   3786       O  
ATOM   4331  CB  ASN I  74     -10.278   6.297  35.437  1.00 66.44           C  
ANISOU 4331  CB  ASN I  74     5331  11452   8461   2119   -250   3188       C  
ATOM   4332  CG  ASN I  74      -9.673   5.577  36.631  1.00 62.57           C  
ANISOU 4332  CG  ASN I  74     5177  10587   8008   1911   -185   2646       C  
ATOM   4333  OD1 ASN I  74      -8.690   4.849  36.493  1.00 61.25           O  
ANISOU 4333  OD1 ASN I  74     5261  10428   7584   1755   -272   2365       O  
ATOM   4334  ND2 ASN I  74     -10.246   5.776  37.800  1.00 60.94           N  
ANISOU 4334  ND2 ASN I  74     4964  10071   8120   1910    -21   2516       N  
ATOM   4335  N   SER I  75      -9.621   7.846  32.302  1.00 74.37           N  
ANISOU 4335  N   SER I  75     5927  13245   9087   2520   -352   4348       N  
ATOM   4336  CA  SER I  75      -9.947   8.180  30.883  1.00 79.00           C  
ANISOU 4336  CA  SER I  75     6208  14435   9372   2645   -513   4890       C  
ATOM   4337  C   SER I  75      -9.173   7.334  29.902  1.00 78.80           C  
ANISOU 4337  C   SER I  75     6341  14857   8744   2447   -726   4691       C  
ATOM   4338  O   SER I  75      -9.762   6.541  29.192  1.00 81.35           O  
ANISOU 4338  O   SER I  75     6524  15778   8606   2288  -1010   4635       O  
ATOM   4339  CB  SER I  75      -9.609   9.631  30.555  1.00 81.43           C  
ANISOU 4339  CB  SER I  75     6371  14510  10057   2961   -245   5475       C  
ATOM   4340  OG  SER I  75     -10.550  10.503  31.130  1.00 84.34           O  
ANISOU 4340  OG  SER I  75     6476  14602  10968   3185    -53   5799       O  
ATOM   4341  N   LYS I  76      -7.865   7.556  29.805  1.00 76.74           N  
ANISOU 4341  N   LYS I  76     6342  14327   8489   2454   -574   4598       N  
ATOM   4342  CA  LYS I  76      -7.002   6.594  29.142  1.00 75.97           C  
ANISOU 4342  CA  LYS I  76     6466  14517   7883   2232   -719   4252       C  
ATOM   4343  C   LYS I  76      -7.114   5.375  30.063  1.00 72.40           C  
ANISOU 4343  C   LYS I  76     6235  13871   7403   1971   -807   3606       C  
ATOM   4344  O   LYS I  76      -7.980   5.370  30.934  1.00 72.24           O  
ANISOU 4344  O   LYS I  76     6132  13655   7661   1980   -794   3545       O  
ATOM   4345  CB  LYS I  76      -5.569   7.119  29.083  1.00 75.02           C  
ANISOU 4345  CB  LYS I  76     6580  14038   7886   2304   -495   4263       C  
ATOM   4346  CG  LYS I  76      -5.438   8.598  28.641  1.00 78.02           C  
ANISOU 4346  CG  LYS I  76     6761  14317   8568   2610   -283   4922       C  
ATOM   4347  CD  LYS I  76      -4.028   9.147  29.014  1.00 76.91           C  
ANISOU 4347  CD  LYS I  76     6882  13623   8718   2653     -4   4823       C  
ATOM   4348  CE  LYS I  76      -2.937   8.886  27.938  1.00 77.09           C  
ANISOU 4348  CE  LYS I  76     7021  13953   8317   2590    -35   4842       C  
ATOM   4349  NZ  LYS I  76      -3.058   9.881  26.810  1.00 81.63           N  
ANISOU 4349  NZ  LYS I  76     7320  14865   8830   2819     24   5553       N  
ATOM   4350  N   ASN I  77      -6.302   4.337  29.908  1.00 69.13           N  
ANISOU 4350  N   ASN I  77     6081  13497   6687   1746   -876   3145       N  
ATOM   4351  CA  ASN I  77      -6.450   3.220  30.834  1.00 66.32           C  
ANISOU 4351  CA  ASN I  77     5906  12916   6375   1524   -931   2603       C  
ATOM   4352  C   ASN I  77      -5.104   2.915  31.396  1.00 63.20           C  
ANISOU 4352  C   ASN I  77     5849  12070   6095   1460   -781   2268       C  
ATOM   4353  O   ASN I  77      -4.601   1.817  31.233  1.00 62.04           O  
ANISOU 4353  O   ASN I  77     5873  11987   5711   1258   -851   1874       O  
ATOM   4354  CB  ASN I  77      -6.995   1.972  30.150  1.00 68.49           C  
ANISOU 4354  CB  ASN I  77     6123  13708   6193   1266  -1180   2309       C  
ATOM   4355  CG  ASN I  77      -8.489   1.877  30.210  1.00 71.47           C  
ANISOU 4355  CG  ASN I  77     6204  14387   6564   1238  -1344   2433       C  
ATOM   4356  OD1 ASN I  77      -9.122   2.387  31.134  1.00 71.40           O  
ANISOU 4356  OD1 ASN I  77     6109  14069   6951   1362  -1255   2566       O  
ATOM   4357  ND2 ASN I  77      -9.072   1.197  29.233  1.00 74.68           N  
ANISOU 4357  ND2 ASN I  77     6441  15416   6518   1056  -1576   2363       N  
ATOM   4358  N   THR I  78      -4.523   3.902  32.063  1.00 61.99           N  
ANISOU 4358  N   THR I  78     5771  11454   6329   1626   -560   2427       N  
ATOM   4359  CA  THR I  78      -3.109   3.880  32.356  1.00 59.19           C  
ANISOU 4359  CA  THR I  78     5678  10752   6061   1599   -416   2231       C  
ATOM   4360  C   THR I  78      -2.853   4.217  33.797  1.00 56.47           C  
ANISOU 4360  C   THR I  78     5466   9851   6140   1609   -251   2073       C  
ATOM   4361  O   THR I  78      -3.540   5.048  34.387  1.00 57.94           O  
ANISOU 4361  O   THR I  78     5526   9850   6637   1730   -144   2260       O  
ATOM   4362  CB  THR I  78      -2.348   4.893  31.488  1.00 60.91           C  
ANISOU 4362  CB  THR I  78     5849  11021   6274   1772   -288   2611       C  
ATOM   4363  OG1 THR I  78      -2.553   4.584  30.109  1.00 64.22           O  
ANISOU 4363  OG1 THR I  78     6140  12029   6232   1747   -442   2769       O  
ATOM   4364  CG2 THR I  78      -0.880   4.839  31.777  1.00 58.97           C  
ANISOU 4364  CG2 THR I  78     5850  10434   6121   1729   -145   2401       C  
ATOM   4365  N   LEU I  79      -1.865   3.535  34.351  1.00 53.31           N  
ANISOU 4365  N   LEU I  79     5304   9212   5740   1473   -224   1721       N  
ATOM   4366  CA  LEU I  79      -1.412   3.744  35.694  1.00 50.36           C  
ANISOU 4366  CA  LEU I  79     5071   8382   5684   1439    -89   1537       C  
ATOM   4367  C   LEU I  79      -0.044   4.407  35.516  1.00 50.40           C  
ANISOU 4367  C   LEU I  79     5179   8177   5795   1499     67   1609       C  
ATOM   4368  O   LEU I  79       0.609   4.217  34.495  1.00 51.14           O  
ANISOU 4368  O   LEU I  79     5294   8473   5665   1512     37   1675       O  
ATOM   4369  CB  LEU I  79      -1.305   2.384  36.401  1.00 47.19           C  
ANISOU 4369  CB  LEU I  79     4821   7926   5182   1234   -198   1137       C  
ATOM   4370  CG  LEU I  79      -0.716   2.303  37.808  1.00 44.89           C  
ANISOU 4370  CG  LEU I  79     4685   7254   5117   1150   -103    916       C  
ATOM   4371  CD1 LEU I  79      -1.632   2.912  38.850  1.00 44.99           C  
ANISOU 4371  CD1 LEU I  79     4623   7097   5372   1175    -17    943       C  
ATOM   4372  CD2 LEU I  79      -0.440   0.893  38.170  1.00 43.81           C  
ANISOU 4372  CD2 LEU I  79     4674   7121   4850    978   -213    617       C  
ATOM   4373  N   TYR I  80       0.369   5.225  36.473  1.00 50.01           N  
ANISOU 4373  N   TYR I  80     5179   7741   6082   1526    248   1591       N  
ATOM   4374  CA  TYR I  80       1.666   5.879  36.393  1.00 49.94           C  
ANISOU 4374  CA  TYR I  80     5251   7512   6211   1556    404   1636       C  
ATOM   4375  C   TYR I  80       2.432   5.726  37.690  1.00 47.75           C  
ANISOU 4375  C   TYR I  80     5127   6916   6102   1411    466   1327       C  
ATOM   4376  O   TYR I  80       1.836   5.468  38.741  1.00 46.77           O  
ANISOU 4376  O   TYR I  80     5025   6694   6052   1323    446   1143       O  
ATOM   4377  CB  TYR I  80       1.510   7.364  36.095  1.00 51.88           C  
ANISOU 4377  CB  TYR I  80     5353   7609   6752   1740    615   1995       C  
ATOM   4378  CG  TYR I  80       0.800   7.653  34.798  1.00 54.72           C  
ANISOU 4378  CG  TYR I  80     5520   8322   6949   1904    558   2398       C  
ATOM   4379  CD1 TYR I  80      -0.537   8.045  34.793  1.00 56.58           C  
ANISOU 4379  CD1 TYR I  80     5556   8655   7286   2017    548   2624       C  
ATOM   4380  CD2 TYR I  80       1.458   7.522  33.575  1.00 55.52           C  
ANISOU 4380  CD2 TYR I  80     5618   8698   6780   1943    515   2567       C  
ATOM   4381  CE1 TYR I  80      -1.207   8.299  33.609  1.00 59.38           C  
ANISOU 4381  CE1 TYR I  80     5696   9400   7467   2164    469   3036       C  
ATOM   4382  CE2 TYR I  80       0.799   7.784  32.385  1.00 58.91           C  
ANISOU 4382  CE2 TYR I  80     5852   9528   7002   2077    447   2959       C  
ATOM   4383  CZ  TYR I  80      -0.544   8.171  32.415  1.00 61.11           C  
ANISOU 4383  CZ  TYR I  80     5917   9927   7378   2187    411   3206       C  
ATOM   4384  OH  TYR I  80      -1.229   8.436  31.251  1.00 65.63           O  
ANISOU 4384  OH  TYR I  80     6254  10954   7728   2318    320   3640       O  
ATOM   4385  N   LEU I  81       3.753   5.853  37.594  1.00 46.25           N  
ANISOU 4385  N   LEU I  81     5024   6604   5945   1378    535   1281       N  
ATOM   4386  CA  LEU I  81       4.608   5.974  38.760  1.00 44.85           C  
ANISOU 4386  CA  LEU I  81     4946   6152   5944   1244    610   1049       C  
ATOM   4387  C   LEU I  81       5.663   7.017  38.447  1.00 46.92           C  
ANISOU 4387  C   LEU I  81     5191   6225   6412   1292    799   1179       C  
ATOM   4388  O   LEU I  81       6.539   6.807  37.611  1.00 48.38           O  
ANISOU 4388  O   LEU I  81     5397   6502   6483   1322    787   1259       O  
ATOM   4389  CB  LEU I  81       5.256   4.642  39.091  1.00 43.04           C  
ANISOU 4389  CB  LEU I  81     4832   6004   5515   1105    450    809       C  
ATOM   4390  CG  LEU I  81       6.051   4.563  40.384  1.00 41.71           C  
ANISOU 4390  CG  LEU I  81     4738   5648   5463    948    470    590       C  
ATOM   4391  CD1 LEU I  81       5.113   4.695  41.574  1.00 40.77           C  
ANISOU 4391  CD1 LEU I  81     4613   5457   5421    866    480    459       C  
ATOM   4392  CD2 LEU I  81       6.808   3.266  40.404  1.00 40.15           C  
ANISOU 4392  CD2 LEU I  81     4612   5543   5100    867    330    465       C  
ATOM   4393  N   GLN I  82       5.514   8.186  39.049  1.00 47.70           N  
ANISOU 4393  N   GLN I  82     5237   6051   6836   1303   1002   1205       N  
ATOM   4394  CA  GLN I  82       6.495   9.255  38.911  1.00 48.90           C  
ANISOU 4394  CA  GLN I  82     5364   5960   7258   1315   1219   1291       C  
ATOM   4395  C   GLN I  82       7.587   9.010  39.939  1.00 47.11           C  
ANISOU 4395  C   GLN I  82     5230   5607   7061   1099   1205    971       C  
ATOM   4396  O   GLN I  82       7.315   8.931  41.120  1.00 46.93           O  
ANISOU 4396  O   GLN I  82     5244   5507   7080    954   1196    720       O  
ATOM   4397  CB  GLN I  82       5.821  10.615  39.147  1.00 51.07           C  
ANISOU 4397  CB  GLN I  82     5526   5956   7924   1405   1484   1430       C  
ATOM   4398  CG  GLN I  82       6.717  11.828  38.980  1.00 52.70           C  
ANISOU 4398  CG  GLN I  82     5684   5854   8487   1418   1759   1534       C  
ATOM   4399  CD  GLN I  82       7.373  11.885  37.621  1.00 53.67           C  
ANISOU 4399  CD  GLN I  82     5765   6120   8507   1556   1758   1864       C  
ATOM   4400  OE1 GLN I  82       8.588  12.101  37.516  1.00 55.39           O  
ANISOU 4400  OE1 GLN I  82     6013   6231   8801   1480   1836   1821       O  
ATOM   4401  NE2 GLN I  82       6.593  11.670  36.572  1.00 53.91           N  
ANISOU 4401  NE2 GLN I  82     5715   6429   8341   1743   1666   2191       N  
ATOM   4402  N   MET I  83       8.813   8.845  39.485  1.00 46.39           N  
ANISOU 4402  N   MET I  83     5163   5537   6925   1071   1195    992       N  
ATOM   4403  CA  MET I  83       9.893   8.472  40.383  1.00 45.83           C  
ANISOU 4403  CA  MET I  83     5145   5420   6848    871   1138    732       C  
ATOM   4404  C   MET I  83      10.930   9.564  40.419  1.00 48.02           C  
ANISOU 4404  C   MET I  83     5368   5462   7415    810   1348    741       C  
ATOM   4405  O   MET I  83      11.660   9.752  39.441  1.00 48.95           O  
ANISOU 4405  O   MET I  83     5452   5587   7558    901   1413    937       O  
ATOM   4406  CB  MET I  83      10.576   7.166  39.929  1.00 44.25           C  
ANISOU 4406  CB  MET I  83     4996   5444   6372    869    941    718       C  
ATOM   4407  CG  MET I  83       9.755   5.890  40.071  1.00 43.22           C  
ANISOU 4407  CG  MET I  83     4924   5518   5979    870    733    636       C  
ATOM   4408  SD  MET I  83      10.307   4.590  38.923  1.00 45.54           S  
ANISOU 4408  SD  MET I  83     5255   6033   6016    945    610    691       S  
ATOM   4409  CE  MET I  83      11.317   3.516  39.893  1.00 41.94           C  
ANISOU 4409  CE  MET I  83     4828   5563   5543    795    489    498       C  
ATOM   4410  N   ASN I  84      11.042  10.256  41.549  1.00 48.77           N  
ANISOU 4410  N   ASN I  84     5450   5362   7719    631   1465    506       N  
ATOM   4411  CA  ASN I  84      12.079  11.284  41.681  1.00 50.40           C  
ANISOU 4411  CA  ASN I  84     5594   5333   8225    519   1673    453       C  
ATOM   4412  C   ASN I  84      13.193  10.951  42.680  1.00 49.81           C  
ANISOU 4412  C   ASN I  84     5516   5325   8085    252   1569    165       C  
ATOM   4413  O   ASN I  84      13.099  10.001  43.445  1.00 48.40           O  
ANISOU 4413  O   ASN I  84     5384   5357   7651    147   1351      8       O  
ATOM   4414  CB  ASN I  84      11.426  12.610  42.035  1.00 53.23           C  
ANISOU 4414  CB  ASN I  84     5900   5369   8957    509   1970    412       C  
ATOM   4415  CG  ASN I  84      10.335  12.977  41.069  1.00 54.93           C  
ANISOU 4415  CG  ASN I  84     6070   5538   9263    788   2070    761       C  
ATOM   4416  OD1 ASN I  84       9.477  13.786  41.383  1.00 56.59           O  
ANISOU 4416  OD1 ASN I  84     6231   5525   9743    829   2275    760       O  
ATOM   4417  ND2 ASN I  84      10.354  12.376  39.885  1.00 54.85           N  
ANISOU 4417  ND2 ASN I  84     6060   5759   9022    977   1933   1063       N  
ATOM   4418  N   SER I  85      14.249  11.756  42.672  1.00 51.95           N  
ANISOU 4418  N   SER I  85     5711   5428   8600    137   1729    122       N  
ATOM   4419  CA  SER I  85      15.368  11.559  43.584  1.00 52.09           C  
ANISOU 4419  CA  SER I  85     5681   5541   8571   -134   1631   -129       C  
ATOM   4420  C   SER I  85      15.868  10.121  43.615  1.00 49.03           C  
ANISOU 4420  C   SER I  85     5310   5474   7847   -119   1324    -80       C  
ATOM   4421  O   SER I  85      16.145   9.588  44.684  1.00 48.05           O  
ANISOU 4421  O   SER I  85     5167   5530   7559   -315   1156   -274       O  
ATOM   4422  CB  SER I  85      14.971  11.970  45.004  1.00 54.21           C  
ANISOU 4422  CB  SER I  85     5954   5781   8861   -397   1670   -496       C  
ATOM   4423  OG  SER I  85      14.455  13.286  45.066  1.00 56.51           O  
ANISOU 4423  OG  SER I  85     6226   5730   9517   -420   1998   -585       O  
ATOM   4424  N   LEU I  86      15.969   9.498  42.447  1.00 48.16           N  
ANISOU 4424  N   LEU I  86     5223   5438   7638    108   1270    184       N  
ATOM   4425  CA  LEU I  86      16.351   8.087  42.334  1.00 46.71           C  
ANISOU 4425  CA  LEU I  86     5056   5501   7191    157   1033    239       C  
ATOM   4426  C   LEU I  86      17.692   7.761  42.967  1.00 47.98           C  
ANISOU 4426  C   LEU I  86     5106   5765   7360    -21    931    153       C  
ATOM   4427  O   LEU I  86      18.627   8.605  43.009  1.00 49.62           O  
ANISOU 4427  O   LEU I  86     5209   5866   7779   -143   1058    115       O  
ATOM   4428  CB  LEU I  86      16.319   7.597  40.887  1.00 45.80           C  
ANISOU 4428  CB  LEU I  86     4976   5434   6990    404   1051    488       C  
ATOM   4429  CG  LEU I  86      14.878   7.473  40.386  1.00 45.97           C  
ANISOU 4429  CG  LEU I  86     5088   5490   6888    565   1044    576       C  
ATOM   4430  CD1 LEU I  86      14.833   7.166  38.893  1.00 46.11           C  
ANISOU 4430  CD1 LEU I  86     5125   5606   6789    775   1082    809       C  
ATOM   4431  CD2 LEU I  86      14.069   6.455  41.199  1.00 43.85           C  
ANISOU 4431  CD2 LEU I  86     4886   5364   6410    514    841    433       C  
ATOM   4432  N   ARG I  87      17.762   6.529  43.478  1.00 46.65           N  
ANISOU 4432  N   ARG I  87     4938   5806   6980    -39    707    142       N  
ATOM   4433  CA  ARG I  87      18.933   6.012  44.166  1.00 48.03           C  
ANISOU 4433  CA  ARG I  87     4977   6140   7133   -187    567    120       C  
ATOM   4434  C   ARG I  87      19.315   4.729  43.473  1.00 46.60           C  
ANISOU 4434  C   ARG I  87     4788   6045   6872     -3    473    305       C  
ATOM   4435  O   ARG I  87      18.439   4.061  42.909  1.00 43.96           O  
ANISOU 4435  O   ARG I  87     4575   5707   6420    163    455    361       O  
ATOM   4436  CB  ARG I  87      18.578   5.628  45.603  1.00 48.45           C  
ANISOU 4436  CB  ARG I  87     5015   6383   7010   -382    390    -33       C  
ATOM   4437  CG  ARG I  87      18.264   6.753  46.536  1.00 50.76           C  
ANISOU 4437  CG  ARG I  87     5303   6639   7346   -623    478   -291       C  
ATOM   4438  CD  ARG I  87      18.539   6.310  47.994  1.00 52.62           C  
ANISOU 4438  CD  ARG I  87     5444   7178   7369   -880    275   -420       C  
ATOM   4439  NE  ARG I  87      17.695   5.200  48.475  1.00 50.65           N  
ANISOU 4439  NE  ARG I  87     5271   7094   6880   -813    107   -349       N  
ATOM   4440  CZ  ARG I  87      16.558   5.343  49.165  1.00 49.57           C  
ANISOU 4440  CZ  ARG I  87     5234   6984   6614   -886    124   -504       C  
ATOM   4441  NH1 ARG I  87      16.064   6.552  49.444  1.00 50.48           N  
ANISOU 4441  NH1 ARG I  87     5397   6953   6831  -1014    317   -754       N  
ATOM   4442  NH2 ARG I  87      15.917   4.263  49.578  1.00 48.55           N  
ANISOU 4442  NH2 ARG I  87     5150   7008   6286   -828    -28   -406       N  
ATOM   4443  N   ALA I  88      20.590   4.342  43.590  1.00 46.76           N  
ANISOU 4443  N   ALA I  88     4650   6150   6964    -49    415    383       N  
ATOM   4444  CA  ALA I  88      21.002   3.027  43.125  1.00 45.97           C  
ANISOU 4444  CA  ALA I  88     4519   6114   6835    111    345    540       C  
ATOM   4445  C   ALA I  88      20.030   1.946  43.658  1.00 45.65           C  
ANISOU 4445  C   ALA I  88     4568   6159   6616    149    195    531       C  
ATOM   4446  O   ALA I  88      19.645   1.031  42.943  1.00 44.87           O  
ANISOU 4446  O   ALA I  88     4550   6020   6480    319    214    592       O  
ATOM   4447  CB  ALA I  88      22.398   2.742  43.548  1.00 46.31           C  
ANISOU 4447  CB  ALA I  88     4339   6266   6992     27    274    632       C  
ATOM   4448  N   GLU I  89      19.589   2.082  44.903  1.00 46.33           N  
ANISOU 4448  N   GLU I  89     4643   6367   6591    -27     66    435       N  
ATOM   4449  CA  GLU I  89      18.757   1.060  45.537  1.00 44.91           C  
ANISOU 4449  CA  GLU I  89     4522   6284   6259    -13    -73    456       C  
ATOM   4450  C   GLU I  89      17.475   0.840  44.750  1.00 42.96           C  
ANISOU 4450  C   GLU I  89     4464   5914   5944    142      1    412       C  
ATOM   4451  O   GLU I  89      16.869  -0.219  44.847  1.00 42.36           O  
ANISOU 4451  O   GLU I  89     4438   5862   5795    208    -72    453       O  
ATOM   4452  CB  GLU I  89      18.425   1.438  46.985  1.00 46.37           C  
ANISOU 4452  CB  GLU I  89     4673   6650   6297   -250   -191    340       C  
ATOM   4453  CG  GLU I  89      19.614   1.375  47.953  1.00 50.61           C  
ANISOU 4453  CG  GLU I  89     4987   7423   6819   -435   -332    407       C  
ATOM   4454  CD  GLU I  89      20.620   2.528  47.815  1.00 53.62           C  
ANISOU 4454  CD  GLU I  89     5254   7784   7337   -572   -245    311       C  
ATOM   4455  OE1 GLU I  89      20.773   3.115  46.704  1.00 53.90           O  
ANISOU 4455  OE1 GLU I  89     5348   7588   7545   -451    -64    297       O  
ATOM   4456  OE2 GLU I  89      21.281   2.847  48.837  1.00 56.67           O  
ANISOU 4456  OE2 GLU I  89     5474   8410   7648   -819   -359    255       O  
ATOM   4457  N   ASP I  90      17.074   1.847  43.974  1.00 42.53           N  
ANISOU 4457  N   ASP I  90     4493   5736   5930    192    150    348       N  
ATOM   4458  CA  ASP I  90      15.793   1.846  43.312  1.00 41.17           C  
ANISOU 4458  CA  ASP I  90     4464   5504   5675    311    203    319       C  
ATOM   4459  C   ASP I  90      15.845   1.016  42.052  1.00 41.77           C  
ANISOU 4459  C   ASP I  90     4582   5560   5730    493    248    404       C  
ATOM   4460  O   ASP I  90      14.797   0.737  41.440  1.00 41.73           O  
ANISOU 4460  O   ASP I  90     4676   5565   5616    582    259    382       O  
ATOM   4461  CB  ASP I  90      15.395   3.265  42.948  1.00 42.16           C  
ANISOU 4461  CB  ASP I  90     4624   5516   5880    310    357    279       C  
ATOM   4462  CG  ASP I  90      14.925   4.053  44.139  1.00 43.41           C  
ANISOU 4462  CG  ASP I  90     4778   5665   6050    131    358    123       C  
ATOM   4463  OD1 ASP I  90      14.128   3.520  44.906  1.00 44.08           O  
ANISOU 4463  OD1 ASP I  90     4906   5839   6003     77    254     55       O  
ATOM   4464  OD2 ASP I  90      15.338   5.207  44.326  1.00 44.88           O  
ANISOU 4464  OD2 ASP I  90     4916   5750   6387     30    485     52       O  
ATOM   4465  N   THR I  91      17.049   0.626  41.643  1.00 41.84           N  
ANISOU 4465  N   THR I  91     4503   5557   5838    536    285    484       N  
ATOM   4466  CA  THR I  91      17.171  -0.101  40.403  1.00 41.49           C  
ANISOU 4466  CA  THR I  91     4498   5492   5773    689    374    518       C  
ATOM   4467  C   THR I  91      16.553  -1.475  40.530  1.00 42.02           C  
ANISOU 4467  C   THR I  91     4613   5575   5776    722    296    472       C  
ATOM   4468  O   THR I  91      16.832  -2.202  41.487  1.00 43.29           O  
ANISOU 4468  O   THR I  91     4703   5741   6005    666    194    511       O  
ATOM   4469  CB  THR I  91      18.608  -0.067  39.788  1.00 42.21           C  
ANISOU 4469  CB  THR I  91     4480   5546   6012    741    490    607       C  
ATOM   4470  OG1 THR I  91      19.024  -1.379  39.453  1.00 42.16           O  
ANISOU 4470  OG1 THR I  91     4444   5520   6054    825    512    618       O  
ATOM   4471  CG2 THR I  91      19.573   0.529  40.702  1.00 42.55           C  
ANISOU 4471  CG2 THR I  91     4377   5594   6195    614    444    653       C  
ATOM   4472  N   ALA I  92      15.637  -1.782  39.609  1.00 41.72           N  
ANISOU 4472  N   ALA I  92     4685   5562   5604    798    341    398       N  
ATOM   4473  CA  ALA I  92      14.865  -3.023  39.646  1.00 41.30           C  
ANISOU 4473  CA  ALA I  92     4686   5507   5498    804    290    310       C  
ATOM   4474  C   ALA I  92      13.989  -3.156  38.428  1.00 41.90           C  
ANISOU 4474  C   ALA I  92     4857   5665   5396    860    352    208       C  
ATOM   4475  O   ALA I  92      13.893  -2.241  37.589  1.00 42.25           O  
ANISOU 4475  O   ALA I  92     4923   5796   5334    908    420    249       O  
ATOM   4476  CB  ALA I  92      13.995  -3.073  40.871  1.00 40.09           C  
ANISOU 4476  CB  ALA I  92     4547   5374   5310    707    146    299       C  
ATOM   4477  N   VAL I  93      13.338  -4.313  38.330  1.00 41.89           N  
ANISOU 4477  N   VAL I  93     4898   5654   5364    843    331     86       N  
ATOM   4478  CA  VAL I  93      12.322  -4.525  37.304  1.00 42.24           C  
ANISOU 4478  CA  VAL I  93     5015   5834   5200    847    352    -47       C  
ATOM   4479  C   VAL I  93      11.020  -4.112  37.973  1.00 40.97           C  
ANISOU 4479  C   VAL I  93     4877   5739   4949    792    215    -36       C  
ATOM   4480  O   VAL I  93      10.789  -4.533  39.087  1.00 41.14           O  
ANISOU 4480  O   VAL I  93     4886   5671   5073    731    134    -29       O  
ATOM   4481  CB  VAL I  93      12.206  -6.012  36.904  1.00 42.92           C  
ANISOU 4481  CB  VAL I  93     5124   5857   5328    818    419   -237       C  
ATOM   4482  CG1 VAL I  93      10.796  -6.281  36.390  1.00 44.57           C  
ANISOU 4482  CG1 VAL I  93     5386   6226   5321    752    361   -393       C  
ATOM   4483  CG2 VAL I  93      13.226  -6.402  35.887  1.00 43.09           C  
ANISOU 4483  CG2 VAL I  93     5134   5852   5385    874    604   -311       C  
ATOM   4484  N   TYR I  94      10.222  -3.249  37.344  1.00 40.76           N  
ANISOU 4484  N   TYR I  94     4865   5875   4748    820    201      1       N  
ATOM   4485  CA  TYR I  94       8.987  -2.727  37.979  1.00 40.68           C  
ANISOU 4485  CA  TYR I  94     4850   5913   4692    787     99     35       C  
ATOM   4486  C   TYR I  94       7.719  -3.310  37.348  1.00 41.15           C  
ANISOU 4486  C   TYR I  94     4917   6147   4571    754     39    -75       C  
ATOM   4487  O   TYR I  94       7.570  -3.311  36.140  1.00 42.80           O  
ANISOU 4487  O   TYR I  94     5120   6545   4596    782     72   -100       O  
ATOM   4488  CB  TYR I  94       8.941  -1.186  37.941  1.00 40.56           C  
ANISOU 4488  CB  TYR I  94     4801   5917   4691    850    139    204       C  
ATOM   4489  CG  TYR I  94       9.867  -0.514  38.926  1.00 39.50           C  
ANISOU 4489  CG  TYR I  94     4646   5611   4750    820    174    262       C  
ATOM   4490  CD1 TYR I  94      11.218  -0.428  38.691  1.00 39.41           C  
ANISOU 4490  CD1 TYR I  94     4612   5531   4830    840    252    303       C  
ATOM   4491  CD2 TYR I  94       9.372   0.053  40.084  1.00 38.68           C  
ANISOU 4491  CD2 TYR I  94     4531   5437   4727    753    137    256       C  
ATOM   4492  CE1 TYR I  94      12.065   0.188  39.607  1.00 40.07           C  
ANISOU 4492  CE1 TYR I  94     4650   5498   5077    779    267    338       C  
ATOM   4493  CE2 TYR I  94      10.198   0.665  41.001  1.00 39.09           C  
ANISOU 4493  CE2 TYR I  94     4554   5379   4918    681    166    261       C  
ATOM   4494  CZ  TYR I  94      11.553   0.735  40.772  1.00 39.39           C  
ANISOU 4494  CZ  TYR I  94     4557   5368   5041    687    219    304       C  
ATOM   4495  OH  TYR I  94      12.404   1.366  41.697  1.00 38.26           O  
ANISOU 4495  OH  TYR I  94     4358   5152   5026    582    234    294       O  
ATOM   4496  N   TYR I  95       6.822  -3.821  38.172  1.00 40.37           N  
ANISOU 4496  N   TYR I  95     4817   6012   4509    678    -48   -142       N  
ATOM   4497  CA  TYR I  95       5.648  -4.526  37.666  1.00 42.19           C  
ANISOU 4497  CA  TYR I  95     5035   6396   4600    613   -109   -275       C  
ATOM   4498  C   TYR I  95       4.400  -3.760  38.041  1.00 42.43           C  
ANISOU 4498  C   TYR I  95     5008   6529   4582    621   -190   -179       C  
ATOM   4499  O   TYR I  95       4.264  -3.351  39.198  1.00 41.57           O  
ANISOU 4499  O   TYR I  95     4899   6287   4608    611   -202   -114       O  
ATOM   4500  CB  TYR I  95       5.503  -5.879  38.363  1.00 41.94           C  
ANISOU 4500  CB  TYR I  95     5026   6210   4701    510   -123   -425       C  
ATOM   4501  CG  TYR I  95       6.551  -6.864  38.011  1.00 42.13           C  
ANISOU 4501  CG  TYR I  95     5081   6094   4832    502    -17   -535       C  
ATOM   4502  CD1 TYR I  95       6.512  -7.534  36.812  1.00 43.77           C  
ANISOU 4502  CD1 TYR I  95     5302   6404   4924    461     56   -736       C  
ATOM   4503  CD2 TYR I  95       7.573  -7.146  38.897  1.00 41.63           C  
ANISOU 4503  CD2 TYR I  95     5015   5811   4992    528     21   -441       C  
ATOM   4504  CE1 TYR I  95       7.456  -8.448  36.498  1.00 45.41           C  
ANISOU 4504  CE1 TYR I  95     5532   6448   5275    457    198   -861       C  
ATOM   4505  CE2 TYR I  95       8.548  -8.042  38.578  1.00 42.76           C  
ANISOU 4505  CE2 TYR I  95     5157   5803   5287    545    142   -508       C  
ATOM   4506  CZ  TYR I  95       8.475  -8.699  37.389  1.00 45.06           C  
ANISOU 4506  CZ  TYR I  95     5473   6146   5503    515    247   -728       C  
ATOM   4507  OH  TYR I  95       9.471  -9.582  37.063  1.00 47.92           O  
ANISOU 4507  OH  TYR I  95     5828   6322   6057    539    413   -815       O  
ATOM   4508  N   CYS I  96       3.457  -3.584  37.119  1.00 43.22           N  
ANISOU 4508  N   CYS I  96     5044   6886   4491    628   -240   -170       N  
ATOM   4509  CA  CYS I  96       2.142  -3.173  37.605  1.00 43.69           C  
ANISOU 4509  CA  CYS I  96     5023   7021   4557    621   -316   -100       C  
ATOM   4510  C   CYS I  96       1.283  -4.453  37.840  1.00 44.40           C  
ANISOU 4510  C   CYS I  96     5102   7140   4629    474   -390   -307       C  
ATOM   4511  O   CYS I  96       1.420  -5.465  37.131  1.00 45.27           O  
ANISOU 4511  O   CYS I  96     5234   7319   4646    385   -388   -501       O  
ATOM   4512  CB  CYS I  96       1.488  -2.074  36.741  1.00 44.83           C  
ANISOU 4512  CB  CYS I  96     5052   7412   4569    730   -333    113       C  
ATOM   4513  SG  CYS I  96       0.768  -2.690  35.236  1.00 50.98           S  
ANISOU 4513  SG  CYS I  96     5740   8620   5010    666   -434     36       S  
ATOM   4514  N   ALA I  97       0.484  -4.444  38.902  1.00 43.37           N  
ANISOU 4514  N   ALA I  97     4941   6921   4615    436   -423   -288       N  
ATOM   4515  CA  ALA I  97      -0.288  -5.614  39.253  1.00 43.18           C  
ANISOU 4515  CA  ALA I  97     4900   6883   4623    295   -471   -456       C  
ATOM   4516  C   ALA I  97      -1.658  -5.187  39.668  1.00 43.61           C  
ANISOU 4516  C   ALA I  97     4842   7048   4680    286   -530   -382       C  
ATOM   4517  O   ALA I  97      -1.842  -4.152  40.344  1.00 42.92           O  
ANISOU 4517  O   ALA I  97     4729   6900   4676    375   -494   -223       O  
ATOM   4518  CB  ALA I  97       0.369  -6.349  40.384  1.00 41.85           C  
ANISOU 4518  CB  ALA I  97     4818   6436   4647    242   -419   -498       C  
ATOM   4519  N   ARG I  98      -2.619  -6.016  39.295  1.00 44.51           N  
ANISOU 4519  N   ARG I  98     4877   7308   4727    164   -600   -521       N  
ATOM   4520  CA  ARG I  98      -4.001  -5.754  39.611  1.00 45.04           C  
ANISOU 4520  CA  ARG I  98     4803   7505   4805    141   -660   -460       C  
ATOM   4521  C   ARG I  98      -4.399  -6.437  40.926  1.00 44.61           C  
ANISOU 4521  C   ARG I  98     4776   7237   4935     42   -624   -522       C  
ATOM   4522  O   ARG I  98      -4.185  -7.629  41.119  1.00 45.74           O  
ANISOU 4522  O   ARG I  98     4977   7251   5151    -83   -604   -681       O  
ATOM   4523  CB  ARG I  98      -4.877  -6.211  38.448  1.00 47.39           C  
ANISOU 4523  CB  ARG I  98     4961   8139   4905     41   -772   -566       C  
ATOM   4524  CG  ARG I  98      -6.339  -5.787  38.521  1.00 48.96           C  
ANISOU 4524  CG  ARG I  98     4955   8555   5093     41   -855   -450       C  
ATOM   4525  CD  ARG I  98      -7.160  -7.040  38.407  1.00 50.72           C  
ANISOU 4525  CD  ARG I  98     5105   8868   5300   -183   -920   -697       C  
ATOM   4526  NE  ARG I  98      -8.101  -7.083  37.320  1.00 53.01           N  
ANISOU 4526  NE  ARG I  98     5189   9587   5365   -268  -1062   -726       N  
ATOM   4527  CZ  ARG I  98      -8.779  -8.169  36.944  1.00 55.50           C  
ANISOU 4527  CZ  ARG I  98     5418  10049   5619   -504  -1129   -993       C  
ATOM   4528  NH1 ARG I  98      -8.625  -9.341  37.561  1.00 53.66           N  
ANISOU 4528  NH1 ARG I  98     5294   9517   5579   -664  -1040  -1242       N  
ATOM   4529  NH2 ARG I  98      -9.626  -8.074  35.917  1.00 58.56           N  
ANISOU 4529  NH2 ARG I  98     5589  10908   5755   -589  -1283   -999       N  
ATOM   4530  N   GLU I  99      -4.935  -5.654  41.849  1.00 44.08           N  
ANISOU 4530  N   GLU I  99     4666   7122   4962    103   -586   -384       N  
ATOM   4531  CA  GLU I  99      -5.456  -6.168  43.097  1.00 43.54           C  
ANISOU 4531  CA  GLU I  99     4601   6915   5025     10   -544   -412       C  
ATOM   4532  C   GLU I  99      -6.887  -6.675  42.897  1.00 45.29           C  
ANISOU 4532  C   GLU I  99     4662   7298   5249    -92   -605   -472       C  
ATOM   4533  O   GLU I  99      -7.719  -5.995  42.275  1.00 46.55           O  
ANISOU 4533  O   GLU I  99     4665   7679   5342    -31   -661   -389       O  
ATOM   4534  CB  GLU I  99      -5.476  -5.053  44.152  1.00 42.22           C  
ANISOU 4534  CB  GLU I  99     4447   6658   4936     97   -449   -282       C  
ATOM   4535  CG  GLU I  99      -5.935  -5.491  45.534  1.00 41.69           C  
ANISOU 4535  CG  GLU I  99     4392   6488   4960     -4   -385   -299       C  
ATOM   4536  CD  GLU I  99      -5.249  -4.699  46.621  1.00 42.10           C  
ANISOU 4536  CD  GLU I  99     4536   6425   5035     27   -282   -249       C  
ATOM   4537  OE1 GLU I  99      -5.804  -4.643  47.720  1.00 43.19           O  
ANISOU 4537  OE1 GLU I  99     4657   6546   5207    -37   -205   -248       O  
ATOM   4538  OE2 GLU I  99      -4.167  -4.107  46.387  1.00 41.29           O  
ANISOU 4538  OE2 GLU I  99     4513   6267   4907     98   -267   -224       O  
ATOM   4539  N   ARG I 100      -7.179  -7.844  43.451  1.00 44.76           N  
ANISOU 4539  N   ARG I 100     4608   7120   5278   -245   -588   -586       N  
ATOM   4540  CA  ARG I 100      -8.535  -8.323  43.515  1.00 46.82           C  
ANISOU 4540  CA  ARG I 100     4710   7496   5584   -363   -623   -641       C  
ATOM   4541  C   ARG I 100      -8.732  -8.954  44.894  1.00 47.03           C  
ANISOU 4541  C   ARG I 100     4780   7317   5774   -450   -525   -620       C  
ATOM   4542  O   ARG I 100      -7.753  -9.380  45.517  1.00 45.12           O  
ANISOU 4542  O   ARG I 100     4682   6871   5590   -454   -462   -597       O  
ATOM   4543  CB  ARG I 100      -8.818  -9.310  42.381  1.00 48.50           C  
ANISOU 4543  CB  ARG I 100     4854   7843   5730   -515   -707   -853       C  
ATOM   4544  CG  ARG I 100     -10.063 -10.082  42.575  1.00 49.99           C  
ANISOU 4544  CG  ARG I 100     4890   8093   6011   -691   -725   -953       C  
ATOM   4545  CD  ARG I 100     -10.456 -10.944  41.405  1.00 53.00           C  
ANISOU 4545  CD  ARG I 100     5173   8658   6305   -880   -809  -1209       C  
ATOM   4546  NE  ARG I 100     -11.912 -11.141  41.468  1.00 55.91           N  
ANISOU 4546  NE  ARG I 100     5313   9215   6713  -1010   -871  -1236       N  
ATOM   4547  CZ  ARG I 100     -12.562 -12.165  40.936  1.00 59.15           C  
ANISOU 4547  CZ  ARG I 100     5608   9722   7146  -1256   -908  -1492       C  
ATOM   4548  NH1 ARG I 100     -11.886 -13.113  40.286  1.00 60.28           N  
ANISOU 4548  NH1 ARG I 100     5855   9766   7285  -1400   -866  -1770       N  
ATOM   4549  NH2 ARG I 100     -13.885 -12.228  41.049  1.00 60.89           N  
ANISOU 4549  NH2 ARG I 100     5596  10132   7408  -1365   -970  -1485       N  
ATOM   4550  N   TRP I 101      -9.981  -8.964  45.383  1.00 48.11           N  
ANISOU 4550  N   TRP I 101     4773   7530   5979   -511   -509   -593       N  
ATOM   4551  CA  TRP I 101     -10.294  -9.462  46.717  1.00 47.39           C  
ANISOU 4551  CA  TRP I 101     4702   7290   6015   -593   -401   -541       C  
ATOM   4552  C   TRP I 101     -11.371 -10.501  46.640  1.00 50.13           C  
ANISOU 4552  C   TRP I 101     4908   7662   6478   -771   -409   -640       C  
ATOM   4553  O   TRP I 101     -12.371 -10.305  45.962  1.00 52.03           O  
ANISOU 4553  O   TRP I 101     4968   8110   6693   -803   -485   -690       O  
ATOM   4554  CB  TRP I 101     -10.852  -8.342  47.583  1.00 47.64           C  
ANISOU 4554  CB  TRP I 101     4682   7378   6043   -501   -316   -414       C  
ATOM   4555  CG  TRP I 101      -9.844  -7.341  48.103  1.00 46.20           C  
ANISOU 4555  CG  TRP I 101     4642   7123   5790   -374   -251   -336       C  
ATOM   4556  CD1 TRP I 101      -8.917  -6.649  47.383  1.00 44.49           C  
ANISOU 4556  CD1 TRP I 101     4501   6908   5496   -254   -296   -326       C  
ATOM   4557  CD2 TRP I 101      -9.701  -6.905  49.452  1.00 45.14           C  
ANISOU 4557  CD2 TRP I 101     4574   6928   5649   -381   -120   -279       C  
ATOM   4558  NE1 TRP I 101      -8.187  -5.833  48.209  1.00 42.69           N  
ANISOU 4558  NE1 TRP I 101     4380   6598   5242   -195   -201   -277       N  
ATOM   4559  CE2 TRP I 101      -8.658  -5.970  49.481  1.00 42.96           C  
ANISOU 4559  CE2 TRP I 101     4411   6611   5301   -281    -96   -263       C  
ATOM   4560  CE3 TRP I 101     -10.341  -7.236  50.644  1.00 46.34           C  
ANISOU 4560  CE3 TRP I 101     4697   7076   5832   -483    -11   -247       C  
ATOM   4561  CZ2 TRP I 101      -8.251  -5.364  50.631  1.00 43.22           C  
ANISOU 4561  CZ2 TRP I 101     4523   6615   5282   -298     21   -253       C  
ATOM   4562  CZ3 TRP I 101      -9.933  -6.634  51.790  1.00 45.66           C  
ANISOU 4562  CZ3 TRP I 101     4698   6984   5666   -490    108   -221       C  
ATOM   4563  CH2 TRP I 101      -8.897  -5.705  51.781  1.00 44.54           C  
ANISOU 4563  CH2 TRP I 101     4664   6816   5442   -409    120   -241       C  
ATOM   4564  N   HIS I 102     -11.178 -11.596  47.360  1.00 50.78           N  
ANISOU 4564  N   HIS I 102     5052   7538   6703   -890   -324   -643       N  
ATOM   4565  CA  HIS I 102     -12.270 -12.517  47.663  1.00 52.51           C  
ANISOU 4565  CA  HIS I 102     5134   7731   7086  -1067   -277   -694       C  
ATOM   4566  C   HIS I 102     -12.698 -12.173  49.121  1.00 52.33           C  
ANISOU 4566  C   HIS I 102     5106   7686   7093  -1045   -155   -503       C  
ATOM   4567  O   HIS I 102     -13.419 -11.195  49.331  1.00 52.35           O  
ANISOU 4567  O   HIS I 102     5012   7849   7029   -971   -145   -452       O  
ATOM   4568  CB  HIS I 102     -11.782 -13.961  47.462  1.00 53.53           C  
ANISOU 4568  CB  HIS I 102     5322   7619   7399  -1212   -223   -807       C  
ATOM   4569  CG  HIS I 102     -12.849 -15.006  47.576  1.00 55.54           C  
ANISOU 4569  CG  HIS I 102     5427   7810   7865  -1424   -161   -903       C  
ATOM   4570  ND1 HIS I 102     -13.998 -14.989  46.817  1.00 57.89           N  
ANISOU 4570  ND1 HIS I 102     5527   8327   8143  -1544   -248  -1072       N  
ATOM   4571  CD2 HIS I 102     -12.915 -16.131  48.331  1.00 57.08           C  
ANISOU 4571  CD2 HIS I 102     5626   7747   8316  -1547    -15   -840       C  
ATOM   4572  CE1 HIS I 102     -14.740 -16.039  47.123  1.00 59.73           C  
ANISOU 4572  CE1 HIS I 102     5651   8430   8612  -1747   -155  -1142       C  
ATOM   4573  NE2 HIS I 102     -14.105 -16.750  48.039  1.00 59.18           N  
ANISOU 4573  NE2 HIS I 102     5707   8052   8728  -1747     -1   -997       N  
ATOM   4574  N   VAL I 103     -12.223 -12.930  50.116  1.00 52.29           N  
ANISOU 4574  N   VAL I 103     5193   7494   7180  -1102    -48   -384       N  
ATOM   4575  CA  VAL I 103     -12.242 -12.459  51.489  1.00 51.30           C  
ANISOU 4575  CA  VAL I 103     5109   7401   6981  -1068     60   -199       C  
ATOM   4576  C   VAL I 103     -11.217 -11.333  51.688  1.00 50.01           C  
ANISOU 4576  C   VAL I 103     5086   7298   6619   -916     34   -152       C  
ATOM   4577  O   VAL I 103     -11.552 -10.296  52.267  1.00 49.32           O  
ANISOU 4577  O   VAL I 103     4983   7332   6422   -858     96   -127       O  
ATOM   4578  CB  VAL I 103     -11.939 -13.572  52.466  1.00 51.80           C  
ANISOU 4578  CB  VAL I 103     5217   7302   7165  -1168    167    -32       C  
ATOM   4579  CG1 VAL I 103     -12.079 -13.066  53.878  1.00 51.34           C  
ANISOU 4579  CG1 VAL I 103     5180   7363   6965  -1164    276    146       C  
ATOM   4580  CG2 VAL I 103     -12.872 -14.678  52.229  1.00 54.84           C  
ANISOU 4580  CG2 VAL I 103     5466   7580   7792  -1329    217    -93       C  
ATOM   4581  N   ARG I 104      -9.981 -11.544  51.207  1.00 48.87           N  
ANISOU 4581  N   ARG I 104     5062   7053   6452   -861    -33   -156       N  
ATOM   4582  CA  ARG I 104      -8.915 -10.515  51.268  1.00 47.52           C  
ANISOU 4582  CA  ARG I 104     5012   6929   6115   -732    -66   -128       C  
ATOM   4583  C   ARG I 104      -8.173 -10.365  49.934  1.00 46.78           C  
ANISOU 4583  C   ARG I 104     4964   6801   6009   -645   -171   -237       C  
ATOM   4584  O   ARG I 104      -8.375 -11.153  49.024  1.00 49.41           O  
ANISOU 4584  O   ARG I 104     5254   7080   6441   -699   -215   -348       O  
ATOM   4585  CB  ARG I 104      -7.919 -10.838  52.373  1.00 47.03           C  
ANISOU 4585  CB  ARG I 104     5049   6822   5997   -755    -23     46       C  
ATOM   4586  CG  ARG I 104      -8.565 -10.932  53.727  1.00 48.52           C  
ANISOU 4586  CG  ARG I 104     5198   7103   6133   -850     88    170       C  
ATOM   4587  CD  ARG I 104      -8.973  -9.568  54.227  1.00 47.25           C  
ANISOU 4587  CD  ARG I 104     5036   7110   5808   -817    154     93       C  
ATOM   4588  NE  ARG I 104      -9.621  -9.694  55.506  1.00 48.28           N  
ANISOU 4588  NE  ARG I 104     5128   7351   5866   -924    285    183       N  
ATOM   4589  CZ  ARG I 104     -10.891  -9.418  55.734  1.00 49.82           C  
ANISOU 4589  CZ  ARG I 104     5216   7608   6106   -957    391    122       C  
ATOM   4590  NH1 ARG I 104     -11.667  -8.980  54.760  1.00 48.90           N  
ANISOU 4590  NH1 ARG I 104     5000   7465   6113   -884    363     -7       N  
ATOM   4591  NH2 ARG I 104     -11.382  -9.601  56.955  1.00 52.73           N  
ANISOU 4591  NH2 ARG I 104     5558   8090   6388  -1066    528    214       N  
ATOM   4592  N   GLY I 105      -7.294  -9.374  49.833  1.00 45.01           N  
ANISOU 4592  N   GLY I 105     4826   6614   5664   -530   -195   -221       N  
ATOM   4593  CA  GLY I 105      -6.644  -9.047  48.566  1.00 43.20           C  
ANISOU 4593  CA  GLY I 105     4630   6387   5398   -436   -277   -305       C  
ATOM   4594  C   GLY I 105      -5.572  -9.983  48.068  1.00 42.84           C  
ANISOU 4594  C   GLY I 105     4663   6197   5419   -446   -303   -325       C  
ATOM   4595  O   GLY I 105      -4.869 -10.607  48.856  1.00 43.14           O  
ANISOU 4595  O   GLY I 105     4754   6117   5521   -476   -262   -209       O  
ATOM   4596  N   TYR I 106      -5.462 -10.060  46.744  1.00 43.13           N  
ANISOU 4596  N   TYR I 106     4687   6262   5437   -419   -360   -460       N  
ATOM   4597  CA  TYR I 106      -4.361 -10.723  46.049  1.00 43.21           C  
ANISOU 4597  CA  TYR I 106     4772   6144   5501   -404   -356   -521       C  
ATOM   4598  C   TYR I 106      -4.098 -10.065  44.671  1.00 43.90           C  
ANISOU 4598  C   TYR I 106     4864   6372   5444   -325   -418   -631       C  
ATOM   4599  O   TYR I 106      -4.933  -9.349  44.139  1.00 44.20           O  
ANISOU 4599  O   TYR I 106     4817   6611   5367   -302   -477   -655       O  
ATOM   4600  CB  TYR I 106      -4.616 -12.225  45.905  1.00 44.94           C  
ANISOU 4600  CB  TYR I 106     4961   6196   5920   -540   -297   -625       C  
ATOM   4601  CG  TYR I 106      -5.941 -12.561  45.275  1.00 47.40           C  
ANISOU 4601  CG  TYR I 106     5155   6625   6231   -666   -329   -806       C  
ATOM   4602  CD1 TYR I 106      -6.024 -12.881  43.921  1.00 48.94           C  
ANISOU 4602  CD1 TYR I 106     5319   6904   6371   -728   -363  -1045       C  
ATOM   4603  CD2 TYR I 106      -7.123 -12.541  46.023  1.00 48.14           C  
ANISOU 4603  CD2 TYR I 106     5149   6782   6359   -739   -323   -746       C  
ATOM   4604  CE1 TYR I 106      -7.257 -13.180  43.307  1.00 50.73           C  
ANISOU 4604  CE1 TYR I 106     5406   7304   6563   -876   -417  -1226       C  
ATOM   4605  CE2 TYR I 106      -8.387 -12.832  45.412  1.00 50.48           C  
ANISOU 4605  CE2 TYR I 106     5300   7220   6661   -869   -367   -910       C  
ATOM   4606  CZ  TYR I 106      -8.436 -13.156  44.050  1.00 51.78           C  
ANISOU 4606  CZ  TYR I 106     5424   7493   6757   -943   -426  -1150       C  
ATOM   4607  OH  TYR I 106      -9.640 -13.490  43.435  1.00 53.95           O  
ANISOU 4607  OH  TYR I 106     5531   7956   7013  -1104   -487  -1325       O  
ATOM   4608  N   PHE I 107      -2.910 -10.279  44.116  1.00 44.20           N  
ANISOU 4608  N   PHE I 107     4983   6318   5492   -273   -395   -663       N  
ATOM   4609  CA  PHE I 107      -2.536  -9.703  42.854  1.00 43.54           C  
ANISOU 4609  CA  PHE I 107     4910   6377   5257   -202   -433   -742       C  
ATOM   4610  C   PHE I 107      -2.738 -10.804  41.848  1.00 46.38           C  
ANISOU 4610  C   PHE I 107     5245   6739   5637   -323   -413   -984       C  
ATOM   4611  O   PHE I 107      -1.964 -11.758  41.810  1.00 47.27           O  
ANISOU 4611  O   PHE I 107     5415   6634   5910   -358   -318  -1063       O  
ATOM   4612  CB  PHE I 107      -1.066  -9.299  42.883  1.00 41.93           C  
ANISOU 4612  CB  PHE I 107     4802   6069   5060    -87   -393   -648       C  
ATOM   4613  CG  PHE I 107      -0.737  -8.265  43.920  1.00 40.35           C  
ANISOU 4613  CG  PHE I 107     4627   5861   4845     -9   -397   -461       C  
ATOM   4614  CD1 PHE I 107      -1.722  -7.446  44.438  1.00 40.40           C  
ANISOU 4614  CD1 PHE I 107     4578   5976   4797     -5   -416   -406       C  
ATOM   4615  CD2 PHE I 107       0.573  -8.076  44.337  1.00 39.35           C  
ANISOU 4615  CD2 PHE I 107     4562   5626   4762     49   -366   -362       C  
ATOM   4616  CE1 PHE I 107      -1.419  -6.476  45.364  1.00 39.60           C  
ANISOU 4616  CE1 PHE I 107     4501   5860   4685     38   -384   -297       C  
ATOM   4617  CE2 PHE I 107       0.896  -7.118  45.254  1.00 38.46           C  
ANISOU 4617  CE2 PHE I 107     4464   5535   4615     78   -365   -244       C  
ATOM   4618  CZ  PHE I 107      -0.098  -6.310  45.774  1.00 38.59           C  
ANISOU 4618  CZ  PHE I 107     4444   5644   4575     65   -363   -232       C  
ATOM   4619  N   ASP I 108      -3.776 -10.677  41.025  1.00 47.80           N  
ANISOU 4619  N   ASP I 108     5322   7172   5667   -396   -492  -1106       N  
ATOM   4620  CA  ASP I 108      -4.188 -11.772  40.189  1.00 48.79           C  
ANISOU 4620  CA  ASP I 108     5401   7334   5801   -575   -473  -1391       C  
ATOM   4621  C   ASP I 108      -3.635 -11.619  38.795  1.00 50.28           C  
ANISOU 4621  C   ASP I 108     5611   7718   5775   -569   -483  -1545       C  
ATOM   4622  O   ASP I 108      -3.622 -12.576  38.027  1.00 52.88           O  
ANISOU 4622  O   ASP I 108     5938   8049   6107   -727   -422  -1840       O  
ATOM   4623  CB  ASP I 108      -5.712 -11.964  40.232  1.00 50.60           C  
ANISOU 4623  CB  ASP I 108     5475   7744   6008   -717   -554  -1462       C  
ATOM   4624  CG  ASP I 108      -6.495 -10.802  39.625  1.00 51.27           C  
ANISOU 4624  CG  ASP I 108     5429   8219   5833   -647   -701  -1351       C  
ATOM   4625  OD1 ASP I 108      -5.927  -9.700  39.428  1.00 50.37           O  
ANISOU 4625  OD1 ASP I 108     5354   8188   5596   -464   -725  -1163       O  
ATOM   4626  OD2 ASP I 108      -7.707 -11.005  39.348  1.00 53.01           O  
ANISOU 4626  OD2 ASP I 108     5484   8660   5998   -777   -785  -1434       O  
ATOM   4627  N   HIS I 109      -3.137 -10.424  38.483  1.00 48.87           N  
ANISOU 4627  N   HIS I 109     5456   7692   5422   -397   -534  -1355       N  
ATOM   4628  CA  HIS I 109      -2.488 -10.183  37.185  1.00 50.22           C  
ANISOU 4628  CA  HIS I 109     5653   8064   5366   -371   -527  -1448       C  
ATOM   4629  C   HIS I 109      -1.295  -9.223  37.222  1.00 48.94           C  
ANISOU 4629  C   HIS I 109     5582   7829   5186   -168   -484  -1229       C  
ATOM   4630  O   HIS I 109      -1.343  -8.131  37.796  1.00 47.35           O  
ANISOU 4630  O   HIS I 109     5365   7630   4995    -29   -525   -970       O  
ATOM   4631  CB  HIS I 109      -3.490  -9.716  36.139  1.00 52.18           C  
ANISOU 4631  CB  HIS I 109     5750   8774   5300   -430   -666  -1476       C  
ATOM   4632  CG  HIS I 109      -4.421 -10.790  35.674  1.00 55.87           C  
ANISOU 4632  CG  HIS I 109     6122   9386   5721   -683   -699  -1794       C  
ATOM   4633  ND1 HIS I 109      -5.739 -10.863  36.076  1.00 56.81           N  
ANISOU 4633  ND1 HIS I 109     6090   9624   5871   -778   -802  -1773       N  
ATOM   4634  CD2 HIS I 109      -4.221 -11.845  34.850  1.00 58.72           C  
ANISOU 4634  CD2 HIS I 109     6506   9780   6025   -882   -620  -2169       C  
ATOM   4635  CE1 HIS I 109      -6.312 -11.910  35.509  1.00 59.60           C  
ANISOU 4635  CE1 HIS I 109     6372  10091   6183  -1034   -804  -2117       C  
ATOM   4636  NE2 HIS I 109      -5.409 -12.530  34.772  1.00 60.69           N  
ANISOU 4636  NE2 HIS I 109     6620  10168   6271  -1109   -685  -2379       N  
ATOM   4637  N   TRP I 110      -0.224  -9.639  36.565  1.00 49.74           N  
ANISOU 4637  N   TRP I 110     5766   7858   5274   -165   -378  -1359       N  
ATOM   4638  CA  TRP I 110       1.006  -8.897  36.545  1.00 47.70           C  
ANISOU 4638  CA  TRP I 110     5585   7512   5028      1   -317  -1185       C  
ATOM   4639  C   TRP I 110       1.465  -8.670  35.121  1.00 49.68           C  
ANISOU 4639  C   TRP I 110     5838   8024   5014     11   -283  -1274       C  
ATOM   4640  O   TRP I 110       1.382  -9.560  34.273  1.00 52.14           O  
ANISOU 4640  O   TRP I 110     6149   8439   5222   -134   -227  -1569       O  
ATOM   4641  CB  TRP I 110       2.079  -9.723  37.223  1.00 47.52           C  
ANISOU 4641  CB  TRP I 110     5648   7113   5295     12   -184  -1224       C  
ATOM   4642  CG  TRP I 110       1.841 -10.054  38.695  1.00 46.27           C  
ANISOU 4642  CG  TRP I 110     5487   6704   5387      1   -200  -1101       C  
ATOM   4643  CD1 TRP I 110       0.866 -10.848  39.202  1.00 46.68           C  
ANISOU 4643  CD1 TRP I 110     5497   6694   5547   -127   -218  -1191       C  
ATOM   4644  CD2 TRP I 110       2.674  -9.677  39.813  1.00 44.15           C  
ANISOU 4644  CD2 TRP I 110     5253   6241   5280    103   -186   -870       C  
ATOM   4645  NE1 TRP I 110       1.013 -10.962  40.566  1.00 45.67           N  
ANISOU 4645  NE1 TRP I 110     5379   6356   5619    -97   -213  -1004       N  
ATOM   4646  CE2 TRP I 110       2.112 -10.252  40.962  1.00 43.72           C  
ANISOU 4646  CE2 TRP I 110     5176   6049   5388     34   -204   -814       C  
ATOM   4647  CE3 TRP I 110       3.843  -8.913  39.944  1.00 42.94           C  
ANISOU 4647  CE3 TRP I 110     5134   6044   5138    226   -161   -710       C  
ATOM   4648  CZ2 TRP I 110       2.671 -10.093  42.220  1.00 41.80           C  
ANISOU 4648  CZ2 TRP I 110     4940   5671   5270     80   -208   -600       C  
ATOM   4649  CZ3 TRP I 110       4.372  -8.724  41.202  1.00 41.09           C  
ANISOU 4649  CZ3 TRP I 110     4899   5669   5043    259   -176   -523       C  
ATOM   4650  CH2 TRP I 110       3.793  -9.326  42.321  1.00 40.88           C  
ANISOU 4650  CH2 TRP I 110     4849   5550   5134    184   -204   -468       C  
ATOM   4651  N   GLY I 111       1.997  -7.485  34.855  1.00 48.87           N  
ANISOU 4651  N   GLY I 111     5738   8023   4808    169   -291  -1030       N  
ATOM   4652  CA  GLY I 111       2.660  -7.244  33.578  1.00 49.82           C  
ANISOU 4652  CA  GLY I 111     5870   8367   4691    197   -226  -1067       C  
ATOM   4653  C   GLY I 111       4.014  -7.928  33.551  1.00 49.94           C  
ANISOU 4653  C   GLY I 111     5989   8106   4879    207    -49  -1205       C  
ATOM   4654  O   GLY I 111       4.452  -8.513  34.533  1.00 48.76           O  
ANISOU 4654  O   GLY I 111     5885   7605   5036    211      7  -1221       O  
ATOM   4655  N   GLN I 112       4.694  -7.872  32.422  1.00 52.07           N  
ANISOU 4655  N   GLN I 112     6279   8550   4953    216     51  -1285       N  
ATOM   4656  CA  GLN I 112       5.985  -8.534  32.349  1.00 52.60           C  
ANISOU 4656  CA  GLN I 112     6424   8349   5213    237    248  -1418       C  
ATOM   4657  C   GLN I 112       7.118  -7.600  32.799  1.00 51.11           C  
ANISOU 4657  C   GLN I 112     6254   7990   5175    421    291  -1117       C  
ATOM   4658  O   GLN I 112       8.284  -8.015  32.796  1.00 52.18           O  
ANISOU 4658  O   GLN I 112     6424   7907   5495    465    449  -1165       O  
ATOM   4659  CB  GLN I 112       6.231  -9.134  30.944  1.00 56.41           C  
ANISOU 4659  CB  GLN I 112     6924   9070   5441    124    387  -1730       C  
ATOM   4660  CG  GLN I 112       6.714 -10.639  30.937  1.00 58.72           C  
ANISOU 4660  CG  GLN I 112     7267   9051   5993      5    601  -2108       C  
ATOM   4661  CD  GLN I 112       5.618 -11.695  31.334  1.00 59.95           C  
ANISOU 4661  CD  GLN I 112     7399   9113   6267   -185    559  -2371       C  
ATOM   4662  OE1 GLN I 112       4.908 -11.563  32.340  1.00 58.41           O  
ANISOU 4662  OE1 GLN I 112     7172   8810   6212   -169    408  -2200       O  
ATOM   4663  NE2 GLN I 112       5.520 -12.751  30.548  1.00 63.36           N  
ANISOU 4663  NE2 GLN I 112     7843   9572   6658   -376    722  -2805       N  
ATOM   4664  N   GLY I 113       6.762  -6.360  33.178  1.00 48.78           N  
ANISOU 4664  N   GLY I 113     5919   7785   4829    519    170   -821       N  
ATOM   4665  CA  GLY I 113       7.680  -5.367  33.763  1.00 47.03           C  
ANISOU 4665  CA  GLY I 113     5701   7391   4777    658    200   -553       C  
ATOM   4666  C   GLY I 113       8.624  -4.570  32.857  1.00 48.30           C  
ANISOU 4666  C   GLY I 113     5857   7666   4829    758    313   -415       C  
ATOM   4667  O   GLY I 113       8.893  -4.967  31.727  1.00 50.38           O  
ANISOU 4667  O   GLY I 113     6133   8118   4890    727    409   -554       O  
ATOM   4668  N   THR I 114       9.116  -3.436  33.362  1.00 46.43           N  
ANISOU 4668  N   THR I 114     5597   7317   4726    862    318   -156       N  
ATOM   4669  CA  THR I 114      10.196  -2.667  32.725  1.00 47.49           C  
ANISOU 4669  CA  THR I 114     5719   7473   4854    957    450      1       C  
ATOM   4670  C   THR I 114      11.339  -2.483  33.708  1.00 46.25           C  
ANISOU 4670  C   THR I 114     5558   6999   5017    988    502     70       C  
ATOM   4671  O   THR I 114      11.118  -2.276  34.900  1.00 44.98           O  
ANISOU 4671  O   THR I 114     5387   6672   5031    963    411    114       O  
ATOM   4672  CB  THR I 114       9.811  -1.217  32.329  1.00 48.09           C  
ANISOU 4672  CB  THR I 114     5734   7707   4833   1054    440    301       C  
ATOM   4673  OG1 THR I 114       8.638  -0.821  33.045  1.00 47.86           O  
ANISOU 4673  OG1 THR I 114     5670   7670   4844   1047    308    372       O  
ATOM   4674  CG2 THR I 114       9.621  -1.040  30.830  1.00 50.25           C  
ANISOU 4674  CG2 THR I 114     5974   8360   4759   1081    489    368       C  
ATOM   4675  N   LEU I 115      12.548  -2.491  33.157  1.00 47.20           N  
ANISOU 4675  N   LEU I 115     5668   7080   5185   1033    651     87       N  
ATOM   4676  CA  LEU I 115      13.787  -2.374  33.874  1.00 45.95           C  
ANISOU 4676  CA  LEU I 115     5471   6679   5309   1056    710    157       C  
ATOM   4677  C   LEU I 115      14.072  -0.917  34.116  1.00 45.68           C  
ANISOU 4677  C   LEU I 115     5389   6609   5357   1101    724    389       C  
ATOM   4678  O   LEU I 115      14.075  -0.115  33.179  1.00 47.25           O  
ANISOU 4678  O   LEU I 115     5574   6952   5426   1166    812    530       O  
ATOM   4679  CB  LEU I 115      14.930  -2.914  33.013  1.00 46.80           C  
ANISOU 4679  CB  LEU I 115     5565   6780   5436   1093    897     87       C  
ATOM   4680  CG  LEU I 115      15.997  -3.759  33.724  1.00 47.14           C  
ANISOU 4680  CG  LEU I 115     5556   6572   5785   1093    950     37       C  
ATOM   4681  CD1 LEU I 115      17.384  -3.615  33.116  1.00 47.54           C  
ANISOU 4681  CD1 LEU I 115     5540   6579   5945   1161   1144     98       C  
ATOM   4682  CD2 LEU I 115      16.029  -3.503  35.244  1.00 45.07           C  
ANISOU 4682  CD2 LEU I 115     5241   6148   5734   1054    791    151       C  
ATOM   4683  N   VAL I 116      14.346  -0.574  35.362  1.00 43.46           N  
ANISOU 4683  N   VAL I 116     5073   6144   5296   1056    655    431       N  
ATOM   4684  CA  VAL I 116      14.839   0.741  35.649  1.00 43.99           C  
ANISOU 4684  CA  VAL I 116     5085   6126   5504   1066    711    593       C  
ATOM   4685  C   VAL I 116      16.214   0.512  36.246  1.00 44.52           C  
ANISOU 4685  C   VAL I 116     5076   6049   5789   1025    743    588       C  
ATOM   4686  O   VAL I 116      16.350  -0.224  37.236  1.00 44.16           O  
ANISOU 4686  O   VAL I 116     5009   5935   5836    958    636    512       O  
ATOM   4687  CB  VAL I 116      13.929   1.451  36.660  1.00 43.04           C  
ANISOU 4687  CB  VAL I 116     4968   5942   5442   1009    615    607       C  
ATOM   4688  CG1 VAL I 116      14.509   2.802  37.029  1.00 43.33           C  
ANISOU 4688  CG1 VAL I 116     4942   5841   5680    988    711    721       C  
ATOM   4689  CG2 VAL I 116      12.543   1.615  36.080  1.00 43.66           C  
ANISOU 4689  CG2 VAL I 116     5084   6173   5330   1063    577    643       C  
ATOM   4690  N   THR I 117      17.259   1.071  35.646  1.00 45.04           N  
ANISOU 4690  N   THR I 117     5080   6090   5942   1067    889    693       N  
ATOM   4691  CA  THR I 117      18.558   0.923  36.293  1.00 44.80           C  
ANISOU 4691  CA  THR I 117     4939   5944   6139   1018    902    708       C  
ATOM   4692  C   THR I 117      19.133   2.299  36.601  1.00 45.53           C  
ANISOU 4692  C   THR I 117     4951   5950   6399    961    969    816       C  
ATOM   4693  O   THR I 117      19.076   3.204  35.756  1.00 46.78           O  
ANISOU 4693  O   THR I 117     5119   6117   6539   1023   1109    933       O  
ATOM   4694  CB  THR I 117      19.520  -0.053  35.538  1.00 45.92           C  
ANISOU 4694  CB  THR I 117     5039   6092   6317   1092   1023    685       C  
ATOM   4695  OG1 THR I 117      20.728   0.598  35.176  1.00 46.99           O  
ANISOU 4695  OG1 THR I 117     5067   6184   6603   1110   1167    802       O  
ATOM   4696  CG2 THR I 117      18.899  -0.646  34.282  1.00 47.09           C  
ANISOU 4696  CG2 THR I 117     5293   6376   6222   1170   1112    596       C  
ATOM   4697  N   VAL I 118      19.569   2.497  37.840  1.00 44.07           N  
ANISOU 4697  N   VAL I 118     4681   5696   6367    830    870    777       N  
ATOM   4698  CA  VAL I 118      20.061   3.788  38.238  1.00 45.08           C  
ANISOU 4698  CA  VAL I 118     4728   5730   6669    728    940    813       C  
ATOM   4699  C   VAL I 118      21.526   3.631  38.582  1.00 46.86           C  
ANISOU 4699  C   VAL I 118     4786   5944   7074    656    946    842       C  
ATOM   4700  O   VAL I 118      21.862   2.946  39.530  1.00 47.58           O  
ANISOU 4700  O   VAL I 118     4798   6094   7185    572    792    799       O  
ATOM   4701  CB  VAL I 118      19.371   4.288  39.502  1.00 44.95           C  
ANISOU 4701  CB  VAL I 118     4729   5685   6667    577    826    694       C  
ATOM   4702  CG1 VAL I 118      19.857   5.670  39.854  1.00 46.25           C  
ANISOU 4702  CG1 VAL I 118     4810   5721   7041    447    945    677       C  
ATOM   4703  CG2 VAL I 118      17.843   4.289  39.363  1.00 44.79           C  
ANISOU 4703  CG2 VAL I 118     4847   5684   6487    644    794    663       C  
ATOM   4704  N   SER I 119      22.401   4.296  37.850  1.00 47.34           N  
ANISOU 4704  N   SER I 119     4768   5946   7274    685   1123    945       N  
ATOM   4705  CA  SER I 119      23.813   4.144  38.079  1.00 49.13           C  
ANISOU 4705  CA  SER I 119     4806   6173   7686    624   1140    990       C  
ATOM   4706  C   SER I 119      24.528   5.410  37.615  1.00 51.26           C  
ANISOU 4706  C   SER I 119     4989   6336   8152    577   1338   1072       C  
ATOM   4707  O   SER I 119      24.128   6.020  36.626  1.00 51.61           O  
ANISOU 4707  O   SER I 119     5121   6325   8164    684   1510   1168       O  
ATOM   4708  CB  SER I 119      24.317   2.908  37.320  1.00 49.49           C  
ANISOU 4708  CB  SER I 119     4833   6272   7698    782   1189   1048       C  
ATOM   4709  OG  SER I 119      25.717   2.735  37.405  1.00 50.63           O  
ANISOU 4709  OG  SER I 119     4769   6412   8054    759   1237   1129       O  
ATOM   4710  N   SER I 120      25.562   5.822  38.345  1.00 52.66           N  
ANISOU 4710  N   SER I 120     4976   6499   8534    406   1313   1048       N  
ATOM   4711  CA  SER I 120      26.369   6.952  37.923  1.00 54.86           C  
ANISOU 4711  CA  SER I 120     5142   6655   9047    341   1517   1118       C  
ATOM   4712  C   SER I 120      27.663   6.452  37.361  1.00 55.78           C  
ANISOU 4712  C   SER I 120     5092   6818   9285    407   1602   1244       C  
ATOM   4713  O   SER I 120      28.528   7.254  37.022  1.00 58.75           O  
ANISOU 4713  O   SER I 120     5334   7108   9880    346   1772   1318       O  
ATOM   4714  CB  SER I 120      26.663   7.904  39.071  1.00 56.19           C  
ANISOU 4714  CB  SER I 120     5190   6770   9390     62   1468    966       C  
ATOM   4715  OG  SER I 120      27.434   7.257  40.051  1.00 57.15           O  
ANISOU 4715  OG  SER I 120     5132   7067   9514    -81   1260    906       O  
ATOM   4716  N   ALA I 121      27.782   5.133  37.243  1.00 91.77           N  
ANISOU 4716  N   ALA I 121     9651   8174  17042   4372   5347   5263       N  
ATOM   4717  CA  ALA I 121      28.974   4.518  36.699  1.00 86.69           C  
ANISOU 4717  CA  ALA I 121     9168   7920  15849   3945   4780   4890       C  
ATOM   4718  C   ALA I 121      29.199   4.937  35.270  1.00 88.55           C  
ANISOU 4718  C   ALA I 121     9238   8419  15986   4056   4480   5315       C  
ATOM   4719  O   ALA I 121      28.273   5.006  34.471  1.00 91.87           O  
ANISOU 4719  O   ALA I 121     9206   9084  16615   4385   4271   5879       O  
ATOM   4720  CB  ALA I 121      28.857   3.034  36.759  1.00 83.79           C  
ANISOU 4720  CB  ALA I 121     8518   8072  15246   3716   4226   4652       C  
ATOM   4721  N   SER I 122      30.451   5.205  34.954  1.00 86.87           N  
ANISOU 4721  N   SER I 122     9390   8161  15456   3784   4449   5065       N  
ATOM   4722  CA  SER I 122      30.843   5.503  33.594  1.00 88.70           C  
ANISOU 4722  CA  SER I 122     9563   8661  15479   3869   4220   5440       C  
ATOM   4723  C   SER I 122      32.091   4.691  33.284  1.00 84.30           C  
ANISOU 4723  C   SER I 122     9166   8447  14416   3463   3853   5002       C  
ATOM   4724  O   SER I 122      32.654   4.073  34.178  1.00 80.32           O  
ANISOU 4724  O   SER I 122     8808   7903  13807   3131   3801   4448       O  
ATOM   4725  CB  SER I 122      31.119   6.988  33.444  1.00 93.22           C  
ANISOU 4725  CB  SER I 122    10413   8654  16353   4040   4811   5749       C  
ATOM   4726  OG  SER I 122      32.271   7.368  34.164  1.00 91.25           O  
ANISOU 4726  OG  SER I 122    10604   7965  16103   3651   5110   5240       O  
ATOM   4727  N   THR I 123      32.509   4.669  32.026  1.00 85.01           N  
ANISOU 4727  N   THR I 123     9244   8876  14180   3529   3622   5281       N  
ATOM   4728  CA  THR I 123      33.591   3.796  31.614  1.00 81.46           C  
ANISOU 4728  CA  THR I 123     8901   8790  13258   3230   3315   4930       C  
ATOM   4729  C   THR I 123      34.786   3.891  32.563  1.00 78.65           C  
ANISOU 4729  C   THR I 123     8783   8086  13013   2822   3578   4405       C  
ATOM   4730  O   THR I 123      35.318   4.966  32.816  1.00 80.54           O  
ANISOU 4730  O   THR I 123     9220   7827  13553   2746   4028   4453       O  
ATOM   4731  CB  THR I 123      34.046   4.073  30.166  1.00 84.83           C  
ANISOU 4731  CB  THR I 123     9431   9476  13323   3406   3275   5347       C  
ATOM   4732  OG1 THR I 123      32.907   4.172  29.316  1.00 89.19           O  
ANISOU 4732  OG1 THR I 123     9808  10308  13774   3810   2984   5884       O  
ATOM   4733  CG2 THR I 123      34.910   2.938  29.655  1.00 82.51           C  
ANISOU 4733  CG2 THR I 123     9218   9634  12499   3197   2935   5011       C  
ATOM   4734  N   LYS I 124      35.182   2.747  33.112  1.00 74.81           N  
ANISOU 4734  N   LYS I 124     8267   7841  12315   2549   3253   3908       N  
ATOM   4735  CA  LYS I 124      36.390   2.665  33.930  1.00 72.36           C  
ANISOU 4735  CA  LYS I 124     8128   7309  12055   2157   3338   3425       C  
ATOM   4736  C   LYS I 124      37.104   1.351  33.696  1.00 68.76           C  
ANISOU 4736  C   LYS I 124     7580   7310  11236   1974   2937   3119       C  
ATOM   4737  O   LYS I 124      36.467   0.302  33.675  1.00 66.41           O  
ANISOU 4737  O   LYS I 124     7157   7353  10720   2043   2580   3024       O  
ATOM   4738  CB  LYS I 124      36.074   2.805  35.414  1.00 71.08           C  
ANISOU 4738  CB  LYS I 124     8134   6758  12113   2030   3469   3071       C  
ATOM   4739  CG  LYS I 124      37.321   2.824  36.258  1.00 70.20           C  
ANISOU 4739  CG  LYS I 124     8229   6409  12036   1618   3451   2590       C  
ATOM   4740  CD  LYS I 124      37.010   2.855  37.736  1.00 70.70           C  
ANISOU 4740  CD  LYS I 124     8588   6131  12144   1518   3520   2204       C  
ATOM   4741  CE  LYS I 124      38.252   2.489  38.555  1.00 70.31           C  
ANISOU 4741  CE  LYS I 124     8698   6021  11996   1097   3251   1695       C  
ATOM   4742  NZ  LYS I 124      38.672   1.043  38.389  1.00 65.90           N  
ANISOU 4742  NZ  LYS I 124     7891   6010  11137   1017   2801   1546       N  
ATOM   4743  N   GLY I 125      38.425   1.414  33.512  1.00 69.15           N  
ANISOU 4743  N   GLY I 125     7659   7324  11289   1745   3024   2989       N  
ATOM   4744  CA  GLY I 125      39.240   0.202  33.344  1.00 66.58           C  
ANISOU 4744  CA  GLY I 125     7239   7367  10690   1602   2732   2708       C  
ATOM   4745  C   GLY I 125      39.571  -0.448  34.678  1.00 62.89           C  
ANISOU 4745  C   GLY I 125     6787   6812  10298   1328   2510   2218       C  
ATOM   4746  O   GLY I 125      39.771   0.238  35.669  1.00 63.76           O  
ANISOU 4746  O   GLY I 125     7028   6522  10675   1138   2633   2041       O  
ATOM   4747  N   PRO I 126      39.661  -1.780  34.708  1.00 60.03           N  
ANISOU 4747  N   PRO I 126     6344   6797   9669   1314   2174   1991       N  
ATOM   4748  CA  PRO I 126      39.916  -2.508  35.959  1.00 58.21           C  
ANISOU 4748  CA  PRO I 126     6152   6515   9451   1111   1943   1588       C  
ATOM   4749  C   PRO I 126      41.325  -2.361  36.532  1.00 59.06           C  
ANISOU 4749  C   PRO I 126     6220   6468   9750    814   1910   1358       C  
ATOM   4750  O   PRO I 126      42.291  -2.111  35.794  1.00 60.51           O  
ANISOU 4750  O   PRO I 126     6235   6692  10065    758   2045   1491       O  
ATOM   4751  CB  PRO I 126      39.718  -3.968  35.554  1.00 55.96           C  
ANISOU 4751  CB  PRO I 126     5772   6625   8866   1209   1635   1488       C  
ATOM   4752  CG  PRO I 126      40.150  -3.999  34.117  1.00 57.75           C  
ANISOU 4752  CG  PRO I 126     5939   7092   8912   1353   1717   1709       C  
ATOM   4753  CD  PRO I 126      39.680  -2.671  33.536  1.00 60.47           C  
ANISOU 4753  CD  PRO I 126     6333   7274   9368   1488   2012   2091       C  
ATOM   4754  N   SER I 127      41.425  -2.530  37.848  1.00 58.38           N  
ANISOU 4754  N   SER I 127     6285   6209   9688    636   1725   1043       N  
ATOM   4755  CA  SER I 127      42.706  -2.796  38.504  1.00 59.35           C  
ANISOU 4755  CA  SER I 127     6323   6295   9931    358   1476    788       C  
ATOM   4756  C   SER I 127      42.832  -4.304  38.573  1.00 56.99           C  
ANISOU 4756  C   SER I 127     5912   6351   9392    452   1189    671       C  
ATOM   4757  O   SER I 127      41.848  -4.983  38.877  1.00 55.77           O  
ANISOU 4757  O   SER I 127     5900   6289   9002    604   1122    630       O  
ATOM   4758  CB  SER I 127      42.714  -2.256  39.928  1.00 60.80           C  
ANISOU 4758  CB  SER I 127     6840   6117  10143    144   1347    492       C  
ATOM   4759  OG  SER I 127      42.349  -0.888  39.947  1.00 64.52           O  
ANISOU 4759  OG  SER I 127     7522   6175  10817    101   1665    567       O  
ATOM   4760  N   VAL I 128      44.020  -4.830  38.311  1.00 56.85           N  
ANISOU 4760  N   VAL I 128     5615   6489   9497    370   1059    644       N  
ATOM   4761  CA  VAL I 128      44.215  -6.275  38.292  1.00 55.55           C  
ANISOU 4761  CA  VAL I 128     5349   6608   9148    498    844    555       C  
ATOM   4762  C   VAL I 128      45.228  -6.716  39.353  1.00 56.80           C  
ANISOU 4762  C   VAL I 128     5408   6738   9435    316    486    361       C  
ATOM   4763  O   VAL I 128      46.365  -6.246  39.381  1.00 60.35           O  
ANISOU 4763  O   VAL I 128     5581   7114  10235    121    422    383       O  
ATOM   4764  CB  VAL I 128      44.658  -6.762  36.888  1.00 56.51           C  
ANISOU 4764  CB  VAL I 128     5250   6977   9245    690   1052    738       C  
ATOM   4765  CG1 VAL I 128      45.081  -8.231  36.923  1.00 55.26           C  
ANISOU 4765  CG1 VAL I 128     5000   7021   8974    815    868    615       C  
ATOM   4766  CG2 VAL I 128      43.532  -6.517  35.879  1.00 55.43           C  
ANISOU 4766  CG2 VAL I 128     5285   6927   8848    900   1256    918       C  
ATOM   4767  N   PHE I 129      44.810  -7.613  40.235  1.00 55.08           N  
ANISOU 4767  N   PHE I 129     5392   6567   8968    379    237    208       N  
ATOM   4768  CA  PHE I 129      45.658  -8.038  41.339  1.00 56.95           C  
ANISOU 4768  CA  PHE I 129     5612   6788   9238    248   -169     57       C  
ATOM   4769  C   PHE I 129      45.865  -9.539  41.236  1.00 55.91           C  
ANISOU 4769  C   PHE I 129     5349   6880   9013    462   -287     83       C  
ATOM   4770  O   PHE I 129      45.009 -10.235  40.722  1.00 54.56           O  
ANISOU 4770  O   PHE I 129     5282   6793   8654    658   -112    119       O  
ATOM   4771  CB  PHE I 129      45.043  -7.658  42.691  1.00 56.91           C  
ANISOU 4771  CB  PHE I 129     6097   6566   8960    152   -335   -131       C  
ATOM   4772  CG  PHE I 129      44.849  -6.177  42.872  1.00 59.91           C  
ANISOU 4772  CG  PHE I 129     6691   6636   9438    -46   -192   -203       C  
ATOM   4773  CD1 PHE I 129      45.944  -5.314  42.948  1.00 63.72           C  
ANISOU 4773  CD1 PHE I 129     6984   6960  10267   -354   -382   -272       C  
ATOM   4774  CD2 PHE I 129      43.561  -5.629  42.958  1.00 58.98           C  
ANISOU 4774  CD2 PHE I 129     6930   6337   9142     75    157   -182       C  
ATOM   4775  CE1 PHE I 129      45.763  -3.937  43.107  1.00 66.07           C  
ANISOU 4775  CE1 PHE I 129     7522   6885  10697   -556   -227   -359       C  
ATOM   4776  CE2 PHE I 129      43.372  -4.251  43.121  1.00 61.19           C  
ANISOU 4776  CE2 PHE I 129     7446   6263   9540    -66    353   -242       C  
ATOM   4777  CZ  PHE I 129      44.478  -3.403  43.186  1.00 64.68           C  
ANISOU 4777  CZ  PHE I 129     7770   6511  10296   -391    163   -350       C  
ATOM   4778  N   PRO I 130      47.021 -10.045  41.697  1.00 58.48           N  
ANISOU 4778  N   PRO I 130     5420   7277   9523    420   -605     77       N  
ATOM   4779  CA  PRO I 130      47.308 -11.469  41.651  1.00 57.34           C  
ANISOU 4779  CA  PRO I 130     5155   7285   9346    657   -688    128       C  
ATOM   4780  C   PRO I 130      46.721 -12.192  42.849  1.00 56.34           C  
ANISOU 4780  C   PRO I 130     5417   7108   8881    724   -939     46       C  
ATOM   4781  O   PRO I 130      46.898 -11.741  43.981  1.00 58.18           O  
ANISOU 4781  O   PRO I 130     5870   7252   8984    572  -1264    -42       O  
ATOM   4782  CB  PRO I 130      48.845 -11.511  41.744  1.00 60.87           C  
ANISOU 4782  CB  PRO I 130     5100   7802  10228    589   -932    225       C  
ATOM   4783  CG  PRO I 130      49.182 -10.362  42.562  1.00 63.71           C  
ANISOU 4783  CG  PRO I 130     5501   8018  10687    249  -1255    126       C  
ATOM   4784  CD  PRO I 130      48.190  -9.281  42.172  1.00 62.45           C  
ANISOU 4784  CD  PRO I 130     5658   7698  10371    144   -909     56       C  
ATOM   4785  N   LEU I 131      46.041 -13.307  42.605  1.00 53.91           N  
ANISOU 4785  N   LEU I 131     5232   6828   8422    946   -786     76       N  
ATOM   4786  CA  LEU I 131      45.660 -14.195  43.698  1.00 55.30           C  
ANISOU 4786  CA  LEU I 131     5716   6940   8356   1051   -964     82       C  
ATOM   4787  C   LEU I 131      46.707 -15.306  43.878  1.00 57.83           C  
ANISOU 4787  C   LEU I 131     5792   7339   8840   1228  -1193    189       C  
ATOM   4788  O   LEU I 131      46.791 -16.276  43.106  1.00 56.65           O  
ANISOU 4788  O   LEU I 131     5486   7204   8834   1427   -999    237       O  
ATOM   4789  CB  LEU I 131      44.248 -14.745  43.515  1.00 52.71           C  
ANISOU 4789  CB  LEU I 131     5649   6517   7863   1149   -675     86       C  
ATOM   4790  CG  LEU I 131      43.187 -13.649  43.349  1.00 51.61           C  
ANISOU 4790  CG  LEU I 131     5673   6298   7638   1028   -437     51       C  
ATOM   4791  CD1 LEU I 131      41.828 -14.221  42.938  1.00 49.41           C  
ANISOU 4791  CD1 LEU I 131     5467   5952   7354   1109   -189    105       C  
ATOM   4792  CD2 LEU I 131      43.078 -12.790  44.621  1.00 52.93           C  
ANISOU 4792  CD2 LEU I 131     6206   6329   7577    921   -531     -6       C  
ATOM   4793  N   ALA I 132      47.533 -15.125  44.902  1.00 61.29           N  
ANISOU 4793  N   ALA I 132     6218   7808   9262   1161  -1631    222       N  
ATOM   4794  CA  ALA I 132      48.702 -15.962  45.083  1.00 64.82           C  
ANISOU 4794  CA  ALA I 132     6312   8350   9966   1328  -1915    386       C  
ATOM   4795  C   ALA I 132      48.333 -17.378  45.520  1.00 65.33           C  
ANISOU 4795  C   ALA I 132     6612   8339   9869   1623  -1878    510       C  
ATOM   4796  O   ALA I 132      47.446 -17.558  46.363  1.00 64.87           O  
ANISOU 4796  O   ALA I 132     7055   8172   9419   1635  -1877    501       O  
ATOM   4797  CB  ALA I 132      49.682 -15.323  46.060  1.00 68.83           C  
ANISOU 4797  CB  ALA I 132     6706   8925  10521   1141  -2520    399       C  
ATOM   4798  N   PRO I 133      49.003 -18.386  44.925  1.00 66.76           N  
ANISOU 4798  N   PRO I 133     6448   8533  10383   1881  -1768    649       N  
ATOM   4799  CA  PRO I 133      48.787 -19.736  45.377  1.00 67.60           C  
ANISOU 4799  CA  PRO I 133     6764   8507  10415   2165  -1742    794       C  
ATOM   4800  C   PRO I 133      49.445 -19.876  46.732  1.00 72.55           C  
ANISOU 4800  C   PRO I 133     7463   9203  10901   2235  -2293    993       C  
ATOM   4801  O   PRO I 133      50.667 -19.742  46.860  1.00 76.26           O  
ANISOU 4801  O   PRO I 133     7474   9821  11678   2268  -2667   1131       O  
ATOM   4802  CB  PRO I 133      49.516 -20.581  44.337  1.00 68.83           C  
ANISOU 4802  CB  PRO I 133     6518   8630  11005   2432  -1469    870       C  
ATOM   4803  CG  PRO I 133      50.523 -19.692  43.726  1.00 70.33           C  
ANISOU 4803  CG  PRO I 133     6180   9004  11538   2327  -1505    881       C  
ATOM   4804  CD  PRO I 133      50.079 -18.289  43.918  1.00 68.20           C  
ANISOU 4804  CD  PRO I 133     6042   8817  11053   1949  -1637    715       C  
ATOM   4805  N   SER I 134      48.616 -20.086  47.746  1.00 73.23           N  
ANISOU 4805  N   SER I 134     8122   9183  10520   2251  -2350   1027       N  
ATOM   4806  CA  SER I 134      49.088 -20.298  49.114  1.00 78.29           C  
ANISOU 4806  CA  SER I 134     9020   9881  10847   2363  -2876   1231       C  
ATOM   4807  C   SER I 134      49.126 -21.784  49.405  1.00 80.01           C  
ANISOU 4807  C   SER I 134     9322   9949  11129   2751  -2774   1540       C  
ATOM   4808  O   SER I 134      48.180 -22.497  49.098  1.00 77.33           O  
ANISOU 4808  O   SER I 134     9221   9372  10789   2838  -2275   1541       O  
ATOM   4809  CB  SER I 134      48.149 -19.613  50.107  1.00 78.45           C  
ANISOU 4809  CB  SER I 134     9739   9839  10231   2207  -2903   1114       C  
ATOM   4810  OG  SER I 134      46.823 -19.567  49.585  1.00 74.57           O  
ANISOU 4810  OG  SER I 134     9468   9168   9696   2137  -2281    987       O  
ATOM   4811  N   SER I 135      50.212 -22.248  50.008  1.00 85.70           N  
ANISOU 4811  N   SER I 135     9829  10782  11950   2974  -3271   1825       N  
ATOM   4812  CA  SER I 135      50.347 -23.667  50.313  1.00 88.93           C  
ANISOU 4812  CA  SER I 135    10308  11018  12465   3393  -3176   2181       C  
ATOM   4813  C   SER I 135      49.314 -24.124  51.354  1.00 89.96           C  
ANISOU 4813  C   SER I 135    11213  10957  12012   3493  -3029   2328       C  
ATOM   4814  O   SER I 135      48.223 -24.627  50.993  1.00 87.26           O  
ANISOU 4814  O   SER I 135    11125  10331  11697   3487  -2424   2270       O  
ATOM   4815  CB  SER I 135      51.703 -23.932  50.914  1.00 95.33           C  
ANISOU 4815  CB  SER I 135    10741  12023  13456   3626  -3836   2518       C  
ATOM   4816  OG  SER I 135      51.504 -24.205  52.283  1.00 99.60           O  
ANISOU 4816  OG  SER I 135    11886  12571  13387   3775  -4217   2766       O  
ATOM   4817  N   GLY I 141      47.099 -32.591  45.832  1.00 86.29           N  
ANISOU 4817  N   GLY I 141    10895   7294  14595   4589    485   2043       N  
ATOM   4818  CA  GLY I 141      48.466 -32.359  45.359  1.00 90.13           C  
ANISOU 4818  CA  GLY I 141    10962   8055  15229   4902    388   2070       C  
ATOM   4819  C   GLY I 141      48.527 -31.427  44.155  1.00 87.45           C  
ANISOU 4819  C   GLY I 141    10413   8013  14800   4653    432   1601       C  
ATOM   4820  O   GLY I 141      49.240 -31.672  43.182  1.00 90.11           O  
ANISOU 4820  O   GLY I 141    10588   8273  15377   4879    688   1440       O  
ATOM   4821  N   THR I 142      47.811 -30.318  44.262  1.00 83.90           N  
ANISOU 4821  N   THR I 142     9987   7903  13989   4232    222   1431       N  
ATOM   4822  CA  THR I 142      47.511 -29.419  43.154  1.00 80.02           C  
ANISOU 4822  CA  THR I 142     9413   7640  13351   3936    281   1004       C  
ATOM   4823  C   THR I 142      47.116 -28.085  43.805  1.00 75.83           C  
ANISOU 4823  C   THR I 142     8806   7548  12459   3611    -50   1045       C  
ATOM   4824  O   THR I 142      46.496 -28.078  44.860  1.00 76.42           O  
ANISOU 4824  O   THR I 142     9097   7586  12352   3517   -177   1244       O  
ATOM   4825  CB  THR I 142      46.308 -29.960  42.332  1.00 79.22           C  
ANISOU 4825  CB  THR I 142     9684   7147  13269   3683    527    618       C  
ATOM   4826  OG1 THR I 142      45.189 -29.080  42.456  1.00 75.03           O  
ANISOU 4826  OG1 THR I 142     9218   6813  12479   3253    372    494       O  
ATOM   4827  CG2 THR I 142      45.859 -31.301  42.862  1.00 83.64           C  
ANISOU 4827  CG2 THR I 142    10544   7139  14097   3795    694    773       C  
ATOM   4828  N   ALA I 143      47.457 -26.961  43.193  1.00 72.81           N  
ANISOU 4828  N   ALA I 143     8163   7533  11968   3459   -130    872       N  
ATOM   4829  CA  ALA I 143      47.244 -25.669  43.843  1.00 70.23           C  
ANISOU 4829  CA  ALA I 143     7775   7566  11342   3185   -434    910       C  
ATOM   4830  C   ALA I 143      46.395 -24.709  42.995  1.00 66.06           C  
ANISOU 4830  C   ALA I 143     7295   7170  10637   2845   -330    591       C  
ATOM   4831  O   ALA I 143      46.328 -24.863  41.785  1.00 65.94           O  
ANISOU 4831  O   ALA I 143     7268   7091  10697   2849   -100    351       O  
ATOM   4832  CB  ALA I 143      48.593 -25.041  44.188  1.00 72.26           C  
ANISOU 4832  CB  ALA I 143     7608   8149  11699   3305   -739   1105       C  
ATOM   4833  N   ALA I 144      45.748 -23.729  43.624  1.00 63.17           N  
ANISOU 4833  N   ALA I 144     7027   6969  10007   2588   -486    601       N  
ATOM   4834  CA  ALA I 144      44.882 -22.799  42.895  1.00 59.45           C  
ANISOU 4834  CA  ALA I 144     6581   6605   9403   2304   -389    371       C  
ATOM   4835  C   ALA I 144      45.399 -21.365  42.966  1.00 58.38           C  
ANISOU 4835  C   ALA I 144     6244   6789   9147   2163   -553    362       C  
ATOM   4836  O   ALA I 144      45.853 -20.909  44.028  1.00 59.95           O  
ANISOU 4836  O   ALA I 144     6452   7094   9234   2147   -817    505       O  
ATOM   4837  CB  ALA I 144      43.497 -22.868  43.424  1.00 57.99           C  
ANISOU 4837  CB  ALA I 144     6667   6250   9116   2130   -312    393       C  
ATOM   4838  N   LEU I 145      45.356 -20.665  41.835  1.00 56.21           N  
ANISOU 4838  N   LEU I 145     5832   6643   8884   2059   -416    196       N  
ATOM   4839  CA  LEU I 145      45.862 -19.298  41.761  1.00 55.94           C  
ANISOU 4839  CA  LEU I 145     5590   6844   8823   1910   -505    200       C  
ATOM   4840  C   LEU I 145      45.064 -18.542  40.724  1.00 53.71           C  
ANISOU 4840  C   LEU I 145     5355   6619   8434   1760   -309     57       C  
ATOM   4841  O   LEU I 145      44.414 -19.163  39.873  1.00 52.79           O  
ANISOU 4841  O   LEU I 145     5370   6411   8279   1803   -161    -64       O  
ATOM   4842  CB  LEU I 145      47.346 -19.278  41.403  1.00 58.98           C  
ANISOU 4842  CB  LEU I 145     5572   7352   9485   2059   -523    294       C  
ATOM   4843  CG  LEU I 145      47.692 -19.876  40.040  1.00 60.34           C  
ANISOU 4843  CG  LEU I 145     5653   7485   9787   2270   -162    217       C  
ATOM   4844  CD1 LEU I 145      47.586 -18.806  38.946  1.00 59.38           C  
ANISOU 4844  CD1 LEU I 145     5468   7511   9583   2148     61    135       C  
ATOM   4845  CD2 LEU I 145      49.071 -20.524  40.041  1.00 63.72           C  
ANISOU 4845  CD2 LEU I 145     5721   7910  10578   2563   -113    395       C  
ATOM   4846  N   GLY I 146      45.100 -17.208  40.787  1.00 52.61           N  
ANISOU 4846  N   GLY I 146     5134   6606   8248   1583   -342     72       N  
ATOM   4847  CA  GLY I 146      44.254 -16.427  39.898  1.00 50.98           C  
ANISOU 4847  CA  GLY I 146     4989   6447   7933   1473   -171      8       C  
ATOM   4848  C   GLY I 146      44.524 -14.957  39.774  1.00 50.70           C  
ANISOU 4848  C   GLY I 146     4833   6506   7924   1321   -132     56       C  
ATOM   4849  O   GLY I 146      45.595 -14.470  40.131  1.00 52.77           O  
ANISOU 4849  O   GLY I 146     4883   6812   8355   1266   -230    111       O  
ATOM   4850  N   CYS I 147      43.549 -14.262  39.210  1.00 49.58           N  
ANISOU 4850  N   CYS I 147     4795   6372   7671   1250      0     56       N  
ATOM   4851  CA  CYS I 147      43.576 -12.812  39.145  1.00 49.86           C  
ANISOU 4851  CA  CYS I 147     4781   6416   7745   1112     87    124       C  
ATOM   4852  C   CYS I 147      42.273 -12.236  39.598  1.00 49.11           C  
ANISOU 4852  C   CYS I 147     4892   6213   7556   1039    130    148       C  
ATOM   4853  O   CYS I 147      41.206 -12.818  39.363  1.00 49.24           O  
ANISOU 4853  O   CYS I 147     4985   6213   7510   1097    146    156       O  
ATOM   4854  CB  CYS I 147      43.903 -12.339  37.747  1.00 50.76           C  
ANISOU 4854  CB  CYS I 147     4766   6651   7871   1180    316    202       C  
ATOM   4855  SG  CYS I 147      45.642 -12.556  37.533  1.00 54.04           S  
ANISOU 4855  SG  CYS I 147     4847   7132   8554   1243    385    257       S  
ATOM   4856  N   LEU I 148      42.366 -11.122  40.309  1.00 49.25           N  
ANISOU 4856  N   LEU I 148     4990   6116   7608    908    149    158       N  
ATOM   4857  CA  LEU I 148      41.182 -10.387  40.722  1.00 48.72           C  
ANISOU 4857  CA  LEU I 148     5123   5898   7490    888    305    210       C  
ATOM   4858  C   LEU I 148      41.156  -9.188  39.814  1.00 49.55           C  
ANISOU 4858  C   LEU I 148     5125   6001   7699    862    496    324       C  
ATOM   4859  O   LEU I 148      42.087  -8.373  39.853  1.00 51.05           O  
ANISOU 4859  O   LEU I 148     5258   6127   8013    735    506    305       O  
ATOM   4860  CB  LEU I 148      41.347  -9.949  42.165  1.00 49.60           C  
ANISOU 4860  CB  LEU I 148     5525   5818   7505    793    237    111       C  
ATOM   4861  CG  LEU I 148      40.482  -8.817  42.641  1.00 50.35           C  
ANISOU 4861  CG  LEU I 148     5878   5679   7572    777    492    138       C  
ATOM   4862  CD1 LEU I 148      39.033  -9.245  42.488  1.00 49.77           C  
ANISOU 4862  CD1 LEU I 148     5791   5590   7528    939    724    299       C  
ATOM   4863  CD2 LEU I 148      40.856  -8.572  44.089  1.00 52.21           C  
ANISOU 4863  CD2 LEU I 148     6526   5727   7587    693    366    -35       C  
ATOM   4864  N   VAL I 149      40.164  -9.125  38.929  1.00 48.43           N  
ANISOU 4864  N   VAL I 149     4928   5931   7543    977    614    467       N  
ATOM   4865  CA  VAL I 149      39.992  -7.929  38.123  1.00 49.53           C  
ANISOU 4865  CA  VAL I 149     5017   6047   7754   1004    817    649       C  
ATOM   4866  C   VAL I 149      38.901  -7.086  38.758  1.00 49.96           C  
ANISOU 4866  C   VAL I 149     5206   5874   7902   1034   1005    753       C  
ATOM   4867  O   VAL I 149      37.741  -7.489  38.844  1.00 50.05           O  
ANISOU 4867  O   VAL I 149     5185   5893   7938   1137   1016    847       O  
ATOM   4868  CB  VAL I 149      39.679  -8.251  36.684  1.00 50.31           C  
ANISOU 4868  CB  VAL I 149     5009   6379   7729   1149    794    783       C  
ATOM   4869  CG1 VAL I 149      40.308  -9.594  36.318  1.00 49.78           C  
ANISOU 4869  CG1 VAL I 149     4912   6482   7520   1183    618    612       C  
ATOM   4870  CG2 VAL I 149      38.158  -8.283  36.465  1.00 51.11           C  
ANISOU 4870  CG2 VAL I 149     5084   6495   7842   1249    744    934       C  
ATOM   4871  N   LYS I 150      39.295  -5.920  39.234  1.00 51.30           N  
ANISOU 4871  N   LYS I 150     5514   5799   8178    939   1176    737       N  
ATOM   4872  CA  LYS I 150      38.503  -5.196  40.204  1.00 53.18           C  
ANISOU 4872  CA  LYS I 150     6009   5726   8469    970   1404    738       C  
ATOM   4873  C   LYS I 150      38.019  -3.844  39.639  1.00 55.56           C  
ANISOU 4873  C   LYS I 150     6308   5831   8970   1064   1726    980       C  
ATOM   4874  O   LYS I 150      38.772  -3.143  38.954  1.00 57.07           O  
ANISOU 4874  O   LYS I 150     6424   5995   9264    985   1777   1051       O  
ATOM   4875  CB  LYS I 150      39.358  -5.046  41.477  1.00 54.09           C  
ANISOU 4875  CB  LYS I 150     6436   5636   8481    775   1289    438       C  
ATOM   4876  CG  LYS I 150      38.760  -4.300  42.650  1.00 56.84           C  
ANISOU 4876  CG  LYS I 150     7234   5605   8757    802   1540    339       C  
ATOM   4877  CD  LYS I 150      37.874  -5.175  43.489  1.00 56.81           C  
ANISOU 4877  CD  LYS I 150     7403   5612   8569    963   1626    346       C  
ATOM   4878  CE  LYS I 150      37.255  -4.342  44.608  1.00 61.19           C  
ANISOU 4878  CE  LYS I 150     8486   5754   9011   1057   2009    269       C  
ATOM   4879  NZ  LYS I 150      36.248  -5.094  45.391  1.00 60.83           N  
ANISOU 4879  NZ  LYS I 150     8598   5674   8839   1270   2264    373       N  
ATOM   4880  N   ASP I 151      36.743  -3.539  39.874  1.00 55.97           N  
ANISOU 4880  N   ASP I 151     6396   5742   9127   1262   1977   1164       N  
ATOM   4881  CA  ASP I 151      36.134  -2.221  39.604  1.00 58.72           C  
ANISOU 4881  CA  ASP I 151     6788   5812   9711   1417   2351   1423       C  
ATOM   4882  C   ASP I 151      36.112  -1.714  38.161  1.00 59.64           C  
ANISOU 4882  C   ASP I 151     6643   6091   9926   1531   2354   1764       C  
ATOM   4883  O   ASP I 151      36.653  -0.638  37.874  1.00 61.52           O  
ANISOU 4883  O   ASP I 151     6983   6096  10294   1488   2566   1845       O  
ATOM   4884  CB  ASP I 151      36.781  -1.150  40.475  1.00 61.86           C  
ANISOU 4884  CB  ASP I 151     7598   5754  10151   1261   2571   1193       C  
ATOM   4885  CG  ASP I 151      36.399  -1.261  41.943  1.00 63.77           C  
ANISOU 4885  CG  ASP I 151     8266   5722  10242   1275   2723    942       C  
ATOM   4886  OD1 ASP I 151      35.357  -1.887  42.261  1.00 64.11           O  
ANISOU 4886  OD1 ASP I 151     8240   5842  10277   1485   2858   1079       O  
ATOM   4887  OD2 ASP I 151      37.140  -0.697  42.777  1.00 65.43           O  
ANISOU 4887  OD2 ASP I 151     8901   5617  10344   1073   2712    619       O  
ATOM   4888  N   TYR I 152      35.473  -2.452  37.259  1.00 58.90           N  
ANISOU 4888  N   TYR I 152     6253   6363   9763   1675   2117   1972       N  
ATOM   4889  CA  TYR I 152      35.407  -2.022  35.860  1.00 60.77           C  
ANISOU 4889  CA  TYR I 152     6335   6793   9963   1827   2072   2313       C  
ATOM   4890  C   TYR I 152      33.954  -1.728  35.421  1.00 63.10           C  
ANISOU 4890  C   TYR I 152     6394   7127  10454   2119   2087   2732       C  
ATOM   4891  O   TYR I 152      33.016  -2.168  36.078  1.00 63.26           O  
ANISOU 4891  O   TYR I 152     6270   7104  10661   2174   2080   2739       O  
ATOM   4892  CB  TYR I 152      36.105  -3.043  34.945  1.00 58.57           C  
ANISOU 4892  CB  TYR I 152     5987   6922   9346   1754   1715   2196       C  
ATOM   4893  CG  TYR I 152      35.421  -4.383  34.919  1.00 57.76           C  
ANISOU 4893  CG  TYR I 152     5736   7083   9126   1755   1332   2078       C  
ATOM   4894  CD1 TYR I 152      34.343  -4.616  34.080  1.00 59.49           C  
ANISOU 4894  CD1 TYR I 152     5756   7519   9330   1920   1068   2338       C  
ATOM   4895  CD2 TYR I 152      35.833  -5.412  35.755  1.00 55.67           C  
ANISOU 4895  CD2 TYR I 152     5522   6822   8808   1577   1202   1723       C  
ATOM   4896  CE1 TYR I 152      33.713  -5.829  34.056  1.00 59.97           C  
ANISOU 4896  CE1 TYR I 152     5660   7757   9370   1857    685   2211       C  
ATOM   4897  CE2 TYR I 152      35.194  -6.646  35.741  1.00 54.86           C  
ANISOU 4897  CE2 TYR I 152     5289   6885   8672   1556    891   1629       C  
ATOM   4898  CZ  TYR I 152      34.139  -6.849  34.882  1.00 57.65           C  
ANISOU 4898  CZ  TYR I 152     5431   7415   9058   1669    632   1854       C  
ATOM   4899  OH  TYR I 152      33.484  -8.075  34.858  1.00 59.00           O  
ANISOU 4899  OH  TYR I 152     5447   7692   9281   1586    283   1743       O  
ATOM   4900  N   PHE I 153      33.794  -0.946  34.354  1.00 65.78           N  
ANISOU 4900  N   PHE I 153     6677   7525  10792   2319   2137   3124       N  
ATOM   4901  CA  PHE I 153      32.502  -0.696  33.725  1.00 69.50           C  
ANISOU 4901  CA  PHE I 153     6861   8112  11433   2619   2021   3591       C  
ATOM   4902  C   PHE I 153      32.716  -0.131  32.327  1.00 72.55           C  
ANISOU 4902  C   PHE I 153     7292   8696  11577   2808   1931   3967       C  
ATOM   4903  O   PHE I 153      33.569   0.727  32.116  1.00 72.14           O  
ANISOU 4903  O   PHE I 153     7475   8437  11497   2800   2283   4039       O  
ATOM   4904  CB  PHE I 153      31.663   0.270  34.570  1.00 71.94           C  
ANISOU 4904  CB  PHE I 153     7120   7979  12235   2815   2503   3819       C  
ATOM   4905  CG  PHE I 153      30.325   0.623  33.970  1.00 76.11           C  
ANISOU 4905  CG  PHE I 153     7252   8596  13071   3168   2417   4385       C  
ATOM   4906  CD1 PHE I 153      29.168  -0.045  34.355  1.00 77.67           C  
ANISOU 4906  CD1 PHE I 153     7037   8885  13590   3236   2250   4491       C  
ATOM   4907  CD2 PHE I 153      30.214   1.667  33.071  1.00 80.47           C  
ANISOU 4907  CD2 PHE I 153     7808   9102  13665   3444   2533   4865       C  
ATOM   4908  CE1 PHE I 153      27.916   0.288  33.819  1.00 82.80           C  
ANISOU 4908  CE1 PHE I 153     7204   9619  14636   3558   2121   5063       C  
ATOM   4909  CE2 PHE I 153      28.971   2.014  32.525  1.00 86.03           C  
ANISOU 4909  CE2 PHE I 153     8101   9901  14686   3805   2397   5448       C  
ATOM   4910  CZ  PHE I 153      27.817   1.313  32.899  1.00 86.98           C  
ANISOU 4910  CZ  PHE I 153     7734  10147  15169   3854   2157   5542       C  
ATOM   4911  N   PRO I 154      31.935  -0.617  31.360  1.00 75.46           N  
ANISOU 4911  N   PRO I 154     7453   9452  11766   2972   1441   4223       N  
ATOM   4912  CA  PRO I 154      30.933  -1.653  31.584  1.00 75.08           C  
ANISOU 4912  CA  PRO I 154     7065   9607  11856   2917    985   4140       C  
ATOM   4913  C   PRO I 154      31.476  -3.054  31.287  1.00 72.20           C  
ANISOU 4913  C   PRO I 154     6818   9555  11057   2659    525   3685       C  
ATOM   4914  O   PRO I 154      32.644  -3.200  31.018  1.00 69.36           O  
ANISOU 4914  O   PRO I 154     6785   9247  10322   2556    629   3440       O  
ATOM   4915  CB  PRO I 154      29.865  -1.300  30.560  1.00 80.36           C  
ANISOU 4915  CB  PRO I 154     7454  10507  12573   3218    611   4688       C  
ATOM   4916  CG  PRO I 154      30.652  -0.711  29.391  1.00 82.46           C  
ANISOU 4916  CG  PRO I 154     8096  10924  12311   3370    636   4889       C  
ATOM   4917  CD  PRO I 154      31.922  -0.113  29.971  1.00 79.27           C  
ANISOU 4917  CD  PRO I 154     8031  10171  11918   3230   1286   4657       C  
ATOM   4918  N   GLU I 155      30.609  -4.057  31.378  1.00 73.60           N  
ANISOU 4918  N   GLU I 155     6701   9888  11376   2562     66   3597       N  
ATOM   4919  CA  GLU I 155      30.837  -5.414  30.888  1.00 73.39           C  
ANISOU 4919  CA  GLU I 155     6772  10135  10977   2356   -466   3224       C  
ATOM   4920  C   GLU I 155      31.155  -5.325  29.369  1.00 76.96           C  
ANISOU 4920  C   GLU I 155     7524  10920  10797   2506   -821   3340       C  
ATOM   4921  O   GLU I 155      30.691  -4.404  28.692  1.00 80.85           O  
ANISOU 4921  O   GLU I 155     7966  11494  11261   2770   -860   3808       O  
ATOM   4922  CB  GLU I 155      29.527  -6.200  31.116  1.00 76.03           C  
ANISOU 4922  CB  GLU I 155     6629  10514  11747   2255   -917   3282       C  
ATOM   4923  CG  GLU I 155      29.647  -7.703  31.176  1.00 76.06           C  
ANISOU 4923  CG  GLU I 155     6678  10593  11627   1959  -1321   2823       C  
ATOM   4924  CD  GLU I 155      29.979  -8.175  32.568  1.00 72.36           C  
ANISOU 4924  CD  GLU I 155     6205   9834  11454   1792   -882   2557       C  
ATOM   4925  OE1 GLU I 155      29.407  -7.576  33.506  1.00 72.79           O  
ANISOU 4925  OE1 GLU I 155     6012   9648  11999   1879   -461   2798       O  
ATOM   4926  OE2 GLU I 155      30.802  -9.125  32.732  1.00 70.09           O  
ANISOU 4926  OE2 GLU I 155     6195   9543  10892   1613   -929   2134       O  
ATOM   4927  N   PRO I 156      31.919  -6.288  28.811  1.00 75.97           N  
ANISOU 4927  N   PRO I 156     7755  10975  10136   2384  -1054   2943       N  
ATOM   4928  CA  PRO I 156      32.518  -7.485  29.368  1.00 72.25           C  
ANISOU 4928  CA  PRO I 156     7392  10437   9623   2126  -1072   2422       C  
ATOM   4929  C   PRO I 156      34.015  -7.335  29.581  1.00 69.08           C  
ANISOU 4929  C   PRO I 156     7308   9939   9001   2116   -548   2216       C  
ATOM   4930  O   PRO I 156      34.575  -6.255  29.354  1.00 69.31           O  
ANISOU 4930  O   PRO I 156     7447   9916   8973   2265   -140   2474       O  
ATOM   4931  CB  PRO I 156      32.287  -8.501  28.250  1.00 76.40           C  
ANISOU 4931  CB  PRO I 156     8152  11231   9643   2091  -1723   2206       C  
ATOM   4932  CG  PRO I 156      32.468  -7.692  27.002  1.00 80.62           C  
ANISOU 4932  CG  PRO I 156     9012  12000   9621   2382  -1760   2522       C  
ATOM   4933  CD  PRO I 156      32.044  -6.272  27.340  1.00 80.71           C  
ANISOU 4933  CD  PRO I 156     8719  11893  10054   2570  -1406   3060       C  
ATOM   4934  N   VAL I 157      34.654  -8.422  30.008  1.00 66.12           N  
ANISOU 4934  N   VAL I 157     7037   9516   8570   1939   -564   1789       N  
ATOM   4935  CA  VAL I 157      36.110  -8.472  30.080  1.00 64.11           C  
ANISOU 4935  CA  VAL I 157     7014   9212   8133   1938   -159   1603       C  
ATOM   4936  C   VAL I 157      36.657  -9.860  29.716  1.00 64.55           C  
ANISOU 4936  C   VAL I 157     7313   9347   7866   1887   -351   1197       C  
ATOM   4937  O   VAL I 157      36.208 -10.865  30.262  1.00 64.11           O  
ANISOU 4937  O   VAL I 157     7159   9208   7992   1723   -625    946       O  
ATOM   4938  CB  VAL I 157      36.593  -8.139  31.486  1.00 60.08           C  
ANISOU 4938  CB  VAL I 157     6321   8430   8077   1789    198   1533       C  
ATOM   4939  CG1 VAL I 157      38.086  -8.400  31.603  1.00 58.96           C  
ANISOU 4939  CG1 VAL I 157     6304   8255   7842   1748    479   1330       C  
ATOM   4940  CG2 VAL I 157      36.326  -6.736  31.796  1.00 60.86           C  
ANISOU 4940  CG2 VAL I 157     6309   8371   8446   1854    498   1865       C  
ATOM   4941  N   THR I 158      37.636  -9.926  28.821  1.00 65.91           N  
ANISOU 4941  N   THR I 158     7814   9633   7597   2048   -135   1153       N  
ATOM   4942  CA  THR I 158      38.290 -11.199  28.563  1.00 67.25           C  
ANISOU 4942  CA  THR I 158     8241   9803   7508   2051   -176    766       C  
ATOM   4943  C   THR I 158      39.492 -11.383  29.503  1.00 63.98           C  
ANISOU 4943  C   THR I 158     7651   9219   7441   1983    236    652       C  
ATOM   4944  O   THR I 158      40.305 -10.458  29.660  1.00 63.48           O  
ANISOU 4944  O   THR I 158     7459   9119   7542   2023    653    871       O  
ATOM   4945  CB  THR I 158      38.793 -11.290  27.118  1.00 72.00           C  
ANISOU 4945  CB  THR I 158     9346  10589   7424   2318    -69    766       C  
ATOM   4946  OG1 THR I 158      39.926 -10.430  26.968  1.00 72.55           O  
ANISOU 4946  OG1 THR I 158     9397  10647   7522   2470    564   1027       O  
ATOM   4947  CG2 THR I 158      37.720 -10.863  26.152  1.00 76.45           C  
ANISOU 4947  CG2 THR I 158    10110  11360   7578   2420   -503    965       C  
ATOM   4948  N   VAL I 159      39.572 -12.547  30.153  1.00 61.55           N  
ANISOU 4948  N   VAL I 159     7307   8784   7293   1868     82    340       N  
ATOM   4949  CA  VAL I 159      40.835 -13.001  30.740  1.00 60.33           C  
ANISOU 4949  CA  VAL I 159     7064   8518   7339   1885    395    220       C  
ATOM   4950  C   VAL I 159      41.276 -14.279  30.060  1.00 63.13           C  
ANISOU 4950  C   VAL I 159     7745   8852   7390   2031    394    -78       C  
ATOM   4951  O   VAL I 159      40.474 -15.181  29.836  1.00 64.89           O  
ANISOU 4951  O   VAL I 159     8172   9021   7464   1966     20   -322       O  
ATOM   4952  CB  VAL I 159      40.725 -13.332  32.215  1.00 56.78           C  
ANISOU 4952  CB  VAL I 159     6340   7890   7342   1687    285    143       C  
ATOM   4953  CG1 VAL I 159      40.800 -12.078  33.037  1.00 55.53           C  
ANISOU 4953  CG1 VAL I 159     5935   7680   7482   1578    438    374       C  
ATOM   4954  CG2 VAL I 159      39.431 -14.069  32.476  1.00 58.16           C  
ANISOU 4954  CG2 VAL I 159     6536   7990   7571   1554   -113     15       C  
ATOM   4955  N   SER I 160      42.544 -14.351  29.698  1.00 64.63           N  
ANISOU 4955  N   SER I 160     7982   9048   7527   2231    837    -52       N  
ATOM   4956  CA  SER I 160      43.098 -15.610  29.261  1.00 67.27           C  
ANISOU 4956  CA  SER I 160     8607   9282   7670   2412    951   -336       C  
ATOM   4957  C   SER I 160      44.317 -15.821  30.140  1.00 65.73           C  
ANISOU 4957  C   SER I 160     8026   8976   7972   2450   1261   -262       C  
ATOM   4958  O   SER I 160      44.656 -14.946  30.939  1.00 62.74           O  
ANISOU 4958  O   SER I 160     7232   8622   7985   2305   1312    -29       O  
ATOM   4959  CB  SER I 160      43.439 -15.598  27.768  1.00 72.27           C  
ANISOU 4959  CB  SER I 160     9746  10028   7685   2720   1249   -353       C  
ATOM   4960  OG  SER I 160      44.300 -14.530  27.470  1.00 72.69           O  
ANISOU 4960  OG  SER I 160     9619  10191   7809   2862   1767     14       O  
ATOM   4961  N   TRP I 161      44.931 -16.994  30.042  1.00 67.75           N  
ANISOU 4961  N   TRP I 161     8423   9082   8236   2636   1414   -466       N  
ATOM   4962  CA  TRP I 161      46.122 -17.263  30.809  1.00 67.60           C  
ANISOU 4962  CA  TRP I 161     7996   8974   8716   2722   1668   -347       C  
ATOM   4963  C   TRP I 161      47.274 -17.662  29.889  1.00 72.99           C  
ANISOU 4963  C   TRP I 161     8800   9624   9309   3112   2266   -313       C  
ATOM   4964  O   TRP I 161      47.095 -18.424  28.932  1.00 76.58           O  
ANISOU 4964  O   TRP I 161     9809   9993   9294   3338   2407   -566       O  
ATOM   4965  CB  TRP I 161      45.848 -18.344  31.848  1.00 65.72           C  
ANISOU 4965  CB  TRP I 161     7697   8531   8741   2623   1343   -524       C  
ATOM   4966  CG  TRP I 161      45.048 -17.876  32.992  1.00 61.30           C  
ANISOU 4966  CG  TRP I 161     6915   7985   8391   2300    933   -453       C  
ATOM   4967  CD1 TRP I 161      43.682 -17.873  33.095  1.00 59.84           C  
ANISOU 4967  CD1 TRP I 161     6902   7776   8058   2086    578   -560       C  
ATOM   4968  CD2 TRP I 161      45.546 -17.345  34.221  1.00 58.86           C  
ANISOU 4968  CD2 TRP I 161     6191   7695   8477   2167    846   -252       C  
ATOM   4969  NE1 TRP I 161      43.297 -17.355  34.318  1.00 56.08           N  
ANISOU 4969  NE1 TRP I 161     6165   7291   7853   1872    386   -417       N  
ATOM   4970  CE2 TRP I 161      44.420 -17.026  35.027  1.00 55.59           C  
ANISOU 4970  CE2 TRP I 161     5806   7253   8062   1911    517   -261       C  
ATOM   4971  CE3 TRP I 161      46.825 -17.075  34.709  1.00 60.03           C  
ANISOU 4971  CE3 TRP I 161     5943   7877   8990   2231    991    -60       C  
ATOM   4972  CZ2 TRP I 161      44.541 -16.485  36.301  1.00 53.42           C  
ANISOU 4972  CZ2 TRP I 161     5312   6965   8020   1750    363   -133       C  
ATOM   4973  CZ3 TRP I 161      46.946 -16.524  35.988  1.00 58.29           C  
ANISOU 4973  CZ3 TRP I 161     5456   7662   9030   2015    710     55       C  
ATOM   4974  CH2 TRP I 161      45.806 -16.253  36.772  1.00 54.94           C  
ANISOU 4974  CH2 TRP I 161     5205   7193   8478   1791    416     -5       C  
ATOM   4975  N   ASN I 162      48.457 -17.132  30.190  1.00 73.94           N  
ANISOU 4975  N   ASN I 162     8402   9787   9905   3187   2623      0       N  
ATOM   4976  CA  ASN I 162      49.646 -17.341  29.376  1.00 79.36           C  
ANISOU 4976  CA  ASN I 162     9053  10441  10658   3578   3317    152       C  
ATOM   4977  C   ASN I 162      49.358 -17.171  27.889  1.00 83.44           C  
ANISOU 4977  C   ASN I 162    10221  11027  10456   3828   3701     90       C  
ATOM   4978  O   ASN I 162      49.721 -18.032  27.069  1.00 87.88           O  
ANISOU 4978  O   ASN I 162    11237  11462  10690   4207   4123    -77       O  
ATOM   4979  CB  ASN I 162      50.270 -18.705  29.672  1.00 82.05           C  
ANISOU 4979  CB  ASN I 162     9365  10560  11250   3845   3452     15       C  
ATOM   4980  CG  ASN I 162      50.912 -18.755  31.036  1.00 80.15           C  
ANISOU 4980  CG  ASN I 162     8416  10295  11744   3699   3181    217       C  
ATOM   4981  OD1 ASN I 162      50.660 -19.661  31.812  1.00 78.75           O  
ANISOU 4981  OD1 ASN I 162     8267   9970  11683   3671   2836     62       O  
ATOM   4982  ND2 ASN I 162      51.731 -17.763  31.343  1.00 81.39           N  
ANISOU 4982  ND2 ASN I 162     7950  10580  12394   3588   3301    574       N  
ATOM   4983  N   SER I 163      48.695 -16.061  27.560  1.00 81.64           N  
ANISOU 4983  N   SER I 163    10089  10977   9952   3643   3554    228       N  
ATOM   4984  CA  SER I 163      48.371 -15.714  26.179  1.00 86.56           C  
ANISOU 4984  CA  SER I 163    11344  11714   9830   3876   3844    250       C  
ATOM   4985  C   SER I 163      47.559 -16.781  25.426  1.00 89.39           C  
ANISOU 4985  C   SER I 163    12530  12006   9429   4017   3577   -219       C  
ATOM   4986  O   SER I 163      47.744 -16.975  24.216  1.00 95.02           O  
ANISOU 4986  O   SER I 163    13892  12731   9481   4372   3991   -284       O  
ATOM   4987  CB  SER I 163      49.647 -15.368  25.402  1.00 92.34           C  
ANISOU 4987  CB  SER I 163    11993  12445  10649   4253   4763    602       C  
ATOM   4988  OG  SER I 163      50.325 -14.272  25.992  1.00 90.41           O  
ANISOU 4988  OG  SER I 163    10984  12235  11133   4053   4950   1040       O  
ATOM   4989  N   GLY I 164      46.661 -17.459  26.143  1.00 85.37           N  
ANISOU 4989  N   GLY I 164    12026  11399   9014   3731   2894   -544       N  
ATOM   4990  CA  GLY I 164      45.778 -18.463  25.541  1.00 87.89           C  
ANISOU 4990  CA  GLY I 164    13057  11599   8740   3743   2497  -1021       C  
ATOM   4991  C   GLY I 164      46.310 -19.883  25.581  1.00 90.70           C  
ANISOU 4991  C   GLY I 164    13669  11624   9170   3957   2713  -1363       C  
ATOM   4992  O   GLY I 164      45.557 -20.825  25.350  1.00 92.46           O  
ANISOU 4992  O   GLY I 164    14399  11649   9084   3869   2298  -1806       O  
ATOM   4993  N   ALA I 165      47.607 -20.022  25.868  1.00 91.71           N  
ANISOU 4993  N   ALA I 165    13415  11662   9767   4232   3356  -1137       N  
ATOM   4994  CA  ALA I 165      48.289 -21.319  25.930  1.00 94.97           C  
ANISOU 4994  CA  ALA I 165    13994  11732  10359   4529   3699  -1363       C  
ATOM   4995  C   ALA I 165      47.862 -22.140  27.138  1.00 90.78           C  
ANISOU 4995  C   ALA I 165    13159  10982  10351   4253   3166  -1526       C  
ATOM   4996  O   ALA I 165      47.819 -23.367  27.068  1.00 93.24           O  
ANISOU 4996  O   ALA I 165    13867  10939  10623   4385   3182  -1869       O  
ATOM   4997  CB  ALA I 165      49.791 -21.127  25.952  1.00 97.98           C  
ANISOU 4997  CB  ALA I 165    13889  12109  11228   4908   4520   -964       C  
ATOM   4998  N   LEU I 166      47.567 -21.466  28.249  1.00 84.60           N  
ANISOU 4998  N   LEU I 166    11727  10370  10048   3893   2747  -1269       N  
ATOM   4999  CA  LEU I 166      47.057 -22.160  29.427  1.00 81.21           C  
ANISOU 4999  CA  LEU I 166    11068   9751  10039   3635   2261  -1368       C  
ATOM   5000  C   LEU I 166      45.537 -22.087  29.417  1.00 78.97           C  
ANISOU 5000  C   LEU I 166    11052   9488   9466   3242   1613  -1602       C  
ATOM   5001  O   LEU I 166      44.937 -21.026  29.625  1.00 75.95           O  
ANISOU 5001  O   LEU I 166    10427   9370   9060   2986   1338  -1413       O  
ATOM   5002  CB  LEU I 166      47.633 -21.581  30.721  1.00 77.21           C  
ANISOU 5002  CB  LEU I 166     9782   9378  10178   3506   2186   -974       C  
ATOM   5003  CG  LEU I 166      47.863 -22.538  31.899  1.00 76.25           C  
ANISOU 5003  CG  LEU I 166     9404   9015  10550   3511   2014   -947       C  
ATOM   5004  CD1 LEU I 166      47.413 -21.862  33.212  1.00 70.71           C  
ANISOU 5004  CD1 LEU I 166     8268   8466  10132   3148   1538   -737       C  
ATOM   5005  CD2 LEU I 166      47.125 -23.858  31.711  1.00 78.06           C  
ANISOU 5005  CD2 LEU I 166    10176   8869  10613   3517   1862  -1335       C  
ATOM   5006  N   THR I 167      44.908 -23.226  29.177  1.00 81.86           N  
ANISOU 5006  N   THR I 167    11891   9533   9678   3192   1378  -2000       N  
ATOM   5007  CA  THR I 167      43.484 -23.229  28.939  1.00 81.49           C  
ANISOU 5007  CA  THR I 167    12094   9485   9384   2828    760  -2233       C  
ATOM   5008  C   THR I 167      42.773 -24.192  29.875  1.00 79.80           C  
ANISOU 5008  C   THR I 167    11764   8928   9630   2553    392  -2368       C  
ATOM   5009  O   THR I 167      41.648 -23.940  30.301  1.00 76.84           O  
ANISOU 5009  O   THR I 167    11190   8598   9409   2186    -87  -2328       O  
ATOM   5010  CB  THR I 167      43.178 -23.565  27.454  1.00 88.02           C  
ANISOU 5010  CB  THR I 167    13726  10254   9465   2949    705  -2637       C  
ATOM   5011  OG1 THR I 167      41.858 -23.116  27.126  1.00 88.10           O  
ANISOU 5011  OG1 THR I 167    13822  10428   9225   2597     41  -2719       O  
ATOM   5012  CG2 THR I 167      43.316 -25.078  27.164  1.00 93.24           C  
ANISOU 5012  CG2 THR I 167    14953  10400  10076   3073    785  -3110       C  
ATOM   5013  N   SER I 168      43.448 -25.288  30.197  1.00 82.17           N  
ANISOU 5013  N   SER I 168    12165   8860  10194   2762    678  -2474       N  
ATOM   5014  CA  SER I 168      42.850 -26.350  30.991  1.00 82.27           C  
ANISOU 5014  CA  SER I 168    12161   8457  10640   2551    424  -2593       C  
ATOM   5015  C   SER I 168      42.799 -25.986  32.481  1.00 76.27           C  
ANISOU 5015  C   SER I 168    10767   7805  10406   2410    347  -2161       C  
ATOM   5016  O   SER I 168      43.718 -25.363  33.004  1.00 73.38           O  
ANISOU 5016  O   SER I 168    10023   7688  10170   2602    602  -1830       O  
ATOM   5017  CB  SER I 168      43.612 -27.654  30.740  1.00 87.30           C  
ANISOU 5017  CB  SER I 168    13202   8612  11355   2882    808  -2841       C  
ATOM   5018  OG  SER I 168      43.431 -28.579  31.791  1.00 86.85           O  
ANISOU 5018  OG  SER I 168    12977   8165  11858   2791    742  -2761       O  
ATOM   5019  N   GLY I 169      41.708 -26.350  33.148  1.00 75.10           N  
ANISOU 5019  N   GLY I 169    10521   7462  10553   2064    -10  -2163       N  
ATOM   5020  CA  GLY I 169      41.562 -26.071  34.579  1.00 71.24           C  
ANISOU 5020  CA  GLY I 169     9567   7033  10466   1958    -41  -1767       C  
ATOM   5021  C   GLY I 169      41.268 -24.610  34.897  1.00 66.90           C  
ANISOU 5021  C   GLY I 169     8662   6944   9813   1818   -154  -1495       C  
ATOM   5022  O   GLY I 169      41.298 -24.180  36.059  1.00 64.15           O  
ANISOU 5022  O   GLY I 169     8006   6690   9677   1778   -136  -1183       O  
ATOM   5023  N   VAL I 170      40.969 -23.842  33.858  1.00 66.80           N  
ANISOU 5023  N   VAL I 170     8755   7190   9435   1763   -266  -1615       N  
ATOM   5024  CA  VAL I 170      40.640 -22.437  34.023  1.00 63.50           C  
ANISOU 5024  CA  VAL I 170     8045   7150   8933   1650   -343  -1363       C  
ATOM   5025  C   VAL I 170      39.152 -22.198  34.313  1.00 63.36           C  
ANISOU 5025  C   VAL I 170     7871   7108   9095   1317   -689  -1300       C  
ATOM   5026  O   VAL I 170      38.260 -22.725  33.630  1.00 66.28           O  
ANISOU 5026  O   VAL I 170     8407   7333   9443   1133  -1006  -1527       O  
ATOM   5027  CB  VAL I 170      41.037 -21.622  32.792  1.00 64.24           C  
ANISOU 5027  CB  VAL I 170     8302   7536   8569   1794   -246  -1416       C  
ATOM   5028  CG1 VAL I 170      40.421 -20.257  32.865  1.00 61.67           C  
ANISOU 5028  CG1 VAL I 170     7724   7511   8198   1646   -373  -1169       C  
ATOM   5029  CG2 VAL I 170      42.548 -21.518  32.693  1.00 64.76           C  
ANISOU 5029  CG2 VAL I 170     8327   7679   8599   2124    203  -1323       C  
ATOM   5030  N   HIS I 171      38.900 -21.396  35.339  1.00 59.60           N  
ANISOU 5030  N   HIS I 171     7072   6754   8821   1242   -628   -989       N  
ATOM   5031  CA  HIS I 171      37.547 -21.037  35.726  1.00 59.23           C  
ANISOU 5031  CA  HIS I 171     6800   6686   9019    994   -819   -837       C  
ATOM   5032  C   HIS I 171      37.469 -19.525  35.875  1.00 56.55           C  
ANISOU 5032  C   HIS I 171     6261   6653   8573   1020   -728   -587       C  
ATOM   5033  O   HIS I 171      37.977 -18.950  36.832  1.00 53.97           O  
ANISOU 5033  O   HIS I 171     5840   6375   8291   1091   -504   -405       O  
ATOM   5034  CB  HIS I 171      37.141 -21.714  37.046  1.00 58.97           C  
ANISOU 5034  CB  HIS I 171     6647   6359   9399    907   -709   -674       C  
ATOM   5035  CG  HIS I 171      35.664 -21.797  37.245  1.00 60.71           C  
ANISOU 5035  CG  HIS I 171     6635   6433  10001    645   -864   -552       C  
ATOM   5036  ND1 HIS I 171      34.796 -20.835  36.773  1.00 61.21           N  
ANISOU 5036  ND1 HIS I 171     6469   6709  10078    541  -1031   -437       N  
ATOM   5037  CD2 HIS I 171      34.896 -22.731  37.855  1.00 63.75           C  
ANISOU 5037  CD2 HIS I 171     6922   6457  10843    475   -852   -477       C  
ATOM   5038  CE1 HIS I 171      33.553 -21.176  37.073  1.00 63.92           C  
ANISOU 5038  CE1 HIS I 171     6531   6847  10908    317  -1136   -296       C  
ATOM   5039  NE2 HIS I 171      33.584 -22.323  37.729  1.00 65.67           N  
ANISOU 5039  NE2 HIS I 171     6826   6710  11417    255  -1013   -320       N  
ATOM   5040  N   THR I 172      36.850 -18.869  34.913  1.00 57.81           N  
ANISOU 5040  N   THR I 172     6395   6999   8572    969   -928   -583       N  
ATOM   5041  CA  THR I 172      36.644 -17.448  35.039  1.00 55.79           C  
ANISOU 5041  CA  THR I 172     5954   6961   8284   1002   -817   -316       C  
ATOM   5042  C   THR I 172      35.192 -17.221  35.463  1.00 56.78           C  
ANISOU 5042  C   THR I 172     5782   7006   8785    837   -949   -108       C  
ATOM   5043  O   THR I 172      34.279 -17.662  34.784  1.00 60.18           O  
ANISOU 5043  O   THR I 172     6132   7409   9323    698  -1307   -168       O  
ATOM   5044  CB  THR I 172      36.950 -16.751  33.722  1.00 57.47           C  
ANISOU 5044  CB  THR I 172     6317   7434   8084   1123   -881   -340       C  
ATOM   5045  OG1 THR I 172      38.371 -16.727  33.512  1.00 55.99           O  
ANISOU 5045  OG1 THR I 172     6304   7311   7659   1310   -593   -421       O  
ATOM   5046  CG2 THR I 172      36.420 -15.342  33.741  1.00 56.62           C  
ANISOU 5046  CG2 THR I 172     6005   7485   8024   1140   -818    -29       C  
ATOM   5047  N   PHE I 173      34.977 -16.573  36.603  1.00 54.19           N  
ANISOU 5047  N   PHE I 173     5296   6617   8679    853   -660    135       N  
ATOM   5048  CA  PHE I 173      33.645 -16.525  37.192  1.00 55.36           C  
ANISOU 5048  CA  PHE I 173     5144   6617   9272    744   -634    373       C  
ATOM   5049  C   PHE I 173      32.832 -15.331  36.646  1.00 56.96           C  
ANISOU 5049  C   PHE I 173     5104   6989   9550    787   -692    622       C  
ATOM   5050  O   PHE I 173      33.393 -14.294  36.284  1.00 56.09           O  
ANISOU 5050  O   PHE I 173     5105   7054   9152    925   -583    671       O  
ATOM   5051  CB  PHE I 173      33.732 -16.472  38.730  1.00 53.53           C  
ANISOU 5051  CB  PHE I 173     4959   6192   9190    798   -218    526       C  
ATOM   5052  CG  PHE I 173      34.093 -17.789  39.387  1.00 53.45           C  
ANISOU 5052  CG  PHE I 173     5099   5955   9255    758   -180    414       C  
ATOM   5053  CD1 PHE I 173      35.359 -18.339  39.249  1.00 52.45           C  
ANISOU 5053  CD1 PHE I 173     5232   5863   8834    839   -244    185       C  
ATOM   5054  CD2 PHE I 173      33.189 -18.440  40.196  1.00 55.57           C  
ANISOU 5054  CD2 PHE I 173     5231   5949   9935    675    -12    601       C  
ATOM   5055  CE1 PHE I 173      35.702 -19.526  39.872  1.00 52.26           C  
ANISOU 5055  CE1 PHE I 173     5347   5607   8904    853   -190    137       C  
ATOM   5056  CE2 PHE I 173      33.514 -19.627  40.811  1.00 56.09           C  
ANISOU 5056  CE2 PHE I 173     5461   5770  10079    664     64    556       C  
ATOM   5057  CZ  PHE I 173      34.787 -20.159  40.657  1.00 54.71           C  
ANISOU 5057  CZ  PHE I 173     5570   5638   9581    765    -42    322       C  
ATOM   5058  N   PRO I 174      31.507 -15.479  36.552  1.00 59.60           N  
ANISOU 5058  N   PRO I 174     5063   7249  10333    674   -865    819       N  
ATOM   5059  CA  PRO I 174      30.684 -14.329  36.254  1.00 61.15           C  
ANISOU 5059  CA  PRO I 174     4961   7566  10706    771   -854   1149       C  
ATOM   5060  C   PRO I 174      30.974 -13.273  37.298  1.00 58.27           C  
ANISOU 5060  C   PRO I 174     4698   7112  10330    956   -268   1332       C  
ATOM   5061  O   PRO I 174      31.380 -13.626  38.403  1.00 56.78           O  
ANISOU 5061  O   PRO I 174     4701   6738  10135    957     58   1260       O  
ATOM   5062  CB  PRO I 174      29.273 -14.849  36.457  1.00 65.47           C  
ANISOU 5062  CB  PRO I 174     5000   7951  11924    612  -1001   1378       C  
ATOM   5063  CG  PRO I 174      29.379 -16.293  36.243  1.00 66.91           C  
ANISOU 5063  CG  PRO I 174     5270   7998  12156    368  -1338   1069       C  
ATOM   5064  CD  PRO I 174      30.723 -16.707  36.697  1.00 62.57           C  
ANISOU 5064  CD  PRO I 174     5224   7398  11152    447  -1079    778       C  
ATOM   5065  N   ALA I 175      30.735 -12.003  36.966  1.00 58.76           N  
ANISOU 5065  N   ALA I 175     4673   7272  10379   1118   -151   1569       N  
ATOM   5066  CA  ALA I 175      31.144 -10.875  37.808  1.00 56.72           C  
ANISOU 5066  CA  ALA I 175     4624   6886  10040   1283    375   1665       C  
ATOM   5067  C   ALA I 175      30.038 -10.394  38.726  1.00 59.52           C  
ANISOU 5067  C   ALA I 175     4744   7000  10872   1403    814   1997       C  
ATOM   5068  O   ALA I 175      28.861 -10.576  38.418  1.00 63.64           O  
ANISOU 5068  O   ALA I 175     4789   7521  11870   1402    687   2276       O  
ATOM   5069  CB  ALA I 175      31.616  -9.744  36.941  1.00 56.43           C  
ANISOU 5069  CB  ALA I 175     4691   7010   9741   1407    347   1737       C  
ATOM   5070  N   VAL I 176      30.396  -9.789  39.855  1.00 58.29           N  
ANISOU 5070  N   VAL I 176     4920   6620  10605   1513   1328   1972       N  
ATOM   5071  CA  VAL I 176      29.394  -9.184  40.705  1.00 61.16           C  
ANISOU 5071  CA  VAL I 176     5169   6716  11354   1704   1876   2288       C  
ATOM   5072  C   VAL I 176      29.166  -7.793  40.231  1.00 63.95           C  
ANISOU 5072  C   VAL I 176     5464   7047  11787   1903   2045   2507       C  
ATOM   5073  O   VAL I 176      30.122  -7.101  39.889  1.00 61.71           O  
ANISOU 5073  O   VAL I 176     5496   6819  11132   1892   1981   2329       O  
ATOM   5074  CB  VAL I 176      29.837  -8.974  42.137  1.00 60.28           C  
ANISOU 5074  CB  VAL I 176     5592   6328  10986   1785   2395   2150       C  
ATOM   5075  CG1 VAL I 176      29.341 -10.055  43.026  1.00 62.23           C  
ANISOU 5075  CG1 VAL I 176     5812   6427  11406   1759   2604   2220       C  
ATOM   5076  CG2 VAL I 176      31.311  -8.806  42.221  1.00 57.26           C  
ANISOU 5076  CG2 VAL I 176     5695   6024  10038   1670   2192   1760       C  
ATOM   5077  N   LEU I 177      27.902  -7.374  40.256  1.00 68.21           N  
ANISOU 5077  N   LEU I 177     5571   7466  12878   2097   2312   2934       N  
ATOM   5078  CA  LEU I 177      27.539  -6.003  40.011  1.00 70.60           C  
ANISOU 5078  CA  LEU I 177     5824   7648  13354   2367   2619   3223       C  
ATOM   5079  C   LEU I 177      27.419  -5.385  41.397  1.00 72.05           C  
ANISOU 5079  C   LEU I 177     6420   7400  13554   2569   3419   3221       C  
ATOM   5080  O   LEU I 177      26.420  -5.570  42.098  1.00 75.84           O  
ANISOU 5080  O   LEU I 177     6670   7671  14475   2736   3885   3503       O  
ATOM   5081  CB  LEU I 177      26.194  -5.940  39.276  1.00 76.14           C  
ANISOU 5081  CB  LEU I 177     5771   8454  14706   2507   2445   3737       C  
ATOM   5082  CG  LEU I 177      26.091  -4.994  38.071  1.00 77.45           C  
ANISOU 5082  CG  LEU I 177     5748   8800  14880   2667   2153   4006       C  
ATOM   5083  CD1 LEU I 177      24.687  -5.026  37.444  1.00 82.59           C  
ANISOU 5083  CD1 LEU I 177     5585   9570  16227   2808   1887   4556       C  
ATOM   5084  CD2 LEU I 177      26.551  -3.584  38.440  1.00 76.96           C  
ANISOU 5084  CD2 LEU I 177     6141   8433  14666   2911   2746   4034       C  
ATOM   5085  N   GLN I 178      28.451  -4.662  41.797  1.00 69.70           N  
ANISOU 5085  N   GLN I 178     6756   6948  12779   2549   3587   2899       N  
ATOM   5086  CA  GLN I 178      28.512  -4.112  43.145  1.00 72.14           C  
ANISOU 5086  CA  GLN I 178     7653   6831  12925   2700   4254   2767       C  
ATOM   5087  C   GLN I 178      27.633  -2.886  43.272  1.00 77.29           C  
ANISOU 5087  C   GLN I 178     8253   7131  13984   3070   4891   3123       C  
ATOM   5088  O   GLN I 178      27.388  -2.189  42.286  1.00 78.47           O  
ANISOU 5088  O   GLN I 178     8052   7356  14405   3176   4752   3394       O  
ATOM   5089  CB  GLN I 178      29.949  -3.702  43.477  1.00 69.58           C  
ANISOU 5089  CB  GLN I 178     8003   6437  11997   2497   4097   2273       C  
ATOM   5090  CG  GLN I 178      30.983  -4.515  42.740  1.00 65.38           C  
ANISOU 5090  CG  GLN I 178     7356   6308  11179   2179   3387   2020       C  
ATOM   5091  CD  GLN I 178      32.404  -4.245  43.210  1.00 64.62           C  
ANISOU 5091  CD  GLN I 178     7812   6140  10600   1963   3221   1574       C  
ATOM   5092  OE1 GLN I 178      33.295  -3.936  42.401  1.00 63.49           O  
ANISOU 5092  OE1 GLN I 178     7606   6150  10367   1803   2890   1468       O  
ATOM   5093  NE2 GLN I 178      32.633  -4.376  44.513  1.00 65.47           N  
ANISOU 5093  NE2 GLN I 178     8458   6018  10402   1959   3436   1337       N  
ATOM   5094  N   SER I 179      27.185  -2.624  44.495  1.00 81.01           N  
ANISOU 5094  N   SER I 179     9128   7194  14457   3303   5624   3135       N  
ATOM   5095  CA  SER I 179      26.471  -1.399  44.831  1.00 86.58           C  
ANISOU 5095  CA  SER I 179     9971   7443  15481   3706   6386   3400       C  
ATOM   5096  C   SER I 179      26.956  -0.221  43.987  1.00 86.70           C  
ANISOU 5096  C   SER I 179    10052   7387  15503   3716   6226   3392       C  
ATOM   5097  O   SER I 179      26.151   0.538  43.401  1.00 89.58           O  
ANISOU 5097  O   SER I 179     9989   7638  16408   4027   6480   3864       O  
ATOM   5098  CB  SER I 179      26.705  -1.053  46.306  1.00 89.57           C  
ANISOU 5098  CB  SER I 179    11290   7345  15399   3842   7065   3072       C  
ATOM   5099  OG  SER I 179      25.668  -1.544  47.144  1.00 94.63           O  
ANISOU 5099  OG  SER I 179    11839   7807  16310   4133   7743   3377       O  
ATOM   5100  N   SER I 180      28.279  -0.068  43.936  1.00 82.11           N  
ANISOU 5100  N   SER I 180     9974   6852  14371   3386   5819   2903       N  
ATOM   5101  CA  SER I 180      28.869   1.135  43.357  1.00 82.35           C  
ANISOU 5101  CA  SER I 180    10211   6684  14394   3369   5805   2855       C  
ATOM   5102  C   SER I 180      28.522   1.334  41.887  1.00 81.73           C  
ANISOU 5102  C   SER I 180     9433   6926  14694   3452   5453   3319       C  
ATOM   5103  O   SER I 180      28.694   2.418  41.347  1.00 83.60           O  
ANISOU 5103  O   SER I 180     9747   6949  15069   3561   5595   3471       O  
ATOM   5104  CB  SER I 180      30.375   1.096  43.505  1.00 78.96           C  
ANISOU 5104  CB  SER I 180    10285   6300  13418   2944   5358   2295       C  
ATOM   5105  OG  SER I 180      30.918   0.219  42.535  1.00 74.75           O  
ANISOU 5105  OG  SER I 180     9291   6326  12786   2685   4651   2297       O  
ATOM   5106  N   GLY I 181      28.040   0.286  41.240  1.00 79.98           N  
ANISOU 5106  N   GLY I 181     8578   7194  14617   3398   4976   3543       N  
ATOM   5107  CA  GLY I 181      27.691   0.377  39.831  1.00 80.32           C  
ANISOU 5107  CA  GLY I 181     8027   7588  14902   3474   4528   3959       C  
ATOM   5108  C   GLY I 181      28.764  -0.301  39.012  1.00 75.65           C  
ANISOU 5108  C   GLY I 181     7471   7437  13834   3113   3817   3662       C  
ATOM   5109  O   GLY I 181      28.552  -0.603  37.845  1.00 76.16           O  
ANISOU 5109  O   GLY I 181     7123   7891  13922   3118   3313   3908       O  
ATOM   5110  N   LEU I 182      29.904  -0.578  39.641  1.00 72.08           N  
ANISOU 5110  N   LEU I 182     7523   6923  12940   2820   3768   3140       N  
ATOM   5111  CA  LEU I 182      31.068  -1.138  38.949  1.00 67.95           C  
ANISOU 5111  CA  LEU I 182     7061   6750  12008   2512   3219   2859       C  
ATOM   5112  C   LEU I 182      31.163  -2.647  39.064  1.00 65.08           C  
ANISOU 5112  C   LEU I 182     6546   6725  11457   2308   2790   2633       C  
ATOM   5113  O   LEU I 182      30.890  -3.186  40.130  1.00 65.91           O  
ANISOU 5113  O   LEU I 182     6776   6689  11577   2286   2982   2489       O  
ATOM   5114  CB  LEU I 182      32.337  -0.534  39.524  1.00 66.84           C  
ANISOU 5114  CB  LEU I 182     7466   6331  11600   2298   3366   2461       C  
ATOM   5115  CG  LEU I 182      32.367   0.984  39.427  1.00 70.87           C  
ANISOU 5115  CG  LEU I 182     8196   6407  12325   2443   3806   2630       C  
ATOM   5116  CD1 LEU I 182      33.680   1.532  39.936  1.00 70.45           C  
ANISOU 5116  CD1 LEU I 182     8628   6064  12077   2138   3838   2207       C  
ATOM   5117  CD2 LEU I 182      32.079   1.444  38.001  1.00 71.88           C  
ANISOU 5117  CD2 LEU I 182     7954   6744  12612   2629   3684   3109       C  
ATOM   5118  N   TYR I 183      31.583  -3.323  37.989  1.00 62.90           N  
ANISOU 5118  N   TYR I 183     6073   6852  10974   2179   2261   2600       N  
ATOM   5119  CA  TYR I 183      31.751  -4.779  38.004  1.00 60.12           C  
ANISOU 5119  CA  TYR I 183     5622   6768  10454   1983   1854   2358       C  
ATOM   5120  C   TYR I 183      33.072  -5.225  38.621  1.00 56.99           C  
ANISOU 5120  C   TYR I 183     5601   6348   9703   1756   1801   1918       C  
ATOM   5121  O   TYR I 183      33.989  -4.447  38.716  1.00 56.47           O  
ANISOU 5121  O   TYR I 183     5800   6153   9505   1694   1934   1793       O  
ATOM   5122  CB  TYR I 183      31.631  -5.348  36.592  1.00 60.66           C  
ANISOU 5122  CB  TYR I 183     5415   7230  10401   1963   1317   2462       C  
ATOM   5123  CG  TYR I 183      30.247  -5.210  35.965  1.00 65.54           C  
ANISOU 5123  CG  TYR I 183     5570   7948  11385   2145   1149   2896       C  
ATOM   5124  CD1 TYR I 183      29.926  -4.108  35.180  1.00 68.05           C  
ANISOU 5124  CD1 TYR I 183     5792   8284  11779   2380   1203   3282       C  
ATOM   5125  CD2 TYR I 183      29.271  -6.206  36.127  1.00 66.51           C  
ANISOU 5125  CD2 TYR I 183     5307   8137  11828   2072    898   2958       C  
ATOM   5126  CE1 TYR I 183      28.683  -3.996  34.590  1.00 73.31           C  
ANISOU 5126  CE1 TYR I 183     5980   9073  12801   2562    959   3722       C  
ATOM   5127  CE2 TYR I 183      28.035  -6.102  35.525  1.00 71.27           C  
ANISOU 5127  CE2 TYR I 183     5388   8846  12845   2200    645   3373       C  
ATOM   5128  CZ  TYR I 183      27.741  -4.988  34.767  1.00 74.93           C  
ANISOU 5128  CZ  TYR I 183     5750   9364  13354   2459    652   3761       C  
ATOM   5129  OH  TYR I 183      26.509  -4.844  34.165  1.00 80.29           O  
ANISOU 5129  OH  TYR I 183     5861  10170  14476   2616    334   4231       O  
ATOM   5130  N   SER I 184      33.138  -6.484  39.060  1.00 56.38           N  
ANISOU 5130  N   SER I 184     5510   6372   9540   1630   1596   1717       N  
ATOM   5131  CA  SER I 184      34.386  -7.177  39.461  1.00 53.25           C  
ANISOU 5131  CA  SER I 184     5366   6037   8831   1444   1417   1355       C  
ATOM   5132  C   SER I 184      34.192  -8.650  39.195  1.00 52.28           C  
ANISOU 5132  C   SER I 184     5066   6107   8691   1369   1087   1272       C  
ATOM   5133  O   SER I 184      33.075  -9.142  39.307  1.00 54.30           O  
ANISOU 5133  O   SER I 184     5088   6329   9214   1407   1092   1437       O  
ATOM   5134  CB  SER I 184      34.669  -7.028  40.960  1.00 53.56           C  
ANISOU 5134  CB  SER I 184     5781   5795   8773   1412   1680   1178       C  
ATOM   5135  OG  SER I 184      35.706  -6.102  41.225  1.00 53.85           O  
ANISOU 5135  OG  SER I 184     6106   5693   8661   1317   1736   1002       O  
ATOM   5136  N   LEU I 185      35.272  -9.353  38.870  1.00 50.47           N  
ANISOU 5136  N   LEU I 185     4926   6034   8215   1263    832   1031       N  
ATOM   5137  CA  LEU I 185      35.230 -10.804  38.640  1.00 50.25           C  
ANISOU 5137  CA  LEU I 185     4816   6115   8162   1194    547    898       C  
ATOM   5138  C   LEU I 185      36.595 -11.419  38.941  1.00 48.98           C  
ANISOU 5138  C   LEU I 185     4844   5991   7776   1133    454    643       C  
ATOM   5139  O   LEU I 185      37.609 -10.723  38.932  1.00 48.34           O  
ANISOU 5139  O   LEU I 185     4856   5933   7578   1118    514    582       O  
ATOM   5140  CB  LEU I 185      34.835 -11.140  37.192  1.00 51.32           C  
ANISOU 5140  CB  LEU I 185     4770   6471   8260   1205    228    940       C  
ATOM   5141  CG  LEU I 185      35.815 -10.921  36.014  1.00 51.95           C  
ANISOU 5141  CG  LEU I 185     4968   6764   8007   1252    116    852       C  
ATOM   5142  CD1 LEU I 185      37.093 -11.757  36.134  1.00 49.81           C  
ANISOU 5142  CD1 LEU I 185     4858   6515   7553   1215     91    582       C  
ATOM   5143  CD2 LEU I 185      35.129 -11.208  34.662  1.00 54.18           C  
ANISOU 5143  CD2 LEU I 185     5179   7244   8161   1294   -227    913       C  
ATOM   5144  N   SER I 186      36.627 -12.723  39.193  1.00 48.68           N  
ANISOU 5144  N   SER I 186     4818   5929   7748   1097    309    525       N  
ATOM   5145  CA  SER I 186      37.900 -13.422  39.348  1.00 47.63           C  
ANISOU 5145  CA  SER I 186     4801   5837   7459   1095    203    334       C  
ATOM   5146  C   SER I 186      38.042 -14.599  38.402  1.00 48.58           C  
ANISOU 5146  C   SER I 186     4885   6032   7542   1110      0    196       C  
ATOM   5147  O   SER I 186      37.054 -15.212  37.976  1.00 50.91           O  
ANISOU 5147  O   SER I 186     5105   6283   7954   1061   -133    198       O  
ATOM   5148  CB  SER I 186      38.086 -13.894  40.776  1.00 47.09           C  
ANISOU 5148  CB  SER I 186     4905   5602   7383   1093    264    320       C  
ATOM   5149  OG  SER I 186      38.076 -12.793  41.642  1.00 46.96           O  
ANISOU 5149  OG  SER I 186     5050   5490   7301   1085    438    375       O  
ATOM   5150  N   SER I 187      39.281 -14.899  38.059  1.00 47.91           N  
ANISOU 5150  N   SER I 187     4846   6031   7327   1176    -21     71       N  
ATOM   5151  CA  SER I 187      39.576 -16.032  37.208  1.00 49.43           C  
ANISOU 5151  CA  SER I 187     5103   6236   7442   1243   -129    -99       C  
ATOM   5152  C   SER I 187      40.658 -16.849  37.873  1.00 49.24           C  
ANISOU 5152  C   SER I 187     5109   6127   7472   1330    -98   -164       C  
ATOM   5153  O   SER I 187      41.743 -16.354  38.101  1.00 49.69           O  
ANISOU 5153  O   SER I 187     5080   6269   7530   1382    -25   -118       O  
ATOM   5154  CB  SER I 187      40.047 -15.556  35.844  1.00 50.44           C  
ANISOU 5154  CB  SER I 187     5269   6555   7340   1339    -80   -130       C  
ATOM   5155  OG  SER I 187      40.681 -16.614  35.159  1.00 52.24           O  
ANISOU 5155  OG  SER I 187     5646   6759   7442   1464    -77   -323       O  
ATOM   5156  N   VAL I 188      40.351 -18.087  38.229  1.00 50.36           N  
ANISOU 5156  N   VAL I 188     5338   6077   7720   1338   -169   -236       N  
ATOM   5157  CA  VAL I 188      41.320 -18.923  38.922  1.00 51.40           C  
ANISOU 5157  CA  VAL I 188     5497   6106   7928   1467   -148   -234       C  
ATOM   5158  C   VAL I 188      41.691 -20.139  38.081  1.00 54.23           C  
ANISOU 5158  C   VAL I 188     5969   6337   8300   1603   -126   -418       C  
ATOM   5159  O   VAL I 188      40.856 -20.675  37.350  1.00 56.14           O  
ANISOU 5159  O   VAL I 188     6347   6463   8522   1522   -206   -579       O  
ATOM   5160  CB  VAL I 188      40.775 -19.421  40.252  1.00 51.53           C  
ANISOU 5160  CB  VAL I 188     5594   5924   8059   1426   -164   -103       C  
ATOM   5161  CG1 VAL I 188      39.331 -19.810  40.090  1.00 51.69           C  
ANISOU 5161  CG1 VAL I 188     5637   5776   8228   1278   -166   -105       C  
ATOM   5162  CG2 VAL I 188      41.613 -20.627  40.744  1.00 52.94           C  
ANISOU 5162  CG2 VAL I 188     5840   5946   8329   1604   -175    -83       C  
ATOM   5163  N   VAL I 189      42.942 -20.582  38.175  1.00 55.59           N  
ANISOU 5163  N   VAL I 189     6087   6504   8532   1812    -30   -399       N  
ATOM   5164  CA  VAL I 189      43.348 -21.762  37.431  1.00 57.83           C  
ANISOU 5164  CA  VAL I 189     6530   6601   8842   2002     83   -574       C  
ATOM   5165  C   VAL I 189      43.932 -22.795  38.372  1.00 59.47           C  
ANISOU 5165  C   VAL I 189     6720   6588   9289   2173    102   -456       C  
ATOM   5166  O   VAL I 189      44.538 -22.446  39.386  1.00 59.25           O  
ANISOU 5166  O   VAL I 189     6500   6667   9346   2217     22   -226       O  
ATOM   5167  CB  VAL I 189      44.344 -21.415  36.320  1.00 59.66           C  
ANISOU 5167  CB  VAL I 189     6726   6997   8943   2203    318   -633       C  
ATOM   5168  CG1 VAL I 189      45.695 -21.084  36.894  1.00 60.17           C  
ANISOU 5168  CG1 VAL I 189     6441   7186   9234   2365    422   -399       C  
ATOM   5169  CG2 VAL I 189      44.463 -22.552  35.335  1.00 63.27           C  
ANISOU 5169  CG2 VAL I 189     7513   7223   9305   2397    482   -896       C  
ATOM   5170  N   THR I 190      43.707 -24.069  38.060  1.00 62.06           N  
ANISOU 5170  N   THR I 190     7284   6579   9716   2260    170   -613       N  
ATOM   5171  CA  THR I 190      44.134 -25.154  38.918  1.00 63.68           C  
ANISOU 5171  CA  THR I 190     7516   6505  10175   2448    217   -463       C  
ATOM   5172  C   THR I 190      45.311 -25.845  38.288  1.00 67.12           C  
ANISOU 5172  C   THR I 190     7957   6829  10718   2809    469   -519       C  
ATOM   5173  O   THR I 190      45.322 -26.130  37.094  1.00 69.11           O  
ANISOU 5173  O   THR I 190     8438   6981  10840   2882    647   -807       O  
ATOM   5174  CB  THR I 190      43.003 -26.147  39.204  1.00 65.40           C  
ANISOU 5174  CB  THR I 190     7980   6317  10553   2285    174   -534       C  
ATOM   5175  OG1 THR I 190      42.021 -25.518  40.050  1.00 61.92           O  
ANISOU 5175  OG1 THR I 190     7459   5969  10098   2025     41   -360       O  
ATOM   5176  CG2 THR I 190      43.571 -27.424  39.875  1.00 68.16           C  
ANISOU 5176  CG2 THR I 190     8420   6297  11180   2556    308   -373       C  
ATOM   5177  N   VAL I 191      46.297 -26.131  39.122  1.00 68.91           N  
ANISOU 5177  N   VAL I 191     7952   7060  11170   3064    483   -223       N  
ATOM   5178  CA  VAL I 191      47.655 -26.278  38.663  1.00 71.91           C  
ANISOU 5178  CA  VAL I 191     8098   7497  11728   3428    726   -134       C  
ATOM   5179  C   VAL I 191      48.396 -27.230  39.571  1.00 75.71           C  
ANISOU 5179  C   VAL I 191     8446   7772  12549   3749    720    173       C  
ATOM   5180  O   VAL I 191      48.176 -27.239  40.782  1.00 75.16           O  
ANISOU 5180  O   VAL I 191     8338   7729  12492   3670    425    420       O  
ATOM   5181  CB  VAL I 191      48.333 -24.887  38.665  1.00 70.05           C  
ANISOU 5181  CB  VAL I 191     7439   7718  11460   3344    636     21       C  
ATOM   5182  CG1 VAL I 191      49.625 -24.865  39.458  1.00 72.77           C  
ANISOU 5182  CG1 VAL I 191     7300   8190  12160   3575    526    391       C  
ATOM   5183  CG2 VAL I 191      48.478 -24.344  37.248  1.00 70.66           C  
ANISOU 5183  CG2 VAL I 191     7572   7918  11359   3368    954   -188       C  
ATOM   5184  N   PRO I 192      49.251 -28.067  38.979  1.00 80.28           N  
ANISOU 5184  N   PRO I 192     9005   8118  13380   4154   1080    175       N  
ATOM   5185  CA  PRO I 192      50.121 -28.958  39.732  1.00 84.60           C  
ANISOU 5185  CA  PRO I 192     9348   8473  14324   4551   1111    534       C  
ATOM   5186  C   PRO I 192      51.086 -28.199  40.652  1.00 84.83           C  
ANISOU 5186  C   PRO I 192     8782   8917  14534   4607    757    962       C  
ATOM   5187  O   PRO I 192      51.850 -27.349  40.187  1.00 84.79           O  
ANISOU 5187  O   PRO I 192     8357   9223  14636   4614    811   1011       O  
ATOM   5188  CB  PRO I 192      50.890 -29.711  38.633  1.00 89.92           C  
ANISOU 5188  CB  PRO I 192    10083   8860  15222   4988   1677    410       C  
ATOM   5189  CG  PRO I 192      50.509 -29.051  37.320  1.00 88.05           C  
ANISOU 5189  CG  PRO I 192    10093   8751  14610   4803   1906     -5       C  
ATOM   5190  CD  PRO I 192      49.213 -28.391  37.544  1.00 82.48           C  
ANISOU 5190  CD  PRO I 192     9608   8204  13525   4272   1502   -202       C  
ATOM   5191  N   SER I 193      51.068 -28.529  41.942  1.00 85.68           N  
ANISOU 5191  N   SER I 193     8871   9003  14680   4646    390   1282       N  
ATOM   5192  CA  SER I 193      51.845 -27.790  42.939  1.00 86.85           C  
ANISOU 5192  CA  SER I 193     8563   9543  14894   4626   -115   1640       C  
ATOM   5193  C   SER I 193      53.366 -27.963  42.837  1.00 92.56           C  
ANISOU 5193  C   SER I 193     8634  10370  16166   5032    -91   1986       C  
ATOM   5194  O   SER I 193      54.126 -27.214  43.451  1.00 94.48           O  
ANISOU 5194  O   SER I 193     8385  10965  16549   4957   -558   2240       O  
ATOM   5195  CB  SER I 193      51.335 -28.104  44.350  1.00 86.88           C  
ANISOU 5195  CB  SER I 193     8860   9496  14654   4580   -519   1884       C  
ATOM   5196  OG  SER I 193      50.917 -29.454  44.436  1.00 89.57           O  
ANISOU 5196  OG  SER I 193     9569   9354  15108   4834   -227   1954       O  
ATOM   5197  N   SER I 194      53.815 -28.936  42.058  1.00 96.44           N  
ANISOU 5197  N   SER I 194     9108  10529  17008   5457    451   1995       N  
ATOM   5198  CA  SER I 194      55.251 -29.111  41.853  1.00102.86           C  
ANISOU 5198  CA  SER I 194     9232  11409  18442   5897    602   2362       C  
ATOM   5199  C   SER I 194      55.720 -28.140  40.781  1.00102.15           C  
ANISOU 5199  C   SER I 194     8781  11564  18467   5781    927   2205       C  
ATOM   5200  O   SER I 194      56.904 -27.907  40.599  1.00106.86           O  
ANISOU 5200  O   SER I 194     8666  12314  19623   6022   1030   2528       O  
ATOM   5201  CB  SER I 194      55.550 -30.540  41.401  1.00107.91           C  
ANISOU 5201  CB  SER I 194    10047  11528  19426   6463   1186   2438       C  
ATOM   5202  OG  SER I 194      54.972 -30.780  40.124  1.00106.39           O  
ANISOU 5202  OG  SER I 194    10378  11042  19001   6440   1816   1934       O  
ATOM   5203  N   SER I 195      54.762 -27.551  40.090  1.00 96.92           N  
ANISOU 5203  N   SER I 195     8588  10936  17301   5408   1085   1753       N  
ATOM   5204  CA  SER I 195      55.042 -26.790  38.883  1.00 97.03           C  
ANISOU 5204  CA  SER I 195     8459  11091  17315   5359   1543   1581       C  
ATOM   5205  C   SER I 195      55.484 -25.326  39.059  1.00 95.91           C  
ANISOU 5205  C   SER I 195     7759  11393  17289   5002   1220   1721       C  
ATOM   5206  O   SER I 195      55.762 -24.660  38.066  1.00 96.81           O  
ANISOU 5206  O   SER I 195     7731  11609  17444   4978   1652   1652       O  
ATOM   5207  CB  SER I 195      53.803 -26.801  37.988  1.00 92.45           C  
ANISOU 5207  CB  SER I 195     8654  10351  16121   5136   1809   1055       C  
ATOM   5208  OG  SER I 195      52.773 -26.030  38.596  1.00 86.93           O  
ANISOU 5208  OG  SER I 195     8172   9852  15004   4618   1286    907       O  
ATOM   5209  N   LEU I 196      55.527 -24.801  40.281  1.00 94.59           N  
ANISOU 5209  N   LEU I 196     7346  11454  17139   4719    490   1903       N  
ATOM   5210  CA  LEU I 196      55.734 -23.355  40.436  1.00 92.86           C  
ANISOU 5210  CA  LEU I 196     6760  11569  16953   4284    156   1918       C  
ATOM   5211  C   LEU I 196      57.194 -22.885  40.384  1.00 99.40           C  
ANISOU 5211  C   LEU I 196     6640  12574  18553   4385    127   2317       C  
ATOM   5212  O   LEU I 196      57.504 -21.857  39.766  1.00100.00           O  
ANISOU 5212  O   LEU I 196     6394  12790  18810   4162    330   2310       O  
ATOM   5213  CB  LEU I 196      55.026 -22.832  41.678  1.00 89.24           C  
ANISOU 5213  CB  LEU I 196     6591  11244  16073   3877   -581   1838       C  
ATOM   5214  CG  LEU I 196      53.788 -23.662  42.037  1.00 85.49           C  
ANISOU 5214  CG  LEU I 196     6884  10538  15062   3901   -572   1631       C  
ATOM   5215  CD1 LEU I 196      54.168 -24.522  43.239  1.00 89.45           C  
ANISOU 5215  CD1 LEU I 196     7336  10976  15675   4148  -1005   1958       C  
ATOM   5216  CD2 LEU I 196      52.555 -22.819  42.340  1.00 78.59           C  
ANISOU 5216  CD2 LEU I 196     6507   9738  13617   3447   -777   1339       C  
ATOM   5217  N   GLY I 197      58.101 -23.623  41.006  1.00104.61           N  
ANISOU 5217  N   GLY I 197     6803  13211  19732   4726   -108   2709       N  
ATOM   5218  CA  GLY I 197      59.487 -23.225  40.900  1.00111.92           C  
ANISOU 5218  CA  GLY I 197     6716  14289  21521   4830   -122   3132       C  
ATOM   5219  C   GLY I 197      59.887 -23.194  39.433  1.00114.03           C  
ANISOU 5219  C   GLY I 197     6802  14436  22087   5106    896   3139       C  
ATOM   5220  O   GLY I 197      60.944 -22.645  39.070  1.00119.58           O  
ANISOU 5220  O   GLY I 197     6658  15247  23531   5139   1108   3475       O  
ATOM   5221  N   THR I 198      59.035 -23.784  38.591  1.00109.81           N  
ANISOU 5221  N   THR I 198     7084  13663  20974   5298   1524   2776       N  
ATOM   5222  CA  THR I 198      59.366 -24.017  37.186  1.00112.89           C  
ANISOU 5222  CA  THR I 198     7533  13880  21480   5685   2548   2750       C  
ATOM   5223  C   THR I 198      58.449 -23.290  36.204  1.00107.61           C  
ANISOU 5223  C   THR I 198     7531  13244  20114   5405   2912   2326       C  
ATOM   5224  O   THR I 198      58.858 -22.898  35.119  1.00110.91           O  
ANISOU 5224  O   THR I 198     7850  13658  20633   5564   3634   2385       O  
ATOM   5225  CB  THR I 198      59.308 -25.520  36.851  1.00115.51           C  
ANISOU 5225  CB  THR I 198     8319  13820  21751   6277   3064   2683       C  
ATOM   5226  OG1 THR I 198      60.188 -26.243  37.742  1.00121.04           O  
ANISOU 5226  OG1 THR I 198     8381  14472  23138   6617   2760   3152       O  
ATOM   5227  CG2 THR I 198      59.784 -25.761  35.432  1.00120.30           C  
ANISOU 5227  CG2 THR I 198     9022  14224  22463   6740   4164   2665       C  
ATOM   5228  N   GLN I 199      57.201 -23.108  36.592  1.00100.70           N  
ANISOU 5228  N   GLN I 199     7327  12397  18536   5014   2428   1944       N  
ATOM   5229  CA  GLN I 199      56.159 -22.747  35.645  1.00 96.26           C  
ANISOU 5229  CA  GLN I 199     7510  11809  17254   4843   2735   1528       C  
ATOM   5230  C   GLN I 199      55.694 -21.296  35.892  1.00 91.30           C  
ANISOU 5230  C   GLN I 199     6800  11457  16433   4280   2320   1476       C  
ATOM   5231  O   GLN I 199      55.457 -20.890  37.035  1.00 87.77           O  
ANISOU 5231  O   GLN I 199     6211  11130  16008   3931   1611   1503       O  
ATOM   5232  CB  GLN I 199      54.996 -23.742  35.796  1.00 92.99           C  
ANISOU 5232  CB  GLN I 199     7914  11148  16270   4855   2567   1143       C  
ATOM   5233  CG  GLN I 199      54.535 -24.484  34.538  1.00 94.73           C  
ANISOU 5233  CG  GLN I 199     8863  11089  16042   5144   3194    788       C  
ATOM   5234  CD  GLN I 199      54.104 -23.574  33.386  1.00 93.79           C  
ANISOU 5234  CD  GLN I 199     9086  11125  15426   4992   3514    587       C  
ATOM   5235  OE1 GLN I 199      54.562 -23.753  32.257  1.00 98.59           O  
ANISOU 5235  OE1 GLN I 199     9896  11631  15933   5356   4223    557       O  
ATOM   5236  NE2 GLN I 199      53.226 -22.606  33.663  1.00 87.62           N  
ANISOU 5236  NE2 GLN I 199     8410  10570  14313   4502   3033    475       N  
ATOM   5237  N   THR I 200      55.590 -20.521  34.816  1.00 90.91           N  
ANISOU 5237  N   THR I 200     6889  11478  16175   4229   2802   1418       N  
ATOM   5238  CA  THR I 200      55.273 -19.100  34.905  1.00 88.09           C  
ANISOU 5238  CA  THR I 200     6419  11321  15731   3757   2551   1427       C  
ATOM   5239  C   THR I 200      53.810 -18.820  34.557  1.00 82.34           C  
ANISOU 5239  C   THR I 200     6480  10601  14204   3526   2423   1046       C  
ATOM   5240  O   THR I 200      53.364 -19.124  33.461  1.00 83.02           O  
ANISOU 5240  O   THR I 200     7095  10619  13829   3734   2873    861       O  
ATOM   5241  CB  THR I 200      56.177 -18.276  33.967  1.00 92.64           C  
ANISOU 5241  CB  THR I 200     6539  11959  16699   3845   3195   1728       C  
ATOM   5242  OG1 THR I 200      57.194 -17.621  34.734  1.00 95.38           O  
ANISOU 5242  OG1 THR I 200     5983  12397  17859   3621   2877   2083       O  
ATOM   5243  CG2 THR I 200      55.352 -17.231  33.209  1.00 89.35           C  
ANISOU 5243  CG2 THR I 200     6584  11624  15741   3600   3366   1582       C  
ATOM   5244  N   TYR I 201      53.057 -18.240  35.477  1.00 76.86           N  
ANISOU 5244  N   TYR I 201     5879   9982  13341   3115   1809    937       N  
ATOM   5245  CA  TYR I 201      51.635 -18.084  35.205  1.00 72.64           C  
ANISOU 5245  CA  TYR I 201     6002   9439  12157   2936   1685    629       C  
ATOM   5246  C   TYR I 201      51.210 -16.624  35.085  1.00 70.31           C  
ANISOU 5246  C   TYR I 201     5691   9273  11749   2592   1611    665       C  
ATOM   5247  O   TYR I 201      51.273 -15.867  36.053  1.00 69.14           O  
ANISOU 5247  O   TYR I 201     5291   9165  11815   2280   1207    733       O  
ATOM   5248  CB  TYR I 201      50.795 -18.798  36.264  1.00 69.45           C  
ANISOU 5248  CB  TYR I 201     5882   8937  11569   2821   1175    457       C  
ATOM   5249  CG  TYR I 201      51.044 -20.280  36.338  1.00 71.95           C  
ANISOU 5249  CG  TYR I 201     6314   9051  11971   3162   1275    416       C  
ATOM   5250  CD1 TYR I 201      50.323 -21.153  35.536  1.00 71.99           C  
ANISOU 5250  CD1 TYR I 201     6877   8869  11608   3321   1507    137       C  
ATOM   5251  CD2 TYR I 201      51.995 -20.814  37.211  1.00 74.65           C  
ANISOU 5251  CD2 TYR I 201     6225   9360  12778   3324   1100    659       C  
ATOM   5252  CE1 TYR I 201      50.534 -22.515  35.588  1.00 74.58           C  
ANISOU 5252  CE1 TYR I 201     7365   8924  12046   3626   1637     75       C  
ATOM   5253  CE2 TYR I 201      52.212 -22.186  37.275  1.00 77.23           C  
ANISOU 5253  CE2 TYR I 201     6674   9449  13219   3680   1237    661       C  
ATOM   5254  CZ  TYR I 201      51.480 -23.027  36.451  1.00 77.29           C  
ANISOU 5254  CZ  TYR I 201     7274   9217  12874   3828   1545    356       C  
ATOM   5255  OH  TYR I 201      51.679 -24.384  36.481  1.00 79.74           O  
ANISOU 5255  OH  TYR I 201     7764   9209  13326   4172   1725    329       O  
ATOM   5256  N   ILE I 202      50.776 -16.229  33.895  1.00 70.38           N  
ANISOU 5256  N   ILE I 202     6027   9323  11391   2668   1998    618       N  
ATOM   5257  CA  ILE I 202      50.388 -14.845  33.679  1.00 69.19           C  
ANISOU 5257  CA  ILE I 202     5872   9258  11157   2403   2003    710       C  
ATOM   5258  C   ILE I 202      48.905 -14.728  33.315  1.00 65.88           C  
ANISOU 5258  C   ILE I 202     6029   8864  10137   2316   1832    494       C  
ATOM   5259  O   ILE I 202      48.351 -15.572  32.612  1.00 66.30           O  
ANISOU 5259  O   ILE I 202     6520   8896   9776   2511   1904    298       O  
ATOM   5260  CB  ILE I 202      51.277 -14.181  32.607  1.00 73.73           C  
ANISOU 5260  CB  ILE I 202     6221   9876  11919   2561   2633    993       C  
ATOM   5261  CG1 ILE I 202      52.719 -14.077  33.106  1.00 77.59           C  
ANISOU 5261  CG1 ILE I 202     5953  10333  13195   2554   2731   1277       C  
ATOM   5262  CG2 ILE I 202      50.757 -12.797  32.253  1.00 72.68           C  
ANISOU 5262  CG2 ILE I 202     6184   9783  11647   2330   2694   1111       C  
ATOM   5263  CD1 ILE I 202      53.639 -13.386  32.157  1.00 82.27           C  
ANISOU 5263  CD1 ILE I 202     6209  10926  14126   2681   3413   1628       C  
ATOM   5264  N   CYS I 203      48.242 -13.705  33.826  1.00 63.04           N  
ANISOU 5264  N   CYS I 203     5665   8520   9767   2017   1573    523       N  
ATOM   5265  CA  CYS I 203      46.871 -13.479  33.411  1.00 60.52           C  
ANISOU 5265  CA  CYS I 203     5772   8234   8988   1963   1443    409       C  
ATOM   5266  C   CYS I 203      46.783 -12.279  32.471  1.00 62.08           C  
ANISOU 5266  C   CYS I 203     6026   8509   9054   1972   1749    625       C  
ATOM   5267  O   CYS I 203      47.446 -11.260  32.667  1.00 62.43           O  
ANISOU 5267  O   CYS I 203     5753   8511   9456   1839   1916    842       O  
ATOM   5268  CB  CYS I 203      45.905 -13.382  34.601  1.00 56.60           C  
ANISOU 5268  CB  CYS I 203     5329   7664   8512   1714    998    298       C  
ATOM   5269  SG  CYS I 203      46.042 -11.892  35.652  1.00 56.61           S  
ANISOU 5269  SG  CYS I 203     5093   7584   8832   1398    874    433       S  
ATOM   5270  N   ASN I 204      45.973 -12.443  31.430  1.00 63.25           N  
ANISOU 5270  N   ASN I 204     6596   8747   8690   2128   1794    571       N  
ATOM   5271  CA  ASN I 204      45.807 -11.447  30.396  1.00 65.52           C  
ANISOU 5271  CA  ASN I 204     7043   9126   8726   2221   2081    812       C  
ATOM   5272  C   ASN I 204      44.415 -10.846  30.480  1.00 63.94           C  
ANISOU 5272  C   ASN I 204     7012   8957   8324   2085   1734    829       C  
ATOM   5273  O   ASN I 204      43.428 -11.434  30.021  1.00 64.45           O  
ANISOU 5273  O   ASN I 204     7396   9102   7990   2148   1440    672       O  
ATOM   5274  CB  ASN I 204      46.000 -12.102  29.040  1.00 69.62           C  
ANISOU 5274  CB  ASN I 204     7988   9746   8718   2568   2385    767       C  
ATOM   5275  CG  ASN I 204      47.288 -12.885  28.954  1.00 72.16           C  
ANISOU 5275  CG  ASN I 204     8156  10000   9260   2777   2789    742       C  
ATOM   5276  OD1 ASN I 204      47.275 -14.112  28.996  1.00 72.55           O  
ANISOU 5276  OD1 ASN I 204     8398   9987   9179   2898   2675    457       O  
ATOM   5277  ND2 ASN I 204      48.410 -12.180  28.844  1.00 74.18           N  
ANISOU 5277  ND2 ASN I 204     8024  10231   9929   2822   3285   1068       N  
ATOM   5278  N   VAL I 205      44.331  -9.678  31.099  1.00 62.48           N  
ANISOU 5278  N   VAL I 205     6592   8675   8473   1890   1754   1019       N  
ATOM   5279  CA  VAL I 205      43.061  -8.986  31.204  1.00 60.67           C  
ANISOU 5279  CA  VAL I 205     6468   8436   8149   1814   1528   1106       C  
ATOM   5280  C   VAL I 205      42.919  -7.954  30.083  1.00 63.60           C  
ANISOU 5280  C   VAL I 205     6993   8877   8296   1979   1815   1453       C  
ATOM   5281  O   VAL I 205      43.809  -7.112  29.854  1.00 64.42           O  
ANISOU 5281  O   VAL I 205     6960   8891   8625   1982   2241   1702       O  
ATOM   5282  CB  VAL I 205      42.902  -8.330  32.592  1.00 58.05           C  
ANISOU 5282  CB  VAL I 205     5906   7891   8258   1548   1408   1085       C  
ATOM   5283  CG1 VAL I 205      41.443  -7.881  32.827  1.00 55.99           C  
ANISOU 5283  CG1 VAL I 205     5741   7592   7941   1526   1204   1153       C  
ATOM   5284  CG2 VAL I 205      43.346  -9.317  33.682  1.00 55.70           C  
ANISOU 5284  CG2 VAL I 205     5487   7535   8141   1428   1185    810       C  
ATOM   5285  N   ASN I 206      41.796  -8.044  29.373  1.00 64.64           N  
ANISOU 5285  N   ASN I 206     7394   9159   8009   2113   1559   1500       N  
ATOM   5286  CA  ASN I 206      41.474  -7.076  28.334  1.00 68.55           C  
ANISOU 5286  CA  ASN I 206     8081   9740   8223   2311   1742   1880       C  
ATOM   5287  C   ASN I 206      40.095  -6.498  28.568  1.00 68.03           C  
ANISOU 5287  C   ASN I 206     7960   9663   8226   2278   1406   2031       C  
ATOM   5288  O   ASN I 206      39.103  -7.239  28.569  1.00 68.65           O  
ANISOU 5288  O   ASN I 206     8084   9855   8144   2261    922   1861       O  
ATOM   5289  CB  ASN I 206      41.559  -7.718  26.938  1.00 73.73           C  
ANISOU 5289  CB  ASN I 206     9198  10640   8175   2606   1762   1866       C  
ATOM   5290  CG  ASN I 206      41.270  -6.729  25.800  1.00 79.06           C  
ANISOU 5290  CG  ASN I 206    10157  11435   8448   2868   1954   2317       C  
ATOM   5291  OD1 ASN I 206      40.191  -6.133  25.723  1.00 80.04           O  
ANISOU 5291  OD1 ASN I 206    10270  11603   8540   2888   1642   2529       O  
ATOM   5292  ND2 ASN I 206      42.225  -6.594  24.889  1.00 82.79           N  
ANISOU 5292  ND2 ASN I 206    10890  11956   8611   3111   2497   2506       N  
ATOM   5293  N   HIS I 207      40.049  -5.180  28.798  1.00 68.60           N  
ANISOU 5293  N   HIS I 207     7898   9551   8618   2263   1687   2362       N  
ATOM   5294  CA  HIS I 207      38.789  -4.395  28.897  1.00 68.72           C  
ANISOU 5294  CA  HIS I 207     7845   9511   8753   2325   1514   2632       C  
ATOM   5295  C   HIS I 207      38.710  -3.480  27.688  1.00 73.62           C  
ANISOU 5295  C   HIS I 207     8678  10219   9074   2611   1735   3115       C  
ATOM   5296  O   HIS I 207      39.428  -2.469  27.598  1.00 75.08           O  
ANISOU 5296  O   HIS I 207     8852  10193   9483   2629   2247   3392       O  
ATOM   5297  CB  HIS I 207      38.778  -3.561  30.180  1.00 66.13           C  
ANISOU 5297  CB  HIS I 207     7280   8815   9031   2122   1724   2629       C  
ATOM   5298  CG  HIS I 207      37.506  -2.803  30.416  1.00 67.39           C  
ANISOU 5298  CG  HIS I 207     7349   8855   9402   2226   1652   2898       C  
ATOM   5299  ND1 HIS I 207      36.286  -3.420  30.624  1.00 66.58           N  
ANISOU 5299  ND1 HIS I 207     7116   8878   9303   2261   1235   2848       N  
ATOM   5300  CD2 HIS I 207      37.278  -1.475  30.532  1.00 69.04           C  
ANISOU 5300  CD2 HIS I 207     7538   8777   9918   2308   1990   3238       C  
ATOM   5301  CE1 HIS I 207      35.362  -2.504  30.838  1.00 67.35           C  
ANISOU 5301  CE1 HIS I 207     7082   8804   9704   2394   1337   3176       C  
ATOM   5302  NE2 HIS I 207      35.937  -1.317  30.783  1.00 69.16           N  
ANISOU 5302  NE2 HIS I 207     7411   8771  10094   2441   1799   3406       N  
ATOM   5303  N   LYS I 208      37.871  -3.850  26.732  1.00 76.82           N  
ANISOU 5303  N   LYS I 208     9298  10924   8968   2829   1329   3231       N  
ATOM   5304  CA  LYS I 208      37.879  -3.134  25.468  1.00 82.76           C  
ANISOU 5304  CA  LYS I 208    10365  11817   9262   3157   1503   3700       C  
ATOM   5305  C   LYS I 208      37.366  -1.702  25.518  1.00 84.56           C  
ANISOU 5305  C   LYS I 208    10455  11835   9838   3291   1745   4237       C  
ATOM   5306  O   LYS I 208      38.007  -0.805  24.990  1.00 87.91           O  
ANISOU 5306  O   LYS I 208    11033  12134  10236   3443   2275   4620       O  
ATOM   5307  CB  LYS I 208      37.207  -3.940  24.364  1.00 87.21           C  
ANISOU 5307  CB  LYS I 208    11296  12772   9068   3359    925   3651       C  
ATOM   5308  CG  LYS I 208      38.252  -4.685  23.540  1.00 90.09           C  
ANISOU 5308  CG  LYS I 208    12133  13287   8812   3479   1166   3437       C  
ATOM   5309  CD  LYS I 208      37.786  -6.060  23.078  1.00 91.72           C  
ANISOU 5309  CD  LYS I 208    12653  13740   8458   3462    520   2983       C  
ATOM   5310  CE  LYS I 208      37.120  -5.968  21.705  1.00 99.42           C  
ANISOU 5310  CE  LYS I 208    14167  15032   8577   3780     99   3227       C  
ATOM   5311  NZ  LYS I 208      38.078  -5.493  20.661  1.00104.41           N  
ANISOU 5311  NZ  LYS I 208    15349  15732   8590   4140    752   3537       N  
ATOM   5312  N   PRO I 209      36.229  -1.483  26.177  1.00 83.00           N  
ANISOU 5312  N   PRO I 209     9954  11551  10030   3250   1428   4291       N  
ATOM   5313  CA  PRO I 209      35.677  -0.129  26.230  1.00 85.71           C  
ANISOU 5313  CA  PRO I 209    10176  11646  10744   3435   1695   4819       C  
ATOM   5314  C   PRO I 209      36.609   0.962  26.790  1.00 84.42           C  
ANISOU 5314  C   PRO I 209     9988  11007  11081   3317   2426   4930       C  
ATOM   5315  O   PRO I 209      36.375   2.133  26.546  1.00 88.12           O  
ANISOU 5315  O   PRO I 209    10482  11236  11765   3516   2757   5420       O  
ATOM   5316  CB  PRO I 209      34.428  -0.278  27.117  1.00 83.93           C  
ANISOU 5316  CB  PRO I 209     9564  11347  10980   3368   1334   4748       C  
ATOM   5317  CG  PRO I 209      34.314  -1.749  27.461  1.00 80.16           C  
ANISOU 5317  CG  PRO I 209     9012  11097  10349   3125    843   4202       C  
ATOM   5318  CD  PRO I 209      35.284  -2.511  26.647  1.00 80.61           C  
ANISOU 5318  CD  PRO I 209     9438  11403   9785   3110    803   3960       C  
ATOM   5319  N   SER I 210      37.645   0.592  27.534  1.00 80.57           N  
ANISOU 5319  N   SER I 210     9441  10358  10815   2989   2641   4495       N  
ATOM   5320  CA  SER I 210      38.556   1.581  28.117  1.00 80.58           C  
ANISOU 5320  CA  SER I 210     9382   9882  11352   2792   3216   4540       C  
ATOM   5321  C   SER I 210      39.998   1.380  27.647  1.00 82.20           C  
ANISOU 5321  C   SER I 210     9652  10120  11460   2684   3565   4491       C  
ATOM   5322  O   SER I 210      40.941   1.852  28.284  1.00 81.99           O  
ANISOU 5322  O   SER I 210     9473   9737  11943   2394   3901   4376       O  
ATOM   5323  CB  SER I 210      38.506   1.535  29.643  1.00 76.16           C  
ANISOU 5323  CB  SER I 210     8636   9006  11296   2462   3153   4099       C  
ATOM   5324  OG  SER I 210      39.069   0.330  30.136  1.00 71.22           O  
ANISOU 5324  OG  SER I 210     7937   8580  10542   2228   2875   3594       O  
ATOM   5325  N   ASN I 211      40.166   0.684  26.528  1.00 84.39           N  
ANISOU 5325  N   ASN I 211    10158  10805  11101   2923   3485   4583       N  
ATOM   5326  CA  ASN I 211      41.489   0.429  25.980  1.00 86.72           C  
ANISOU 5326  CA  ASN I 211    10518  11145  11285   2910   3915   4596       C  
ATOM   5327  C   ASN I 211      42.418  -0.077  27.048  1.00 83.18           C  
ANISOU 5327  C   ASN I 211     9742  10536  11328   2518   3921   4124       C  
ATOM   5328  O   ASN I 211      43.596   0.308  27.075  1.00 85.69           O  
ANISOU 5328  O   ASN I 211     9877  10634  12047   2367   4393   4222       O  
ATOM   5329  CB  ASN I 211      42.104   1.693  25.388  1.00 92.24           C  
ANISOU 5329  CB  ASN I 211    11268  11547  12231   3014   4611   5166       C  
ATOM   5330  CG  ASN I 211      41.818   1.846  23.910  1.00 98.41           C  
ANISOU 5330  CG  ASN I 211    12501  12614  12276   3494   4779   5680       C  
ATOM   5331  OD1 ASN I 211      40.949   1.168  23.358  1.00 99.20           O  
ANISOU 5331  OD1 ASN I 211    12883  13119  11692   3739   4254   5616       O  
ATOM   5332  ND2 ASN I 211      42.547   2.749  23.258  1.00103.74           N  
ANISOU 5332  ND2 ASN I 211    13266  13063  13088   3623   5498   6209       N  
ATOM   5333  N   THR I 212      41.897  -0.932  27.926  1.00 77.92           N  
ANISOU 5333  N   THR I 212     8972   9968  10666   2356   3393   3657       N  
ATOM   5334  CA  THR I 212      42.710  -1.467  29.006  1.00 74.85           C  
ANISOU 5334  CA  THR I 212     8306   9452  10680   2017   3309   3227       C  
ATOM   5335  C   THR I 212      43.176  -2.897  28.768  1.00 73.30           C  
ANISOU 5335  C   THR I 212     8142   9571  10137   2075   3124   2916       C  
ATOM   5336  O   THR I 212      42.371  -3.827  28.659  1.00 70.77           O  
ANISOU 5336  O   THR I 212     7988   9498   9404   2180   2697   2697       O  
ATOM   5337  CB  THR I 212      42.003  -1.327  30.365  1.00 71.32           C  
ANISOU 5337  CB  THR I 212     7749   8786  10562   1781   2976   2943       C  
ATOM   5338  OG1 THR I 212      41.908   0.066  30.685  1.00 73.50           O  
ANISOU 5338  OG1 THR I 212     8010   8646  11270   1693   3276   3181       O  
ATOM   5339  CG2 THR I 212      42.779  -2.076  31.483  1.00 68.22           C  
ANISOU 5339  CG2 THR I 212     7154   8340  10428   1474   2765   2487       C  
ATOM   5340  N   LYS I 213      44.492  -3.039  28.666  1.00 74.53           N  
ANISOU 5340  N   LYS I 213     8110   9675  10534   2007   3479   2924       N  
ATOM   5341  CA  LYS I 213      45.136  -4.337  28.619  1.00 74.05           C  
ANISOU 5341  CA  LYS I 213     8011   9814  10311   2059   3401   2635       C  
ATOM   5342  C   LYS I 213      46.163  -4.462  29.740  1.00 72.57           C  
ANISOU 5342  C   LYS I 213     7363   9432  10778   1734   3365   2432       C  
ATOM   5343  O   LYS I 213      47.110  -3.677  29.827  1.00 74.81           O  
ANISOU 5343  O   LYS I 213     7333   9493  11600   1571   3719   2648       O  
ATOM   5344  CB  LYS I 213      45.801  -4.566  27.262  1.00 78.83           C  
ANISOU 5344  CB  LYS I 213     8837  10585  10529   2400   3914   2892       C  
ATOM   5345  CG  LYS I 213      44.923  -5.325  26.284  1.00 80.44           C  
ANISOU 5345  CG  LYS I 213     9595  11101   9867   2731   3676   2806       C  
ATOM   5346  CD  LYS I 213      45.640  -5.594  24.946  1.00 86.84           C  
ANISOU 5346  CD  LYS I 213    10771  12056  10170   3118   4245   3021       C  
ATOM   5347  CE  LYS I 213      45.627  -4.368  24.029  1.00 91.82           C  
ANISOU 5347  CE  LYS I 213    11607  12648  10631   3326   4738   3601       C  
ATOM   5348  NZ  LYS I 213      46.303  -4.630  22.701  1.00 98.42           N  
ANISOU 5348  NZ  LYS I 213    12903  13623  10868   3760   5378   3847       N  
ATOM   5349  N   VAL I 214      45.959  -5.449  30.604  1.00 68.86           N  
ANISOU 5349  N   VAL I 214     6846   9033  10284   1631   2903   2039       N  
ATOM   5350  CA  VAL I 214      46.914  -5.728  31.666  1.00 68.55           C  
ANISOU 5350  CA  VAL I 214     6412   8868  10766   1370   2756   1850       C  
ATOM   5351  C   VAL I 214      47.368  -7.194  31.664  1.00 67.77           C  
ANISOU 5351  C   VAL I 214     6273   8958  10517   1527   2638   1627       C  
ATOM   5352  O   VAL I 214      46.595  -8.106  31.404  1.00 66.42           O  
ANISOU 5352  O   VAL I 214     6424   8946   9865   1703   2428   1436       O  
ATOM   5353  CB  VAL I 214      46.355  -5.339  33.060  1.00 65.66           C  
ANISOU 5353  CB  VAL I 214     6033   8303  10610   1061   2317   1616       C  
ATOM   5354  CG1 VAL I 214      47.398  -5.583  34.128  1.00 66.36           C  
ANISOU 5354  CG1 VAL I 214     5765   8283  11164    794   2079   1439       C  
ATOM   5355  CG2 VAL I 214      45.897  -3.873  33.087  1.00 66.23           C  
ANISOU 5355  CG2 VAL I 214     6191   8106  10866    934   2492   1818       C  
ATOM   5356  N   ASP I 215      48.650  -7.403  31.910  1.00 70.37           N  
ANISOU 5356  N   ASP I 215     6177   9237  11323   1465   2787   1679       N  
ATOM   5357  CA  ASP I 215      49.200  -8.736  32.091  1.00 70.16           C  
ANISOU 5357  CA  ASP I 215     6038   9323  11298   1619   2688   1504       C  
ATOM   5358  C   ASP I 215      49.735  -8.778  33.518  1.00 69.47           C  
ANISOU 5358  C   ASP I 215     5558   9120  11718   1309   2232   1366       C  
ATOM   5359  O   ASP I 215      50.736  -8.114  33.811  1.00 73.70           O  
ANISOU 5359  O   ASP I 215     5617   9529  12856   1098   2305   1537       O  
ATOM   5360  CB  ASP I 215      50.370  -8.963  31.124  1.00 75.45           C  
ANISOU 5360  CB  ASP I 215     6474  10032  12162   1885   3308   1768       C  
ATOM   5361  CG  ASP I 215      49.942  -9.014  29.678  1.00 77.58           C  
ANISOU 5361  CG  ASP I 215     7253  10425  11798   2249   3778   1894       C  
ATOM   5362  OD1 ASP I 215      48.942  -9.695  29.374  1.00 75.70           O  
ANISOU 5362  OD1 ASP I 215     7534  10309  10920   2397   3517   1643       O  
ATOM   5363  OD2 ASP I 215      50.615  -8.383  28.845  1.00 81.85           O  
ANISOU 5363  OD2 ASP I 215     7686  10930  12481   2382   4396   2257       O  
ATOM   5364  N   LYS I 216      49.092  -9.527  34.414  1.00 65.57           N  
ANISOU 5364  N   LYS I 216     5261   8653  11000   1266   1747   1079       N  
ATOM   5365  CA  LYS I 216      49.657  -9.680  35.758  1.00 65.65           C  
ANISOU 5365  CA  LYS I 216     4986   8584  11374   1033   1288    966       C  
ATOM   5366  C   LYS I 216      50.473 -10.962  35.932  1.00 67.67           C  
ANISOU 5366  C   LYS I 216     4989   8932  11790   1241   1215    954       C  
ATOM   5367  O   LYS I 216      50.026 -12.068  35.578  1.00 66.53           O  
ANISOU 5367  O   LYS I 216     5127   8863  11288   1517   1277    836       O  
ATOM   5368  CB  LYS I 216      48.597  -9.605  36.842  1.00 61.71           C  
ANISOU 5368  CB  LYS I 216     4849   8011  10587    863    844    726       C  
ATOM   5369  CG  LYS I 216      49.128  -9.073  38.171  1.00 63.27           C  
ANISOU 5369  CG  LYS I 216     4885   8063  11093    536    405    636       C  
ATOM   5370  CD  LYS I 216      48.840  -7.562  38.328  1.00 65.01           C  
ANISOU 5370  CD  LYS I 216     5214   8053  11435    247    460    642       C  
ATOM   5371  CE  LYS I 216      49.949  -6.639  37.772  1.00 69.50           C  
ANISOU 5371  CE  LYS I 216     5309   8502  12594     62    706    870       C  
ATOM   5372  NZ  LYS I 216      51.131  -6.531  38.700  1.00 74.11           N  
ANISOU 5372  NZ  LYS I 216     5461   8998  13701   -243    248    821       N  
ATOM   5373  N   LYS I 217      51.669 -10.819  36.489  1.00 70.46           N  
ANISOU 5373  N   LYS I 217     4794   9248  12729   1103   1057   1083       N  
ATOM   5374  CA  LYS I 217      52.448 -11.983  36.843  1.00 72.68           C  
ANISOU 5374  CA  LYS I 217     4779   9598  13239   1311    916   1119       C  
ATOM   5375  C   LYS I 217      51.960 -12.507  38.200  1.00 70.42           C  
ANISOU 5375  C   LYS I 217     4737   9301  12717   1202    268    902       C  
ATOM   5376  O   LYS I 217      52.050 -11.805  39.209  1.00 71.55           O  
ANISOU 5376  O   LYS I 217     4834   9378  12974    874   -201    835       O  
ATOM   5377  CB  LYS I 217      53.919 -11.585  36.927  1.00 78.97           C  
ANISOU 5377  CB  LYS I 217     4795  10369  14840   1201    943   1406       C  
ATOM   5378  CG  LYS I 217      54.845 -12.528  36.220  1.00 82.98           C  
ANISOU 5378  CG  LYS I 217     4913  10940  15675   1614   1402   1641       C  
ATOM   5379  CD  LYS I 217      54.961 -13.836  36.962  1.00 82.84           C  
ANISOU 5379  CD  LYS I 217     4906  10966  15602   1840   1031   1559       C  
ATOM   5380  CE  LYS I 217      56.184 -14.620  36.473  1.00 88.91           C  
ANISOU 5380  CE  LYS I 217     5083  11745  16954   2230   1448   1871       C  
ATOM   5381  NZ  LYS I 217      57.429 -13.818  36.513  1.00 94.24           N  
ANISOU 5381  NZ  LYS I 217     4874  12410  18524   2031   1481   2229       N  
ATOM   5382  N   VAL I 218      51.448 -13.732  38.237  1.00 67.82           N  
ANISOU 5382  N   VAL I 218     4721   9002  12045   1478    259    791       N  
ATOM   5383  CA  VAL I 218      51.011 -14.326  39.506  1.00 66.64           C  
ANISOU 5383  CA  VAL I 218     4822   8824  11675   1431   -259    659       C  
ATOM   5384  C   VAL I 218      52.131 -15.147  40.181  1.00 71.02           C  
ANISOU 5384  C   VAL I 218     4956   9415  12614   1579   -563    824       C  
ATOM   5385  O   VAL I 218      52.457 -16.248  39.740  1.00 72.54           O  
ANISOU 5385  O   VAL I 218     5060   9600  12901   1931   -316    909       O  
ATOM   5386  CB  VAL I 218      49.743 -15.201  39.317  1.00 62.40           C  
ANISOU 5386  CB  VAL I 218     4844   8239  10627   1601   -140    482       C  
ATOM   5387  CG1 VAL I 218      49.259 -15.748  40.639  1.00 61.21           C  
ANISOU 5387  CG1 VAL I 218     4968   8025  10266   1562   -565    413       C  
ATOM   5388  CG2 VAL I 218      48.616 -14.391  38.659  1.00 59.09           C  
ANISOU 5388  CG2 VAL I 218     4760   7809   9883   1473     81    373       C  
ATOM   5389  N   GLU I 219      52.732 -14.618  41.245  1.00 73.92           N  
ANISOU 5389  N   GLU I 219     5080   9801  13205   1326  -1122    872       N  
ATOM   5390  CA  GLU I 219      53.844 -15.338  41.891  1.00 79.11           C  
ANISOU 5390  CA  GLU I 219     5262  10524  14271   1473  -1508   1090       C  
ATOM   5391  C   GLU I 219      53.463 -15.992  43.212  1.00 79.11           C  
ANISOU 5391  C   GLU I 219     5663  10522  13873   1515  -2070   1034       C  
ATOM   5392  O   GLU I 219      52.714 -15.412  44.004  1.00 77.59           O  
ANISOU 5392  O   GLU I 219     5971  10284  13227   1266  -2368    833       O  
ATOM   5393  CB  GLU I 219      55.067 -14.429  42.112  1.00 84.55           C  
ANISOU 5393  CB  GLU I 219     5245  11255  15626   1183  -1842   1262       C  
ATOM   5394  CG  GLU I 219      55.420 -13.564  40.923  1.00 85.60           C  
ANISOU 5394  CG  GLU I 219     5005  11347  16171   1080  -1260   1364       C  
ATOM   5395  CD  GLU I 219      56.902 -13.469  40.680  1.00 92.55           C  
ANISOU 5395  CD  GLU I 219     4932  12264  17968   1087  -1245   1722       C  
ATOM   5396  OE1 GLU I 219      57.631 -13.123  41.627  1.00 97.91           O  
ANISOU 5396  OE1 GLU I 219     5189  12964  19048    800  -1967   1790       O  
ATOM   5397  OE2 GLU I 219      57.341 -13.735  39.539  1.00 93.70           O  
ANISOU 5397  OE2 GLU I 219     4752  12409  18441   1385   -513   1946       O  
ATOM   5398  N   PRO I 220      53.971 -17.212  43.441  1.00 81.80           N  
ANISOU 5398  N   PRO I 220     5823  10882  14376   1875  -2146   1240       N  
ATOM   5399  CA  PRO I 220      53.933 -17.991  44.693  1.00 84.01           C  
ANISOU 5399  CA  PRO I 220     6361  11168  14392   2010  -2683   1330       C  
ATOM   5400  C   PRO I 220      54.472 -17.246  45.936  1.00 88.97           C  
ANISOU 5400  C   PRO I 220     6919  11901  14985   1701  -3530   1346       C  
ATOM   5401  O   PRO I 220      55.616 -16.761  45.953  1.00 93.98           O  
ANISOU 5401  O   PRO I 220     6869  12634  16204   1552  -3888   1502       O  
ATOM   5402  CB  PRO I 220      54.814 -19.220  44.381  1.00 87.68           C  
ANISOU 5402  CB  PRO I 220     6353  11624  15337   2473  -2523   1650       C  
ATOM   5403  CG  PRO I 220      55.376 -18.988  42.979  1.00 88.41           C  
ANISOU 5403  CG  PRO I 220     5934  11711  15947   2562  -1881   1705       C  
ATOM   5404  CD  PRO I 220      54.406 -18.042  42.310  1.00 82.74           C  
ANISOU 5404  CD  PRO I 220     5630  10962  14845   2262  -1532   1391       C  
TER    5405      PRO I 220                                                      
ATOM   5406  N   ILE M   2       4.190  -8.576  60.191  1.00 60.84           N  
ANISOU 5406  N   ILE M   2     7521   8542   7054    -28   -484  -2246       N  
ATOM   5407  CA  ILE M   2       5.122  -7.499  59.745  1.00 61.21           C  
ANISOU 5407  CA  ILE M   2     7577   8192   7487    -41   -593  -2415       C  
ATOM   5408  C   ILE M   2       6.379  -8.027  59.004  1.00 58.92           C  
ANISOU 5408  C   ILE M   2     7368   7736   7285   -165   -709  -2110       C  
ATOM   5409  O   ILE M   2       6.992  -7.281  58.249  1.00 59.45           O  
ANISOU 5409  O   ILE M   2     7429   7442   7718   -177   -776  -2096       O  
ATOM   5410  CB  ILE M   2       5.533  -6.544  60.924  1.00 64.94           C  
ANISOU 5410  CB  ILE M   2     7984   8757   7933    -22   -651  -2937       C  
ATOM   5411  CG1 ILE M   2       5.897  -5.120  60.421  1.00 66.64           C  
ANISOU 5411  CG1 ILE M   2     8154   8465   8700     14   -710  -3181       C  
ATOM   5412  CG2 ILE M   2       6.677  -7.167  61.781  1.00 65.87           C  
ANISOU 5412  CG2 ILE M   2     8124   9197   7706   -151   -772  -2950       C  
ATOM   5413  CD1 ILE M   2       4.909  -3.980  60.804  1.00 69.12           C  
ANISOU 5413  CD1 ILE M   2     8360   8658   9245    174   -614  -3607       C  
ATOM   5414  N   GLU M   3       6.772  -9.283  59.201  1.00 56.60           N  
ANISOU 5414  N   GLU M   3     7127   7691   6688   -249   -727  -1851       N  
ATOM   5415  CA  GLU M   3       7.956  -9.790  58.510  1.00 53.92           C  
ANISOU 5415  CA  GLU M   3     6847   7200   6440   -343   -823  -1585       C  
ATOM   5416  C   GLU M   3       7.900 -11.285  58.251  1.00 51.24           C  
ANISOU 5416  C   GLU M   3     6556   7017   5897   -392   -785  -1224       C  
ATOM   5417  O   GLU M   3       7.803 -12.077  59.178  1.00 52.61           O  
ANISOU 5417  O   GLU M   3     6713   7512   5763   -420   -767  -1170       O  
ATOM   5418  CB  GLU M   3       9.223  -9.447  59.293  1.00 55.98           C  
ANISOU 5418  CB  GLU M   3     7091   7531   6648   -419   -960  -1766       C  
ATOM   5419  CG  GLU M   3      10.510  -9.699  58.499  1.00 55.14           C  
ANISOU 5419  CG  GLU M   3     7019   7220   6713   -500  -1060  -1520       C  
ATOM   5420  CD  GLU M   3      11.766  -9.942  59.375  1.00 58.15           C  
ANISOU 5420  CD  GLU M   3     7377   7810   6908   -593  -1190  -1566       C  
ATOM   5421  OE1 GLU M   3      11.805  -9.487  60.576  1.00 61.09           O  
ANISOU 5421  OE1 GLU M   3     7688   8435   7089   -607  -1238  -1893       O  
ATOM   5422  OE2 GLU M   3      12.732 -10.586  58.841  1.00 56.40           O  
ANISOU 5422  OE2 GLU M   3     7178   7526   6724   -648  -1245  -1281       O  
ATOM   5423  N   LEU M   4       7.992 -11.670  56.986  1.00 48.51           N  
ANISOU 5423  N   LEU M   4     6246   6450   5735   -402   -774   -975       N  
ATOM   5424  CA  LEU M   4       7.757 -13.051  56.600  1.00 47.03           C  
ANISOU 5424  CA  LEU M   4     6090   6346   5433   -440   -725   -690       C  
ATOM   5425  C   LEU M   4       9.070 -13.757  56.300  1.00 46.63           C  
ANISOU 5425  C   LEU M   4     6077   6235   5407   -503   -804   -501       C  
ATOM   5426  O   LEU M   4       9.923 -13.219  55.621  1.00 45.66           O  
ANISOU 5426  O   LEU M   4     5959   5919   5472   -508   -870   -495       O  
ATOM   5427  CB  LEU M   4       6.814 -13.125  55.407  1.00 45.70           C  
ANISOU 5427  CB  LEU M   4     5911   6042   5412   -402   -648   -587       C  
ATOM   5428  CG  LEU M   4       5.304 -13.052  55.679  1.00 46.60           C  
ANISOU 5428  CG  LEU M   4     5973   6289   5444   -350   -541   -654       C  
ATOM   5429  CD1 LEU M   4       4.954 -12.374  56.967  1.00 49.30           C  
ANISOU 5429  CD1 LEU M   4     6275   6814   5644   -302   -519   -906       C  
ATOM   5430  CD2 LEU M   4       4.591 -12.360  54.566  1.00 45.68           C  
ANISOU 5430  CD2 LEU M   4     5809   6005   5541   -284   -503   -645       C  
ATOM   5431  N   THR M   5       9.232 -14.963  56.835  1.00 47.04           N  
ANISOU 5431  N   THR M   5     6133   6455   5287   -547   -793   -322       N  
ATOM   5432  CA  THR M   5      10.489 -15.692  56.739  1.00 46.67           C  
ANISOU 5432  CA  THR M   5     6098   6372   5261   -590   -861   -138       C  
ATOM   5433  C   THR M   5      10.351 -17.026  56.019  1.00 46.40           C  
ANISOU 5433  C   THR M   5     6079   6245   5305   -605   -803    100       C  
ATOM   5434  O   THR M   5       9.678 -17.947  56.528  1.00 48.48           O  
ANISOU 5434  O   THR M   5     6317   6628   5476   -628   -741    228       O  
ATOM   5435  CB  THR M   5      11.018 -15.973  58.128  1.00 48.40           C  
ANISOU 5435  CB  THR M   5     6272   6877   5241   -623   -914   -112       C  
ATOM   5436  OG1 THR M   5      11.567 -14.763  58.651  1.00 49.79           O  
ANISOU 5436  OG1 THR M   5     6426   7102   5389   -627  -1004   -374       O  
ATOM   5437  CG2 THR M   5      12.082 -17.032  58.084  1.00 47.87           C  
ANISOU 5437  CG2 THR M   5     6194   6797   5199   -652   -956    161       C  
ATOM   5438  N   GLN M   6      10.993 -17.137  54.850  1.00 44.70           N  
ANISOU 5438  N   GLN M   6     5885   5825   5274   -593   -822    154       N  
ATOM   5439  CA  GLN M   6      11.018 -18.396  54.082  1.00 43.43           C  
ANISOU 5439  CA  GLN M   6     5727   5555   5220   -600   -774    308       C  
ATOM   5440  C   GLN M   6      12.423 -18.931  54.021  1.00 43.23           C  
ANISOU 5440  C   GLN M   6     5692   5471   5263   -594   -830    440       C  
ATOM   5441  O   GLN M   6      13.355 -18.163  53.947  1.00 42.99           O  
ANISOU 5441  O   GLN M   6     5655   5428   5250   -583   -903    402       O  
ATOM   5442  CB  GLN M   6      10.581 -18.147  52.656  1.00 42.23           C  
ANISOU 5442  CB  GLN M   6     5575   5279   5192   -572   -739    234       C  
ATOM   5443  CG  GLN M   6       9.141 -17.744  52.488  1.00 42.32           C  
ANISOU 5443  CG  GLN M   6     5571   5340   5168   -569   -678    137       C  
ATOM   5444  CD  GLN M   6       8.845 -17.341  51.048  1.00 41.27           C  
ANISOU 5444  CD  GLN M   6     5405   5146   5130   -535   -662     93       C  
ATOM   5445  OE1 GLN M   6       8.618 -16.167  50.751  1.00 42.21           O  
ANISOU 5445  OE1 GLN M   6     5495   5260   5283   -492   -673     38       O  
ATOM   5446  NE2 GLN M   6       8.909 -18.304  50.142  1.00 40.03           N  
ANISOU 5446  NE2 GLN M   6     5229   4953   5028   -548   -638    121       N  
ATOM   5447  N   PRO M   7      12.585 -20.261  54.011  1.00 44.75           N  
ANISOU 5447  N   PRO M   7     5864   5602   5536   -601   -793    603       N  
ATOM   5448  CA  PRO M   7      13.942 -20.786  53.854  1.00 44.13           C  
ANISOU 5448  CA  PRO M   7     5760   5450   5559   -570   -834    733       C  
ATOM   5449  C   PRO M   7      14.343 -20.416  52.447  1.00 42.91           C  
ANISOU 5449  C   PRO M   7     5612   5173   5520   -525   -829    623       C  
ATOM   5450  O   PRO M   7      13.491 -20.265  51.589  1.00 42.17           O  
ANISOU 5450  O   PRO M   7     5530   5043   5451   -522   -779    502       O  
ATOM   5451  CB  PRO M   7      13.760 -22.297  54.032  1.00 44.88           C  
ANISOU 5451  CB  PRO M   7     5816   5448   5789   -576   -772    912       C  
ATOM   5452  CG  PRO M   7      12.378 -22.565  53.559  1.00 45.38           C  
ANISOU 5452  CG  PRO M   7     5896   5453   5896   -613   -695    806       C  
ATOM   5453  CD  PRO M   7      11.560 -21.324  53.926  1.00 45.34           C  
ANISOU 5453  CD  PRO M   7     5922   5621   5683   -632   -708    664       C  
ATOM   5454  N   PRO M   8      15.623 -20.167  52.223  1.00 43.81           N  
ANISOU 5454  N   PRO M   8     5695   5275   5676   -491   -884    678       N  
ATOM   5455  CA  PRO M   8      16.049 -19.656  50.910  1.00 42.31           C  
ANISOU 5455  CA  PRO M   8     5480   5038   5560   -445   -878    608       C  
ATOM   5456  C   PRO M   8      15.865 -20.692  49.815  1.00 42.97           C  
ANISOU 5456  C   PRO M   8     5539   5038   5748   -396   -794    563       C  
ATOM   5457  O   PRO M   8      15.688 -20.317  48.649  1.00 43.15           O  
ANISOU 5457  O   PRO M   8     5530   5098   5767   -363   -766    468       O  
ATOM   5458  CB  PRO M   8      17.544 -19.358  51.083  1.00 41.88           C  
ANISOU 5458  CB  PRO M   8     5370   5007   5535   -426   -954    719       C  
ATOM   5459  CG  PRO M   8      17.841 -19.531  52.490  1.00 43.95           C  
ANISOU 5459  CG  PRO M   8     5634   5351   5715   -469  -1016    814       C  
ATOM   5460  CD  PRO M   8      16.736 -20.339  53.153  1.00 44.35           C  
ANISOU 5460  CD  PRO M   8     5722   5415   5714   -494   -957    833       C  
ATOM   5461  N   SER M   9      15.903 -21.983  50.171  1.00 43.79           N  
ANISOU 5461  N   SER M   9     5637   5041   5959   -388   -755    628       N  
ATOM   5462  CA  SER M   9      15.858 -23.016  49.131  1.00 44.28           C  
ANISOU 5462  CA  SER M   9     5660   4989   6174   -338   -679    523       C  
ATOM   5463  C   SER M   9      15.345 -24.369  49.612  1.00 45.35           C  
ANISOU 5463  C   SER M   9     5788   4950   6491   -365   -628    566       C  
ATOM   5464  O   SER M   9      15.555 -24.764  50.748  1.00 46.65           O  
ANISOU 5464  O   SER M   9     5947   5085   6695   -386   -649    776       O  
ATOM   5465  CB  SER M   9      17.236 -23.169  48.473  1.00 44.06           C  
ANISOU 5465  CB  SER M   9     5563   4958   6219   -240   -679    551       C  
ATOM   5466  OG  SER M   9      17.928 -24.245  49.062  1.00 46.12           O  
ANISOU 5466  OG  SER M   9     5789   5077   6659   -199   -665    689       O  
ATOM   5467  N   VAL M  10      14.681 -25.083  48.719  1.00 45.66           N  
ANISOU 5467  N   VAL M  10     5803   4891   6653   -369   -565    373       N  
ATOM   5468  CA  VAL M  10      14.075 -26.356  49.056  1.00 46.80           C  
ANISOU 5468  CA  VAL M  10     5920   4820   7042   -415   -516    392       C  
ATOM   5469  C   VAL M  10      14.121 -27.178  47.803  1.00 48.06           C  
ANISOU 5469  C   VAL M  10     6019   4850   7393   -370   -460    118       C  
ATOM   5470  O   VAL M  10      13.903 -26.642  46.716  1.00 47.30           O  
ANISOU 5470  O   VAL M  10     5911   4922   7139   -351   -456   -112       O  
ATOM   5471  CB  VAL M  10      12.612 -26.202  49.488  1.00 45.87           C  
ANISOU 5471  CB  VAL M  10     5829   4752   6845   -530   -509    383       C  
ATOM   5472  CG1 VAL M  10      11.969 -27.537  49.513  1.00 47.74           C  
ANISOU 5472  CG1 VAL M  10     6006   4745   7387   -591   -456    366       C  
ATOM   5473  CG2 VAL M  10      12.524 -25.575  50.850  1.00 45.41           C  
ANISOU 5473  CG2 VAL M  10     5808   4839   6609   -566   -550    625       C  
ATOM   5474  N   SER M  11      14.417 -28.471  47.952  1.00 50.58           N  
ANISOU 5474  N   SER M  11     6277   4883   8059   -345   -415    142       N  
ATOM   5475  CA  SER M  11      14.547 -29.354  46.800  1.00 52.03           C  
ANISOU 5475  CA  SER M  11     6384   4913   8472   -290   -357   -183       C  
ATOM   5476  C   SER M  11      13.809 -30.653  47.036  1.00 54.45           C  
ANISOU 5476  C   SER M  11     6633   4876   9181   -369   -315   -229       C  
ATOM   5477  O   SER M  11      13.665 -31.087  48.174  1.00 55.28           O  
ANISOU 5477  O   SER M  11     6729   4818   9458   -420   -317     98       O  
ATOM   5478  CB  SER M  11      16.017 -29.607  46.497  1.00 52.83           C  
ANISOU 5478  CB  SER M  11     6432   4968   8675   -132   -333   -165       C  
ATOM   5479  OG  SER M  11      16.648 -30.192  47.603  1.00 54.46           O  
ANISOU 5479  OG  SER M  11     6612   4965   9114   -103   -335    175       O  
ATOM   5480  N   VAL M  12      13.339 -31.263  45.952  1.00 56.78           N  
ANISOU 5480  N   VAL M  12     6864   5082   9626   -386   -279   -633       N  
ATOM   5481  CA  VAL M  12      12.576 -32.515  46.015  1.00 59.87           C  
ANISOU 5481  CA  VAL M  12     7176   5107  10464   -484   -245   -750       C  
ATOM   5482  C   VAL M  12      12.910 -33.442  44.873  1.00 62.55           C  
ANISOU 5482  C   VAL M  12     7413   5254  11100   -413   -195  -1212       C  
ATOM   5483  O   VAL M  12      13.275 -33.009  43.788  1.00 62.41           O  
ANISOU 5483  O   VAL M  12     7380   5511  10823   -326   -189  -1534       O  
ATOM   5484  CB  VAL M  12      11.081 -32.250  45.901  1.00 59.02           C  
ANISOU 5484  CB  VAL M  12     7079   5125  10221   -655   -275   -863       C  
ATOM   5485  CG1 VAL M  12      10.537 -31.900  47.237  1.00 58.04           C  
ANISOU 5485  CG1 VAL M  12     7004   5032  10016   -744   -296   -422       C  
ATOM   5486  CG2 VAL M  12      10.828 -31.130  44.896  1.00 56.53           C  
ANISOU 5486  CG2 VAL M  12     6798   5251   9430   -634   -307  -1116       C  
ATOM   5487  N   ALA M  13      12.741 -34.729  45.096  1.00 66.07           N  
ANISOU 5487  N   ALA M  13     7765   5235  12103   -452   -155  -1256       N  
ATOM   5488  CA  ALA M  13      12.910 -35.647  44.000  1.00 69.57           C  
ANISOU 5488  CA  ALA M  13     8095   5469  12869   -399   -107  -1786       C  
ATOM   5489  C   ALA M  13      11.652 -35.590  43.126  1.00 70.16           C  
ANISOU 5489  C   ALA M  13     8135   5717  12806   -554   -143  -2230       C  
ATOM   5490  O   ALA M  13      10.541 -35.399  43.630  1.00 69.78           O  
ANISOU 5490  O   ALA M  13     8112   5694  12706   -727   -186  -2063       O  
ATOM   5491  CB  ALA M  13      13.162 -37.041  44.525  1.00 73.50           C  
ANISOU 5491  CB  ALA M  13     8482   5355  14089   -387    -52  -1692       C  
ATOM   5492  N   PRO M  14      11.822 -35.725  41.809  1.00 71.29           N  
ANISOU 5492  N   PRO M  14     8200   6038  12850   -487   -126  -2793       N  
ATOM   5493  CA  PRO M  14      10.650 -35.752  40.972  1.00 72.27           C  
ANISOU 5493  CA  PRO M  14     8257   6355  12847   -638   -171  -3225       C  
ATOM   5494  C   PRO M  14       9.609 -36.698  41.546  1.00 74.49           C  
ANISOU 5494  C   PRO M  14     8477   6177  13647   -843   -188  -3206       C  
ATOM   5495  O   PRO M  14       9.905 -37.842  41.884  1.00 78.58           O  
ANISOU 5495  O   PRO M  14     8917   6146  14794   -837   -143  -3226       O  
ATOM   5496  CB  PRO M  14      11.183 -36.282  39.638  1.00 75.90           C  
ANISOU 5496  CB  PRO M  14     8586   6908  13343   -520   -130  -3871       C  
ATOM   5497  CG  PRO M  14      12.499 -36.932  39.961  1.00 77.62           C  
ANISOU 5497  CG  PRO M  14     8788   6754  13952   -328    -47  -3776       C  
ATOM   5498  CD  PRO M  14      13.036 -36.091  41.069  1.00 73.40           C  
ANISOU 5498  CD  PRO M  14     8396   6292  13201   -277    -59  -3087       C  
ATOM   5499  N   GLY M  15       8.389 -36.222  41.676  1.00 73.17           N  
ANISOU 5499  N   GLY M  15     8325   6223  13253  -1022   -250  -3131       N  
ATOM   5500  CA  GLY M  15       7.326 -37.085  42.156  1.00 76.20           C  
ANISOU 5500  CA  GLY M  15     8622   6217  14113  -1236   -269  -3108       C  
ATOM   5501  C   GLY M  15       7.013 -36.873  43.623  1.00 74.55           C  
ANISOU 5501  C   GLY M  15     8485   5869  13970  -1306   -264  -2424       C  
ATOM   5502  O   GLY M  15       5.899 -37.118  44.071  1.00 75.83           O  
ANISOU 5502  O   GLY M  15     8590   5932  14291  -1498   -289  -2292       O  
ATOM   5503  N   GLN M  16       7.987 -36.416  44.389  1.00 72.20           N  
ANISOU 5503  N   GLN M  16     8293   5606  13534  -1153   -233  -1987       N  
ATOM   5504  CA  GLN M  16       7.740 -36.220  45.804  1.00 70.72           C  
ANISOU 5504  CA  GLN M  16     8150   5360  13360  -1209   -228  -1360       C  
ATOM   5505  C   GLN M  16       7.050 -34.929  46.146  1.00 67.02           C  
ANISOU 5505  C   GLN M  16     7784   5381  12298  -1256   -270  -1152       C  
ATOM   5506  O   GLN M  16       6.853 -34.080  45.277  1.00 66.42           O  
ANISOU 5506  O   GLN M  16     7753   5694  11790  -1229   -304  -1439       O  
ATOM   5507  CB  GLN M  16       8.999 -36.427  46.618  1.00 70.74           C  
ANISOU 5507  CB  GLN M  16     8180   5171  13525  -1050   -186   -959       C  
ATOM   5508  CG  GLN M  16       8.982 -37.836  47.175  1.00 76.72           C  
ANISOU 5508  CG  GLN M  16     8789   5334  15029  -1108   -141   -775       C  
ATOM   5509  CD  GLN M  16      10.346 -38.445  47.197  1.00 79.12           C  
ANISOU 5509  CD  GLN M  16     9053   5334  15674   -915    -89   -719       C  
ATOM   5510  OE1 GLN M  16      11.266 -37.877  47.771  1.00 76.95           O  
ANISOU 5510  OE1 GLN M  16     8852   5257  15128   -775    -87   -372       O  
ATOM   5511  NE2 GLN M  16      10.505 -39.589  46.540  1.00 83.14           N  
ANISOU 5511  NE2 GLN M  16     9432   5368  16791   -901    -47  -1094       N  
ATOM   5512  N   THR M  17       6.635 -34.796  47.402  1.00 65.83           N  
ANISOU 5512  N   THR M  17     7644   5227  12141  -1323   -262   -651       N  
ATOM   5513  CA  THR M  17       5.801 -33.675  47.800  1.00 62.64           C  
ANISOU 5513  CA  THR M  17     7309   5243  11249  -1378   -290   -484       C  
ATOM   5514  C   THR M  17       6.730 -32.587  48.283  1.00 59.99           C  
ANISOU 5514  C   THR M  17     7109   5194  10490  -1219   -299   -252       C  
ATOM   5515  O   THR M  17       7.660 -32.875  49.028  1.00 61.00           O  
ANISOU 5515  O   THR M  17     7247   5178  10753  -1134   -279     45       O  
ATOM   5516  CB  THR M  17       4.831 -34.090  48.907  1.00 63.48           C  
ANISOU 5516  CB  THR M  17     7327   5251  11542  -1529   -269    -93       C  
ATOM   5517  OG1 THR M  17       3.924 -35.046  48.381  1.00 67.18           O  
ANISOU 5517  OG1 THR M  17     7653   5447  12425  -1701   -273   -334       O  
ATOM   5518  CG2 THR M  17       4.025 -32.948  49.375  1.00 61.15           C  
ANISOU 5518  CG2 THR M  17     7090   5389  10756  -1557   -282     64       C  
ATOM   5519  N   ALA M  18       6.522 -31.352  47.832  1.00 57.00           N  
ANISOU 5519  N   ALA M  18     6815   5210   9633  -1178   -332   -383       N  
ATOM   5520  CA  ALA M  18       7.334 -30.232  48.321  1.00 54.62           C  
ANISOU 5520  CA  ALA M  18     6628   5160   8963  -1050   -350   -177       C  
ATOM   5521  C   ALA M  18       6.568 -29.366  49.331  1.00 53.63           C  
ANISOU 5521  C   ALA M  18     6540   5289   8547  -1096   -356     93       C  
ATOM   5522  O   ALA M  18       5.386 -29.079  49.159  1.00 52.82           O  
ANISOU 5522  O   ALA M  18     6404   5326   8338  -1186   -356      9       O  
ATOM   5523  CB  ALA M  18       7.872 -29.371  47.174  1.00 52.32           C  
ANISOU 5523  CB  ALA M  18     6387   5110   8384   -944   -377   -462       C  
ATOM   5524  N   ARG M  19       7.264 -28.969  50.400  1.00 53.12           N  
ANISOU 5524  N   ARG M  19     6527   5303   8353  -1029   -361    402       N  
ATOM   5525  CA  ARG M  19       6.683 -28.114  51.430  1.00 51.38           C  
ANISOU 5525  CA  ARG M  19     6333   5357   7833  -1049   -363    613       C  
ATOM   5526  C   ARG M  19       7.534 -26.865  51.605  1.00 49.50           C  
ANISOU 5526  C   ARG M  19     6197   5342   7270   -935   -407    611       C  
ATOM   5527  O   ARG M  19       8.741 -26.928  51.854  1.00 50.41           O  
ANISOU 5527  O   ARG M  19     6337   5405   7412   -858   -431    715       O  
ATOM   5528  CB  ARG M  19       6.476 -28.889  52.728  1.00 53.33           C  
ANISOU 5528  CB  ARG M  19     6492   5545   8226  -1110   -328    998       C  
ATOM   5529  CG  ARG M  19       5.224 -29.816  52.678  1.00 55.37           C  
ANISOU 5529  CG  ARG M  19     6626   5648   8762  -1260   -283   1029       C  
ATOM   5530  CD  ARG M  19       5.179 -30.776  53.825  1.00 57.60           C  
ANISOU 5530  CD  ARG M  19     6781   5818   9286  -1319   -242   1467       C  
ATOM   5531  NE  ARG M  19       5.702 -32.078  53.436  1.00 60.88           N  
ANISOU 5531  NE  ARG M  19     7117   5786  10228  -1339   -229   1489       N  
ATOM   5532  CZ  ARG M  19       4.949 -33.141  53.137  1.00 64.12           C  
ANISOU 5532  CZ  ARG M  19     7397   5882  11083  -1474   -200   1469       C  
ATOM   5533  NH1 ARG M  19       3.603 -33.088  53.182  1.00 64.52           N  
ANISOU 5533  NH1 ARG M  19     7376   6044  11094  -1613   -183   1455       N  
ATOM   5534  NH2 ARG M  19       5.547 -34.270  52.783  1.00 66.30           N  
ANISOU 5534  NH2 ARG M  19     7600   5713  11879  -1470   -187   1450       N  
ATOM   5535  N   ILE M  20       6.930 -25.719  51.343  1.00 47.12           N  
ANISOU 5535  N   ILE M  20     5937   5265   6702   -923   -420    473       N  
ATOM   5536  CA  ILE M  20       7.634 -24.471  51.474  1.00 45.47           C  
ANISOU 5536  CA  ILE M  20     5804   5222   6249   -832   -465    451       C  
ATOM   5537  C   ILE M  20       6.978 -23.664  52.581  1.00 45.67           C  
ANISOU 5537  C   ILE M  20     5836   5472   6045   -841   -458    548       C  
ATOM   5538  O   ILE M  20       5.776 -23.392  52.555  1.00 45.73           O  
ANISOU 5538  O   ILE M  20     5810   5583   5983   -881   -423    489       O  
ATOM   5539  CB  ILE M  20       7.628 -23.666  50.181  1.00 44.24           C  
ANISOU 5539  CB  ILE M  20     5668   5130   6011   -783   -486    216       C  
ATOM   5540  CG1 ILE M  20       8.317 -24.445  49.080  1.00 44.73           C  
ANISOU 5540  CG1 ILE M  20     5703   5044   6248   -758   -485     81       C  
ATOM   5541  CG2 ILE M  20       8.364 -22.357  50.380  1.00 41.75           C  
ANISOU 5541  CG2 ILE M  20     5408   4937   5517   -703   -533    231       C  
ATOM   5542  CD1 ILE M  20       8.154 -23.806  47.750  1.00 44.45           C  
ANISOU 5542  CD1 ILE M  20     5640   5148   6102   -719   -496   -125       C  
ATOM   5543  N   SER M  21       7.767 -23.313  53.582  1.00 45.99           N  
ANISOU 5543  N   SER M  21     5899   5615   5960   -802   -492    683       N  
ATOM   5544  CA  SER M  21       7.197 -22.685  54.746  1.00 46.35           C  
ANISOU 5544  CA  SER M  21     5926   5911   5773   -807   -480    744       C  
ATOM   5545  C   SER M  21       7.396 -21.170  54.730  1.00 44.96           C  
ANISOU 5545  C   SER M  21     5809   5859   5416   -739   -523    549       C  
ATOM   5546  O   SER M  21       8.245 -20.650  54.013  1.00 43.49           O  
ANISOU 5546  O   SER M  21     5670   5571   5283   -695   -576    453       O  
ATOM   5547  CB  SER M  21       7.792 -23.271  56.001  1.00 47.52           C  
ANISOU 5547  CB  SER M  21     6021   6170   5863   -818   -490   1012       C  
ATOM   5548  OG  SER M  21       9.099 -22.783  56.110  1.00 47.76           O  
ANISOU 5548  OG  SER M  21     6097   6216   5835   -761   -568    992       O  
ATOM   5549  N   CYS M  22       6.596 -20.481  55.539  1.00 45.59           N  
ANISOU 5549  N   CYS M  22     5863   6154   5306   -730   -496    497       N  
ATOM   5550  CA  CYS M  22       6.560 -19.029  55.594  1.00 44.86           C  
ANISOU 5550  CA  CYS M  22     5801   6138   5104   -664   -523    281       C  
ATOM   5551  C   CYS M  22       6.058 -18.681  56.987  1.00 47.33           C  
ANISOU 5551  C   CYS M  22     6062   6745   5178   -653   -494    263       C  
ATOM   5552  O   CYS M  22       4.897 -18.989  57.362  1.00 48.96           O  
ANISOU 5552  O   CYS M  22     6200   7097   5307   -671   -412    314       O  
ATOM   5553  CB  CYS M  22       5.595 -18.487  54.540  1.00 43.99           C  
ANISOU 5553  CB  CYS M  22     5684   5948   5083   -639   -484    148       C  
ATOM   5554  SG  CYS M  22       5.291 -16.712  54.589  1.00 43.37           S  
ANISOU 5554  SG  CYS M  22     5604   5905   4969   -545   -494    -83       S  
ATOM   5555  N   SER M  23       6.935 -18.078  57.782  1.00 47.65           N  
ANISOU 5555  N   SER M  23     6110   6912   5082   -629   -563    187       N  
ATOM   5556  CA  SER M  23       6.591 -17.819  59.170  1.00 50.20           C  
ANISOU 5556  CA  SER M  23     6359   7592   5122   -616   -542    144       C  
ATOM   5557  C   SER M  23       6.817 -16.365  59.640  1.00 50.91           C  
ANISOU 5557  C   SER M  23     6456   7775   5112   -556   -591   -200       C  
ATOM   5558  O   SER M  23       7.633 -15.644  59.082  1.00 50.03           O  
ANISOU 5558  O   SER M  23     6403   7447   5161   -545   -672   -336       O  
ATOM   5559  CB  SER M  23       7.319 -18.814  60.072  1.00 51.67           C  
ANISOU 5559  CB  SER M  23     6482   7976   5174   -663   -572    425       C  
ATOM   5560  OG  SER M  23       8.718 -18.631  59.968  1.00 51.60           O  
ANISOU 5560  OG  SER M  23     6516   7873   5217   -666   -683    414       O  
ATOM   5561  N   GLY M  24       6.055 -15.947  60.650  1.00 52.66           N  
ANISOU 5561  N   GLY M  24     6599   8318   5092   -516   -536   -348       N  
ATOM   5562  CA  GLY M  24       6.133 -14.602  61.215  1.00 54.55           C  
ANISOU 5562  CA  GLY M  24     6819   8656   5250   -453   -570   -740       C  
ATOM   5563  C   GLY M  24       5.127 -14.492  62.347  1.00 57.36           C  
ANISOU 5563  C   GLY M  24     7060   9442   5291   -401   -476   -856       C  
ATOM   5564  O   GLY M  24       4.257 -15.360  62.460  1.00 57.80           O  
ANISOU 5564  O   GLY M  24     7057   9651   5254   -416   -377   -603       O  
ATOM   5565  N   ASP M  25       5.227 -13.437  63.165  1.00 59.31           N  
ANISOU 5565  N   ASP M  25     7256   9889   5389   -342   -502  -1250       N  
ATOM   5566  CA  ASP M  25       4.391 -13.279  64.363  1.00 62.60           C  
ANISOU 5566  CA  ASP M  25     7536  10808   5442   -277   -412  -1416       C  
ATOM   5567  C   ASP M  25       2.904 -13.300  64.091  1.00 62.48           C  
ANISOU 5567  C   ASP M  25     7474  10801   5465   -203   -257  -1386       C  
ATOM   5568  O   ASP M  25       2.385 -12.444  63.389  1.00 61.87           O  
ANISOU 5568  O   ASP M  25     7434  10413   5661   -127   -223  -1604       O  
ATOM   5569  CB  ASP M  25       4.720 -11.978  65.085  1.00 66.46           C  
ANISOU 5569  CB  ASP M  25     7980  11425   5845   -214   -468  -1960       C  
ATOM   5570  CG  ASP M  25       5.984 -12.077  65.945  1.00 69.61           C  
ANISOU 5570  CG  ASP M  25     8336  12123   5990   -290   -608  -2015       C  
ATOM   5571  OD1 ASP M  25       6.791 -13.010  65.741  1.00 68.93           O  
ANISOU 5571  OD1 ASP M  25     8285  12006   5900   -383   -677  -1621       O  
ATOM   5572  OD2 ASP M  25       6.196 -11.211  66.824  1.00 72.95           O  
ANISOU 5572  OD2 ASP M  25     8675  12817   6224   -255   -654  -2473       O  
ATOM   5573  N   SER M  26       2.214 -14.272  64.664  1.00 63.24           N  
ANISOU 5573  N   SER M  26     7462  11267   5301   -226   -163  -1085       N  
ATOM   5574  CA  SER M  26       0.774 -14.410  64.462  1.00 63.60           C  
ANISOU 5574  CA  SER M  26     7432  11369   5364   -173    -15  -1009       C  
ATOM   5575  C   SER M  26       0.355 -14.486  63.005  1.00 59.99           C  
ANISOU 5575  C   SER M  26     7076  10401   5318   -193     -5   -890       C  
ATOM   5576  O   SER M  26      -0.728 -14.010  62.681  1.00 59.88           O  
ANISOU 5576  O   SER M  26     7012  10345   5393   -112     89  -1002       O  
ATOM   5577  CB  SER M  26       0.015 -13.242  65.093  1.00 66.80           C  
ANISOU 5577  CB  SER M  26     7743  12009   5630    -21     70  -1466       C  
ATOM   5578  OG  SER M  26       0.349 -13.066  66.444  1.00 70.46           O  
ANISOU 5578  OG  SER M  26     8089  13012   5669      9     63  -1661       O  
ATOM   5579  N   LEU M  27       1.172 -15.086  62.140  1.00 57.27           N  
ANISOU 5579  N   LEU M  27     6846   9712   5200   -292    -98   -668       N  
ATOM   5580  CA  LEU M  27       0.807 -15.202  60.740  1.00 54.95           C  
ANISOU 5580  CA  LEU M  27     6623   9012   5243   -314    -94   -569       C  
ATOM   5581  C   LEU M  27      -0.586 -15.812  60.608  1.00 55.91           C  
ANISOU 5581  C   LEU M  27     6639   9258   5345   -328     26   -383       C  
ATOM   5582  O   LEU M  27      -1.377 -15.396  59.760  1.00 55.44           O  
ANISOU 5582  O   LEU M  27     6569   9025   5469   -285     66   -447       O  
ATOM   5583  CB  LEU M  27       1.808 -16.046  59.980  1.00 53.03           C  
ANISOU 5583  CB  LEU M  27     6480   8492   5177   -420   -188   -331       C  
ATOM   5584  CG  LEU M  27       2.284 -15.499  58.627  1.00 50.97           C  
ANISOU 5584  CG  LEU M  27     6323   7818   5226   -407   -256   -419       C  
ATOM   5585  CD1 LEU M  27       2.678 -16.604  57.697  1.00 48.79           C  
ANISOU 5585  CD1 LEU M  27     6096   7328   5114   -503   -290   -164       C  
ATOM   5586  CD2 LEU M  27       1.284 -14.601  57.971  1.00 50.67           C  
ANISOU 5586  CD2 LEU M  27     6250   7674   5330   -319   -197   -575       C  
ATOM   5587  N   GLY M  28      -0.909 -16.757  61.492  1.00 57.41           N  
ANISOU 5587  N   GLY M  28     6721   9782   5311   -388     84   -133       N  
ATOM   5588  CA  GLY M  28      -2.169 -17.476  61.420  1.00 57.81           C  
ANISOU 5588  CA  GLY M  28     6646   9954   5366   -434    191     98       C  
ATOM   5589  C   GLY M  28      -3.388 -16.603  61.586  1.00 59.36           C  
ANISOU 5589  C   GLY M  28     6738  10333   5483   -310    301   -116       C  
ATOM   5590  O   GLY M  28      -4.515 -17.056  61.411  1.00 60.11           O  
ANISOU 5590  O   GLY M  28     6715  10518   5605   -341    390     51       O  
ATOM   5591  N   SER M  29      -3.176 -15.351  61.958  1.00 60.10           N  
ANISOU 5591  N   SER M  29     6855  10481   5498   -169    299   -495       N  
ATOM   5592  CA  SER M  29      -4.291 -14.425  62.091  1.00 61.92           C  
ANISOU 5592  CA  SER M  29     6980  10841   5707    -20    411   -738       C  
ATOM   5593  C   SER M  29      -4.297 -13.467  60.908  1.00 59.58           C  
ANISOU 5593  C   SER M  29     6770  10100   5768     55    367   -930       C  
ATOM   5594  O   SER M  29      -4.978 -12.451  60.914  1.00 60.33           O  
ANISOU 5594  O   SER M  29     6793  10191   5936    207    439  -1179       O  
ATOM   5595  CB  SER M  29      -4.204 -13.647  63.406  1.00 65.32           C  
ANISOU 5595  CB  SER M  29     7328  11665   5824    108    461  -1072       C  
ATOM   5596  OG  SER M  29      -3.102 -12.750  63.380  1.00 65.77           O  
ANISOU 5596  OG  SER M  29     7508  11496   5985    150    349  -1402       O  
ATOM   5597  N   LYS M  30      -3.506 -13.794  59.896  1.00 56.72           N  
ANISOU 5597  N   LYS M  30     6541   9377   5635    -43    254   -795       N  
ATOM   5598  CA  LYS M  30      -3.477 -13.008  58.676  1.00 55.29           C  
ANISOU 5598  CA  LYS M  30     6412   8819   5778     12    209   -880       C  
ATOM   5599  C   LYS M  30      -3.679 -13.926  57.497  1.00 52.79           C  
ANISOU 5599  C   LYS M  30     6114   8339   5607   -111    174   -591       C  
ATOM   5600  O   LYS M  30      -3.245 -15.061  57.535  1.00 52.05           O  
ANISOU 5600  O   LYS M  30     6061   8263   5452   -249    136   -387       O  
ATOM   5601  CB  LYS M  30      -2.125 -12.321  58.528  1.00 54.42