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Entry: 5LE5
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HEADER    HYDROLASE                               29-JUN-16   5LE5              
TITLE     NATIVE HUMAN 20S PROTEASOME AT 1.8 ANGSTROM                           
CAVEAT     5LE5    6V1 U 47 HAS WRONG CHIRALITY AT ATOM C1                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND   3 CHAIN: A, O;                                                         
COMPND   4 SYNONYM: MACROPAIN SUBUNIT C3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND   5 SUBUNIT C3,PROTEASOME COMPONENT C3;                                  
COMPND   6 EC: 3.4.25.1;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND   9 CHAIN: B, P;                                                         
COMPND  10 SYNONYM: MACROPAIN SUBUNIT C9,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  11 SUBUNIT C9,PROTEASOME COMPONENT C9,PROTEASOME SUBUNIT L;             
COMPND  12 EC: 3.4.25.1;                                                        
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-7;                           
COMPND  15 CHAIN: C, Q;                                                         
COMPND  16 SYNONYM: PROTEASOME SUBUNIT RC6-1,PROTEASOME SUBUNIT XAPC7;          
COMPND  17 EC: 3.4.25.1;                                                        
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  20 CHAIN: D, R;                                                         
COMPND  21 SYNONYM: MACROPAIN ZETA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  22 ZETA CHAIN,PROTEASOME ZETA CHAIN;                                    
COMPND  23 EC: 3.4.25.1;                                                        
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  26 CHAIN: E, S;                                                         
COMPND  27 SYNONYM: 30 KDA PROSOMAL PROTEIN,PROS-30,MACROPAIN SUBUNIT C2,       
COMPND  28 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2,PROTEASOME COMPONENT 
COMPND  29 C2,PROTEASOME NU CHAIN;                                              
COMPND  30 EC: 3.4.25.1;                                                        
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND  33 CHAIN: F, T;                                                         
COMPND  34 SYNONYM: MACROPAIN SUBUNIT C8,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  35 SUBUNIT C8,PROTEASOME COMPONENT C8;                                  
COMPND  36 EC: 3.4.25.1;                                                        
COMPND  37 MOL_ID: 7;                                                           
COMPND  38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  39 CHAIN: G, U;                                                         
COMPND  40 SYNONYM: 27 KDA PROSOMAL PROTEIN,P27K,MACROPAIN IOTA CHAIN,          
COMPND  41 MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN,PROTEASOME IOTA      
COMPND  42 CHAIN;                                                               
COMPND  43 EC: 3.4.25.1;                                                        
COMPND  44 MOL_ID: 8;                                                           
COMPND  45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  46 CHAIN: H, V;                                                         
COMPND  47 SYNONYM: MACROPAIN CHAIN Z,MULTICATALYTIC ENDOPEPTIDASE COMPLEX CHAIN
COMPND  48 Z,PROTEASOME SUBUNIT Z;                                              
COMPND  49 EC: 3.4.25.1;                                                        
COMPND  50 MOL_ID: 9;                                                           
COMPND  51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  52 CHAIN: I, W;                                                         
COMPND  53 SYNONYM: PROTEASOME CHAIN 13,PROTEASOME COMPONENT C10-II,PROTEASOME  
COMPND  54 THETA CHAIN;                                                         
COMPND  55 EC: 3.4.25.1;                                                        
COMPND  56 MOL_ID: 10;                                                          
COMPND  57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  58 CHAIN: J, X;                                                         
COMPND  59 SYNONYM: MACROPAIN SUBUNIT C7-I,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  60 SUBUNIT C7-I,PROTEASOME COMPONENT C7-I;                              
COMPND  61 EC: 3.4.25.1;                                                        
COMPND  62 MOL_ID: 11;                                                          
COMPND  63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  64 CHAIN: K, Y;                                                         
COMPND  65 SYNONYM: MACROPAIN EPSILON CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  66 EPSILON CHAIN,PROTEASOME CHAIN 6,PROTEASOME EPSILON CHAIN,PROTEASOME 
COMPND  67 SUBUNIT MB1,PROTEASOME SUBUNIT X;                                    
COMPND  68 EC: 3.4.25.1;                                                        
COMPND  69 MOL_ID: 12;                                                          
COMPND  70 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  71 CHAIN: L, Z;                                                         
COMPND  72 SYNONYM: MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  73 SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN;           
COMPND  74 EC: 3.4.25.1;                                                        
COMPND  75 MOL_ID: 13;                                                          
COMPND  76 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  77 CHAIN: M, a;                                                         
COMPND  78 SYNONYM: 26 KDA PROSOMAL PROTEIN,PROS-26,MACROPAIN BETA CHAIN,       
COMPND  79 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN,PROTEASOME BETA      
COMPND  80 CHAIN,PROTEASOME CHAIN 3,HSN3;                                       
COMPND  81 EC: 3.4.25.1;                                                        
COMPND  82 MOL_ID: 14;                                                          
COMPND  83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  84 CHAIN: N, b;                                                         
COMPND  85 SYNONYM: MACROPAIN DELTA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  86 DELTA CHAIN,PROTEASOME DELTA CHAIN,PROTEASOME SUBUNIT Y;             
COMPND  87 EC: 3.4.25.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HELA;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: HELA;                                                     
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: HELA;                                                     
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: HELA;                                                     
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 CELL_LINE: HELA;                                                     
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 CELL_LINE: HELA;                                                     
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 CELL_LINE: HELA;                                                     
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 CELL_LINE: HELA;                                                     
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 CELL_LINE: HELA;                                                     
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606;                                                
SOURCE  50 CELL_LINE: HELA;                                                     
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  53 ORGANISM_COMMON: HUMAN;                                              
SOURCE  54 ORGANISM_TAXID: 9606;                                                
SOURCE  55 CELL_LINE: HELA;                                                     
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  58 ORGANISM_COMMON: HUMAN;                                              
SOURCE  59 ORGANISM_TAXID: 9606;                                                
SOURCE  60 CELL_LINE: HELA;                                                     
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 CELL_LINE: HELA;                                                     
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  68 ORGANISM_COMMON: HUMAN;                                              
SOURCE  69 ORGANISM_TAXID: 9606;                                                
SOURCE  70 CELL_LINE: HELA                                                      
KEYWDS    PROTEASOME, MULTICATALYTIC PROTEINASE, NTN-HYDROLASE, HYDROLASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHRADER,F.HENNEBERG,R.MATA,K.TITTMANN,T.R.SCHNEIDER,H.STARK,       
AUTHOR   2 G.BOURENKOV,A.CHARI                                                  
REVDAT   2   06-SEP-17 5LE5    1       REMARK                                   
REVDAT   1   17-AUG-16 5LE5    0                                                
JRNL        AUTH   J.SCHRADER,F.HENNEBERG,R.A.MATA,K.TITTMANN,T.R.SCHNEIDER,    
JRNL        AUTH 2 H.STARK,G.BOURENKOV,A.CHARI                                  
JRNL        TITL   THE INHIBITION MECHANISM OF HUMAN 20S PROTEASOMES ENABLES    
JRNL        TITL 2 NEXT-GENERATION INHIBITOR DESIGN.                            
JRNL        REF    SCIENCE                       V. 353   594 2016              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   27493187                                                     
JRNL        DOI    10.1126/SCIENCE.AAF8993                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 170.66                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 633728                         
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 33221                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 46338                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 2425                         
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 48190                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 217                                     
REMARK   3   SOLVENT ATOMS            : 3512                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.51000                                              
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.436         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 49602 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 47425 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 67038 ; 1.778 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):108980 ; 1.342 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6289 ; 6.837 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2164 ;35.057 ;23.743       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8508 ;15.518 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   346 ;16.877 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7529 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 56229 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11235 ; 0.005 ; 0.020       
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): 25018 ; 0.996 ; 1.684       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25017 ; 0.996 ; 1.684       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31251 ; 1.626 ; 2.519       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31252 ; 1.626 ; 2.519       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 24584 ; 1.651 ; 1.920       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 24584 ; 1.650 ; 1.920       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 35754 ; 2.376 ; 2.793       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 57052 ; 7.679 ;15.000       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 57053 ; 7.679 ;15.001       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 14                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     3    232       O     3    232   26594  0.10  0.05     
REMARK   3    2     B     2    249       P     2    249   28534  0.09  0.05     
REMARK   3    3     C     2    237       Q     2    237   25884  0.12  0.05     
REMARK   3    4     D     9    241       R     9    241   27018  0.09  0.05     
REMARK   3    5     E     4    236       S     4    236   28222  0.09  0.05     
REMARK   3    6     F     6    243       T     6    243   27878  0.10  0.05     
REMARK   3    7     G     2    245       U     2    245   27120  0.10  0.05     
REMARK   3    8     H     1    220       V     1    220   25344  0.08  0.05     
REMARK   3    9     I     1    204       W     1    204   25428  0.07  0.05     
REMARK   3   10     J     1    196       X     1    196   24490  0.09  0.05     
REMARK   3   11     K     1    201       Y     1    201   22636  0.08  0.05     
REMARK   3   12     L     1    213       Z     1    213   24868  0.07  0.05     
REMARK   3   13     M     1    216       a     1    216   25058  0.08  0.05     
REMARK   3   14     N     1    203       b     1    203   23236  0.06  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
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 :   A     3        A   232                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.7411 206.3499   1.1478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2447 T22:   0.2611                                     
REMARK   3      T33:   0.2373 T12:   0.1278                                     
REMARK   3      T13:   0.0878 T23:   0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3408 L22:   1.5487                                     
REMARK   3      L33:   1.7256 L12:   0.3848                                     
REMARK   3      L13:   0.5244 L23:  -0.0528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:   0.0921 S13:   0.0217                       
REMARK   3      S21:  -0.1611 S22:  -0.0859 S23:  -0.3742                       
REMARK   3      S31:   0.1044 S32:   0.5804 S33:   0.0944                       
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 :   B     2        B   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.7613 177.2570   0.0871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5699 T22:   0.1286                                     
REMARK   3      T33:   0.2534 T12:   0.1560                                     
REMARK   3      T13:   0.0749 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7670 L22:   1.5029                                     
REMARK   3      L33:   1.5444 L12:  -0.0637                                     
REMARK   3      L13:   0.0690 L23:  -0.3813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0588 S12:   0.1646 S13:  -0.1475                       
REMARK   3      S21:  -0.2479 S22:  -0.0303 S23:  -0.2903                       
REMARK   3      S31:   0.4300 S32:   0.3535 S33:   0.0891                       
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 :   C     2        C   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8653 169.1041  -3.8865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6607 T22:   0.1235                                     
REMARK   3      T33:   0.3344 T12:  -0.0888                                     
REMARK   3      T13:  -0.0683 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8501 L22:   2.3264                                     
REMARK   3      L33:   1.4568 L12:   0.1954                                     
REMARK   3      L13:   0.2756 L23:  -0.1531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0014 S12:  -0.0064 S13:  -0.5364                       
REMARK   3      S21:  -0.1500 S22:   0.0436 S23:  -0.0827                       
REMARK   3      S31:   0.5244 S32:  -0.0025 S33:  -0.0422                       
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 :   D     9        D   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9666 188.3265  -7.9714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5205 T22:   0.3605                                     
REMARK   3      T33:   0.3442 T12:  -0.1653                                     
REMARK   3      T13:  -0.1867 T23:   0.0796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4990 L22:   1.0136                                     
REMARK   3      L33:   1.9925 L12:  -0.0666                                     
REMARK   3      L13:  -0.9493 L23:  -0.0208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0361 S12:   0.1615 S13:  -0.1340                       
REMARK   3      S21:  -0.1878 S22:  -0.0118 S23:   0.1908                       
REMARK   3      S31:   0.3190 S32:  -0.4647 S33:   0.0479                       
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 :   E     4        E   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8310 219.9040  -9.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2520 T22:   0.2357                                     
REMARK   3      T33:   0.2334 T12:  -0.0651                                     
REMARK   3      T13:  -0.0785 T23:   0.0626                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7876 L22:   0.7366                                     
REMARK   3      L33:   1.4541 L12:  -0.2648                                     
REMARK   3      L13:  -0.0382 L23:   0.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0453 S12:   0.1298 S13:  -0.2271                       
REMARK   3      S21:  -0.1010 S22:  -0.0133 S23:   0.2289                       
REMARK   3      S31:   0.1711 S32:  -0.4867 S33:  -0.0320                       
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 :   F     6        F   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3940 240.1010  -7.5840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1708 T22:   0.0661                                     
REMARK   3      T33:   0.1955 T12:   0.0004                                     
REMARK   3      T13:  -0.0352 T23:   0.0489                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2922 L22:   1.6795                                     
REMARK   3      L33:   0.9771 L12:  -0.5762                                     
REMARK   3      L13:  -0.0271 L23:  -0.1415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0135 S12:   0.0940 S13:   0.1926                       
REMARK   3      S21:  -0.1490 S22:  -0.0134 S23:   0.1237                       
REMARK   3      S31:  -0.0967 S32:  -0.1175 S33:  -0.0001                       
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 :   G     2        G   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0170 233.5870  -3.6720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1775 T22:   0.1578                                     
REMARK   3      T33:   0.2197 T12:  -0.0001                                     
REMARK   3      T13:   0.0469 T23:   0.1001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8475 L22:   1.8684                                     
REMARK   3      L33:   1.2572 L12:   0.2160                                     
REMARK   3      L13:   0.1556 L23:   0.4645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0280 S12:   0.1811 S13:   0.2045                       
REMARK   3      S21:  -0.2583 S22:  -0.0671 S23:  -0.1840                       
REMARK   3      S31:  -0.1669 S32:   0.3194 S33:   0.0391                       
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 :   H     1        H   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3520 213.9320  39.4390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1407 T22:   0.2494                                     
REMARK   3      T33:   0.1902 T12:  -0.0336                                     
REMARK   3      T13:   0.0493 T23:   0.0702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2693 L22:   1.2369                                     
REMARK   3      L33:   0.9382 L12:  -0.0403                                     
REMARK   3      L13:  -0.0026 L23:  -0.1730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0139 S12:  -0.0391 S13:  -0.0712                       
REMARK   3      S21:   0.0634 S22:  -0.1011 S23:  -0.1027                       
REMARK   3      S31:   0.0280 S32:   0.3844 S33:   0.0872                       
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 :   I     1        I   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5710 186.5180  39.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2287 T22:   0.2051                                     
REMARK   3      T33:   0.1795 T12:   0.1049                                     
REMARK   3      T13:   0.0442 T23:   0.0678                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2653 L22:   0.9072                                     
REMARK   3      L33:   2.0659 L12:   0.1506                                     
REMARK   3      L13:   0.4321 L23:  -0.7106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0220 S12:   0.0354 S13:  -0.0343                       
REMARK   3      S21:  -0.0967 S22:  -0.1385 S23:  -0.0896                       
REMARK   3      S31:   0.1683 S32:   0.4455 S33:   0.1166                       
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 :   J     1        J   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1290 170.2650  36.2700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4575 T22:   0.0226                                     
REMARK   3      T33:   0.2064 T12:  -0.0154                                     
REMARK   3      T13:  -0.0236 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7301 L22:   0.7668                                     
REMARK   3      L33:   2.4796 L12:   0.4472                                     
REMARK   3      L13:  -0.0529 L23:  -0.4541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0876 S12:   0.0662 S13:  -0.0536                       
REMARK   3      S21:  -0.2155 S22:   0.0129 S23:   0.1479                       
REMARK   3      S31:   0.5708 S32:  -0.1035 S33:   0.0747                       
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 :   K     1        K   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0340 180.7830  32.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3036 T22:   0.2481                                     
REMARK   3      T33:   0.2749 T12:  -0.1966                                     
REMARK   3      T13:  -0.1183 T23:   0.1071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0978 L22:   1.1776                                     
REMARK   3      L33:   1.8521 L12:  -0.1522                                     
REMARK   3      L13:  -0.5738 L23:   0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0233 S12:   0.1182 S13:  -0.0514                       
REMARK   3      S21:  -0.1943 S22:   0.0713 S23:   0.1433                       
REMARK   3      S31:   0.3700 S32:  -0.3733 S33:  -0.0479                       
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 :   L     1        L   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5750 210.2690  30.8530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1572 T22:   0.4744                                     
REMARK   3      T33:   0.2954 T12:  -0.0427                                     
REMARK   3      T13:  -0.0611 T23:   0.1862                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8674 L22:   1.1851                                     
REMARK   3      L33:   1.0280 L12:   0.2727                                     
REMARK   3      L13:  -0.5798 L23:   0.2962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0195 S12:   0.0178 S13:   0.0631                       
REMARK   3      S21:  -0.0782 S22:   0.0467 S23:   0.2853                       
REMARK   3      S31:  -0.0320 S32:  -0.4444 S33:  -0.0662                       
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 :   M     1        M   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3020 237.9210  33.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2183 T22:   0.1600                                     
REMARK   3      T33:   0.2282 T12:   0.1034                                     
REMARK   3      T13:   0.0508 T23:   0.1037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9610 L22:   0.9089                                     
REMARK   3      L33:   1.7206 L12:   0.2203                                     
REMARK   3      L13:   0.0131 L23:   0.2351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0262 S12:   0.0119 S13:   0.1429                       
REMARK   3      S21:   0.0835 S22:   0.1237 S23:   0.1579                       
REMARK   3      S31:  -0.3834 S32:  -0.3290 S33:  -0.0975                       
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     1        N   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7740 241.4350  35.6530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2699 T22:   0.0547                                     
REMARK   3      T33:   0.1646 T12:  -0.0939                                     
REMARK   3      T13:   0.0344 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0984 L22:   0.8837                                     
REMARK   3      L33:   2.1596 L12:  -0.2423                                     
REMARK   3      L13:   0.1593 L23:   0.0143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:  -0.0112 S13:   0.0989                       
REMARK   3      S21:   0.0778 S22:  -0.0483 S23:  -0.0021                       
REMARK   3      S31:  -0.4575 S32:   0.2121 S33:   0.0111                       
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 :   O     3        O   232                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2410 225.9840 103.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3908 T22:   0.4781                                     
REMARK   3      T33:   0.4088 T12:   0.2166                                     
REMARK   3      T13:   0.1789 T23:   0.0834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0508 L22:   1.5362                                     
REMARK   3      L33:   1.9563 L12:  -0.1248                                     
REMARK   3      L13:   0.4303 L23:  -0.2706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0137 S12:  -0.0883 S13:   0.2239                       
REMARK   3      S21:   0.0999 S22:   0.0016 S23:   0.4025                       
REMARK   3      S31:  -0.3842 S32:  -0.5308 S33:   0.0120                       
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 :   P     2        P   248                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4032 195.1952 105.1713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2435 T22:   0.5445                                     
REMARK   3      T33:   0.4056 T12:   0.0140                                     
REMARK   3      T13:   0.1397 T23:   0.1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8233 L22:   1.1866                                     
REMARK   3      L33:   1.3550 L12:   0.2972                                     
REMARK   3      L13:   0.2283 L23:   0.4350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:  -0.1996 S13:   0.0190                       
REMARK   3      S21:   0.1938 S22:   0.0151 S23:   0.3767                       
REMARK   3      S31:  -0.0194 S32:  -0.5988 S33:  -0.0106                       
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 :   Q     2        Q   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0785 174.7293 109.8867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3860 T22:   0.3004                                     
REMARK   3      T33:   0.3965 T12:  -0.0662                                     
REMARK   3      T13:   0.0413 T23:   0.1027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1515 L22:   1.8139                                     
REMARK   3      L33:   1.8202 L12:   0.3475                                     
REMARK   3      L13:   0.1099 L23:   0.2101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0345 S12:  -0.0142 S13:  -0.4661                       
REMARK   3      S21:   0.1600 S22:   0.0401 S23:   0.3143                       
REMARK   3      S31:   0.4654 S32:  -0.3971 S33:  -0.0746                       
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 :   R     9        R   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.4455 181.2336 113.3494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2725 T22:   0.2240                                     
REMARK   3      T33:   0.2426 T12:   0.0034                                     
REMARK   3      T13:   0.0444 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4826 L22:   0.7388                                     
REMARK   3      L33:   2.1054 L12:   0.0428                                     
REMARK   3      L13:  -0.4379 L23:   0.0782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:  -0.1362 S13:  -0.1481                       
REMARK   3      S21:   0.0346 S22:   0.0789 S23:   0.1127                       
REMARK   3      S31:   0.2197 S32:   0.0898 S33:   0.0090                       
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 :   S     2        S   239                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.2562 209.5574 114.1700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3539 T22:   0.3080                                     
REMARK   3      T33:   0.1903 T12:  -0.1119                                     
REMARK   3      T13:  -0.0058 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1616 L22:   1.1525                                     
REMARK   3      L33:   1.5909 L12:  -0.3885                                     
REMARK   3      L13:  -0.1756 L23:  -0.1969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0792 S12:  -0.2416 S13:  -0.0869                       
REMARK   3      S21:   0.2374 S22:   0.0018 S23:  -0.1789                       
REMARK   3      S31:  -0.1163 S32:   0.5007 S33:   0.0774                       
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 :   T     5        T   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4926 237.6636 111.8472              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6561 T22:   0.1465                                     
REMARK   3      T33:   0.2183 T12:  -0.1142                                     
REMARK   3      T13:   0.0654 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7130 L22:   1.3622                                     
REMARK   3      L33:   1.3891 L12:   0.4326                                     
REMARK   3      L13:  -0.4735 L23:   0.0382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1263 S12:  -0.2745 S13:   0.1434                       
REMARK   3      S21:   0.1873 S22:  -0.0434 S23:  -0.1903                       
REMARK   3      S31:  -0.5340 S32:   0.2954 S33:  -0.0829                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     2        U   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9712 244.8929 107.6624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6671 T22:   0.2212                                     
REMARK   3      T33:   0.3291 T12:   0.1805                                     
REMARK   3      T13:   0.1429 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3828 L22:   1.4285                                     
REMARK   3      L33:   1.1241 L12:   0.1642                                     
REMARK   3      L13:  -0.1323 L23:  -0.2869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:  -0.1873 S13:   0.3731                       
REMARK   3      S21:   0.1902 S22:  -0.0162 S23:   0.0657                       
REMARK   3      S31:  -0.5387 S32:  -0.1354 S33:   0.0153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V     1        V   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0498 230.2012  65.1032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2933 T22:   0.3546                                     
REMARK   3      T33:   0.3084 T12:   0.1708                                     
REMARK   3      T13:   0.1496 T23:   0.1069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7327 L22:   1.0488                                     
REMARK   3      L33:   1.0718 L12:   0.2640                                     
REMARK   3      L13:   0.1175 L23:  -0.0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0197 S12:  -0.0160 S13:  -0.0204                       
REMARK   3      S21:   0.0656 S22:   0.0931 S23:   0.1911                       
REMARK   3      S31:  -0.1892 S32:  -0.4325 S33:  -0.1128                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1950 203.3469  65.4896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1429 T22:   0.4829                                     
REMARK   3      T33:   0.3581 T12:   0.0013                                     
REMARK   3      T13:   0.0542 T23:   0.1910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4097 L22:   0.7497                                     
REMARK   3      L33:   1.7214 L12:   0.0880                                     
REMARK   3      L13:   0.5413 L23:   0.4605                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:  -0.0189 S13:   0.0214                       
REMARK   3      S21:   0.0184 S22:   0.1023 S23:   0.2009                       
REMARK   3      S31:  -0.1351 S32:  -0.5379 S33:  -0.1131                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1915 176.6893  68.9132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2310 T22:   0.2023                                     
REMARK   3      T33:   0.2847 T12:  -0.1425                                     
REMARK   3      T13:  -0.0182 T23:   0.1043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5869 L22:   1.0352                                     
REMARK   3      L33:   2.0114 L12:  -0.1209                                     
REMARK   3      L13:  -0.0721 L23:   0.2334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0599 S12:  -0.0608 S13:  -0.0748                       
REMARK   3      S21:   0.0160 S22:   0.1146 S23:   0.0406                       
REMARK   3      S31:   0.3817 S32:  -0.2102 S33:  -0.0547                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     1        Y   199                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6820 172.7271  73.0605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2624 T22:   0.0566                                     
REMARK   3      T33:   0.1740 T12:   0.0200                                     
REMARK   3      T13:  -0.0071 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2460 L22:   1.0079                                     
REMARK   3      L33:   2.2168 L12:   0.2455                                     
REMARK   3      L13:  -0.5819 L23:   0.1466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0293 S12:  -0.1681 S13:  -0.0009                       
REMARK   3      S21:   0.0482 S22:  -0.0346 S23:  -0.0111                       
REMARK   3      S31:   0.4291 S32:   0.0916 S33:   0.0638                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     1        Z   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4609 195.1449  74.0851              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1496 T22:   0.2194                                     
REMARK   3      T33:   0.1713 T12:  -0.0087                                     
REMARK   3      T13:   0.0080 T23:   0.0574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7084 L22:   1.1722                                     
REMARK   3      L33:   1.4793 L12:  -0.0617                                     
REMARK   3      L13:  -0.4929 L23:  -0.0949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0466 S12:  -0.0645 S13:  -0.0088                       
REMARK   3      S21:   0.0526 S22:  -0.1226 S23:  -0.1517                       
REMARK   3      S31:   0.0743 S32:   0.4201 S33:   0.0760                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   a     1        a   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.8306 227.9290  71.1268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2824 T22:   0.1348                                     
REMARK   3      T33:   0.1642 T12:  -0.1439                                     
REMARK   3      T13:   0.0169 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8724 L22:   1.1425                                     
REMARK   3      L33:   1.7070 L12:  -0.1348                                     
REMARK   3      L13:  -0.1208 L23:  -0.4345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:  -0.0231 S13:   0.0798                       
REMARK   3      S21:   0.1589 S22:  -0.0722 S23:  -0.1055                       
REMARK   3      S31:  -0.3711 S32:   0.3344 S33:   0.0554                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   b     1        b   203                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2458 245.3685  68.0804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4724 T22:   0.0435                                     
REMARK   3      T33:   0.1877 T12:   0.0514                                     
REMARK   3      T13:   0.0823 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3822 L22:   0.9263                                     
REMARK   3      L33:   1.9763 L12:   0.0260                                     
REMARK   3      L13:   0.0865 L23:  -0.2513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0247 S12:  -0.0531 S13:   0.1024                       
REMARK   3      S21:   0.1656 S22:   0.0051 S23:   0.0668                       
REMARK   3      S31:  -0.5124 S32:  -0.1040 S33:   0.0196                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000516.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : CRL TRANSFOCATOR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.1                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 633728                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 170.660                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.91000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.910                              
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: 3UNE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.2 M MAGNESIUM          
REMARK 280  CHLORIDE, 10 % PEG3350, PH 6.5, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       56.72000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      158.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.38500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      158.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.72000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.38500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 127120 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 210690 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1121.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, 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 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     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     LYS B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     LYS B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     GLN B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C   239                                                      
REMARK 465     GLU C   240                                                      
REMARK 465     LYS C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     LYS C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     ALA C   247                                                      
REMARK 465     SER C   248                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PHE D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PHE E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     GLU E   238                                                      
REMARK 465     ARG E   239                                                      
REMARK 465     PRO E   240                                                      
REMARK 465     GLN E   241                                                      
REMARK 465     ARG E   242                                                      
REMARK 465     LYS E   243                                                      
REMARK 465     ALA E   244                                                      
REMARK 465     GLN E   245                                                      
REMARK 465     PRO E   246                                                      
REMARK 465     ALA E   247                                                      
REMARK 465     GLN E   248                                                      
REMARK 465     PRO E   249                                                      
REMARK 465     ALA E   250                                                      
REMARK 465     ASP E   251                                                      
REMARK 465     GLU E   252                                                      
REMARK 465     PRO E   253                                                      
REMARK 465     ALA E   254                                                      
REMARK 465     GLU E   255                                                      
REMARK 465     LYS E   256                                                      
REMARK 465     ALA E   257                                                      
REMARK 465     ASP E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     PRO E   260                                                      
REMARK 465     MET E   261                                                      
REMARK 465     GLU E   262                                                      
REMARK 465     HIS E   263                                                      
REMARK 465     MET F     0                                                      
REMARK 465     SER F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ILE F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F   245                                                      
REMARK 465     GLU F   246                                                      
REMARK 465     ASP F   247                                                      
REMARK 465     GLU F   248                                                      
REMARK 465     SER F   249                                                      
REMARK 465     ASP F   250                                                      
REMARK 465     ASP F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     ASN F   253                                                      
REMARK 465     MET F   254                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ASP G   246                                                      
REMARK 465     ILE H   221                                                      
REMARK 465     GLU H   222                                                      
REMARK 465     VAL H   223                                                      
REMARK 465     LEU H   224                                                      
REMARK 465     GLU H   225                                                      
REMARK 465     GLU H   226                                                      
REMARK 465     THR H   227                                                      
REMARK 465     VAL H   228                                                      
REMARK 465     GLN H   229                                                      
REMARK 465     THR H   230                                                      
REMARK 465     MET H   231                                                      
REMARK 465     ASP H   232                                                      
REMARK 465     THR H   233                                                      
REMARK 465     SER H   234                                                      
REMARK 465     MET I     0                                                      
REMARK 465     PRO J   197                                                      
REMARK 465     LYS J   198                                                      
REMARK 465     GLN J   199                                                      
REMARK 465     GLY J   200                                                      
REMARK 465     SER J   201                                                      
REMARK 465     SER K   202                                                      
REMARK 465     THR K   203                                                      
REMARK 465     PRO K   204                                                      
REMARK 465     GLY M   217                                                      
REMARK 465     PHE M   218                                                      
REMARK 465     GLU M   219                                                      
REMARK 465     PRO N   203                                                      
REMARK 465     PRO N   204                                                      
REMARK 465     ALA N   205                                                      
REMARK 465     MET O     0                                                      
REMARK 465     ALA O     1                                                      
REMARK 465     GLU O     2                                                      
REMARK 465     ALA O   233                                                      
REMARK 465     MET P     1                                                      
REMARK 465     ARG P   249                                                      
REMARK 465     GLU P   250                                                      
REMARK 465     LYS P   251                                                      
REMARK 465     LYS P   252                                                      
REMARK 465     GLU P   253                                                      
REMARK 465     LYS P   254                                                      
REMARK 465     GLU P   255                                                      
REMARK 465     GLN P   256                                                      
REMARK 465     LYS P   257                                                      
REMARK 465     GLU P   258                                                      
REMARK 465     LYS P   259                                                      
REMARK 465     ASP P   260                                                      
REMARK 465     LYS P   261                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     GLN Q   200                                                      
REMARK 465     SER Q   201                                                      
REMARK 465     GLY Q   202                                                      
REMARK 465     GLY Q   203                                                      
REMARK 465     LYS Q   204                                                      
REMARK 465     LYS Q   241                                                      
REMARK 465     LYS Q   242                                                      
REMARK 465     LYS Q   243                                                      
REMARK 465     GLN Q   244                                                      
REMARK 465     LYS Q   245                                                      
REMARK 465     LYS Q   246                                                      
REMARK 465     ALA Q   247                                                      
REMARK 465     SER Q   248                                                      
REMARK 465     MET R     1                                                      
REMARK 465     PHE R     2                                                      
REMARK 465     LEU R     3                                                      
REMARK 465     THR R     4                                                      
REMARK 465     ARG R     5                                                      
REMARK 465     SER R     6                                                      
REMARK 465     GLU R     7                                                      
REMARK 465     TYR R     8                                                      
REMARK 465     MET S     1                                                      
REMARK 465     PRO S   240                                                      
REMARK 465     GLN S   241                                                      
REMARK 465     ARG S   242                                                      
REMARK 465     LYS S   243                                                      
REMARK 465     ALA S   244                                                      
REMARK 465     GLN S   245                                                      
REMARK 465     PRO S   246                                                      
REMARK 465     ALA S   247                                                      
REMARK 465     GLN S   248                                                      
REMARK 465     PRO S   249                                                      
REMARK 465     ALA S   250                                                      
REMARK 465     ASP S   251                                                      
REMARK 465     GLU S   252                                                      
REMARK 465     PRO S   253                                                      
REMARK 465     ALA S   254                                                      
REMARK 465     GLU S   255                                                      
REMARK 465     LYS S   256                                                      
REMARK 465     ALA S   257                                                      
REMARK 465     ASP S   258                                                      
REMARK 465     GLU S   259                                                      
REMARK 465     PRO S   260                                                      
REMARK 465     MET S   261                                                      
REMARK 465     GLU S   262                                                      
REMARK 465     HIS S   263                                                      
REMARK 465     MET T     0                                                      
REMARK 465     SER T     1                                                      
REMARK 465     SER T     2                                                      
REMARK 465     ILE T     3                                                      
REMARK 465     GLY T     4                                                      
REMARK 465     GLU T   245                                                      
REMARK 465     GLU T   246                                                      
REMARK 465     ASP T   247                                                      
REMARK 465     GLU T   248                                                      
REMARK 465     SER T   249                                                      
REMARK 465     ASP T   250                                                      
REMARK 465     ASP T   251                                                      
REMARK 465     ASP T   252                                                      
REMARK 465     ASN T   253                                                      
REMARK 465     MET T   254                                                      
REMARK 465     MET U     1                                                      
REMARK 465     LYS U   185                                                      
REMARK 465     LYS U   186                                                      
REMARK 465     PHE U   187                                                      
REMARK 465     ASP U   188                                                      
REMARK 465     TRP U   189                                                      
REMARK 465     THR U   190                                                      
REMARK 465     PHE U   191                                                      
REMARK 465     GLU U   192                                                      
REMARK 465     GLN U   193                                                      
REMARK 465     ASP U   246                                                      
REMARK 465     ILE V   221                                                      
REMARK 465     GLU V   222                                                      
REMARK 465     VAL V   223                                                      
REMARK 465     LEU V   224                                                      
REMARK 465     GLU V   225                                                      
REMARK 465     GLU V   226                                                      
REMARK 465     THR V   227                                                      
REMARK 465     VAL V   228                                                      
REMARK 465     GLN V   229                                                      
REMARK 465     THR V   230                                                      
REMARK 465     MET V   231                                                      
REMARK 465     ASP V   232                                                      
REMARK 465     THR V   233                                                      
REMARK 465     SER V   234                                                      
REMARK 465     MET W     0                                                      
REMARK 465     PRO X   197                                                      
REMARK 465     LYS X   198                                                      
REMARK 465     GLN X   199                                                      
REMARK 465     GLY X   200                                                      
REMARK 465     SER X   201                                                      
REMARK 465     SER Y   200                                                      
REMARK 465     GLY Y   201                                                      
REMARK 465     SER Y   202                                                      
REMARK 465     THR Y   203                                                      
REMARK 465     PRO Y   204                                                      
REMARK 465     GLY a   217                                                      
REMARK 465     PHE a   218                                                      
REMARK 465     GLU a   219                                                      
REMARK 465     PRO b   204                                                      
REMARK 465     ALA b   205                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     GLU A 140    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     LYS B 199    CG   CD   CE   NZ                                   
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     LYS C  48    CG   CD   CE   NZ                                   
REMARK 470     SER C  49    OG                                                  
REMARK 470     VAL C  50    CG1  CG2                                            
REMARK 470     GLU C 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 193    CG   CD   CE   NZ                                   
REMARK 470     GLN C 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 204    CG   CD   CE   NZ                                   
REMARK 470     GLU C 207    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 223    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 224    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 232    CG1  CG2  CD1                                       
REMARK 470     LYS D 149    CG   CD   CE   NZ                                   
REMARK 470     LYS D 196    CG   CD   CE   NZ                                   
REMARK 470     GLN E  53    CG   CD   OE1  NE2                                  
REMARK 470     SER E  54    OG                                                  
REMARK 470     GLU E  55    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 208    CG   CD   CE   NZ                                   
REMARK 470     GLU F  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 181    CG   CD   CE   NZ                                   
REMARK 470     ARG J  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU J 109    CG   CD   OE1  OE2                                  
REMARK 470     ARG K   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K  89    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 200    CG   CD   CE   NZ                                   
REMARK 470     GLU N 150    CG   CD   OE1  OE2                                  
REMARK 470     GLN O  51    CG   CD   OE1  NE2                                  
REMARK 470     LYS O  52    CG   CD   CE   NZ                                   
REMARK 470     ILE O  54    CG1  CG2  CD1                                       
REMARK 470     LYS O  69    CG   CD   CE   NZ                                   
REMARK 470     LYS O 175    CG   CD   CE   NZ                                   
REMARK 470     ILE P  52    CG1  CG2  CD1                                       
REMARK 470     LYS P 199    CG   CD   CE   NZ                                   
REMARK 470     LYS P 205    CG   CD   CE   NZ                                   
REMARK 470     GLU P 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 210    CG   CD   CE   NZ                                   
REMARK 470     LYS P 229    CG   CD   CE   NZ                                   
REMARK 470     LYS P 231    CG   CD   CE   NZ                                   
REMARK 470     LYS P 239    CG   CD   CE   NZ                                   
REMARK 470     ASP Q  13    CG   OD1  OD2                                       
REMARK 470     ARG Q  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Q  47    CG   CD   CE   NZ                                   
REMARK 470     LYS Q  48    CG   CD   CE   NZ                                   
REMARK 470     SER Q  49    OG                                                  
REMARK 470     LYS Q 174    CG   CD   CE   NZ                                   
REMARK 470     GLU Q 182    CG   CD   OE1  OE2                                  
REMARK 470     LYS Q 189    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 193    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 218    CG   CD   CE   NZ                                   
REMARK 470     ASP R 127    CG   OD1  OD2                                       
REMARK 470     ASP R 129    CG   OD1  OD2                                       
REMARK 470     GLU R 208    CG   CD   OE1  OE2                                  
REMARK 470     PHE S   2    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG S   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN S  53    CG   CD   OE1  NE2                                  
REMARK 470     ASP S 218    CG   OD1  OD2                                       
REMARK 470     GLU S 238    CG   CD   OE1  OE2                                  
REMARK 470     THR T   5    OG1  CG2                                            
REMARK 470     LYS T  56    CG   CD   CE   NZ                                   
REMARK 470     GLU T  60    CG   CD   OE1  OE2                                  
REMARK 470     ASP T 188    CG   OD1  OD2                                       
REMARK 470     GLU T 192    CG   CD   OE1  OE2                                  
REMARK 470     ARG U   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS U  55    CG   CD   CE   NZ                                   
REMARK 470     GLU U 145    CG   CD   OE1  OE2                                  
REMARK 470     GLU U 146    CG   CD   OE1  OE2                                  
REMARK 470     LYS V 180    CG   CD   CE   NZ                                   
REMARK 470     LYS V 194    CG   CD   CE   NZ                                   
REMARK 470     ARG V 203    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS W 191    CG   CD   CE   NZ                                   
REMARK 470     ARG Y  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG Z   1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Z 162    CG   CD   OE1  OE2                                  
REMARK 470     ASP Z 169    CG   OD1  OD2                                       
REMARK 470     GLU a 206    CG   CD   OE1  OE2                                  
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   O    LYS I    16     O    HOH I   401              1.85            
REMARK 500   OD1  ASN P   155     OG1  THR Q    77              1.89            
REMARK 500   OE2  GLU G   192     O    HOH G   401              2.01            
REMARK 500   OD1  ASN B   155     OG1  THR C    77              2.04            
REMARK 500   NH2  ARG J   153     OD2  ASP J   184              2.11            
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    SER B 188   CB    SER B 188   OG      0.085                       
REMARK 500    GLU C 182   CG    GLU C 182   CD      0.419                       
REMARK 500    GLU C 182   CD    GLU C 182   OE2    -0.269                       
REMARK 500    GLU F  94   CD    GLU F  94   OE2    -0.075                       
REMARK 500    GLU G 108   CD    GLU G 108   OE1     0.165                       
REMARK 500    CYS H  31   CB    CYS H  31   SG     -0.107                       
REMARK 500    PRO J  10   C     PRO J  10   O      -0.148                       
REMARK 500    GLU J 154   CA    GLU J 154   C       0.163                       
REMARK 500    ARG J 155   N     ARG J 155   CA     -0.124                       
REMARK 500    SER L   3   CB    SER L   3   OG      0.081                       
REMARK 500    SER N  24   CB    SER N  24   OG     -0.080                       
REMARK 500    LYS Q 189   C     LYS Q 189   O       0.213                       
REMARK 500    SER Z   3   CB    SER Z   3   OG      0.087                       
REMARK 500    SER Z 142   CB    SER Z 142   OG     -0.078                       
REMARK 500    GLU b 150   CD    GLU b 150   OE1     0.104                       
REMARK 500    GLU b 150   CD    GLU b 150   OE2     0.072                       
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    ARG A  88   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG B   4   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B   4   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    GLU C 182   CG  -  CD  -  OE2 ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LEU D 121   C   -  N   -  CA  ANGL. DEV. =  24.4 DEGREES          
REMARK 500    ARG E 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP F  17   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG F  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    MET F 117   CG  -  SD  -  CE  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ARG F 169   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG F 169   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    VAL F 190   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ASP F 206   CB  -  CG  -  OD1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP F 206   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    CYS G  78   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG G  88   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG G 117   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    VAL G 183   CB  -  CA  -  C   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG H  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    MET H  86   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ARG H  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG H 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP J  90   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU K  42   CB  -  CG  -  CD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    MET K  86   CG  -  SD  -  CE  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ARG K 157   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG K 157   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP L 125   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG M 151   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG M 151   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP M 180   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG N  45   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LEU O  73   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ARG P   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG P   4   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG P  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU R 121   C   -  N   -  CA  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    ASP S   7   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG S 101   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG S 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG S 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    MET T  27   CG  -  SD  -  CE  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ASP T  43   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    LEU T 108   CB  -  CG  -  CD2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      77 ANGLE DEVIATIONS.                             
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    LYS A  50       51.04    -63.41                                   
REMARK 500    LYS A  52     -153.39    -47.31                                   
REMARK 500    SER A  53      118.44     24.33                                   
REMARK 500    GLN A 122      -33.12   -141.92                                   
REMARK 500    PHE A 198      -72.65    -84.25                                   
REMARK 500    GLU A 199      106.38     78.59                                   
REMARK 500    GLN A 201      120.83     70.39                                   
REMARK 500    ARG B   8       62.98     62.08                                   
REMARK 500    GLU B  58       85.62     64.01                                   
REMARK 500    SER B 204      157.43     79.98                                   
REMARK 500    LYS B 205      106.61    -51.91                                   
REMARK 500    LYS C  47     -177.48    -66.19                                   
REMARK 500    LYS C  48      -95.97    -75.09                                   
REMARK 500    VAL C  50     -106.82     67.05                                   
REMARK 500    ALA C  51       94.15     72.21                                   
REMARK 500    SER C 201       46.15   -103.51                                   
REMARK 500    LYS C 204     -112.35     68.41                                   
REMARK 500    SER C 216      151.22     60.37                                   
REMARK 500    ARG D  53       70.66     64.66                                   
REMARK 500    LEU D 121        7.34     92.95                                   
REMARK 500    GLU D 126       95.25   -164.83                                   
REMARK 500    ASP D 127      -45.32    158.23                                   
REMARK 500    GLU D 175      -82.69    -54.00                                   
REMARK 500    PHE D 226      124.56    -34.61                                   
REMARK 500    SER E  40     -166.88   -109.89                                   
REMARK 500    HIS E  59      125.46    100.28                                   
REMARK 500    ALA E 151       -0.62     77.40                                   
REMARK 500    ASP E 226     -126.73     53.85                                   
REMARK 500    LEU E 236      -80.75   -109.41                                   
REMARK 500    ARG G   3       79.15     68.61                                   
REMARK 500    TRP G 189       50.80     34.47                                   
REMARK 500    ASP G 209       94.01     66.47                                   
REMARK 500    GLU G 244       50.09    -98.96                                   
REMARK 500    ASN H  30       50.38   -141.66                                   
REMARK 500    ASP H 104     -169.70   -128.70                                   
REMARK 500    SER H 171     -126.09     68.04                                   
REMARK 500    LYS I  16      -70.66    -58.21                                   
REMARK 500    GLN I  30     -125.55     47.65                                   
REMARK 500    ASP I  37       39.37   -140.98                                   
REMARK 500    ASP I 134      -71.04   -129.83                                   
REMARK 500    ASN J  24     -118.19     57.63                                   
REMARK 500    ALA J 122       26.69     82.17                                   
REMARK 500    LEU J 175       79.62   -119.72                                   
REMARK 500    ASP K 105     -155.28   -127.03                                   
REMARK 500    SER K 200      -83.81   -136.21                                   
REMARK 500    PHE L 102       73.67   -156.23                                   
REMARK 500    ASP L 191      -67.11     72.34                                   
REMARK 500    MET M   5      -99.32   -114.23                                   
REMARK 500    THR M   9     -149.33    -88.90                                   
REMARK 500    GLN M 157       89.46   -150.78                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     112 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 GLY C  202     GLY C  203                 -149.96                    
REMARK 500 GLU D  175     GLY D  176                 -140.98                    
REMARK 500 GLU D  175     GLY D  176                  137.13                    
REMARK 500 GLY I   78     ARG I   79                 -149.42                    
REMARK 500 LYS P   54     LEU P   55                  147.42                    
REMARK 500 SER Q   49     VAL Q   50                 -142.46                    
REMARK 500 LEU Q  220     ASN Q  221                   40.93                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG Z  99         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU D 175         10.34                                           
REMARK 500    PRO X  10         11.59                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 483        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH G 590        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH I 549        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH W 517        DISTANCE =  5.97 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G 304   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  14   OG1                                                    
REMARK 620 2 TYR G 125   O    94.3                                              
REMARK 620 3 ASN G 128   O    78.4  92.5                                        
REMARK 620 4 MET G 131   O   161.6 104.1 100.7                                  
REMARK 620 5 HOH G 505   O    73.8 156.5 104.5  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H  91   OE1                                                    
REMARK 620 2 HOH H 425   O    74.1                                              
REMARK 620 3 HOH N 612   O    83.5  87.4                                        
REMARK 620 4 HOH H 530   O    95.6  92.9 179.0                                  
REMARK 620 5 HOH N 615   O   165.3  91.5  93.0  87.9                            
REMARK 620 6 HOH N 680   O   104.6 178.7  92.2  87.5  89.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE H 163   O                                                      
REMARK 620 2 ASP H 166   O   109.7                                              
REMARK 620 3 SER H 169   O   101.3  88.0                                        
REMARK 620 4 ASP Z 213   O   110.8 136.2  99.7                                  
REMARK 620 5 HOH H 501   O    84.4  90.2 174.3  77.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL I 174   O                                                      
REMARK 620 2 ASP I 177   O    87.0                                              
REMARK 620 3 SER I 180   O   107.0  93.2                                        
REMARK 620 4 HOH I 434   O    87.1 164.5 102.3                                  
REMARK 620 5 HOH I 453   O   154.1  87.5  98.5  91.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 204   O                                                      
REMARK 620 2 THR Y 164   O   110.7                                              
REMARK 620 3 ASP Y 167   O   139.9 107.6                                        
REMARK 620 4 SER Y 170   O    95.5 101.8  87.9                                  
REMARK 620 5 HOH Y 500   O    85.7  83.6  87.0 173.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR K 164   O                                                      
REMARK 620 2 ASP K 167   O   110.5                                              
REMARK 620 3 SER K 170   O   103.3  89.5                                        
REMARK 620 4 ASP W 204   O   108.3 137.4  98.1                                  
REMARK 620 5 HOH K 471   O    83.0  90.2 173.3  77.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K L 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA L 183   O                                                      
REMARK 620 2 ASP L 186   O   102.2                                              
REMARK 620 3 THR L 189   O    99.5  81.3                                        
REMARK 620 4 HOH L 449   O   135.2  97.6 123.0                                  
REMARK 620 5 HOH L 466   O    89.2 161.0  81.9  84.3                            
REMARK 620 6 HOH V 442   O    55.9 128.7 141.9  80.5  70.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 213   O                                                      
REMARK 620 2 ILE V 163   O   107.4                                              
REMARK 620 3 ASP V 166   O   135.5 114.7                                        
REMARK 620 4 SER V 169   O    97.5 100.1  89.1                                  
REMARK 620 5 HOH V 473   O    78.2  87.1  89.8 172.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K N 504   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET N 164   O                                                      
REMARK 620 2 ASP N 167   O    93.8                                              
REMARK 620 3 SER N 170   O    97.1  72.1                                        
REMARK 620 4 HOH N 748   O    87.2 166.8  94.7                                  
REMARK 620 5 HOH N 712   O    89.5  85.6 157.1 107.5                            
REMARK 620 6 HOH N 703   O   139.2 121.3 112.0  63.4  74.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K U 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR U  14   OG1                                                    
REMARK 620 2 TYR U 125   O    94.2                                              
REMARK 620 3 ASN U 128   O    79.0  91.7                                        
REMARK 620 4 MET U 131   O   162.5 103.2  99.2                                  
REMARK 620 5 HOH U 456   O    74.3 156.3 106.0  89.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN V  91   OE1                                                    
REMARK 620 2 HOH V 427   O    74.5                                              
REMARK 620 3 HOH V 497   O    96.2  91.7                                        
REMARK 620 4 HOH b 606   O    83.1  87.6 179.1                                  
REMARK 620 5 HOH b 618   O   165.4  91.4  88.0  92.5                            
REMARK 620 6 HOH b 647   O   104.5 178.5  89.5  91.2  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG W 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL W 174   O                                                      
REMARK 620 2 ASP W 177   O    87.8                                              
REMARK 620 3 SER W 180   O   107.1  92.6                                        
REMARK 620 4 HOH W 443   O    88.3 165.8 101.6                                  
REMARK 620 5 HOH W 472   O   156.5  89.5  96.3  88.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K Z 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA Z 183   O                                                      
REMARK 620 2 ASP Z 186   O   100.7                                              
REMARK 620 3 THR Z 189   O    99.5  82.7                                        
REMARK 620 4 HOH Z1449   O   135.2  97.7 123.2                                  
REMARK 620 5 HOH Z1470   O    93.6 159.4  80.4  81.9                            
REMARK 620 6 HOH Z1475   O    57.4 129.1 141.0  79.4  71.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K b 506   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET b 164   O                                                      
REMARK 620 2 ASP b 167   O    95.2                                              
REMARK 620 3 SER b 170   O    96.9  73.4                                        
REMARK 620 4 HOH b 673   O    89.6  85.2 158.0                                  
REMARK 620 5 HOH b 721   O    92.7 166.2  94.5 106.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH J 409   O                                                      
REMARK 620 2 HOH J 454   O    91.3                                              
REMARK 620 3 HOH J 508   O    91.4  89.7                                        
REMARK 620 4 HOH J 522   O    88.6 179.7  90.6                                  
REMARK 620 5 HOH K 496   O   179.4  88.7  89.2  91.3                            
REMARK 620 6 HOH J 432   O    88.6  91.3 179.0  88.4  90.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH X 402   O                                                      
REMARK 620 2 HOH X 433   O    89.8                                              
REMARK 620 3 HOH X 519   O    89.9  87.8                                        
REMARK 620 4 HOH Y 521   O   179.4  90.2  90.8                                  
REMARK 620 5 HOH X 446   O    90.8  92.3 179.3  88.5                            
REMARK 620 6 HOH X 509   O    90.0 179.7  92.3  90.1  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE G 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K G 304                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K N 504                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K U 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL W 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE W 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE Z 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K Z 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE a 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE b 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE b 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K b 506                   
DBREF  5LE5 A    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LE5 B    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LE5 C    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LE5 D    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LE5 E    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LE5 F    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LE5 G    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LE5 H    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LE5 I    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LE5 J    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LE5 K    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LE5 L    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LE5 M    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LE5 N    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LE5 O    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LE5 P    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LE5 Q    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LE5 R    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LE5 S    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LE5 T    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LE5 U    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LE5 V    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LE5 W    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LE5 X    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LE5 Y    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LE5 Z    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LE5 a    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LE5 b    1   205  UNP    P28072   PSB6_HUMAN      35    239             
SEQRES   1 A  234  MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE          
SEQRES   2 A  234  SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU          
SEQRES   3 A  234  ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS          
SEQRES   4 A  234  ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN          
SEQRES   5 A  234  LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL          
SEQRES   6 A  234  GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY          
SEQRES   7 A  234  MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG          
SEQRES   8 A  234  LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO          
SEQRES   9 A  234  ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL          
SEQRES  10 A  234  MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 A  234  GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG          
SEQRES  12 A  234  PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE          
SEQRES  13 A  234  ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN          
SEQRES  14 A  234  GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU          
SEQRES  15 A  234  GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU          
SEQRES  16 A  234  LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE          
SEQRES  17 A  234  GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU          
SEQRES  18 A  234  THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA          
SEQRES   1 B  261  MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER          
SEQRES   2 B  261  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU          
SEQRES   3 B  261  ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA          
SEQRES   4 B  261  ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE          
SEQRES   5 B  261  HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE          
SEQRES   6 B  261  TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY          
SEQRES   7 B  261  ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG          
SEQRES   8 B  261  LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO          
SEQRES   9 B  261  ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE          
SEQRES  10 B  261  LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE          
SEQRES  11 B  261  GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR          
SEQRES  12 B  261  GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR          
SEQRES  13 B  261  GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA          
SEQRES  14 B  261  ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY          
SEQRES  15 B  261  GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS          
SEQRES  16 B  261  VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA          
SEQRES  17 B  261  GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY          
SEQRES  18 B  261  LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU          
SEQRES  19 B  261  GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA          
SEQRES  20 B  261  GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP          
SEQRES  21 B  261  LYS                                                          
SEQRES   1 C  248  MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP          
SEQRES   2 C  248  GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL          
SEQRES   3 C  248  LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP          
SEQRES   4 C  248  ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS          
SEQRES   5 C  248  LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU          
SEQRES   6 C  248  ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA          
SEQRES   7 C  248  ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS          
SEQRES   8 C  248  GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL          
SEQRES   9 C  248  GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG          
SEQRES  10 C  248  TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER          
SEQRES  11 C  248  ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG          
SEQRES  12 C  248  LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP          
SEQRES  13 C  248  LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG          
SEQRES  14 C  248  GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU          
SEQRES  15 C  248  THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU          
SEQRES  16 C  248  LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU          
SEQRES  17 C  248  ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN          
SEQRES  18 C  248  PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS          
SEQRES  19 C  248  GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA          
SEQRES  20 C  248  SER                                                          
SEQRES   1 D  241  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN          
SEQRES   2 D  241  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 D  241  ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 D  241  ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS          
SEQRES   5 D  241  ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU          
SEQRES   6 D  241  LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET          
SEQRES   7 D  241  SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS          
SEQRES   8 D  241  ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN          
SEQRES   9 D  241  GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER          
SEQRES  10 D  241  ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO          
SEQRES  11 D  241  GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE          
SEQRES  12 D  241  GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET          
SEQRES  13 D  241  ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA          
SEQRES  14 D  241  ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN          
SEQRES  15 D  241  GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE          
SEQRES  16 D  241  LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU          
SEQRES  17 D  241  LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN          
SEQRES  18 D  241  PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU          
SEQRES  19 D  241  GLU GLU VAL ILE LYS ASP ILE                                  
SEQRES   1 E  263  MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP          
SEQRES   2 E  263  SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET          
SEQRES   3 E  263  GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS          
SEQRES   4 E  263  SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA          
SEQRES   5 E  263  GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS          
SEQRES   6 E  263  VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR          
SEQRES   7 E  263  ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU          
SEQRES   8 E  263  CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO          
SEQRES   9 E  263  VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN          
SEQRES  10 E  263  ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL          
SEQRES  11 E  263  GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS          
SEQRES  12 E  263  ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS          
SEQRES  13 E  263  ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG          
SEQRES  14 E  263  THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS          
SEQRES  15 E  263  ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU          
SEQRES  16 E  263  ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS          
SEQRES  17 E  263  ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE          
SEQRES  18 E  263  THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU          
SEQRES  19 E  263  GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA          
SEQRES  20 E  263  GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO          
SEQRES  21 E  263  MET GLU HIS                                                  
SEQRES   1 F  255  MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER          
SEQRES   2 F  255  THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR          
SEQRES   3 F  255  ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY          
SEQRES   4 F  255  ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS          
SEQRES   5 F  255  LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS          
SEQRES   6 F  255  ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL          
SEQRES   7 F  255  ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE          
SEQRES   8 F  255  ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY          
SEQRES   9 F  255  TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA          
SEQRES  10 F  255  MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG          
SEQRES  11 F  255  PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL          
SEQRES  12 F  255  ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY          
SEQRES  13 F  255  VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA          
SEQRES  14 F  255  ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET          
SEQRES  15 F  255  LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA          
SEQRES  16 F  255  LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS          
SEQRES  17 F  255  ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR          
SEQRES  18 F  255  ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU          
SEQRES  19 F  255  GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU          
SEQRES  20 F  255  ASP GLU SER ASP ASP ASP ASN MET                              
SEQRES   1 G  246  MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE          
SEQRES   2 G  246  THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU          
SEQRES   3 G  246  TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER          
SEQRES   4 G  246  VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR          
SEQRES   5 G  246  GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR          
SEQRES   6 G  246  VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS          
SEQRES   7 G  246  VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL          
SEQRES   8 G  246  GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS          
SEQRES   9 G  246  TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG          
SEQRES  10 G  246  ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU          
SEQRES  11 G  246  MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE          
SEQRES  12 G  246  ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO          
SEQRES  13 G  246  ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY          
SEQRES  14 G  246  VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS          
SEQRES  15 G  246  VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL          
SEQRES  16 G  246  GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE          
SEQRES  17 G  246  ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR          
SEQRES  18 G  246  VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU          
SEQRES  19 G  246  ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP              
SEQRES   1 H  234  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 H  234  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 H  234  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 H  234  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 H  234  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 H  234  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 H  234  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 H  234  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 H  234  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 H  234  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 H  234  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 H  234  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 H  234  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 H  234  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 H  234  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 H  234  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 H  234  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE          
SEQRES  18 H  234  GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER          
SEQRES   1 I  205  MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA          
SEQRES   2 I  205  MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG          
SEQRES   3 I  205  ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE          
SEQRES   4 I  205  GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY          
SEQRES   5 I  205  LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN          
SEQRES   6 I  205  ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU          
SEQRES   7 I  205  GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL          
SEQRES   8 I  205  ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR          
SEQRES   9 I  205  THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE          
SEQRES  10 I  205  LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO          
SEQRES  11 I  205  MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA          
SEQRES  12 I  205  GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO          
SEQRES  13 I  205  ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN          
SEQRES  14 I  205  ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY          
SEQRES  15 I  205  MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE          
SEQRES  16 I  205  THR THR ARG THR LEU LYS ALA ARG MET ASP                      
SEQRES   1 J  201  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 J  201  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 J  201  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 J  201  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 J  201  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 J  201  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 J  201  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1          
SEQRES   8 J  201  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 J  201  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 J  201  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 J  201  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 J  201  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 J  201  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 J  201  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 J  201  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 J  201  PHE PRO LYS GLN GLY SER                                      
SEQRES   1 K  204  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 K  204  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 K  204  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  204  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 K  204  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 K  204  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 K  204  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 K  204  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 K  204  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 K  204  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 K  204  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 K  204  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 K  204  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 K  204  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 K  204  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 K  204  HIS GLU LYS TYR SER GLY SER THR PRO                          
SEQRES   1 L  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 L  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 L  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 L  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 L  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 L  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 L  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 L  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 L  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 L  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 L  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 L  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 L  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 L  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 L  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 L  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 L  213  SER LEU ARG LYS ASP                                          
SEQRES   1 M  219  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 M  219  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 M  219  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 M  219  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 M  219  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 M  219  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 M  219  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 M  219  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 M  219  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 M  219  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 M  219  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 M  219  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 M  219  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 M  219  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 M  219  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 M  219  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 M  219  TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU                  
SEQRES   1 N  205  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 N  205  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 N  205  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 N  205  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  205  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 N  205  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 N  205  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 N  205  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 N  205  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 N  205  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 N  205  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 N  205  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 N  205  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 N  205  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 N  205  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 N  205  LYS PHE ALA VAL ALA THR LEU PRO PRO ALA                      
SEQRES   1 O  234  MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE          
SEQRES   2 O  234  SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU          
SEQRES   3 O  234  ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS          
SEQRES   4 O  234  ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN          
SEQRES   5 O  234  LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL          
SEQRES   6 O  234  GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY          
SEQRES   7 O  234  MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG          
SEQRES   8 O  234  LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO          
SEQRES   9 O  234  ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL          
SEQRES  10 O  234  MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 O  234  GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG          
SEQRES  12 O  234  PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE          
SEQRES  13 O  234  ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN          
SEQRES  14 O  234  GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU          
SEQRES  15 O  234  GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU          
SEQRES  16 O  234  LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE          
SEQRES  17 O  234  GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU          
SEQRES  18 O  234  THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA          
SEQRES   1 P  261  MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER          
SEQRES   2 P  261  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU          
SEQRES   3 P  261  ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA          
SEQRES   4 P  261  ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE          
SEQRES   5 P  261  HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE          
SEQRES   6 P  261  TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY          
SEQRES   7 P  261  ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG          
SEQRES   8 P  261  LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO          
SEQRES   9 P  261  ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE          
SEQRES  10 P  261  LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE          
SEQRES  11 P  261  GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR          
SEQRES  12 P  261  GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR          
SEQRES  13 P  261  GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA          
SEQRES  14 P  261  ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY          
SEQRES  15 P  261  GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS          
SEQRES  16 P  261  VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA          
SEQRES  17 P  261  GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY          
SEQRES  18 P  261  LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU          
SEQRES  19 P  261  GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA          
SEQRES  20 P  261  GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP          
SEQRES  21 P  261  LYS                                                          
SEQRES   1 Q  248  MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP          
SEQRES   2 Q  248  GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL          
SEQRES   3 Q  248  LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP          
SEQRES   4 Q  248  ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS          
SEQRES   5 Q  248  LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU          
SEQRES   6 Q  248  ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA          
SEQRES   7 Q  248  ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS          
SEQRES   8 Q  248  GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL          
SEQRES   9 Q  248  GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG          
SEQRES  10 Q  248  TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER          
SEQRES  11 Q  248  ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG          
SEQRES  12 Q  248  LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP          
SEQRES  13 Q  248  LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG          
SEQRES  14 Q  248  GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU          
SEQRES  15 Q  248  THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU          
SEQRES  16 Q  248  LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU          
SEQRES  17 Q  248  ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN          
SEQRES  18 Q  248  PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS          
SEQRES  19 Q  248  GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA          
SEQRES  20 Q  248  SER                                                          
SEQRES   1 R  241  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN          
SEQRES   2 R  241  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 R  241  ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 R  241  ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS          
SEQRES   5 R  241  ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU          
SEQRES   6 R  241  LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET          
SEQRES   7 R  241  SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS          
SEQRES   8 R  241  ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN          
SEQRES   9 R  241  GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER          
SEQRES  10 R  241  ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO          
SEQRES  11 R  241  GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE          
SEQRES  12 R  241  GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET          
SEQRES  13 R  241  ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA          
SEQRES  14 R  241  ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN          
SEQRES  15 R  241  GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE          
SEQRES  16 R  241  LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU          
SEQRES  17 R  241  LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN          
SEQRES  18 R  241  PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU          
SEQRES  19 R  241  GLU GLU VAL ILE LYS ASP ILE                                  
SEQRES   1 S  263  MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP          
SEQRES   2 S  263  SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET          
SEQRES   3 S  263  GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS          
SEQRES   4 S  263  SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA          
SEQRES   5 S  263  GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS          
SEQRES   6 S  263  VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR          
SEQRES   7 S  263  ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU          
SEQRES   8 S  263  CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO          
SEQRES   9 S  263  VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN          
SEQRES  10 S  263  ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL          
SEQRES  11 S  263  GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS          
SEQRES  12 S  263  ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS          
SEQRES  13 S  263  ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG          
SEQRES  14 S  263  THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS          
SEQRES  15 S  263  ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU          
SEQRES  16 S  263  ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS          
SEQRES  17 S  263  ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE          
SEQRES  18 S  263  THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU          
SEQRES  19 S  263  GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA          
SEQRES  20 S  263  GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO          
SEQRES  21 S  263  MET GLU HIS                                                  
SEQRES   1 T  255  MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER          
SEQRES   2 T  255  THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR          
SEQRES   3 T  255  ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY          
SEQRES   4 T  255  ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS          
SEQRES   5 T  255  LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS          
SEQRES   6 T  255  ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL          
SEQRES   7 T  255  ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE          
SEQRES   8 T  255  ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY          
SEQRES   9 T  255  TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA          
SEQRES  10 T  255  MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG          
SEQRES  11 T  255  PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL          
SEQRES  12 T  255  ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY          
SEQRES  13 T  255  VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA          
SEQRES  14 T  255  ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET          
SEQRES  15 T  255  LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA          
SEQRES  16 T  255  LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS          
SEQRES  17 T  255  ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR          
SEQRES  18 T  255  ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU          
SEQRES  19 T  255  GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU          
SEQRES  20 T  255  ASP GLU SER ASP ASP ASP ASN MET                              
SEQRES   1 U  246  MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE          
SEQRES   2 U  246  THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU          
SEQRES   3 U  246  TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER          
SEQRES   4 U  246  VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR          
SEQRES   5 U  246  GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR          
SEQRES   6 U  246  VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS          
SEQRES   7 U  246  VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL          
SEQRES   8 U  246  GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS          
SEQRES   9 U  246  TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG          
SEQRES  10 U  246  ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU          
SEQRES  11 U  246  MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE          
SEQRES  12 U  246  ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO          
SEQRES  13 U  246  ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY          
SEQRES  14 U  246  VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS          
SEQRES  15 U  246  VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL          
SEQRES  16 U  246  GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE          
SEQRES  17 U  246  ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR          
SEQRES  18 U  246  VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU          
SEQRES  19 U  246  ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP              
SEQRES   1 V  234  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 V  234  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 V  234  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 V  234  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 V  234  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 V  234  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 V  234  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 V  234  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 V  234  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 V  234  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 V  234  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 V  234  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 V  234  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 V  234  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 V  234  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 V  234  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 V  234  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE          
SEQRES  18 V  234  GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER          
SEQRES   1 W  205  MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA          
SEQRES   2 W  205  MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG          
SEQRES   3 W  205  ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE          
SEQRES   4 W  205  GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY          
SEQRES   5 W  205  LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN          
SEQRES   6 W  205  ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU          
SEQRES   7 W  205  GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL          
SEQRES   8 W  205  ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR          
SEQRES   9 W  205  THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE          
SEQRES  10 W  205  LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO          
SEQRES  11 W  205  MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA          
SEQRES  12 W  205  GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO          
SEQRES  13 W  205  ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN          
SEQRES  14 W  205  ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY          
SEQRES  15 W  205  MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE          
SEQRES  16 W  205  THR THR ARG THR LEU LYS ALA ARG MET ASP                      
SEQRES   1 X  201  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 X  201  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 X  201  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 X  201  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 X  201  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 X  201  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 X  201  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1          
SEQRES   8 X  201  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 X  201  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 X  201  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 X  201  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 X  201  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 X  201  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 X  201  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 X  201  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 X  201  PHE PRO LYS GLN GLY SER                                      
SEQRES   1 Y  204  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 Y  204  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 Y  204  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  204  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  204  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 Y  204  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  204  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 Y  204  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 Y  204  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 Y  204  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 Y  204  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 Y  204  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 Y  204  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 Y  204  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 Y  204  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 Y  204  HIS GLU LYS TYR SER GLY SER THR PRO                          
SEQRES   1 Z  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 Z  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 Z  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 Z  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 Z  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 Z  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 Z  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 Z  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 Z  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 Z  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 Z  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 Z  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 Z  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 Z  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 Z  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 Z  213  SER LEU ARG LYS ASP                                          
SEQRES   1 a  219  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 a  219  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 a  219  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 a  219  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 a  219  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 a  219  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 a  219  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 a  219  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 a  219  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 a  219  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 a  219  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 a  219  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 a  219  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 a  219  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 a  219  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 a  219  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 a  219  TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU                  
SEQRES   1 b  205  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 b  205  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 b  205  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 b  205  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  205  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 b  205  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 b  205  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 b  205  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 b  205  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 b  205  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 b  205  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 b  205  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 b  205  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 b  205  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 b  205  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 b  205  LYS PHE ALA VAL ALA THR LEU PRO PRO ALA                      
MODRES 5LE5 YCM C   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 E  148  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 G   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 YCM G  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 G  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 J   91  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 YCM Q   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 S  148  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 U   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 YCM U  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 U  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LE5 6V1 X   91  CYS  MODIFIED RESIDUE                                   
HET    YCM  C  63      10                                                       
HET    6V1  E 148      15                                                       
HET    6V1  G  47      15                                                       
HET    YCM  G 137      10                                                       
HET    6V1  G 161      15                                                       
HET    6V1  J  91      15                                                       
HET    YCM  Q  63      10                                                       
HET    6V1  S 148      15                                                       
HET    6V1  U  47      15                                                       
HET    YCM  U 137      10                                                       
HET    6V1  U 161      15                                                       
HET    6V1  X  91      15                                                       
HET     CL  A 301       1                                                       
HET     CL  A 302       1                                                       
HET     CL  A 303       1                                                       
HET     CL  A 304       1                                                       
HET     CL  B 301       1                                                       
HET     CL  B 302       1                                                       
HET     CL  C 301       1                                                       
HET     CL  C 302       1                                                       
HET     CL  D 301       1                                                       
HET     CL  D 302       1                                                       
HET     CL  E 301       1                                                       
HET     CL  E 302       1                                                       
HET     CL  E 303       1                                                       
HET     CL  F 301       1                                                       
HET     CL  G 301       1                                                       
HET     CL  G 302       1                                                       
HET    1PE  G 303      16                                                       
HET      K  G 304       1                                                       
HET     MG  H 301       1                                                       
HET     MG  H 302       1                                                       
HET     CL  H 303       1                                                       
HET     CL  H 304       1                                                       
HET     MG  I 301       1                                                       
HET     CL  I 302       1                                                       
HET    1PE  I 303      16                                                       
HET    1PE  I 304      16                                                       
HET     MG  I 305       1                                                       
HET     MG  J 301       1                                                       
HET     MG  K 301       1                                                       
HET     CL  K 302       1                                                       
HET     CL  K 303       1                                                       
HET     CL  K 304       1                                                       
HET     CL  K 305       1                                                       
HET    1PE  L 301      16                                                       
HET      K  L 302       1                                                       
HET     MG  L 303       1                                                       
HET     CL  M 301       1                                                       
HET     CL  M 302       1                                                       
HET     CL  M 303       1                                                       
HET     CL  M 304       1                                                       
HET     CL  N 501       1                                                       
HET     CL  N 502       1                                                       
HET     CL  N 503       1                                                       
HET      K  N 504       1                                                       
HET     CL  O 301       1                                                       
HET     CL  O 302       1                                                       
HET     CL  O 303       1                                                       
HET     CL  O 304       1                                                       
HET     CL  P 301       1                                                       
HET     CL  Q 301       1                                                       
HET     CL  Q 302       1                                                       
HET     CL  R 301       1                                                       
HET     CL  R 302       1                                                       
HET     CL  S 301       1                                                       
HET     CL  S 302       1                                                       
HET     CL  S 303       1                                                       
HET     CL  U 301       1                                                       
HET      K  U 302       1                                                       
HET     MG  V 301       1                                                       
HET     CL  V 302       1                                                       
HET     CL  V 303       1                                                       
HET     MG  W 301       1                                                       
HET     CL  W 302       1                                                       
HET    1PE  W 303      16                                                       
HET     MG  X 301       1                                                       
HET     CL  Y 301       1                                                       
HET     CL  Y 302       1                                                       
HET     CL  Y 303       1                                                       
HET     CL  Y 304       1                                                       
HET     CL  Y 305       1                                                       
HET    1PE  Z 301      16                                                       
HET      K  Z 302       1                                                       
HET     CL  a 301       1                                                       
HET     CL  a 302       1                                                       
HET     CL  a 303       1                                                       
HET    1PE  a 304      16                                                       
HET     CL  b 501       1                                                       
HET     CL  b 502       1                                                       
HET     CL  b 503       1                                                       
HET    1PE  b 504      16                                                       
HET    1PE  b 505      16                                                       
HET      K  b 506       1                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     6V1 (2~{R})-2-AZANYL-3-[(3~{R})-1-ETHYL-2,5-                         
HETNAM   2 6V1  BIS(OXIDANYLIDENE)PYRROLIDIN-3-YL]SULFANYL-PROPANOIC            
HETNAM   3 6V1  ACID                                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     1PE PEG400                                                           
FORMUL   3  YCM    4(C5 H10 N2 O3 S)                                            
FORMUL   5  6V1    8(C9 H14 N2 O4 S)                                            
FORMUL  29   CL    57(CL 1-)                                                    
FORMUL  45  1PE    9(C10 H22 O6)                                                
FORMUL  46    K    6(K 1+)                                                      
FORMUL  47   MG    10(MG 2+)                                                    
FORMUL  11  HOH   *3512(H2 O)                                                   
HELIX    1 AA1 LEU A   18  GLY A   30  1                                  13    
HELIX    2 AA2 MET A   78  GLN A  101  1                                  24    
HELIX    3 AA3 PRO A  105  TYR A  120  1                                  16    
HELIX    4 AA4 ASN A  165  TYR A  177  1                                  13    
HELIX    5 AA5 GLU A  182  GLU A  196  1                                  15    
HELIX    6 AA6 THR A  221  ALA A  231  1                                  11    
HELIX    7 AA7 LEU B   18  HIS B   30  1                                  13    
HELIX    8 AA8 ILE B   79  GLN B  102  1                                  24    
HELIX    9 AA9 PRO B  106  PHE B  124  1                                  19    
HELIX   10 AB1 ASN B  167  TYR B  179  1                                  13    
HELIX   11 AB2 THR B  185  MET B  201  1                                  17    
HELIX   12 AB3 SER B  207  GLU B  209  5                                   3    
HELIX   13 AB4 LYS B  229  ALA B  247  1                                  19    
HELIX   14 AB5 SER C   11  HIS C   15  5                                   5    
HELIX   15 AB6 LEU C   16  LYS C   28  1                                  13    
HELIX   16 AB7 ASP C   55  ARG C   60  5                                   6    
HELIX   17 AB8 LEU C   76  GLU C   99  1                                  24    
HELIX   18 AB9 THR C  103  TYR C  118  1                                  16    
HELIX   19 AC1 GLY C  164  TYR C  176  1                                  13    
HELIX   20 AC2 THR C  183  GLU C  197  1                                  15    
HELIX   21 AC3 ASN C  221  LYS C  234  1                                  14    
HELIX   22 AC4 LEU D   21  LYS D   32  1                                  12    
HELIX   23 AC5 GLU D   60  ILE D   64  5                                   5    
HELIX   24 AC6 ASP D   84  ASN D  104  1                                  21    
HELIX   25 AC7 THR D  108  ASN D  118  1                                  11    
HELIX   26 AC8 ALA D  173  TYR D  185  1                                  13    
HELIX   27 AC9 THR D  190  MET D  206  1                                  17    
HELIX   28 AD1 THR D  230  LYS D  239  1                                  10    
HELIX   29 AD2 ILE E   19  GLY E   32  1                                  14    
HELIX   30 AD3 LEU E   77  ASP E  100  1                                  24    
HELIX   31 AD4 PRO E  104  ILE E  118  1                                  15    
HELIX   32 AD5 PRO E  119  ARG E  122  5                                   4    
HELIX   33 AD6 ARG E  164  MET E  176  1                                  13    
HELIX   34 AD7 SER E  177  CYS E  182  5                                   6    
HELIX   35 AD8 ASN E  183  GLU E  197  1                                  15    
HELIX   36 AD9 ASP E  225  ASP E  228  5                                   4    
HELIX   37 AE1 VAL E  229  GLU E  234  1                                   6    
HELIX   38 AE2 VAL F   20  ASN F   32  1                                  13    
HELIX   39 AE3 LEU F   80  GLY F  103  1                                  24    
HELIX   40 AE4 PRO F  107  TYR F  122  1                                  16    
HELIX   41 AE5 ALA F  168  GLU F  177  1                                  10    
HELIX   42 AE6 LYS F  178  LEU F  179  5                                   2    
HELIX   43 AE7 GLN F  180  MET F  184  5                                   5    
HELIX   44 AE8 THR F  185  HIS F  201  1                                  17    
HELIX   45 AE9 LEU F  219  ASN F  221  5                                   3    
HELIX   46 AF1 PRO F  228  LYS F  244  1                                  17    
HELIX   47 AF2 LEU G   22  GLY G   35  1                                  14    
HELIX   48 AF3 ASP G   62  VAL G   66  5                                   5    
HELIX   49 AF4 MET G   83  GLY G  106  1                                  24    
HELIX   50 AF5 PRO G  110  THR G  126  1                                  17    
HELIX   51 AF6 LYS G  171  LYS G  186  1                                  16    
HELIX   52 AF7 PHE G  187  THR G  190  5                                   4    
HELIX   53 AF8 GLN G  193  SER G  207  1                                  15    
HELIX   54 AF9 LYS G  211  SER G  213  5                                   3    
HELIX   55 AG1 THR G  231  GLU G  244  1                                  14    
HELIX   56 AG2 THR H   48  GLY H   71  1                                  24    
HELIX   57 AG3 ARG H   75  GLN H   91  1                                  17    
HELIX   58 AG4 GLY H  130  PHE H  142  1                                  13    
HELIX   59 AG5 GLU H  147  ASP H  166  1                                  20    
HELIX   60 AG6 SER I    1  TYR I    5  5                                   5    
HELIX   61 AG7 LEU I   55  GLY I   78  1                                  24    
HELIX   62 AG8 LYS I   82  LYS I   97  1                                  16    
HELIX   63 AG9 CYS I  141  TRP I  153  1                                  13    
HELIX   64 AH1 ASP I  158  ASP I  175  1                                  18    
HELIX   65 AH2 GLY J   51  GLY J   72  1                                  22    
HELIX   66 AH3 SER J   76  ARG J   93  1                                  18    
HELIX   67 AH4 GLY J  135  TYR J  147  1                                  13    
HELIX   68 AH5 SER J  152  PHE J  171  1                                  20    
HELIX   69 AH6 GLY K   48  LYS K   71  1                                  24    
HELIX   70 AH7 SER K   75  GLN K   89  1                                  15    
HELIX   71 AH8 GLY K  131  TYR K  143  1                                  13    
HELIX   72 AH9 GLU K  148  ASP K  167  1                                  20    
HELIX   73 AI1 VAL K  192  SER K  200  1                                   9    
HELIX   74 AI2 PHE L   57  ASN L   80  1                                  24    
HELIX   75 AI3 THR L   84  ARG L   99  1                                  16    
HELIX   76 AI4 ALA L  141  VAL L  153  1                                  13    
HELIX   77 AI5 SER L  167  ASP L  186  1                                  20    
HELIX   78 AI6 TYR M   57  GLY M   78  1                                  22    
HELIX   79 AI7 SER M   84  LYS M  102  1                                  19    
HELIX   80 AI8 TYR M  141  ALA M  146  1                                   6    
HELIX   81 AI9 ALA M  146  GLN M  157  1                                  12    
HELIX   82 AJ1 SER M  161  ASP M  180  1                                  20    
HELIX   83 AJ2 TRP M  209  MET M  214  5                                   6    
HELIX   84 AJ3 SER N   48  ASN N   71  1                                  24    
HELIX   85 AJ4 LEU N   75  TYR N   90  1                                  16    
HELIX   86 AJ5 ARG N   91  LEU N   94  5                                   4    
HELIX   87 AJ6 GLY N  129  TYR N  134  5                                   6    
HELIX   88 AJ7 ILE N  135  TYR N  143  1                                   9    
HELIX   89 AJ8 THR N  148  ASP N  167  1                                  20    
HELIX   90 AJ9 LEU N  190  ILE N  194  5                                   5    
HELIX   91 AK1 LEU O   18  GLY O   30  1                                  13    
HELIX   92 AK2 MET O   78  GLN O  101  1                                  24    
HELIX   93 AK3 PRO O  105  TYR O  120  1                                  16    
HELIX   94 AK4 ASN O  165  TYR O  177  1                                  13    
HELIX   95 AK5 GLU O  182  GLU O  196  1                                  15    
HELIX   96 AK6 THR O  221  ALA O  230  1                                  10    
HELIX   97 AK7 LEU P   18  ALA P   31  1                                  14    
HELIX   98 AK8 ILE P   79  GLN P  102  1                                  24    
HELIX   99 AK9 PRO P  106  PHE P  124  1                                  19    
HELIX  100 AL1 ASN P  167  TYR P  179  1                                  13    
HELIX  101 AL2 THR P  185  MET P  201  1                                  17    
HELIX  102 AL3 SER P  207  GLU P  209  5                                   3    
HELIX  103 AL4 LYS P  229  ALA P  247  1                                  19    
HELIX  104 AL5 LEU Q   16  LYS Q   28  1                                  13    
HELIX  105 AL6 ASP Q   55  ARG Q   60  5                                   6    
HELIX  106 AL7 LEU Q   76  GLU Q   99  1                                  24    
HELIX  107 AL8 THR Q  103  TYR Q  118  1                                  16    
HELIX  108 AL9 GLY Q  164  TYR Q  176  1                                  13    
HELIX  109 AM1 ASP Q  178  GLU Q  182  5                                   5    
HELIX  110 AM2 THR Q  183  GLU Q  197  1                                  15    
HELIX  111 AM3 ASN Q  221  ASN Q  239  1                                  19    
HELIX  112 AM4 LEU R   21  LYS R   32  1                                  12    
HELIX  113 AM5 GLU R   60  ILE R   64  5                                   5    
HELIX  114 AM6 LEU R   81  ASN R  104  1                                  24    
HELIX  115 AM7 THR R  108  ASN R  118  1                                  11    
HELIX  116 AM8 ALA R  173  TYR R  185  1                                  13    
HELIX  117 AM9 THR R  190  MET R  206  1                                  17    
HELIX  118 AN1 THR R  230  LYS R  239  1                                  10    
HELIX  119 AN2 ARG S    3  ASP S    7  5                                   5    
HELIX  120 AN3 ILE S   19  GLY S   32  1                                  14    
HELIX  121 AN4 LEU S   77  ASP S  100  1                                  24    
HELIX  122 AN5 PRO S  104  ILE S  118  1                                  15    
HELIX  123 AN6 PRO S  119  ARG S  122  5                                   4    
HELIX  124 AN7 ARG S  164  MET S  180  1                                  17    
HELIX  125 AN8 ASN S  183  GLU S  197  1                                  15    
HELIX  126 AN9 ASP S  225  ASP S  228  5                                   4    
HELIX  127 AO1 VAL S  229  GLU S  234  1                                   6    
HELIX  128 AO2 VAL T   20  ASN T   32  1                                  13    
HELIX  129 AO3 LEU T   80  GLY T  103  1                                  24    
HELIX  130 AO4 PRO T  107  TYR T  122  1                                  16    
HELIX  131 AO5 ALA T  168  GLU T  177  1                                  10    
HELIX  132 AO6 LYS T  178  LEU T  179  5                                   2    
HELIX  133 AO7 GLN T  180  MET T  184  5                                   5    
HELIX  134 AO8 THR T  185  HIS T  201  1                                  17    
HELIX  135 AO9 LEU T  219  ASN T  221  5                                   3    
HELIX  136 AP1 PRO T  228  LYS T  244  1                                  17    
HELIX  137 AP2 LEU U   22  GLY U   35  1                                  14    
HELIX  138 AP3 ASP U   62  VAL U   66  5                                   5    
HELIX  139 AP4 MET U   83  GLY U  106  1                                  24    
HELIX  140 AP5 PRO U  110  THR U  126  1                                  17    
HELIX  141 AP6 LYS U  171  LYS U  184  1                                  14    
HELIX  142 AP7 VAL U  195  SER U  207  1                                  13    
HELIX  143 AP8 LYS U  211  SER U  213  5                                   3    
HELIX  144 AP9 THR U  231  GLU U  244  1                                  14    
HELIX  145 AQ1 THR V   48  GLY V   71  1                                  24    
HELIX  146 AQ2 ARG V   75  TYR V   90  1                                  16    
HELIX  147 AQ3 GLY V  130  PHE V  142  1                                  13    
HELIX  148 AQ4 GLU V  147  ASP V  166  1                                  20    
HELIX  149 AQ5 SER W    1  TYR W    5  5                                   5    
HELIX  150 AQ6 LEU W   55  GLY W   78  1                                  24    
HELIX  151 AQ7 LYS W   82  LYS W   97  1                                  16    
HELIX  152 AQ8 CYS W  141  TRP W  153  1                                  13    
HELIX  153 AQ9 ASP W  158  ASP W  175  1                                  18    
HELIX  154 AR1 GLY X   51  GLY X   72  1                                  22    
HELIX  155 AR2 SER X   76  ARG X   93  1                                  18    
HELIX  156 AR3 GLY X  135  TYR X  147  1                                  13    
HELIX  157 AR4 SER X  152  PHE X  171  1                                  20    
HELIX  158 AR5 GLY Y   48  LYS Y   71  1                                  24    
HELIX  159 AR6 SER Y   75  GLN Y   89  1                                  15    
HELIX  160 AR7 GLY Y  131  TYR Y  143  1                                  13    
HELIX  161 AR8 GLU Y  148  ASP Y  167  1                                  20    
HELIX  162 AR9 VAL Y  192  TYR Y  199  1                                   8    
HELIX  163 AS1 PHE Z   57  ASN Z   80  1                                  24    
HELIX  164 AS2 THR Z   84  ARG Z   99  1                                  16    
HELIX  165 AS3 ALA Z  141  VAL Z  153  1                                  13    
HELIX  166 AS4 SER Z  167  ASP Z  186  1                                  20    
HELIX  167 AS5 TYR a   57  GLY a   78  1                                  22    
HELIX  168 AS6 SER a   84  LYS a  102  1                                  19    
HELIX  169 AS7 TYR a  141  ALA a  146  1                                   6    
HELIX  170 AS8 ALA a  146  GLN a  157  1                                  12    
HELIX  171 AS9 SER a  161  ASP a  180  1                                  20    
HELIX  172 AT1 TRP a  209  MET a  214  5                                   6    
HELIX  173 AT2 SER b   48  ASN b   71  1                                  24    
HELIX  174 AT3 LEU b   75  TYR b   90  1                                  16    
HELIX  175 AT4 ARG b   91  LEU b   94  5                                   4    
HELIX  176 AT5 GLY b  129  TYR b  134  5                                   6    
HELIX  177 AT6 ILE b  135  TYR b  143  1                                   9    
HELIX  178 AT7 THR b  148  ASP b  167  1                                  20    
HELIX  179 AT8 LEU b  190  ILE b  194  5                                   5    
SHEET    1 AA1 5 ALA A 159  MET A 162  0                                        
SHEET    2 AA1 5 SER A  34  LYS A  38 -1  N  GLY A  36   O  THR A 160           
SHEET    3 AA1 5 VAL A  43  GLU A  48 -1  O  ALA A  46   N  VAL A  35           
SHEET    4 AA1 5 ILE A 207  ASN A 213 -1  O  GLY A 210   N  LEU A  45           
SHEET    5 AA1 5 GLY A 216  ARG A 219 -1  O  ARG A 218   N  ILE A 211           
SHEET    1 AA2 5 GLU A  65  THR A  68  0                                        
SHEET    2 AA2 5 ILE A  71  GLY A  77 -1  O  ILE A  71   N  ILE A  67           
SHEET    3 AA2 5 VAL A 131  ASN A 139 -1  O  LEU A 134   N  VAL A  74           
SHEET    4 AA2 5 ARG A 142  SER A 148 -1  O  PHE A 146   N  ILE A 135           
SHEET    5 AA2 5 TYR A 154  ALA A 156 -1  O  PHE A 155   N  GLN A 147           
SHEET    1 AA3 5 ALA B 161  ILE B 164  0                                        
SHEET    2 AA3 5 CYS B  34  ALA B  39 -1  N  CYS B  34   O  ILE B 164           
SHEET    3 AA3 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  LEU B  35           
SHEET    4 AA3 5 VAL B 211  GLU B 219 -1  O  GLU B 212   N  ALA B  47           
SHEET    5 AA3 5 LYS B 222  VAL B 227 -1  O  VAL B 224   N  THR B 217           
SHEET    1 AA4 5 ILE B  65  ASN B  69  0                                        
SHEET    2 AA4 5 MET B  72  GLY B  78 -1  O  CYS B  74   N  TYR B  66           
SHEET    3 AA4 5 VAL B 132  ASP B 140 -1  O  ILE B 137   N  ALA B  73           
SHEET    4 AA4 5 GLY B 144  SER B 150 -1  O  SER B 150   N  LEU B 134           
SHEET    5 AA4 5 TYR B 156  GLY B 158 -1  O  GLY B 157   N  GLN B 149           
SHEET    1 AA5 5 ALA C 158  ILE C 161  0                                        
SHEET    2 AA5 5 ALA C  32  ARG C  36 -1  N  GLY C  34   O  ASN C 159           
SHEET    3 AA5 5 ILE C  40  GLU C  46 -1  O  GLY C  44   N  VAL C  33           
SHEET    4 AA5 5 ILE C 206  ARG C 212 -1  O  GLU C 207   N  VAL C  45           
SHEET    5 AA5 5 LYS C 218  ILE C 219 -1  O  LYS C 218   N  VAL C 210           
SHEET    1 AA6 5 ILE C  62  ASP C  66  0                                        
SHEET    2 AA6 5 VAL C  69  GLY C  75 -1  O  MET C  71   N  YCM C  63           
SHEET    3 AA6 5 ILE C 129  PHE C 136 -1  O  LEU C 132   N  ALA C  72           
SHEET    4 AA6 5 PRO C 142  THR C 147 -1  O  TYR C 145   N  ILE C 133           
SHEET    5 AA6 5 TYR C 153  ALA C 155 -1  O  HIS C 154   N  GLN C 146           
SHEET    1 AA7 5 ALA D 167  ILE D 170  0                                        
SHEET    2 AA7 5 ALA D  37  THR D  42 -1  N  GLY D  39   O  ARG D 168           
SHEET    3 AA7 5 GLY D  45  GLU D  51 -1  O  ALA D  49   N  ILE D  38           
SHEET    4 AA7 5 ILE D 215  VAL D 220 -1  O  ALA D 218   N  LEU D  48           
SHEET    5 AA7 5 HIS D 227  MET D 228 -1  O  HIS D 227   N  THR D 219           
SHEET    1 AA8 5 ILE D  67  ASP D  71  0                                        
SHEET    2 AA8 5 ILE D  74  GLY D  80 -1  O  ILE D  74   N  ILE D  70           
SHEET    3 AA8 5 VAL D 139  ASP D 147 -1  O  GLY D 144   N  GLY D  75           
SHEET    4 AA8 5 GLY D 150  MET D 156 -1  O  GLN D 152   N  GLY D 145           
SHEET    5 AA8 5 PHE D 162  GLN D 164 -1  O  VAL D 163   N  HIS D 155           
SHEET    1 AA9 5 ALA E 158  ILE E 161  0                                        
SHEET    2 AA9 5 THR E  35  LYS E  39 -1  N  GLY E  37   O  MET E 159           
SHEET    3 AA9 5 HIS E  43  LEU E  49 -1  O  VAL E  47   N  VAL E  36           
SHEET    4 AA9 5 VAL E 210  GLY E 216 -1  O  VAL E 215   N  ALA E  44           
SHEET    5 AA9 5 LEU E 219  TYR E 224 -1  O  TYR E 224   N  ILE E 212           
SHEET    1 AB1 5 ILE E  63  ASP E  67  0                                        
SHEET    2 AB1 5 ILE E  70  GLY E  76 -1  O  ILE E  72   N  LEU E  64           
SHEET    3 AB1 5 VAL E 130  ASP E 138 -1  O  GLY E 131   N  ALA E  75           
SHEET    4 AB1 5 GLY E 141  THR E 147 -1  O  PHE E 145   N  ILE E 134           
SHEET    5 AB1 5 TYR E 153  CYS E 156 -1  O  CYS E 156   N  ILE E 144           
SHEET    1 AB2 5 GLY F 162  ILE F 165  0                                        
SHEET    2 AB2 5 ALA F  36  CYS F  41 -1  N  GLY F  38   O  CYS F 163           
SHEET    3 AB2 5 GLY F  44  LEU F  52 -1  O  GLY F  44   N  CYS F  41           
SHEET    4 AB2 5 PHE F 209  GLY F 217 -1  O  SER F 214   N  PHE F  47           
SHEET    5 AB2 5 GLU F 225  ILE F 226 -1  O  GLU F 225   N  TRP F 215           
SHEET    1 AB3 5 LEU F  66  ASP F  70  0                                        
SHEET    2 AB3 5 VAL F  73  GLY F  79 -1  O  VAL F  73   N  VAL F  69           
SHEET    3 AB3 5 CYS F 133  SER F 141 -1  O  MET F 136   N  ALA F  76           
SHEET    4 AB3 5 GLY F 145  ILE F 151 -1  O  ILE F 151   N  PHE F 135           
SHEET    5 AB3 5 SER F 157  GLY F 159 -1  O  TYR F 158   N  MET F 150           
SHEET    1 AB4 5 ALA G 165  GLY G 169  0                                        
SHEET    2 AB4 5 THR G  38  ARG G  43 -1  N  ALA G  41   O  THR G 166           
SHEET    3 AB4 5 6V1 G  47  GLN G  53 -1  O  VAL G  51   N  VAL G  40           
SHEET    4 AB4 5 ILE G 215  THR G 221 -1  O  GLY G 218   N  ILE G  50           
SHEET    5 AB4 5 ARG G 228  ILE G 229 -1  O  ARG G 228   N  VAL G 219           
SHEET    1 AB5 5 LEU G  69  THR G  73  0                                        
SHEET    2 AB5 5 ILE G  76  GLY G  82 -1  O  ILE G  76   N  ILE G  72           
SHEET    3 AB5 5 CYS G 136  ASP G 144 -1  O  ILE G 139   N  VAL G  79           
SHEET    4 AB5 5 GLY G 148  CYS G 154 -1  O  TYR G 152   N  LEU G 140           
SHEET    5 AB5 5 TYR G 160  GLY G 162 -1  O  6V1 G 161   N  LYS G 153           
SHEET    1 AB6 5 TYR H 124  MET H 127  0                                        
SHEET    2 AB6 5 ILE H   3  TYR H   8 -1  N  ILE H   3   O  MET H 127           
SHEET    3 AB6 5 GLY H  11  ASP H  17 -1  O  GLY H  11   N  TYR H   8           
SHEET    4 AB6 5 ILE H 173  SER H 179 -1  O  CYS H 176   N  LEU H  14           
SHEET    5 AB6 5 LYS H 182  THR H 190 -1  O  TYR H 189   N  ILE H 173           
SHEET    1 AB7 2 ALA H  20  GLU H  22  0                                        
SHEET    2 AB7 2 VAL H  25  ASP H  28 -1  O  VAL H  25   N  GLU H  22           
SHEET    1 AB8 5 ILE H  34  SER H  38  0                                        
SHEET    2 AB8 5 ILE H  41  GLY H  47 -1  O  CYS H  43   N  HIS H  35           
SHEET    3 AB8 5 ALA H  96  ASP H 104 -1  O  ALA H  97   N  ALA H  46           
SHEET    4 AB8 5 GLY H 107  ILE H 113 -1  O  ILE H 113   N  LEU H  98           
SHEET    5 AB8 5 THR H 119  LYS H 121 -1  O  ASP H 120   N  SER H 112           
SHEET    1 AB9 6 VAL H 211  PRO H 218  0                                        
SHEET    2 AB9 6 LYS I 193  LEU I 199 -1  O  ILE I 194   N  THR H 217           
SHEET    3 AB9 6 VAL I 184  ILE I 189 -1  N  VAL I 186   O  ARG I 197           
SHEET    4 AB9 6 VAL I  19  ASP I  24 -1  N  ILE I  21   O  HIS I 187           
SHEET    5 AB9 6 ALA I   9  LYS I  14 -1  N  MET I  11   O  ALA I  22           
SHEET    6 AB9 6 PHE I 135  GLY I 139 -1  O  SER I 138   N  VAL I  10           
SHEET    1 AC1 2 PHE I  27  ILE I  29  0                                        
SHEET    2 AC1 2 GLN I  32  THR I  35 -1  O  VAL I  34   N  PHE I  27           
SHEET    1 AC2 5 ILE I  41  PRO I  43  0                                        
SHEET    2 AC2 5 LEU I  48  GLY I  54 -1  O  ILE I  50   N  PHE I  42           
SHEET    3 AC2 5 THR I 104  LEU I 111 -1  O  VAL I 107   N  GLY I  51           
SHEET    4 AC2 5 PRO I 118  LEU I 123 -1  O  PHE I 119   N  GLY I 110           
SHEET    5 AC2 5 PRO I 129  THR I 132 -1  O  MET I 130   N  SER I 122           
SHEET    1 AC3 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC3 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC3 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC3 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC3 5 GLY J 187  ASP J 190 -1  O  HIS J 189   N  ILE J 182           
SHEET    1 AC4 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC4 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC4 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC4 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC4 5 ILE J 194  SER J 195 -1  O  ILE J 194   N  PHE J 178           
SHEET    1 AC5 2 ALA J  21  SER J  23  0                                        
SHEET    2 AC5 2 VAL J  26  LYS J  29 -1  O  MET J  28   N  ALA J  21           
SHEET    1 AC6 5 MET J  35  SER J  39  0                                        
SHEET    2 AC6 5 ILE J  42  GLY J  48 -1  O  LEU J  44   N  PHE J  36           
SHEET    3 AC6 5 VAL J 100  ASP J 108 -1  O  LEU J 103   N  LEU J  45           
SHEET    4 AC6 5 GLY J 112  MET J 118 -1  O  GLY J 112   N  ASP J 108           
SHEET    5 AC6 5 LEU J 124  LYS J 126 -1  O  ALA J 125   N  TYR J 117           
SHEET    1 AC7 5 THR K 125  VAL K 128  0                                        
SHEET    2 AC7 5 THR K   3  PHE K   8 -1  N  ALA K   5   O  PHE K 126           
SHEET    3 AC7 5 GLY K  11  ALA K  16 -1  O  ALA K  15   N  LEU K   4           
SHEET    4 AC7 5 ALA K 173  ARG K 180 -1  O  VAL K 179   N  VAL K  12           
SHEET    5 AC7 5 GLY K 183  ASN K 191 -1  O  ASP K 190   N  VAL K 174           
SHEET    1 AC8 2 ALA K  20  ALA K  22  0                                        
SHEET    2 AC8 2 TYR K  25  SER K  28 -1  O  SER K  28   N  ALA K  20           
SHEET    1 AC9 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AC9 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC9 5 GLY K  98  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC9 5 GLY K 108  ASP K 115 -1  O  TYR K 112   N  ILE K 101           
SHEET    5 AC9 5 ARG K 120  SER K 122 -1  O  ILE K 121   N  TYR K 113           
SHEET    1 AD1 5 PHE L 135  GLY L 139  0                                        
SHEET    2 AD1 5 THR L  11  ALA L  16 -1  N  ILE L  12   O  GLY L 138           
SHEET    3 AD1 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AD1 5 ALA L 192  THR L 199 -1  O  CYS L 196   N  VAL L  23           
SHEET    5 AD1 5 GLY L 202  SER L 209 -1  O  GLU L 206   N  ILE L 195           
SHEET    1 AD2 2 LEU L  29  GLU L  31  0                                        
SHEET    2 AD2 2 SER L  34  THR L  37 -1  O  HIS L  36   N  LEU L  29           
SHEET    1 AD3 5 CYS L  43  THR L  47  0                                        
SHEET    2 AD3 5 THR L  50  GLY L  56 -1  O  THR L  50   N  LEU L  46           
SHEET    3 AD3 5 VAL L 106  LEU L 113 -1  O  ILE L 109   N  GLY L  53           
SHEET    4 AD3 5 GLY L 119  PHE L 124 -1  O  ALA L 120   N  GLY L 112           
SHEET    5 AD3 5 TYR L 130  ASP L 133 -1  O  ASP L 133   N  VAL L 121           
SHEET    1 AD4 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AD4 5 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD4 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD4 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD4 5 ILE M  42  ASN M  46 -1  N  MET M  43   O  LEU M  51           
SHEET    1 AD5 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AD5 7 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD5 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD5 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD5 7 ASN M 108  ALA M 116 -1  O  THR M 109   N  SER M  54           
SHEET    6 AD5 7 GLU M 119  VAL M 125 -1  O  VAL M 125   N  MET M 110           
SHEET    7 AD5 7 ALA M 131  GLU M 133 -1  O  TYR M 132   N  TYR M 124           
SHEET    1 AD6 5 SER M 136  ALA M 138  0                                        
SHEET    2 AD6 5 VAL M  11  PHE M  16 -1  N  GLY M  13   O  LEU M 137           
SHEET    3 AD6 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  PHE M  16           
SHEET    4 AD6 5 PHE M 187  THR M 193 -1  O  ALA M 190   N  ILE M  22           
SHEET    5 AD6 5 GLY M 196  LEU M 203 -1  O  LEU M 203   N  PHE M 187           
SHEET    1 AD7 5 PHE N 125  GLY N 128  0                                        
SHEET    2 AD7 5 ILE N   3  PHE N   8 -1  N  ALA N   5   O  ALA N 126           
SHEET    3 AD7 5 GLY N  11  ALA N  16 -1  O  GLY N  11   N  PHE N   8           
SHEET    4 AD7 5 ILE N 174  ALA N 180 -1  O  ILE N 179   N  VAL N  12           
SHEET    5 AD7 5 GLY N 183  LEU N 189 -1  O  LEU N 189   N  ILE N 174           
SHEET    1 AD8 2 THR N  20  THR N  22  0                                        
SHEET    2 AD8 2 TYR N  25  ASN N  28 -1  O  ASN N  28   N  THR N  20           
SHEET    1 AD9 5 LEU N  34  HIS N  38  0                                        
SHEET    2 AD9 5 ILE N  41  GLY N  47 -1  O  ILE N  41   N  ILE N  37           
SHEET    3 AD9 5 ALA N  96  ASP N 104 -1  O  ALA N 101   N  PHE N  42           
SHEET    4 AD9 5 GLY N 108  VAL N 114 -1  O  TYR N 112   N  ILE N 100           
SHEET    5 AD9 5 VAL N 121  GLN N 123 -1  O  VAL N 121   N  SER N 113           
SHEET    1 AE1 5 ALA O 159  MET O 162  0                                        
SHEET    2 AE1 5 SER O  34  LYS O  38 -1  N  GLY O  36   O  THR O 160           
SHEET    3 AE1 5 VAL O  43  GLU O  48 -1  O  ALA O  46   N  VAL O  35           
SHEET    4 AE1 5 ILE O 207  ASN O 213 -1  O  GLY O 210   N  LEU O  45           
SHEET    5 AE1 5 GLY O 216  ARG O 219 -1  O  ARG O 218   N  ILE O 211           
SHEET    1 AE2 5 GLU O  65  THR O  68  0                                        
SHEET    2 AE2 5 ILE O  71  GLY O  77 -1  O  ILE O  71   N  ILE O  67           
SHEET    3 AE2 5 VAL O 131  ASN O 139 -1  O  LEU O 134   N  VAL O  74           
SHEET    4 AE2 5 ARG O 142  SER O 148 -1  O  PHE O 146   N  ILE O 135           
SHEET    5 AE2 5 TYR O 154  ALA O 156 -1  O  PHE O 155   N  GLN O 147           
SHEET    1 AE3 5 ALA P 161  ILE P 164  0                                        
SHEET    2 AE3 5 CYS P  34  ALA P  39 -1  N  CYS P  34   O  ILE P 164           
SHEET    3 AE3 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  LEU P  35           
SHEET    4 AE3 5 VAL P 211  GLU P 219 -1  O  GLU P 212   N  ALA P  47           
SHEET    5 AE3 5 LYS P 222  VAL P 227 -1  O  VAL P 224   N  THR P 217           
SHEET    1 AE4 5 ILE P  65  ASN P  69  0                                        
SHEET    2 AE4 5 MET P  72  GLY P  78 -1  O  CYS P  74   N  TYR P  66           
SHEET    3 AE4 5 VAL P 132  ASP P 140 -1  O  ILE P 137   N  ALA P  73           
SHEET    4 AE4 5 GLY P 144  SER P 150 -1  O  GLN P 146   N  GLY P 138           
SHEET    5 AE4 5 TYR P 156  GLY P 158 -1  O  GLY P 157   N  GLN P 149           
SHEET    1 AE5 5 ALA Q 158  ILE Q 161  0                                        
SHEET    2 AE5 5 ALA Q  32  ARG Q  36 -1  N  GLY Q  34   O  ASN Q 159           
SHEET    3 AE5 5 ILE Q  40  GLU Q  46 -1  O  GLY Q  44   N  VAL Q  33           
SHEET    4 AE5 5 ILE Q 206  ARG Q 212 -1  O  GLU Q 207   N  VAL Q  45           
SHEET    5 AE5 5 LYS Q 218  LEU Q 220 -1  O  LEU Q 220   N  LEU Q 208           
SHEET    1 AE6 5 ILE Q  62  ASP Q  66  0                                        
SHEET    2 AE6 5 VAL Q  69  GLY Q  75 -1  O  MET Q  71   N  YCM Q  63           
SHEET    3 AE6 5 ILE Q 129  PHE Q 136 -1  O  LEU Q 132   N  ALA Q  72           
SHEET    4 AE6 5 PRO Q 142  THR Q 147 -1  O  TYR Q 145   N  ILE Q 133           
SHEET    5 AE6 5 TYR Q 153  ALA Q 155 -1  O  HIS Q 154   N  GLN Q 146           
SHEET    1 AE7 5 ALA R 167  ILE R 170  0                                        
SHEET    2 AE7 5 ALA R  37  THR R  42 -1  N  GLY R  39   O  ARG R 168           
SHEET    3 AE7 5 GLY R  45  GLU R  51 -1  O  ALA R  49   N  ILE R  38           
SHEET    4 AE7 5 ILE R 215  VAL R 220 -1  O  ALA R 218   N  LEU R  48           
SHEET    5 AE7 5 HIS R 227  MET R 228 -1  O  HIS R 227   N  THR R 219           
SHEET    1 AE8 5 ILE R  67  ASP R  71  0                                        
SHEET    2 AE8 5 ILE R  74  GLY R  80 -1  O  ILE R  74   N  ILE R  70           
SHEET    3 AE8 5 VAL R 139  ASP R 147 -1  O  GLY R 144   N  GLY R  75           
SHEET    4 AE8 5 GLY R 150  MET R 156 -1  O  GLN R 152   N  GLY R 145           
SHEET    5 AE8 5 PHE R 162  GLN R 164 -1  O  VAL R 163   N  HIS R 155           
SHEET    1 AE9 5 ALA S 158  ILE S 161  0                                        
SHEET    2 AE9 5 THR S  35  LYS S  39 -1  N  GLY S  37   O  MET S 159           
SHEET    3 AE9 5 HIS S  43  LEU S  49 -1  O  VAL S  47   N  VAL S  36           
SHEET    4 AE9 5 VAL S 210  GLY S 216 -1  O  VAL S 215   N  ALA S  44           
SHEET    5 AE9 5 LEU S 219  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF1 5 ILE S  63  ASP S  67  0                                        
SHEET    2 AF1 5 ILE S  70  GLY S  76 -1  O  ILE S  72   N  LEU S  64           
SHEET    3 AF1 5 VAL S 130  ASP S 138 -1  O  ALA S 135   N  GLY S  71           
SHEET    4 AF1 5 GLY S 141  THR S 147 -1  O  PHE S 145   N  ILE S 134           
SHEET    5 AF1 5 TYR S 153  CYS S 156 -1  O  CYS S 156   N  ILE S 144           
SHEET    1 AF2 5 GLY T 162  ILE T 165  0                                        
SHEET    2 AF2 5 ALA T  36  CYS T  41 -1  N  GLY T  38   O  CYS T 163           
SHEET    3 AF2 5 GLY T  44  LEU T  52 -1  O  GLY T  44   N  CYS T  41           
SHEET    4 AF2 5 PHE T 209  GLY T 217 -1  O  SER T 214   N  PHE T  47           
SHEET    5 AF2 5 GLU T 225  ILE T 226 -1  O  GLU T 225   N  TRP T 215           
SHEET    1 AF3 5 LEU T  66  ASP T  70  0                                        
SHEET    2 AF3 5 VAL T  73  GLY T  79 -1  O  VAL T  73   N  VAL T  69           
SHEET    3 AF3 5 CYS T 133  SER T 141 -1  O  MET T 136   N  ALA T  76           
SHEET    4 AF3 5 GLY T 145  ILE T 151 -1  O  ILE T 151   N  PHE T 135           
SHEET    5 AF3 5 SER T 157  GLY T 159 -1  O  TYR T 158   N  MET T 150           
SHEET    1 AF4 5 ALA U 165  GLY U 169  0                                        
SHEET    2 AF4 5 THR U  38  ARG U  43 -1  N  ALA U  41   O  THR U 166           
SHEET    3 AF4 5 6V1 U  47  GLN U  53 -1  O  VAL U  51   N  VAL U  40           
SHEET    4 AF4 5 ILE U 215  THR U 221 -1  O  GLY U 218   N  ILE U  50           
SHEET    5 AF4 5 ARG U 228  ILE U 229 -1  O  ARG U 228   N  VAL U 219           
SHEET    1 AF5 5 LEU U  69  THR U  73  0                                        
SHEET    2 AF5 5 ILE U  76  GLY U  82 -1  O  ILE U  76   N  ILE U  72           
SHEET    3 AF5 5 CYS U 136  ASP U 144 -1  O  ILE U 139   N  VAL U  79           
SHEET    4 AF5 5 GLY U 148  CYS U 154 -1  O  TYR U 152   N  LEU U 140           
SHEET    5 AF5 5 TYR U 160  GLY U 162 -1  O  6V1 U 161   N  LYS U 153           
SHEET    1 AF6 5 TYR V 124  MET V 127  0                                        
SHEET    2 AF6 5 ILE V   3  TYR V   8 -1  N  ILE V   3   O  MET V 127           
SHEET    3 AF6 5 GLY V  11  ASP V  17 -1  O  GLY V  11   N  TYR V   8           
SHEET    4 AF6 5 ILE V 173  SER V 179 -1  O  CYS V 176   N  LEU V  14           
SHEET    5 AF6 5 LYS V 182  THR V 190 -1  O  TYR V 189   N  ILE V 173           
SHEET    1 AF7 2 ALA V  20  GLU V  22  0                                        
SHEET    2 AF7 2 VAL V  25  ASP V  28 -1  O  VAL V  25   N  GLU V  22           
SHEET    1 AF8 5 ILE V  34  SER V  38  0                                        
SHEET    2 AF8 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF8 5 ALA V  96  ASP V 104 -1  O  ALA V  97   N  ALA V  46           
SHEET    4 AF8 5 GLY V 107  ILE V 113 -1  O  ILE V 113   N  LEU V  98           
SHEET    5 AF8 5 THR V 119  LYS V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AF9 6 VAL V 211  PRO V 218  0                                        
SHEET    2 AF9 6 LYS W 193  LEU W 199 -1  O  ILE W 194   N  THR V 217           
SHEET    3 AF9 6 VAL W 184  ILE W 189 -1  N  VAL W 186   O  ARG W 197           
SHEET    4 AF9 6 VAL W  19  ASP W  24 -1  N  VAL W  19   O  ILE W 189           
SHEET    5 AF9 6 ALA W   9  LYS W  14 -1  N  MET W  11   O  ALA W  22           
SHEET    6 AF9 6 PHE W 135  GLY W 139 -1  O  SER W 138   N  VAL W  10           
SHEET    1 AG1 2 PHE W  27  ILE W  29  0                                        
SHEET    2 AG1 2 GLN W  32  THR W  35 -1  O  VAL W  34   N  PHE W  27           
SHEET    1 AG2 5 ILE W  41  PRO W  43  0                                        
SHEET    2 AG2 5 LEU W  48  GLY W  54 -1  O  ILE W  50   N  PHE W  42           
SHEET    3 AG2 5 THR W 104  LEU W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG2 5 PRO W 118  LEU W 123 -1  O  PHE W 119   N  GLY W 110           
SHEET    5 AG2 5 PRO W 129  THR W 132 -1  O  MET W 130   N  SER W 122           
SHEET    1 AG3 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG3 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG3 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG3 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG3 5 GLY X 187  ASP X 190 -1  O  HIS X 189   N  ILE X 182           
SHEET    1 AG4 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG4 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG4 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG4 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG4 5 ILE X 194  SER X 195 -1  O  ILE X 194   N  PHE X 178           
SHEET    1 AG5 2 ALA X  21  SER X  23  0                                        
SHEET    2 AG5 2 VAL X  26  LYS X  29 -1  O  MET X  28   N  ALA X  21           
SHEET    1 AG6 5 MET X  35  SER X  39  0                                        
SHEET    2 AG6 5 ILE X  42  GLY X  48 -1  O  LEU X  44   N  PHE X  36           
SHEET    3 AG6 5 VAL X 100  ASP X 108 -1  O  LEU X 103   N  LEU X  45           
SHEET    4 AG6 5 GLY X 112  MET X 118 -1  O  GLY X 112   N  ASP X 108           
SHEET    5 AG6 5 LEU X 124  LYS X 126 -1  O  ALA X 125   N  TYR X 117           
SHEET    1 AG7 5 THR Y 125  VAL Y 128  0                                        
SHEET    2 AG7 5 THR Y   3  PHE Y   8 -1  N  ALA Y   5   O  PHE Y 126           
SHEET    3 AG7 5 GLY Y  11  ALA Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4 AG7 5 ALA Y 173  ARG Y 180 -1  O  VAL Y 179   N  VAL Y  12           
SHEET    5 AG7 5 GLY Y 183  ASN Y 191 -1  O  ASP Y 190   N  VAL Y 174           
SHEET    1 AG8 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG8 2 TYR Y  25  SER Y  28 -1  O  SER Y  28   N  ALA Y  20           
SHEET    1 AG9 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AG9 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AG9 5 GLY Y  98  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AG9 5 GLY Y 108  ASP Y 115 -1  O  TYR Y 112   N  ILE Y 101           
SHEET    5 AG9 5 ARG Y 120  SER Y 122 -1  O  ILE Y 121   N  TYR Y 113           
SHEET    1 AH1 5 PHE Z 135  GLY Z 139  0                                        
SHEET    2 AH1 5 THR Z  11  ALA Z  16 -1  N  ILE Z  12   O  GLY Z 138           
SHEET    3 AH1 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AH1 5 ALA Z 192  THR Z 199 -1  O  CYS Z 196   N  VAL Z  23           
SHEET    5 AH1 5 GLY Z 202  SER Z 209 -1  O  VAL Z 208   N  LEU Z 193           
SHEET    1 AH2 2 LEU Z  29  GLU Z  31  0                                        
SHEET    2 AH2 2 SER Z  34  THR Z  37 -1  O  HIS Z  36   N  LEU Z  29           
SHEET    1 AH3 5 CYS Z  43  THR Z  47  0                                        
SHEET    2 AH3 5 THR Z  50  GLY Z  56 -1  O  ILE Z  52   N  TYR Z  44           
SHEET    3 AH3 5 VAL Z 106  LEU Z 113 -1  O  TYR Z 107   N  SER Z  55           
SHEET    4 AH3 5 GLY Z 119  PHE Z 124 -1  O  ALA Z 120   N  GLY Z 112           
SHEET    5 AH3 5 TYR Z 130  ASP Z 133 -1  O  ASP Z 133   N  VAL Z 121           
SHEET    1 AH4 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH4 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH4 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH4 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH4 5 ILE a  42  ASN a  46 -1  N  MET a  43   O  LEU a  51           
SHEET    1 AH5 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH5 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH5 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH5 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH5 7 ASN a 108  ALA a 116 -1  O  THR a 109   N  SER a  54           
SHEET    6 AH5 7 GLU a 119  VAL a 125 -1  O  VAL a 125   N  MET a 110           
SHEET    7 AH5 7 ALA a 131  GLU a 133 -1  O  TYR a 132   N  TYR a 124           
SHEET    1 AH6 5 SER a 136  ALA a 138  0                                        
SHEET    2 AH6 5 VAL a  11  PHE a  16 -1  N  GLY a  13   O  LEU a 137           
SHEET    3 AH6 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  PHE a  16           
SHEET    4 AH6 5 PHE a 187  THR a 193 -1  O  ALA a 190   N  ILE a  22           
SHEET    5 AH6 5 GLY a 196  LEU a 203 -1  O  GLU a 200   N  ILE a 189           
SHEET    1 AH7 5 PHE b 125  GLY b 128  0                                        
SHEET    2 AH7 5 ILE b   3  PHE b   8 -1  N  ALA b   5   O  ALA b 126           
SHEET    3 AH7 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4 AH7 5 ILE b 174  ALA b 180 -1  O  ILE b 179   N  VAL b  12           
SHEET    5 AH7 5 GLY b 183  LEU b 189 -1  O  LEU b 189   N  ILE b 174           
SHEET    1 AH8 2 THR b  20  THR b  22  0                                        
SHEET    2 AH8 2 TYR b  25  ASN b  28 -1  O  ASN b  28   N  THR b  20           
SHEET    1 AH9 5 LEU b  34  HIS b  38  0                                        
SHEET    2 AH9 5 ILE b  41  GLY b  47 -1  O  ILE b  41   N  ILE b  37           
SHEET    3 AH9 5 ALA b  96  ASP b 104 -1  O  ALA b 101   N  PHE b  42           
SHEET    4 AH9 5 GLY b 108  VAL b 114 -1  O  TYR b 112   N  ILE b 100           
SHEET    5 AH9 5 VAL b 121  ARG b 122 -1  O  VAL b 121   N  SER b 113           
LINK         C   ILE C  62                 N   YCM C  63     1555   1555  1.33  
LINK         C   YCM C  63                 N   ALA C  64     1555   1555  1.34  
LINK         C   THR E 147                 N   6V1 E 148     1555   1555  1.34  
LINK         C   6V1 E 148                 N   PRO E 149     1555   1555  1.33  
LINK         OG1 THR G  14                 K     K G 304     1555   1555  2.73  
LINK         C   ASP G  46                 N   6V1 G  47     1555   1555  1.32  
LINK         C   6V1 G  47                 N   ALA G  48     1555   1555  1.32  
LINK         O   TYR G 125                 K     K G 304     1555   1555  2.53  
LINK         O   ASN G 128                 K     K G 304     1555   1555  2.56  
LINK         O   MET G 131                 K     K G 304     1555   1555  2.50  
LINK         C   CYS G 136                 N   YCM G 137     1555   1555  1.32  
LINK         C   YCM G 137                 N   MET G 138     1555   1555  1.33  
LINK         C   TYR G 160                 N   6V1 G 161     1555   1555  1.33  
LINK         C   6V1 G 161                 N   GLY G 162     1555   1555  1.32  
LINK         OE1 GLN H  91                MG    MG H 301     1555   1555  2.28  
LINK         O   ILE H 163                MG    MG H 302     1555   1555  2.22  
LINK         O   ASP H 166                MG    MG H 302     1555   1555  2.23  
LINK         O   SER H 169                MG    MG H 302     1555   1555  2.19  
LINK         O   VAL I 174                MG    MG I 301     1555   1555  2.21  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.21  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.19  
LINK         O   ASP I 204                MG    MG I 305     1555   1555  2.20  
LINK         C   ASP J  90                 N   6V1 J  91     1555   1555  1.34  
LINK         C   6V1 J  91                 N   LEU J  92     1555   1555  1.34  
LINK         O   THR K 164                MG    MG K 301     1555   1555  2.20  
LINK         O   ASP K 167                MG    MG K 301     1555   1555  2.20  
LINK         O   SER K 170                MG    MG K 301     1555   1555  2.19  
LINK         O   ALA L 183                 K     K L 302     1555   1555  2.60  
LINK         O   ASP L 186                 K     K L 302     1555   1555  2.64  
LINK         O   THR L 189                 K     K L 302     1555   1555  2.61  
LINK         O   ASP L 213                MG    MG L 303     1555   1555  2.20  
LINK         O   MET N 164                 K     K N 504     1555   1555  2.54  
LINK         O   ASP N 167                 K     K N 504     1555   1555  2.61  
LINK         O   SER N 170                 K     K N 504     1555   1555  2.54  
LINK         C   ILE Q  62                 N   YCM Q  63     1555   1555  1.34  
LINK         C   YCM Q  63                 N   ALA Q  64     1555   1555  1.34  
LINK         C   THR S 147                 N   6V1 S 148     1555   1555  1.33  
LINK         C   6V1 S 148                 N   PRO S 149     1555   1555  1.34  
LINK         OG1 THR U  14                 K     K U 302     1555   1555  2.76  
LINK         C   ASP U  46                 N   6V1 U  47     1555   1555  1.33  
LINK         C   6V1 U  47                 N   ALA U  48     1555   1555  1.33  
LINK         O   TYR U 125                 K     K U 302     1555   1555  2.54  
LINK         O   ASN U 128                 K     K U 302     1555   1555  2.56  
LINK         O   MET U 131                 K     K U 302     1555   1555  2.50  
LINK         C   CYS U 136                 N   YCM U 137     1555   1555  1.34  
LINK         C   YCM U 137                 N   MET U 138     1555   1555  1.32  
LINK         C   TYR U 160                 N   6V1 U 161     1555   1555  1.31  
LINK         C   6V1 U 161                 N   GLY U 162     1555   1555  1.34  
LINK         OE1 GLN V  91                MG    MG V 301     1555   1555  2.27  
LINK         O   ILE V 163                MG    MG L 303     1555   1555  2.19  
LINK         O   ASP V 166                MG    MG L 303     1555   1555  2.21  
LINK         O   SER V 169                MG    MG L 303     1555   1555  2.20  
LINK         O   VAL W 174                MG    MG W 301     1555   1555  2.20  
LINK         O   ASP W 177                MG    MG W 301     1555   1555  2.23  
LINK         O   SER W 180                MG    MG W 301     1555   1555  2.19  
LINK         O   ASP W 204                MG    MG K 301     1555   1555  2.18  
LINK         C   ASP X  90                 N   6V1 X  91     1555   1555  1.33  
LINK         C   6V1 X  91                 N   LEU X  92     1555   1555  1.33  
LINK         O   THR Y 164                MG    MG I 305     1555   1555  2.23  
LINK         O   ASP Y 167                MG    MG I 305     1555   1555  2.23  
LINK         O   SER Y 170                MG    MG I 305     1555   1555  2.22  
LINK         O   ALA Z 183                 K     K Z 302     1555   1555  2.62  
LINK         O   ASP Z 186                 K     K Z 302     1555   1555  2.62  
LINK         O   THR Z 189                 K     K Z 302     1555   1555  2.59  
LINK         O   ASP Z 213                MG    MG H 302     1555   1555  2.21  
LINK         O   MET b 164                 K     K b 506     1555   1555  2.53  
LINK         O   ASP b 167                 K     K b 506     1555   1555  2.58  
LINK         O   SER b 170                 K     K b 506     1555   1555  2.54  
LINK         K     K G 304                 O   HOH G 505     1555   1555  2.67  
LINK        MG    MG H 301                 O   HOH H 425     1555   1555  2.19  
LINK        MG    MG H 301                 O   HOH N 612     1555   1555  2.18  
LINK        MG    MG H 301                 O   HOH H 530     1555   1555  2.14  
LINK        MG    MG H 301                 O   HOH N 615     1555   1555  2.22  
LINK        MG    MG H 301                 O   HOH N 680     1555   1555  2.20  
LINK        MG    MG H 302                 O   HOH H 501     1555   1555  2.56  
LINK        MG    MG I 301                 O   HOH I 434     1555   1555  2.52  
LINK        MG    MG I 301                 O   HOH I 453     1555   1555  2.26  
LINK        MG    MG I 305                 O   HOH Y 500     1555   1555  2.52  
LINK        MG    MG J 301                 O   HOH J 409     1555   1555  2.17  
LINK        MG    MG J 301                 O   HOH J 454     1555   1555  2.18  
LINK        MG    MG J 301                 O   HOH J 508     1555   1555  2.16  
LINK        MG    MG J 301                 O   HOH J 522     1555   1555  2.16  
LINK        MG    MG J 301                 O   HOH K 496     1555   1555  2.16  
LINK        MG    MG J 301                 O   HOH J 432     1555   1555  2.16  
LINK        MG    MG K 301                 O   HOH K 471     1555   1555  2.66  
LINK         K     K L 302                 O   HOH L 449     1555   1555  3.20  
LINK         K     K L 302                 O   HOH L 466     1555   1555  2.62  
LINK         K     K L 302                 O   HOH V 442     1555   1555  3.25  
LINK        MG    MG L 303                 O   HOH V 473     1555   1555  2.56  
LINK         K     K N 504                 O   HOH N 748     1555   1555  2.53  
LINK         K     K N 504                 O   HOH N 712     1555   1555  2.45  
LINK         K     K N 504                 O   HOH N 703     1555   1555  3.47  
LINK         K     K U 302                 O   HOH U 456     1555   1555  2.68  
LINK        MG    MG V 301                 O   HOH V 427     1555   1555  2.19  
LINK        MG    MG V 301                 O   HOH V 497     1555   1555  2.15  
LINK        MG    MG V 301                 O   HOH b 606     1555   1555  2.16  
LINK        MG    MG V 301                 O   HOH b 618     1555   1555  2.20  
LINK        MG    MG V 301                 O   HOH b 647     1555   1555  2.21  
LINK        MG    MG W 301                 O   HOH W 443     1555   1555  2.48  
LINK        MG    MG W 301                 O   HOH W 472     1555   1555  1.90  
LINK        MG    MG X 301                 O   HOH X 402     1555   1555  2.19  
LINK        MG    MG X 301                 O   HOH X 433     1555   1555  2.16  
LINK        MG    MG X 301                 O   HOH X 519     1555   1555  2.16  
LINK        MG    MG X 301                 O   HOH Y 521     1555   1555  2.19  
LINK        MG    MG X 301                 O   HOH X 446     1555   1555  2.17  
LINK        MG    MG X 301                 O   HOH X 509     1555   1555  2.16  
LINK         K     K Z 302                 O   HOH Z1449     1555   1555  3.35  
LINK         K     K Z 302                 O   HOH Z1470     1555   1555  2.65  
LINK         K     K Z 302                 O   HOH Z1475     1555   1555  3.16  
LINK         K     K b 506                 O   HOH b 673     1555   1555  2.44  
LINK         K     K b 506                 O   HOH b 721     1555   1555  2.44  
CISPEP   1 GLY C  203    LYS C  204          0         6.85                     
CISPEP   2 ARG H  187    PRO H  188          0       -10.39                     
CISPEP   3 ARG H  187    PRO H  188          0       -10.39                     
CISPEP   4 GLY M  201    PRO M  202          0       -10.25                     
CISPEP   5 GLU S  234    GLY S  235          0         3.51                     
CISPEP   6 GLY S  235    LEU S  236          0       -19.11                     
CISPEP   7 ARG V  187    PRO V  188          0        -9.96                     
CISPEP   8 GLY a  201    PRO a  202          0        -5.03                     
SITE     1 AC1  3 SER A   6  HOH A 486  HOH C 420                               
SITE     1 AC2  1 ARG A 219                                                     
SITE     1 AC3  3 HIS A  87  ARG A  90  HOH H 493                               
SITE     1 AC4  1 HOH A 465                                                     
SITE     1 AC5  5 GLU B  70  GLN B  95   CL B 302  HOH B 494                    
SITE     2 AC5  5 HOH I 539                                                     
SITE     1 AC6  3 PRO B 104   CL B 301  HOH B 465                               
SITE     1 AC7  1 GLY C 162                                                     
SITE     1 AC8  3 ARG C  86  ARG C 117  HOH C 432                               
SITE     1 AC9  3 ILE D 170  GLY D 171  SER D 174                               
SITE     1 AD1  4 THR D 161  HOH D 432  LEU E  77  THR E  78                    
SITE     1 AD2  5 6V1 E 148  ILE E 161  GLY E 162  SER E 165                    
SITE     2 AD2  5 HOH E 513                                                     
SITE     1 AD3  1 SER E 150                                                     
SITE     1 AD4  4 GLY E  32  SER E  33  LYS E  62  GLY E  76                    
SITE     1 AD5  4 ILE F 165  GLY F 166  ARG F 169  HOH F 425                    
SITE     1 AD6  3 HOH G 470  HOH G 497  HOH N 669                               
SITE     1 AD7  4 LYS G 186  GLU G 192  GLN G 193  THR G 197                    
SITE     1 AD8  6 TYR G 103  HOH G 419  HOH G 457  HOH G 524                    
SITE     2 AD8  6 PHE H  88  TYR N  90                                          
SITE     1 AD9  5 THR G  14  TYR G 125  ASN G 128  MET G 131                    
SITE     2 AD9  5 HOH G 505                                                     
SITE     1 AE1  7 GLN H  91  HOH H 425  HOH H 530  ASP N  51                    
SITE     2 AE1  7 HOH N 612  HOH N 615  HOH N 680                               
SITE     1 AE2  5 ILE H 163  ASP H 166  SER H 169  HOH H 501                    
SITE     2 AE2  5 ASP Z 213                                                     
SITE     1 AE3  4 THR H   1  GLY H 128  SER H 129  HOH H 403                    
SITE     1 AE4  4 ASN H  80  ARG H  81  HOH H 533  HOH N 634                    
SITE     1 AE5  5 VAL I 174  ASP I 177  SER I 180  HOH I 434                    
SITE     2 AE5  5 HOH I 453                                                     
SITE     1 AE6  2 ARG I  65  ARG I  69                                          
SITE     1 AE7  4 GLU I  96  LYS I  97  1PE I 304  ASP J  90                    
SITE     1 AE8  5 LEU H  58  TYR H  90  TYR I  95  GLU I  96                    
SITE     2 AE8  5 1PE I 303                                                     
SITE     1 AE9  5 ASP I 204  THR Y 164  ASP Y 167  SER Y 170                    
SITE     2 AE9  5 HOH Y 500                                                     
SITE     1 AF1  6 HOH J 409  HOH J 432  HOH J 454  HOH J 508                    
SITE     2 AF1  6 HOH J 522  HOH K 496                                          
SITE     1 AF2  5 THR K 164  ASP K 167  SER K 170  HOH K 471                    
SITE     2 AF2  5 ASP W 204                                                     
SITE     1 AF3  4 THR K   1  GLY K  47  GLY K 129  SER K 130                    
SITE     1 AF4  2 LYS K  32  ASN K 175                                          
SITE     1 AF5  3 TYR K  66  ARG K  69  HOH K 477                               
SITE     1 AF6  1 SER K 122                                                     
SITE     1 AF7  3 PHE K  54  PHE L 101  HOH L 473                               
SITE     1 AF8  4 ALA L 183  ASP L 186  THR L 189  HOH L 466                    
SITE     1 AF9  5 ASP L 213  ILE V 163  ASP V 166  SER V 169                    
SITE     2 AF9  5 HOH V 473                                                     
SITE     1 AG1  4 PHE M  36  ARG M  37  ASN M  38  HOH N 720                    
SITE     1 AG2  5 ARG M  35   CL M 303  SER N  46  GLY N 128                    
SITE     2 AG2  5 GLY N 129                                                     
SITE     1 AG3  5 TYR M  30  ARG M  35   CL M 302  PRO N 115                    
SITE     2 AG3  5 MET N 116                                                     
SITE     1 AG4  1 ARG M  44                                                     
SITE     1 AG5  4 HOH H 429  THR N  31  ARG N  45  GLN N  53                    
SITE     1 AG6  2 THR N   1  SER N 130                                          
SITE     1 AG7  5 ARG N  19  ARG N  29  GLY N 171  GLY N 172                    
SITE     2 AG7  5 HOH a 453                                                     
SITE     1 AG8  6 ARG N  19  MET N 164  ASP N 167  SER N 170                    
SITE     2 AG8  6 HOH N 712  HOH N 748                                          
SITE     1 AG9  3 SER O   6  PHE O   7  HOH Q 428                               
SITE     1 AH1  3 TYR O 100  MET W  89  HOH W 453                               
SITE     1 AH2  1 ARG O 219                                                     
SITE     1 AH3  2 ARG O  90  LYS U 116                                          
SITE     1 AH4  3 GLU P  70  GLN P  95  HOH P 506                               
SITE     1 AH5  1 ARG Q  95                                                     
SITE     1 AH6  2 ILE Q 161  GLY Q 162                                          
SITE     1 AH7  6 ILE R  31  ILE R 170  GLY R 171  SER R 174                    
SITE     2 AH7  6 HOH R 474  HOH R 515                                          
SITE     1 AH8  3 THR R 161  HOH R 449  THR S  78                               
SITE     1 AH9  4 6V1 S 148  GLY S 162  SER S 165  HOH S 501                    
SITE     1 AI1  1 SER S 150                                                     
SITE     1 AI2  4 GLY S  32  SER S  33  LYS S  62  GLY S  76                    
SITE     1 AI3  4 LYS U 102  HOH U 429  HOH U 432  HOH b 649                    
SITE     1 AI4  5 THR U  14  TYR U 125  ASN U 128  MET U 131                    
SITE     2 AI4  5 HOH U 456                                                     
SITE     1 AI5  7 GLN V  91  HOH V 427  HOH V 497  ASP b  51                    
SITE     2 AI5  7 HOH b 606  HOH b 618  HOH b 647                               
SITE     1 AI6  4 THR V   1  GLY V 128  SER V 129  HOH V 402                    
SITE     1 AI7  3 ASN V  80  ARG V  81  HOH b 613                               
SITE     1 AI8  5 VAL W 174  ASP W 177  SER W 180  HOH W 443                    
SITE     2 AI8  5 HOH W 472                                                     
SITE     1 AI9  2 ARG W  65  ARG W  69                                          
SITE     1 AJ1  4 GLU W  96  LYS W  97  HOH W 450  HOH W 492                    
SITE     1 AJ2  6 HOH X 402  HOH X 433  HOH X 446  HOH X 509                    
SITE     2 AJ2  6 HOH X 519  HOH Y 521                                          
SITE     1 AJ3  4 THR Y   1  GLY Y  47  GLY Y 129  SER Y 130                    
SITE     1 AJ4  4 GLN Y  62  TYR Y  66  ARG Y  69  HOH Y 486                    
SITE     1 AJ5  2 LYS Y  32  ASN Y 175                                          
SITE     1 AJ6  2 ILE Y 121  SER Y 122                                          
SITE     1 AJ7  2 HOH J 435  LEU Y 155                                          
SITE     1 AJ8  4 TYR Z  97  SER Z  98  PHE Z 101  HOH Z1469                    
SITE     1 AJ9  4 ALA Z 183  ASP Z 186  THR Z 189  HOH Z1470                    
SITE     1 AK1  4 PHE a  36  ARG a  37  ASN a  38  HOH b 718                    
SITE     1 AK2  5 TYR a  30  ARG a  35  PRO b 115  MET b 116                    
SITE     2 AK2  5  CL b 502                                                     
SITE     1 AK3  2 MET a  43  ARG a  44                                          
SITE     1 AK4  6 SER H 129  THR N  22  TYR a 141  TYR a 144                    
SITE     2 AK4  6 HOH a 484  HOH a 497                                          
SITE     1 AK5  2 THR b   1  SER b 130                                          
SITE     1 AK6  5 ARG a  35   CL a 302  SER b  46  GLY b 128                    
SITE     2 AK6  5 GLY b 129                                                     
SITE     1 AK7  5 HOH M 465  ARG b  19  ARG b  29  GLY b 171                    
SITE     2 AK7  5 GLY b 172                                                     
SITE     1 AK8  4 TYR U 103  PHE V  88  ARG V  89  HOH b 722                    
SITE     1 AK9  1 THR b  22                                                     
SITE     1 AL1  5 MET b 164  ASP b 167  SER b 170  HOH b 673                    
SITE     2 AL1  5 HOH b 721                                                     
CRYST1  113.440  202.770  316.000  90.00  90.00  90.00 P 21 21 21    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      0.008815  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004932  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003165        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system