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Entry: 5LEY
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HEADER    HYDROLASE                               30-JUN-16   5LEY              
TITLE     HUMAN 20S PROTEASOME COMPLEX WITH OPROZOMIB AT 1.9 ANGSTROM           
CAVEAT     5LEY    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;                                                        
COMPND  88 MOL_ID: 15;                                                          
COMPND  89 MOLECULE: BOUND OPROZOMIB;                                           
COMPND  90 CHAIN: c, d;                                                         
COMPND  91 ENGINEERED: YES                                                      
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;                                                     
SOURCE  71 MOL_ID: 15;                                                          
SOURCE  72 SYNTHETIC: YES;                                                      
SOURCE  73 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  74 ORGANISM_TAXID: 32630                                                
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 5LEY    1       REMARK                                   
REVDAT   1   17-AUG-16 5LEY    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.    1.90 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 : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 170.45                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 526170                         
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 27607                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 34608                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1810                         
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 47908                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 218                                     
REMARK   3   SOLVENT ATOMS            : 3542                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.68000                                             
REMARK   3    B22 (A**2) : 0.87000                                              
REMARK   3    B33 (A**2) : 0.81000                                              
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): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.123        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 49333 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 46869 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 66743 ; 1.971 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):107579 ; 1.410 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6302 ; 7.411 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2126 ;35.203 ;23.711       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8266 ;15.716 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   340 ;18.260 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7538 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 56163 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11209 ; 0.006 ; 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): 25035 ; 1.169 ; 1.876       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25034 ; 1.169 ; 1.876       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31276 ; 1.878 ; 2.807       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31277 ; 1.878 ; 2.807       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 24298 ; 1.903 ; 2.105       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 24298 ; 1.903 ; 2.105       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 35428 ; 2.718 ; 3.064       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 57370 ; 8.391 ;16.741       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 57371 ; 8.391 ;16.742       
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   26024  0.08  0.05     
REMARK   3    2     B     2    249       P     2    249   27818  0.08  0.05     
REMARK   3    3     C     2    237       Q     2    237   25270  0.10  0.05     
REMARK   3    4     D     9    241       R     9    241   26366  0.08  0.05     
REMARK   3    5     E     4    236       S     4    236   27350  0.08  0.05     
REMARK   3    6     F     6    243       T     6    243   28132  0.08  0.05     
REMARK   3    7     G     2    245       U     2    245   26548  0.09  0.05     
REMARK   3    8     H     1    220       V     1    220   24702  0.06  0.05     
REMARK   3    9     I     1    204       W     1    204   25840  0.07  0.05     
REMARK   3   10     J     1    196       X     1    196   24682  0.08  0.05     
REMARK   3   11     K     1    199       Y     1    199   23230  0.08  0.05     
REMARK   3   12     L     1    213       Z     1    213   24746  0.06  0.05     
REMARK   3   13     M     1    216       a     1    216   24976  0.08  0.05     
REMARK   3   14     N     1    201       b     1    201   23110  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):  76.8050 206.1533   1.2023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3582 T22:   0.2863                                     
REMARK   3      T33:   0.1810 T12:   0.1053                                     
REMARK   3      T13:   0.0756 T23:   0.0670                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4729 L22:   1.6927                                     
REMARK   3      L33:   1.6007 L12:   0.3745                                     
REMARK   3      L13:   0.5248 L23:   0.0985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0299 S12:   0.1125 S13:   0.0722                       
REMARK   3      S21:  -0.1248 S22:  -0.0600 S23:  -0.3977                       
REMARK   3      S31:   0.0447 S32:   0.5828 S33:   0.0899                       
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):  64.7246 177.3262   0.2220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6248 T22:   0.1504                                     
REMARK   3      T33:   0.1842 T12:   0.1435                                     
REMARK   3      T13:   0.0650 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7833 L22:   1.7055                                     
REMARK   3      L33:   1.2696 L12:  -0.0921                                     
REMARK   3      L13:   0.0557 L23:  -0.4099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0606 S12:   0.1720 S13:  -0.1550                       
REMARK   3      S21:  -0.2050 S22:  -0.0328 S23:  -0.3086                       
REMARK   3      S31:   0.3221 S32:   0.3610 S33:   0.0933                       
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):  33.8669 169.4919  -3.7365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6987 T22:   0.1431                                     
REMARK   3      T33:   0.2757 T12:  -0.0738                                     
REMARK   3      T13:  -0.0497 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9578 L22:   2.3781                                     
REMARK   3      L33:   1.3461 L12:   0.3357                                     
REMARK   3      L13:   0.3268 L23:  -0.2415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0094 S12:   0.0133 S13:  -0.5609                       
REMARK   3      S21:  -0.1467 S22:   0.0595 S23:  -0.0977                       
REMARK   3      S31:   0.4648 S32:  -0.0007 S33:  -0.0690                       
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):  10.1767 188.2909  -7.7351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5702 T22:   0.3584                                     
REMARK   3      T33:   0.2511 T12:  -0.1298                                     
REMARK   3      T13:  -0.1428 T23:   0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6844 L22:   1.3861                                     
REMARK   3      L33:   1.9391 L12:  -0.2176                                     
REMARK   3      L13:  -0.9687 L23:  -0.0740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0077 S12:   0.1567 S13:  -0.2232                       
REMARK   3      S21:  -0.1576 S22:   0.0006 S23:   0.2139                       
REMARK   3      S31:   0.3164 S32:  -0.4506 S33:   0.0071                       
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:   0.3702 T22:   0.2439                                     
REMARK   3      T33:   0.1576 T12:  -0.0483                                     
REMARK   3      T13:  -0.0564 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9594 L22:   0.8103                                     
REMARK   3      L33:   1.4549 L12:  -0.3935                                     
REMARK   3      L13:   0.0119 L23:  -0.0342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0425 S12:   0.1650 S13:  -0.2582                       
REMARK   3      S21:  -0.0684 S22:  -0.0105 S23:   0.2215                       
REMARK   3      S31:   0.1402 S32:  -0.5036 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:   0.3089 T22:   0.0612                                     
REMARK   3      T33:   0.1473 T12:  -0.0004                                     
REMARK   3      T13:  -0.0229 T23:   0.0540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4270 L22:   1.6511                                     
REMARK   3      L33:   0.9880 L12:  -0.6338                                     
REMARK   3      L13:  -0.0215 L23:   0.0148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0172 S12:   0.1154 S13:   0.2168                       
REMARK   3      S21:  -0.1205 S22:  -0.0405 S23:   0.1232                       
REMARK   3      S31:  -0.1218 S32:  -0.1037 S33:   0.0233                       
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:   0.3107 T22:   0.1722                                     
REMARK   3      T33:   0.1769 T12:  -0.0046                                     
REMARK   3      T13:   0.0489 T23:   0.1044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8809 L22:   2.1982                                     
REMARK   3      L33:   1.2345 L12:   0.2625                                     
REMARK   3      L13:   0.2619 L23:   0.5235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:   0.2109 S13:   0.2280                       
REMARK   3      S21:  -0.2471 S22:  -0.0547 S23:  -0.2104                       
REMARK   3      S31:  -0.2004 S32:   0.3269 S33:   0.0388                       
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:   0.2806 T22:   0.2733                                     
REMARK   3      T33:   0.1190 T12:  -0.0230                                     
REMARK   3      T13:   0.0354 T23:   0.0684                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2417 L22:   1.3995                                     
REMARK   3      L33:   0.8303 L12:  -0.0079                                     
REMARK   3      L13:  -0.0912 L23:  -0.2404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0040 S12:  -0.0381 S13:  -0.1009                       
REMARK   3      S21:   0.0690 S22:  -0.1044 S23:  -0.1268                       
REMARK   3      S31:   0.0023 S32:   0.4120 S33:   0.1004                       
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:   0.3756 T22:   0.2125                                     
REMARK   3      T33:   0.1028 T12:   0.1153                                     
REMARK   3      T13:   0.0547 T23:   0.0681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2625 L22:   1.0180                                     
REMARK   3      L33:   1.8567 L12:   0.2936                                     
REMARK   3      L13:   0.3642 L23:  -0.5267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0136 S12:   0.0536 S13:  -0.0237                       
REMARK   3      S21:  -0.0782 S22:  -0.1607 S23:  -0.1259                       
REMARK   3      S31:   0.1319 S32:   0.4812 S33:   0.1471                       
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:   0.5293 T22:   0.0171                                     
REMARK   3      T33:   0.1326 T12:   0.0058                                     
REMARK   3      T13:  -0.0078 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9303 L22:   0.7691                                     
REMARK   3      L33:   2.5656 L12:   0.4474                                     
REMARK   3      L13:  -0.0976 L23:  -0.2804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0623 S12:   0.0859 S13:  -0.0912                       
REMARK   3      S21:  -0.1697 S22:   0.0231 S23:   0.1310                       
REMARK   3      S31:   0.4770 S32:  -0.0919 S33:   0.0392                       
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   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0340 180.7830  32.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4047 T22:   0.2650                                     
REMARK   3      T33:   0.1893 T12:  -0.1843                                     
REMARK   3      T13:  -0.1036 T23:   0.1148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8001 L22:   1.6662                                     
REMARK   3      L33:   2.0050 L12:  -0.2217                                     
REMARK   3      L13:  -0.4669 L23:   0.2791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0068 S12:   0.1427 S13:  -0.1071                       
REMARK   3      S21:  -0.1642 S22:   0.0475 S23:   0.1370                       
REMARK   3      S31:   0.3613 S32:  -0.4295 S33:  -0.0406                       
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:   0.3222 T22:   0.4492                                     
REMARK   3      T33:   0.2120 T12:  -0.0363                                     
REMARK   3      T13:  -0.0377 T23:   0.1712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8784 L22:   1.2254                                     
REMARK   3      L33:   0.8316 L12:   0.2211                                     
REMARK   3      L13:  -0.3756 L23:   0.2815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:  -0.0165 S13:   0.0537                       
REMARK   3      S21:  -0.0703 S22:   0.0531 S23:   0.3184                       
REMARK   3      S31:  -0.0470 S32:  -0.4664 S33:  -0.0833                       
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:   0.3551 T22:   0.1685                                     
REMARK   3      T33:   0.1514 T12:   0.0953                                     
REMARK   3      T13:   0.0508 T23:   0.0899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8633 L22:   0.9676                                     
REMARK   3      L33:   1.7782 L12:   0.2530                                     
REMARK   3      L13:   0.0281 L23:   0.3263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.0137 S13:   0.1494                       
REMARK   3      S21:   0.0698 S22:   0.0936 S23:   0.1566                       
REMARK   3      S31:  -0.3440 S32:  -0.3426 S33:  -0.0768                       
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:   0.4039 T22:   0.0311                                     
REMARK   3      T33:   0.0851 T12:  -0.0706                                     
REMARK   3      T13:   0.0220 T23:   0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4891 L22:   0.8924                                     
REMARK   3      L33:   1.8418 L12:  -0.2021                                     
REMARK   3      L13:   0.1346 L23:  -0.0379                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0385 S12:   0.0176 S13:   0.0887                       
REMARK   3      S21:   0.0533 S22:  -0.0637 S23:  -0.0090                       
REMARK   3      S31:  -0.3931 S32:   0.1334 S33:   0.0252                       
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:   0.5228 T22:   0.5329                                     
REMARK   3      T33:   0.3576 T12:   0.2067                                     
REMARK   3      T13:   0.1662 T23:   0.0966                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1399 L22:   1.5208                                     
REMARK   3      L33:   1.8262 L12:  -0.0578                                     
REMARK   3      L13:   0.3980 L23:  -0.1624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:  -0.0871 S13:   0.2723                       
REMARK   3      S21:   0.1194 S22:   0.0010 S23:   0.4529                       
REMARK   3      S31:  -0.3698 S32:  -0.5356 S33:   0.0097                       
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):  -8.2590 194.9569 104.7498              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4070 T22:   0.5737                                     
REMARK   3      T33:   0.3329 T12:   0.0176                                     
REMARK   3      T13:   0.1152 T23:   0.1894                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9304 L22:   1.2494                                     
REMARK   3      L33:   1.2513 L12:   0.3284                                     
REMARK   3      L13:   0.0663 L23:   0.4697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0100 S12:  -0.2000 S13:   0.0335                       
REMARK   3      S21:   0.1724 S22:   0.0173 S23:   0.4017                       
REMARK   3      S31:  -0.0481 S32:  -0.5947 S33:  -0.0073                       
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):  15.2946 174.5992 109.5339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5267 T22:   0.3333                                     
REMARK   3      T33:   0.3798 T12:  -0.0429                                     
REMARK   3      T13:   0.0098 T23:   0.1162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6118 L22:   2.0467                                     
REMARK   3      L33:   1.8486 L12:   0.3964                                     
REMARK   3      L13:   0.1115 L23:   0.4236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0611 S12:  -0.0365 S13:  -0.6461                       
REMARK   3      S21:   0.1658 S22:   0.0143 S23:   0.3212                       
REMARK   3      S31:   0.4851 S32:  -0.3978 S33:  -0.0754                       
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):  45.4553 181.2062 112.8154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3835 T22:   0.2373                                     
REMARK   3      T33:   0.1734 T12:   0.0060                                     
REMARK   3      T13:   0.0279 T23:   0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7047 L22:   1.0151                                     
REMARK   3      L33:   2.0740 L12:   0.0760                                     
REMARK   3      L13:  -0.3254 L23:   0.0455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0687 S12:  -0.1537 S13:  -0.1942                       
REMARK   3      S21:   0.0195 S22:   0.0634 S23:   0.1367                       
REMARK   3      S31:   0.2189 S32:   0.0782 S33:   0.0053                       
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     4        S   239                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6999 209.5201 113.8657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4724 T22:   0.3308                                     
REMARK   3      T33:   0.1255 T12:  -0.1028                                     
REMARK   3      T13:  -0.0109 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6418 L22:   1.1925                                     
REMARK   3      L33:   1.5901 L12:  -0.4473                                     
REMARK   3      L13:   0.0210 L23:  -0.1785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:  -0.2820 S13:  -0.1268                       
REMARK   3      S21:   0.2317 S22:  -0.0018 S23:  -0.1569                       
REMARK   3      S31:  -0.0818 S32:   0.5307 S33:   0.0687                       
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):  47.2556 237.3736 111.5819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7289 T22:   0.1706                                     
REMARK   3      T33:   0.1611 T12:  -0.0941                                     
REMARK   3      T13:   0.0445 T23:  -0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9770 L22:   1.4332                                     
REMARK   3      L33:   1.2757 L12:   0.6230                                     
REMARK   3      L13:  -0.4424 L23:   0.0086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1205 S12:  -0.3184 S13:   0.1350                       
REMARK   3      S21:   0.1726 S22:  -0.0512 S23:  -0.2145                       
REMARK   3      S31:  -0.4712 S32:   0.2865 S33:  -0.0694                       
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):  16.7669 244.7515 107.2847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7768 T22:   0.2720                                     
REMARK   3      T33:   0.2725 T12:   0.1752                                     
REMARK   3      T13:   0.1256 T23:  -0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5034 L22:   1.3339                                     
REMARK   3      L33:   1.0230 L12:   0.1739                                     
REMARK   3      L13:  -0.0808 L23:  -0.2709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0012 S12:  -0.2128 S13:   0.4451                       
REMARK   3      S21:   0.2104 S22:  -0.0071 S23:   0.1054                       
REMARK   3      S31:  -0.5056 S32:  -0.1496 S33:   0.0060                       
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):   1.6045 230.5558  65.1743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4341 T22:   0.3799                                     
REMARK   3      T33:   0.2257 T12:   0.1646                                     
REMARK   3      T13:   0.1302 T23:   0.1198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6625 L22:   1.3899                                     
REMARK   3      L33:   0.7115 L12:   0.4839                                     
REMARK   3      L13:   0.0407 L23:   0.0155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:  -0.0372 S13:  -0.0318                       
REMARK   3      S21:   0.0573 S22:   0.0970 S23:   0.2178                       
REMARK   3      S31:  -0.1838 S32:  -0.4730 S33:  -0.0913                       
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):  -6.0266 203.1585  65.1628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3108 T22:   0.5359                                     
REMARK   3      T33:   0.2556 T12:   0.0063                                     
REMARK   3      T13:   0.0597 T23:   0.2144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2154 L22:   0.9865                                     
REMARK   3      L33:   1.5488 L12:   0.0687                                     
REMARK   3      L13:   0.4411 L23:   0.5598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.0598 S13:   0.0472                       
REMARK   3      S21:   0.0121 S22:   0.0590 S23:   0.1807                       
REMARK   3      S31:  -0.1090 S32:  -0.5578 S33:  -0.0611                       
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):  11.3957 176.6133  68.5995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3771 T22:   0.1948                                     
REMARK   3      T33:   0.2069 T12:  -0.1251                                     
REMARK   3      T13:  -0.0180 T23:   0.1092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7302 L22:   0.8943                                     
REMARK   3      L33:   1.7085 L12:  -0.1386                                     
REMARK   3      L13:  -0.1639 L23:   0.1687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:  -0.0823 S13:  -0.0947                       
REMARK   3      S21:   0.0434 S22:   0.1010 S23:   0.0018                       
REMARK   3      S31:   0.3282 S32:  -0.2100 S33:  -0.0602                       
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):  43.7927 172.7839  72.8647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3812 T22:   0.0647                                     
REMARK   3      T33:   0.0844 T12:   0.0354                                     
REMARK   3      T13:  -0.0008 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4578 L22:   1.2740                                     
REMARK   3      L33:   2.1707 L12:   0.5304                                     
REMARK   3      L13:  -0.5637 L23:  -0.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0293 S12:  -0.2174 S13:  -0.0920                       
REMARK   3      S21:   0.0513 S22:  -0.0492 S23:   0.0088                       
REMARK   3      S31:   0.3880 S32:   0.1170 S33:   0.0784                       
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):  65.5340 195.3737  73.9322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2785 T22:   0.2424                                     
REMARK   3      T33:   0.1010 T12:  -0.0016                                     
REMARK   3      T13:   0.0100 T23:   0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8637 L22:   1.1401                                     
REMARK   3      L33:   1.3329 L12:   0.0520                                     
REMARK   3      L13:  -0.4565 L23:  -0.0012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0397 S12:  -0.0889 S13:   0.0074                       
REMARK   3      S21:   0.0649 S22:  -0.1258 S23:  -0.1754                       
REMARK   3      S31:   0.0452 S32:   0.4441 S33:   0.0860                       
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):  60.7492 227.9909  70.9280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4117 T22:   0.1623                                     
REMARK   3      T33:   0.0862 T12:  -0.1180                                     
REMARK   3      T13:   0.0030 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8235 L22:   1.1380                                     
REMARK   3      L33:   1.7435 L12:  -0.0620                                     
REMARK   3      L13:  -0.1998 L23:  -0.4767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0075 S12:  -0.0493 S13:   0.0638                       
REMARK   3      S21:   0.1377 S22:  -0.0775 S23:  -0.0931                       
REMARK   3      S31:  -0.3375 S32:   0.3704 S33:   0.0700                       
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):  33.2357 245.3581  67.9817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5763 T22:   0.0362                                     
REMARK   3      T33:   0.1082 T12:   0.0431                                     
REMARK   3      T13:   0.0644 T23:  -0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5893 L22:   1.0195                                     
REMARK   3      L33:   1.8171 L12:  -0.0414                                     
REMARK   3      L13:  -0.0237 L23:  -0.2250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0033 S12:  -0.0647 S13:   0.0975                       
REMARK   3      S21:   0.1616 S22:   0.0159 S23:   0.0530                       
REMARK   3      S31:  -0.4853 S32:  -0.0443 S33:  -0.0126                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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 5LEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000582.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-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          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 526170                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 170.450                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 5.040                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.830                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 5LE5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
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       56.69500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      157.57000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.32500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      157.57000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.69500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.32500            
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: 30-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 127970 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 207840 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1148.0 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, c,         
REMARK 350                    AND CHAINS: d                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLY K   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     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     PHE S     2                                                      
REMARK 465     ARG S     3                                                      
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     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     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     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     ARG A  59    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 140    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  15    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     GLU B 181    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 183    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 199    CG   CD   CE   NZ                                   
REMARK 470     ASP B 202    CG   OD1  OD2                                       
REMARK 470     VAL B 203    CG1  CG2                                            
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 470     GLU B 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  47    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     LYS C  52    CG   CD   CE   NZ                                   
REMARK 470     PHE C 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 166    CG   CD   CE   NZ                                   
REMARK 470     GLU C 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 174    CG   CD   CE   NZ                                   
REMARK 470     LYS C 189    CG   CD   CE   NZ                                   
REMARK 470     LYS C 193    CG   CD   CE   NZ                                   
REMARK 470     LEU C 196    CG   CD1  CD2                                       
REMARK 470     VAL C 199    CG1  CG2                                            
REMARK 470     GLN C 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 204    CG   CD   CE   NZ                                   
REMARK 470     ILE C 206    CG1  CG2  CD1                                       
REMARK 470     GLU C 207    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 215    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 218    CG   CD   CE   NZ                                   
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     ASP D 129    CG   OD1  OD2                                       
REMARK 470     LYS D 149    CG   CD   CE   NZ                                   
REMARK 470     SER D 172    OG                                                  
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     LYS D 192    CG   CD   CE   NZ                                   
REMARK 470     LYS D 196    CG   CD   CE   NZ                                   
REMARK 470     LYS D 209    CG   CD   CE   NZ                                   
REMARK 470     LYS E  41    CG   CD   CE   NZ                                   
REMARK 470     ARG E  51    CG   CD   NE   CZ   NH1  NH2                        
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     HIS E  59    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E 208    CG   CD   CE   NZ                                   
REMARK 470     GLU E 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 205    CG   CD   CE   NZ                                   
REMARK 470     LYS G  45    CG   CD   CE   NZ                                   
REMARK 470     GLU G 145    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 146    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 181    CG   CD   CE   NZ                                   
REMARK 470     GLU G 196    CG   CD   OE1  OE2                                  
REMARK 470     LYS H   9    CG   CD   CE   NZ                                   
REMARK 470     LYS H 180    CG   CD   CE   NZ                                   
REMARK 470     ASN J  24    CG   OD1  ND2                                       
REMARK 470     GLU J 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 154    CG   CD   OE1  OE2                                  
REMARK 470     ARG K   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 106    CG   CD   CE   NZ                                   
REMARK 470     ARG L   1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 162    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 173    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 200    CG   CD   CE   NZ                                   
REMARK 470     ARG O   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O  17    CG   CD   CE   NZ                                   
REMARK 470     LYS O  50    CG   CD   CE   NZ                                   
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 164    CG   CD   CE   NZ                                   
REMARK 470     GLU O 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS O 175    CG   CD   CE   NZ                                   
REMARK 470     TYR O 177    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU O 179    CG   CD   OE1  OE2                                  
REMARK 470     HIS O 188    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU P  15    CG   CD   OE1  OE2                                  
REMARK 470     ASN P  51    CG   OD1  ND2                                       
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     ARG P 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS P 229    CG   CD   CE   NZ                                   
REMARK 470     LYS P 231    CG   CD   CE   NZ                                   
REMARK 470     GLU P 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 238    CG   CD   CE   NZ                                   
REMARK 470     LYS P 239    CG   CD   CE   NZ                                   
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     VAL Q  50    CG1  CG2                                            
REMARK 470     LYS Q  52    CG   CD   CE   NZ                                   
REMARK 470     LYS Q  61    CG   CD   CE   NZ                                   
REMARK 470     PHE Q 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS Q 166    CG   CD   CE   NZ                                   
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     GLN Q 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS Q 204    CG   CD   CE   NZ                                   
REMARK 470     GLU Q 207    CG   CD   OE1  OE2                                  
REMARK 470     GLN Q 215    CG   CD   OE1  NE2                                  
REMARK 470     LYS Q 218    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 241    CG   CD   CE   NZ                                   
REMARK 470     GLU R 126    CG   CD   OE1  OE2                                  
REMARK 470     ASP R 127    CG   OD1  OD2                                       
REMARK 470     ASP R 129    CG   OD1  OD2                                       
REMARK 470     LYS R 149    CG   CD   CE   NZ                                   
REMARK 470     GLU R 175    CG   CD   OE1  OE2                                  
REMARK 470     GLU R 207    CG   CD   OE1  OE2                                  
REMARK 470     GLU R 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS R 231    CG   CD   CE   NZ                                   
REMARK 470     LYS S  41    CG   CD   CE   NZ                                   
REMARK 470     GLN S  53    CG   CD   OE1  NE2                                  
REMARK 470     LYS S 189    CG   CD   CE   NZ                                   
REMARK 470     LYS S 217    CG   CD   CE   NZ                                   
REMARK 470     ASP S 218    CG   OD1  OD2                                       
REMARK 470     LEU S 236    CG   CD1  CD2                                       
REMARK 470     GLU S 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU S 238    CG   CD   OE1  OE2                                  
REMARK 470     ARG S 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR T   5    OG1  CG2                                            
REMARK 470     LYS T  42    CG   CD   CE   NZ                                   
REMARK 470     LYS T  56    CG   CD   CE   NZ                                   
REMARK 470     GLU T  60    CG   CD   OE1  OE2                                  
REMARK 470     ARG T 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU T 234    CG   CD   OE1  OE2                                  
REMARK 470     LYS T 244    CG   CD   CE   NZ                                   
REMARK 470     ARG U   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS U  55    CG   CD   CE   NZ                                   
REMARK 470     LYS U  59    CG   CD   CE   NZ                                   
REMARK 470     GLU U 145    CG   CD   OE1  OE2                                  
REMARK 470     GLU U 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN U 147    CG   CD   OE1  NE2                                  
REMARK 470     VAL U 170    CG1  CG2                                            
REMARK 470     LYS U 171    CG   CD   CE   NZ                                   
REMARK 470     LYS U 181    CG   CD   CE   NZ                                   
REMARK 470     LYS U 184    CG   CD   CE   NZ                                   
REMARK 470     LYS U 186    CG   CD   CE   NZ                                   
REMARK 470     GLN U 193    CG   CD   OE1  NE2                                  
REMARK 470     ASP U 209    CG   OD1  OD2                                       
REMARK 470     LYS U 226    CG   CD   CE   NZ                                   
REMARK 470     LYS V 180    CG   CD   CE   NZ                                   
REMARK 470     LYS V 182    CG   CD   CE   NZ                                   
REMARK 470     LYS V 194    CG   CD   CE   NZ                                   
REMARK 470     LYS V 195    CG   CD   CE   NZ                                   
REMARK 470     ARG V 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG V 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG V 203    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS V 204    SG                                                  
REMARK 470     GLU V 205    CG   CD   OE1  OE2                                  
REMARK 470     LYS V 206    CG   CD   CE   NZ                                   
REMARK 470     GLU V 220    CG   CD   OE1  OE2                                  
REMARK 470     HIS W 161    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS W 191    CG   CD   CE   NZ                                   
REMARK 470     GLU X 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU X 111    CG   CD   OE1  OE2                                  
REMARK 470     ARG X 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG Z   1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN Z 160    CG   OD1  ND2                                       
REMARK 470     VAL Z 161    CG1  CG2                                            
REMARK 470     GLU Z 162    CG   CD   OE1  OE2                                  
REMARK 470     LYS a 156    CG   CD   CE   NZ                                   
REMARK 470     GLU a 206    CG   CD   OE1  OE2                                  
REMARK 470     VAL b 199    CG1  CG2                                            
REMARK 470     OAS c   2    C2A  OAC                                            
REMARK 470     OAS c   3    C2A  OAC                                            
REMARK 470     OAS d   2    C2A  OAC                                            
REMARK 470     OAS d   3    C2A  OAC                                            
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    HOH X   515     O    HOH Y   531              1.87            
REMARK 500   O    HOH E   458     O    HOH E   527              1.90            
REMARK 500   O    HOH b   480     O    HOH b   520              2.02            
REMARK 500   O    HOH I   488     O    HOH I   500              2.03            
REMARK 500   O    HOH L   436     O    HOH L   468              2.05            
REMARK 500   OG1  THR D    96     O    HOH D   401              2.06            
REMARK 500   NH1  ARG F   169     O    HOH F   401              2.07            
REMARK 500   O    HOH A   464     O    HOH I   529              2.10            
REMARK 500   O    HOH J   523     O    HOH J   532              2.10            
REMARK 500   O    HOH X   511     O    HOH X   515              2.11            
REMARK 500   O    HOH L   493     O    HOH L   515              2.12            
REMARK 500   NZ   LYS J   185     O    HOH J   401              2.15            
REMARK 500   OE1  GLU M   170     O    HOH M   401              2.15            
REMARK 500   O    HOH G   488     O    HOH G   545              2.16            
REMARK 500   OD1  ASN P   155     OG1  THR Q    77              2.17            
REMARK 500   O    HOH N   422     O    HOH N   448              2.17            
REMARK 500   O    HOH X   521     O    HOH X   522              2.19            
REMARK 500   O    HOH a   551     O    HOH a   562              2.19            
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    GLU B  70   CD    GLU B  70   OE1     0.070                       
REMARK 500    GLU B 103   CD    GLU B 103   OE1     0.071                       
REMARK 500    GLU B 103   CD    GLU B 103   OE2     0.076                       
REMARK 500    GLU C 182   CG    GLU C 182   CD      0.092                       
REMARK 500    GLU D 126   CD    GLU D 126   OE2     0.078                       
REMARK 500    TYR F 104   CG    TYR F 104   CD1     0.079                       
REMARK 500    GLU F 218   CD    GLU F 218   OE2     0.068                       
REMARK 500    GLU G 108   CD    GLU G 108   OE1     0.152                       
REMARK 500    GLU G 108   CD    GLU G 108   OE2     0.073                       
REMARK 500    ARG I  69   CD    ARG I  69   NE     -0.105                       
REMARK 500    ARG J 153   NE    ARG J 153   CZ     -0.086                       
REMARK 500    TYR K  40   CE1   TYR K  40   CZ      0.088                       
REMARK 500    GLU N  92   CG    GLU N  92   CD      0.109                       
REMARK 500    GLU N 150   CG    GLU N 150   CD      0.166                       
REMARK 500    GLU P 103   CD    GLU P 103   OE2     0.077                       
REMARK 500    ASP Q  13   CB    ASP Q  13   CG      0.166                       
REMARK 500    TRP R 100   CE3   TRP R 100   CZ3     0.107                       
REMARK 500    GLU R 216   CD    GLU R 216   OE2     0.080                       
REMARK 500    TYR T   7   N     TYR T   7   CA      0.121                       
REMARK 500    GLU U 108   CD    GLU U 108   OE1     0.099                       
REMARK 500    SER Z   3   CB    SER Z   3   OG      0.133                       
REMARK 500    SER Z  78   CB    SER Z  78   OG     -0.091                       
REMARK 500    GLU a  75   CD    GLU a  75   OE1     0.110                       
REMARK 500    GLU a 119   CG    GLU a 119   CD      0.093                       
REMARK 500    GLU b  92   CD    GLU b  92   OE2     0.072                       
REMARK 500    SER b 133   CB    SER b 133   OG      0.094                       
REMARK 500    GLU b 150   CG    GLU b 150   CD      0.144                       
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    LEU A  73   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ASP A 149   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B   4   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B   4   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B  96   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG C 117   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP D   9   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP D 157   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP E  94   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG E 101   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG E 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG E 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP F  17   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP F  43   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP F  83   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    LEU F  87   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG F 114   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    MET F 117   CG  -  SD  -  CE  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    VAL F 190   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ASP F 206   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP F 206   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG F 232   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG F 232   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    CYS G  78   CA  -  CB  -  SG  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG G  88   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG G 117   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG G 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP G 120   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG G 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG H  72   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG H  72   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG H  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG H  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    MET H  86   CG  -  SD  -  CE  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG H 198   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG H 198   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASN I  17   C   -  N   -  CA  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP I  58   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG I  69   NE  -  CZ  -  NH1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG I  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP I 134   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG I 197   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP J  33   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG J  86   CD  -  NE  -  CZ  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ARG J  86   NE  -  CZ  -  NH1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     132 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       48.37    -52.96                                   
REMARK 500    LYS A  52     -146.24    -55.30                                   
REMARK 500    SER A  53      129.27      4.59                                   
REMARK 500    GLN A 122      -34.84   -139.00                                   
REMARK 500    LYS A 175       43.86    -86.09                                   
REMARK 500    ARG A 176      -34.15   -170.66                                   
REMARK 500    PHE A 198      -79.49    -76.11                                   
REMARK 500    GLU A 199      102.59     79.34                                   
REMARK 500    GLN A 201      118.58     72.49                                   
REMARK 500    ARG B   8       63.72     63.96                                   
REMARK 500    ASN B  51       75.45    -64.51                                   
REMARK 500    GLU B  58       92.24     66.07                                   
REMARK 500    VAL B  59      -33.63   -135.32                                   
REMARK 500    ASN B  69     -165.63   -161.12                                   
REMARK 500    ASP B 202       35.93    -82.50                                   
REMARK 500    VAL B 203       63.04   -153.96                                   
REMARK 500    SER B 204     -101.76   -150.62                                   
REMARK 500    GLU B 248      -60.94   -102.51                                   
REMARK 500    ASP C  13       12.05     80.27                                   
REMARK 500    LYS C  47     -117.16     56.79                                   
REMARK 500    VAL C  50     -148.99     72.30                                   
REMARK 500    ALA C  51      102.64    101.38                                   
REMARK 500    GLN C 200      -74.69    -24.34                                   
REMARK 500    SER C 201       56.98   -108.16                                   
REMARK 500    LYS C 204     -107.39     73.98                                   
REMARK 500    ASN C 205       58.30   -114.97                                   
REMARK 500    ASP C 214      -10.29     73.98                                   
REMARK 500    SER C 216      151.65     54.66                                   
REMARK 500    GLU C 237      -60.52   -137.77                                   
REMARK 500    ARG D  53       70.16     68.56                                   
REMARK 500    GLU D 126       13.62   -158.03                                   
REMARK 500    GLU D 175      -74.98    -56.06                                   
REMARK 500    PHE D 226      123.37    -34.01                                   
REMARK 500    SER E  40     -167.79   -106.32                                   
REMARK 500    GLN E  53      -71.05    -45.40                                   
REMARK 500    HIS E  59      123.43    107.07                                   
REMARK 500    ALA E 151        0.48     80.37                                   
REMARK 500    ASP E 226     -125.55     56.79                                   
REMARK 500    ARG G   3       80.41     71.22                                   
REMARK 500    TRP G 189       50.66     37.28                                   
REMARK 500    ASP G 209       87.28     61.94                                   
REMARK 500    ASN H  30       54.78   -144.11                                   
REMARK 500    SER H 171     -127.18     69.85                                   
REMARK 500    GLN I  30     -123.14     46.45                                   
REMARK 500    ASP I  37       42.51   -142.23                                   
REMARK 500    ASP I 134      -67.64   -133.43                                   
REMARK 500    ASN J  24     -121.29     61.07                                   
REMARK 500    ALA J 122       24.33     85.53                                   
REMARK 500    ASP K 105     -156.66   -132.00                                   
REMARK 500    PHE L 102       72.95   -157.76                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     130 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 GLU C  237     GLU C  238                  147.93                    
REMARK 500 ASP D  127     ALA D  128                 -139.40                    
REMARK 500 GLU D  175     GLY D  176                 -139.80                    
REMARK 500 GLU D  175     GLY D  176                  139.96                    
REMARK 500 GLY D  223     GLN D  224                 -143.95                    
REMARK 500 GLY E  235     LEU E  236                  143.17                    
REMARK 500 GLY I   78     ARG I   79                 -128.06                    
REMARK 500 MET J    1     GLU J    2                 -145.55                    
REMARK 500 MET J    1     GLU J    2                 -141.87                    
REMARK 500 LYS P   54     LEU P   55                  146.78                    
REMARK 500 ASP P  202     VAL P  203                  147.99                    
REMARK 500 VAL P  203     SER P  204                 -149.21                    
REMARK 500 GLU P  244     ALA P  245                 -147.32                    
REMARK 500 ALA P  245     LYS P  246                   56.58                    
REMARK 500 LYS Q   47     LYS Q   48                 -134.44                    
REMARK 500 SER Q   49     VAL Q   50                 -137.98                    
REMARK 500 PRO R  130     GLY R  131                  137.27                    
REMARK 500 GLY R  223     GLN R  224                 -144.25                    
REMARK 500 THR T    5     GLY T    6                 -146.38                    
REMARK 500 GLY W   78     ARG W   79                 -130.68                    
REMARK 500 MET X    1     GLU X    2                 -142.28                    
REMARK 500 ILE a  215     SER a  216                 -127.06                    
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 L  99         0.08    SIDE CHAIN                              
REMARK 500    ARG X  86         0.07    SIDE CHAIN                              
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         11.04                                           
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 A 509        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH D 492        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH D 493        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH E 537        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH G 587        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH I 555        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH J 533        DISTANCE =  6.24 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 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  14   OG1                                                    
REMARK 620 2 TYR G 125   O    92.8                                              
REMARK 620 3 ASN G 128   O    80.2  91.7                                        
REMARK 620 4 MET G 131   O   160.5 106.7  98.8                                  
REMARK 620 5 HOH G 462   O    74.5 157.2 104.5  87.0                            
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 465   O    77.3                                              
REMARK 620 3 HOH N 417   O    92.6  86.7                                        
REMARK 620 4 HOH H 511   O    91.7  91.3 174.8                                  
REMARK 620 5 HOH N 405   O   160.5  83.2  88.0  86.9                            
REMARK 620 6 HOH N 490   O   109.8 172.7  94.6  86.7  89.6                      
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   112.0                                              
REMARK 620 3 SER H 169   O    98.5  91.0                                        
REMARK 620 4 ASP Z 213   O   107.7 138.1  96.0                                  
REMARK 620 5 HOH H 484   O    84.9  86.6 176.4  84.0                            
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    85.8                                              
REMARK 620 3 SER I 180   O   103.0  92.4                                        
REMARK 620 4 HOH I 404   O    81.4 162.0 102.8                                  
REMARK 620 5 HOH I 492   O   155.7  88.3 100.9  98.0                            
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   113.2                                              
REMARK 620 3 ASP Y 167   O   139.4 103.4                                        
REMARK 620 4 SER Y 170   O    94.9 103.2  93.2                                  
REMARK 620 5 HOH Y 479   O    84.8  79.7  85.0 176.9                            
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   105.3                                              
REMARK 620 3 SER K 170   O   104.0  94.2                                        
REMARK 620 4 ASP W 204   O   112.0 134.9 100.3                                  
REMARK 620 5 HOH K 462   O    78.8  89.7 174.4  74.1                            
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    98.3                                              
REMARK 620 3 THR L 189   O   100.7  83.1                                        
REMARK 620 4 HOH L 472   O    92.2 163.7  82.7                                  
REMARK 620 5 HOH L 457   O    56.4 126.6 142.0  69.7                            
REMARK 620 N                    1     2     3     4                             
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   105.1                                              
REMARK 620 3 ASP V 166   O   139.9 112.9                                        
REMARK 620 4 SER V 169   O    96.7  97.3  90.9                                  
REMARK 620 5 HOH V 473   O    77.0  85.7  93.1 173.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K N 304   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET N 164   O                                                      
REMARK 620 2 ASP N 167   O    92.2                                              
REMARK 620 3 SER N 170   O    97.4  72.3                                        
REMARK 620 4 HOH N 543   O    91.1 167.0  94.8                                  
REMARK 620 5 HOH N 472   O    87.7  84.5 156.4 108.2                            
REMARK 620 N                    1     2     3     4                             
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    93.6                                              
REMARK 620 3 ASN U 128   O    82.8  94.6                                        
REMARK 620 4 MET U 131   O   161.2 104.9  98.7                                  
REMARK 620 5 HOH U 463   O    73.3 152.4 107.3  88.5                            
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 462   O    89.1                                              
REMARK 620 3 HOH V 470   O    88.4  99.0                                        
REMARK 620 4 HOH b 412   O    89.7 166.0  94.9                                  
REMARK 620 5 HOH b 441   O   175.0  94.3  87.4  87.9                            
REMARK 620 6 HOH b 425   O    94.5  88.0 172.5  78.2  89.4                      
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    83.8                                              
REMARK 620 3 SER W 180   O   102.3  91.3                                        
REMARK 620 4 HOH W 455   O    89.4 164.8 103.5                                  
REMARK 620 5 HOH W 459   O   157.1  89.3  99.6  91.8                            
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    99.2                                              
REMARK 620 3 THR Z 189   O   100.7  84.1                                        
REMARK 620 4 HOH Z 461   O   133.8  97.2 123.9                                  
REMARK 620 5 HOH H 464   O    58.2 125.2 143.9  77.1                            
REMARK 620 6 HOH Z 473   O    95.2 161.5  81.8  80.9  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K b 305   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET b 164   O                                                      
REMARK 620 2 ASP b 167   O    92.6                                              
REMARK 620 3 SER b 170   O    95.7  71.8                                        
REMARK 620 4 HOH b 468   O    92.0  84.4 155.2                                  
REMARK 620 5 HOH b 470   O   141.0 122.2 110.6  76.2                            
REMARK 620 6 HOH b 508   O   101.3 161.6  94.7 106.8  49.9                      
REMARK 620 N                    1     2     3     4     5                       
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 449   O    88.0                                              
REMARK 620 3 HOH J 468   O    84.7  91.1                                        
REMARK 620 4 HOH J 512   O    91.0  91.3 175.0                                  
REMARK 620 5 HOH J 527   O    89.9 174.1  83.2  94.3                            
REMARK 620 6 HOH K 486   O   172.5  87.3  89.5  95.0  94.1                      
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 409   O                                                      
REMARK 620 2 HOH X 440   O    85.0                                              
REMARK 620 3 HOH X 519   O    90.1  89.7                                        
REMARK 620 4 HOH Y 509   O   175.9  98.9  88.7                                  
REMARK 620 5 HOH X 441   O    87.6  99.3 170.5  92.9                            
REMARK 620 6 HOH X 509   O    86.0 170.0  86.0  90.0  84.6                      
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 K G 303                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE H 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE H 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE M 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K N 304                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K U 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE V 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL W 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE W 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE Z 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K Z 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K b 305                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA c 4 through   
REMARK 800  6V9 c 1 bound to THR K 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA c 4 bound to THR K 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA d 4 through   
REMARK 800  6V9 d 1 bound to THR Y 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA d 4 bound to THR Y 1   
DBREF  5LEY A    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LEY B    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LEY C    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LEY D    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LEY E    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LEY F    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LEY G    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LEY H    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LEY I    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LEY J    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LEY K    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LEY L    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LEY M    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LEY N    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LEY O    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LEY P    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LEY Q    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LEY R    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LEY S    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LEY T    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LEY U    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LEY V    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LEY W    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LEY X    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LEY Y    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LEY Z    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LEY a    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LEY b    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LEY c    1     4  PDB    5LEY     5LEY             1      4             
DBREF  5LEY d    1     4  PDB    5LEY     5LEY             1      4             
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                      
SEQRES   1 c    4  6V9 OAS OAS 6VA                                              
SEQRES   1 d    4  6V9 OAS OAS 6VA                                              
MODRES 5LEY YCM C   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 E  148  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 G   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY YCM G  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 G  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 J   91  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY YCM Q   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 S  148  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 U   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY YCM U  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 6V1 U  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LEY 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    6V9  c   1       8                                                       
HET    OAS  c   2       7                                                       
HET    OAS  c   3       7                                                       
HET    6VA  c   4      15                                                       
HET    6V9  d   1       8                                                       
HET    OAS  d   2       7                                                       
HET    OAS  d   3       7                                                       
HET    6VA  d   4      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      K  G 303       1                                                       
HET     MG  H 301       1                                                       
HET     MG  H 302       1                                                       
HET     CL  H 303       1                                                       
HET     CL  H 304       1                                                       
HET    1PE  H 305      16                                                       
HET    1PE  H 306      16                                                       
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    1PE  M 305      16                                                       
HET     CL  N 301       1                                                       
HET     CL  N 302       1                                                       
HET     CL  N 303       1                                                       
HET      K  N 304       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    1PE  V 304      16                                                       
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     CL  b 301       1                                                       
HET     CL  b 302       1                                                       
HET     CL  b 303       1                                                       
HET     CL  b 304       1                                                       
HET      K  b 305       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     6V9 2-METHYL-1,3-THIAZOLE-5-CARBOXYLIC ACID                          
HETNAM     OAS O-ACETYLSERINE                                                   
HETNAM     6VA (3~{R},4~{S})-4-AZANYL-2-METHYL-5-PHENYL-PENTANE-2,3-            
HETNAM   2 6VA  DIOL                                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
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  6V9    2(C5 H5 N O2 S)                                              
FORMUL  29  OAS    4(C5 H9 N O4)                                                
FORMUL  29  6VA    2(C12 H19 N O2)                                              
FORMUL  31   CL    58(CL 1-)                                                    
FORMUL  47    K    6(K 1+)                                                      
FORMUL  48   MG    10(MG 2+)                                                    
FORMUL  52  1PE    9(C10 H22 O6)                                                
FORMUL  14  HOH   *3542(H2 O)                                                   
HELIX    1 AA1 LEU A   18  GLY A   30  1                                  13    
HELIX    2 AA2 ASP A   57  VAL A   61  5                                   5    
HELIX    3 AA3 MET A   78  GLN A  101  1                                  24    
HELIX    4 AA4 PRO A  105  TYR A  120  1                                  16    
HELIX    5 AA5 ASN A  165  LYS A  175  1                                  11    
HELIX    6 AA6 GLU A  182  SER A  197  1                                  16    
HELIX    7 AA7 THR A  221  ILE A  232  1                                  12    
HELIX    8 AA8 LEU B   18  ALA B   31  1                                  14    
HELIX    9 AA9 ILE B   79  GLN B  102  1                                  24    
HELIX   10 AB1 PRO B  106  PHE B  124  1                                  19    
HELIX   11 AB2 ASN B  167  TYR B  179  1                                  13    
HELIX   12 AB3 THR B  185  MET B  201  1                                  17    
HELIX   13 AB4 SER B  207  GLU B  209  5                                   3    
HELIX   14 AB5 LYS B  229  ALA B  247  1                                  19    
HELIX   15 AB6 SER C   11  HIS C   15  5                                   5    
HELIX   16 AB7 LEU C   16  LYS C   28  1                                  13    
HELIX   17 AB8 ASP C   55  ARG C   60  5                                   6    
HELIX   18 AB9 LEU C   76  GLU C   99  1                                  24    
HELIX   19 AC1 THR C  103  TYR C  118  1                                  16    
HELIX   20 AC2 GLY C  164  TYR C  176  1                                  13    
HELIX   21 AC3 THR C  183  VAL C  199  1                                  17    
HELIX   22 AC4 ASN C  221  LYS C  234  1                                  14    
HELIX   23 AC5 LEU D   21  LYS D   32  1                                  12    
HELIX   24 AC6 GLU D   60  ILE D   64  5                                   5    
HELIX   25 AC7 ASP D   84  ASN D  104  1                                  21    
HELIX   26 AC8 THR D  108  ASN D  118  1                                  11    
HELIX   27 AC9 ALA D  173  TYR D  185  1                                  13    
HELIX   28 AD1 THR D  190  MET D  206  1                                  17    
HELIX   29 AD2 THR D  230  LYS D  239  1                                  10    
HELIX   30 AD3 ILE E   19  GLY E   32  1                                  14    
HELIX   31 AD4 LEU E   77  ASP E  100  1                                  24    
HELIX   32 AD5 PRO E  104  ILE E  118  1                                  15    
HELIX   33 AD6 PRO E  119  ARG E  122  5                                   4    
HELIX   34 AD7 ARG E  164  MET E  176  1                                  13    
HELIX   35 AD8 SER E  177  PHE E  179  5                                   3    
HELIX   36 AD9 ASN E  183  GLU E  197  1                                  15    
HELIX   37 AE1 ASP E  225  ASP E  228  5                                   4    
HELIX   38 AE2 VAL E  229  GLU E  234  1                                   6    
HELIX   39 AE3 VAL F   20  ASN F   32  1                                  13    
HELIX   40 AE4 LEU F   80  GLY F  103  1                                  24    
HELIX   41 AE5 PRO F  107  TYR F  122  1                                  16    
HELIX   42 AE6 ALA F  168  GLU F  177  1                                  10    
HELIX   43 AE7 LYS F  178  LEU F  179  5                                   2    
HELIX   44 AE8 GLN F  180  MET F  184  5                                   5    
HELIX   45 AE9 THR F  185  HIS F  201  1                                  17    
HELIX   46 AF1 LEU F  219  ASN F  221  5                                   3    
HELIX   47 AF2 PRO F  228  LYS F  244  1                                  17    
HELIX   48 AF3 LEU G   22  GLY G   35  1                                  14    
HELIX   49 AF4 ASP G   62  VAL G   66  5                                   5    
HELIX   50 AF5 MET G   83  GLY G  106  1                                  24    
HELIX   51 AF6 PRO G  110  THR G  126  1                                  17    
HELIX   52 AF7 LYS G  171  LYS G  186  1                                  16    
HELIX   53 AF8 PHE G  187  THR G  190  5                                   4    
HELIX   54 AF9 GLN G  193  SER G  207  1                                  15    
HELIX   55 AG1 LYS G  211  SER G  213  5                                   3    
HELIX   56 AG2 THR G  231  GLU G  244  1                                  14    
HELIX   57 AG3 THR H   48  GLY H   71  1                                  24    
HELIX   58 AG4 ARG H   75  TYR H   90  1                                  16    
HELIX   59 AG5 GLY H  130  PHE H  142  1                                  13    
HELIX   60 AG6 GLU H  147  ASP H  166  1                                  20    
HELIX   61 AG7 SER I    1  TYR I    5  5                                   5    
HELIX   62 AG8 LEU I   55  GLU I   77  1                                  23    
HELIX   63 AG9 LYS I   82  LYS I   97  1                                  16    
HELIX   64 AH1 CYS I  141  TRP I  153  1                                  13    
HELIX   65 AH2 ASP I  158  ASP I  175  1                                  18    
HELIX   66 AH3 GLY J   51  GLY J   72  1                                  22    
HELIX   67 AH4 SER J   76  ARG J   93  1                                  18    
HELIX   68 AH5 GLY J  135  TYR J  147  1                                  13    
HELIX   69 AH6 SER J  152  PHE J  171  1                                  20    
HELIX   70 AH7 GLY K   48  LYS K   71  1                                  24    
HELIX   71 AH8 SER K   75  GLN K   89  1                                  15    
HELIX   72 AH9 GLY K  131  TYR K  143  1                                  13    
HELIX   73 AI1 GLU K  148  ASP K  167  1                                  20    
HELIX   74 AI2 VAL K  192  SER K  200  1                                   9    
HELIX   75 AI3 PHE L   57  ASN L   80  1                                  24    
HELIX   76 AI4 THR L   84  ARG L   99  1                                  16    
HELIX   77 AI5 ALA L  141  VAL L  153  1                                  13    
HELIX   78 AI6 SER L  167  ASP L  186  1                                  20    
HELIX   79 AI7 TYR M   57  GLY M   78  1                                  22    
HELIX   80 AI8 SER M   84  LYS M  102  1                                  19    
HELIX   81 AI9 TYR M  141  ALA M  146  1                                   6    
HELIX   82 AJ1 ALA M  146  GLN M  157  1                                  12    
HELIX   83 AJ2 SER M  161  ASP M  180  1                                  20    
HELIX   84 AJ3 TRP M  209  MET M  214  5                                   6    
HELIX   85 AJ4 SER N   48  ASN N   71  1                                  24    
HELIX   86 AJ5 LEU N   75  TYR N   90  1                                  16    
HELIX   87 AJ6 ARG N   91  LEU N   94  5                                   4    
HELIX   88 AJ7 GLY N  129  TYR N  134  5                                   6    
HELIX   89 AJ8 ILE N  135  TYR N  143  1                                   9    
HELIX   90 AJ9 THR N  148  ASP N  167  1                                  20    
HELIX   91 AK1 LEU N  190  ILE N  194  5                                   5    
HELIX   92 AK2 LEU O   18  GLY O   30  1                                  13    
HELIX   93 AK3 ASP O   57  VAL O   61  5                                   5    
HELIX   94 AK4 MET O   78  GLN O  101  1                                  24    
HELIX   95 AK5 PRO O  105  TYR O  120  1                                  16    
HELIX   96 AK6 ASN O  165  LYS O  175  1                                  11    
HELIX   97 AK7 GLU O  182  SER O  197  1                                  16    
HELIX   98 AK8 THR O  221  ALA O  230  1                                  10    
HELIX   99 AK9 LEU P   18  ALA P   31  1                                  14    
HELIX  100 AL1 ILE P   79  GLN P  102  1                                  24    
HELIX  101 AL2 PRO P  106  PHE P  124  1                                  19    
HELIX  102 AL3 ASN P  167  TYR P  179  1                                  13    
HELIX  103 AL4 THR P  185  MET P  201  1                                  17    
HELIX  104 AL5 SER P  207  GLU P  209  5                                   3    
HELIX  105 AL6 LYS P  229  GLU P  244  1                                  16    
HELIX  106 AL7 LEU Q   16  LYS Q   28  1                                  13    
HELIX  107 AL8 ASP Q   55  ARG Q   60  5                                   6    
HELIX  108 AL9 LEU Q   76  GLU Q   99  1                                  24    
HELIX  109 AM1 THR Q  103  TYR Q  118  1                                  16    
HELIX  110 AM2 GLY Q  164  TYR Q  176  1                                  13    
HELIX  111 AM3 THR Q  183  GLU Q  197  1                                  15    
HELIX  112 AM4 ASN Q  221  LYS Q  234  1                                  14    
HELIX  113 AM5 LYS Q  234  ASN Q  239  1                                   6    
HELIX  114 AM6 LEU R   21  LYS R   32  1                                  12    
HELIX  115 AM7 GLU R   60  ILE R   64  5                                   5    
HELIX  116 AM8 ASP R   84  ASN R  104  1                                  21    
HELIX  117 AM9 THR R  108  ASN R  118  1                                  11    
HELIX  118 AN1 ALA R  173  TYR R  185  1                                  13    
HELIX  119 AN2 THR R  190  MET R  206  1                                  17    
HELIX  120 AN3 THR R  230  LYS R  239  1                                  10    
HELIX  121 AN4 ILE S   19  GLY S   32  1                                  14    
HELIX  122 AN5 LEU S   77  ASP S  100  1                                  24    
HELIX  123 AN6 PRO S  104  ILE S  118  1                                  15    
HELIX  124 AN7 PRO S  119  ARG S  122  5                                   4    
HELIX  125 AN8 ARG S  164  MET S  176  1                                  13    
HELIX  126 AN9 SER S  177  PHE S  179  5                                   3    
HELIX  127 AO1 ASN S  183  GLU S  197  1                                  15    
HELIX  128 AO2 ASP S  225  ASP S  228  5                                   4    
HELIX  129 AO3 VAL S  229  GLU S  234  1                                   6    
HELIX  130 AO4 VAL T   20  SER T   33  1                                  14    
HELIX  131 AO5 LEU T   80  GLY T  103  1                                  24    
HELIX  132 AO6 PRO T  107  TYR T  122  1                                  16    
HELIX  133 AO7 ALA T  168  GLU T  177  1                                  10    
HELIX  134 AO8 LYS T  178  LEU T  179  5                                   2    
HELIX  135 AO9 GLN T  180  MET T  184  5                                   5    
HELIX  136 AP1 THR T  185  HIS T  201  1                                  17    
HELIX  137 AP2 LEU T  219  ASN T  221  5                                   3    
HELIX  138 AP3 PRO T  228  LYS T  244  1                                  17    
HELIX  139 AP4 LEU U   22  GLY U   35  1                                  14    
HELIX  140 AP5 ASP U   62  VAL U   66  5                                   5    
HELIX  141 AP6 MET U   83  GLY U  106  1                                  24    
HELIX  142 AP7 PRO U  110  THR U  126  1                                  17    
HELIX  143 AP8 LYS U  171  LYS U  184  1                                  14    
HELIX  144 AP9 THR U  194  SER U  207  1                                  14    
HELIX  145 AQ1 LYS U  211  SER U  213  5                                   3    
HELIX  146 AQ2 THR U  231  GLU U  244  1                                  14    
HELIX  147 AQ3 THR V   48  GLY V   71  1                                  24    
HELIX  148 AQ4 ARG V   75  TYR V   90  1                                  16    
HELIX  149 AQ5 GLY V  130  PHE V  142  1                                  13    
HELIX  150 AQ6 GLU V  147  ASP V  166  1                                  20    
HELIX  151 AQ7 SER W    1  TYR W    5  5                                   5    
HELIX  152 AQ8 LEU W   55  GLU W   77  1                                  23    
HELIX  153 AQ9 LYS W   82  LYS W   97  1                                  16    
HELIX  154 AR1 CYS W  141  TRP W  153  1                                  13    
HELIX  155 AR2 ASP W  158  ASP W  175  1                                  18    
HELIX  156 AR3 GLY X   51  GLY X   72  1                                  22    
HELIX  157 AR4 SER X   76  ARG X   93  1                                  18    
HELIX  158 AR5 GLY X  135  TYR X  147  1                                  13    
HELIX  159 AR6 SER X  152  PHE X  171  1                                  20    
HELIX  160 AR7 GLY Y   48  LYS Y   71  1                                  24    
HELIX  161 AR8 SER Y   75  GLN Y   89  1                                  15    
HELIX  162 AR9 GLY Y  131  TYR Y  143  1                                  13    
HELIX  163 AS1 GLU Y  148  ASP Y  167  1                                  20    
HELIX  164 AS2 VAL Y  192  TYR Y  199  1                                   8    
HELIX  165 AS3 PHE Z   57  ASN Z   80  1                                  24    
HELIX  166 AS4 THR Z   84  ARG Z   99  1                                  16    
HELIX  167 AS5 ALA Z  141  VAL Z  153  1                                  13    
HELIX  168 AS6 SER Z  167  ASP Z  186  1                                  20    
HELIX  169 AS7 TYR a   57  GLY a   78  1                                  22    
HELIX  170 AS8 SER a   84  LYS a  102  1                                  19    
HELIX  171 AS9 TYR a  141  ALA a  146  1                                   6    
HELIX  172 AT1 ALA a  146  GLN a  157  1                                  12    
HELIX  173 AT2 SER a  161  ASP a  180  1                                  20    
HELIX  174 AT3 TRP a  209  MET a  214  5                                   6    
HELIX  175 AT4 SER b   48  ASN b   71  1                                  24    
HELIX  176 AT5 LEU b   75  TYR b   90  1                                  16    
HELIX  177 AT6 ARG b   91  LEU b   94  5                                   4    
HELIX  178 AT7 GLY b  129  TYR b  134  5                                   6    
HELIX  179 AT8 ILE b  135  TYR b  143  1                                   9    
HELIX  180 AT9 THR b  148  ASP b  167  1                                  20    
HELIX  181 AU1 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  TRP A 138 -1  O  CYS A 136   N  GLY A  72           
SHEET    4 AA2 5 PRO A 143  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  GLN B 146   N  GLY B 138           
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  ALA C  32   O  ILE C 161           
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  ALA C  64  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  VAL C 134   N  CYS C  70           
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  ALA D  37   O  ILE D 170           
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  GLY E 213   N  LEU E  46           
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  MET F  75   N  PHE F  67           
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  GLN F 147   N  SER F 139           
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  YCM G 137   N  THR G  81           
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  ALA H  16 -1  O  GLY H  15   N  ALA H   4           
SHEET    4 AB6 5 ILE H 173  SER H 179 -1  O  ASP H 174   N  ALA H  16           
SHEET    5 AB6 5 LEU H 183  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  ASP H  28   N  ALA H  20           
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  THR I 196   N  LYS H 215           
SHEET    3 AB9 6 VAL I 184  GLU I 190 -1  N  ILE I 188   O  THR I 195           
SHEET    4 AB9 6 CYS I  18  ASP I  24 -1  N  VAL I  19   O  ILE I 189           
SHEET    5 AB9 6 ALA I   9  LYS I  14 -1  N  MET I  13   O  ALA I  20           
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  VAL I 131 -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 TYR J  12  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 TYR J  12  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  ALA J 114   N  GLY J 106           
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 4 VAL K  34  ASN K  38  0                                        
SHEET    2 AC9 4 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC9 4 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC9 4 ALA K  46  GLY K  47 -1  N  ALA K  46   O  GLY K  98           
SHEET    1 AD1 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AD1 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AD1 5 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AD1 5 GLY K 108  ASP K 115 -1  O  VAL K 114   N  THR K  99           
SHEET    5 AD1 5 ARG K 120  SER K 122 -1  O  ILE K 121   N  TYR K 113           
SHEET    1 AD2 5 PHE L 135  GLY L 139  0                                        
SHEET    2 AD2 5 THR L  11  ALA L  16 -1  N  ILE L  12   O  GLY L 138           
SHEET    3 AD2 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AD2 5 ALA L 192  THR L 199 -1  O  ARG L 194   N  SER L  25           
SHEET    5 AD2 5 GLY L 202  SER L 209 -1  O  GLU L 206   N  ILE L 195           
SHEET    1 AD3 2 LEU L  29  GLU L  31  0                                        
SHEET    2 AD3 2 SER L  34  THR L  37 -1  O  HIS L  36   N  LEU L  29           
SHEET    1 AD4 5 CYS L  43  THR L  47  0                                        
SHEET    2 AD4 5 THR L  50  GLY L  56 -1  O  THR L  50   N  LEU L  46           
SHEET    3 AD4 5 VAL L 106  LEU L 113 -1  O  GLY L 111   N  VAL L  51           
SHEET    4 AD4 5 GLY L 119  PHE L 124 -1  O  TYR L 122   N  ILE L 110           
SHEET    5 AD4 5 TYR L 130  ASP L 133 -1  O  ASP L 133   N  VAL L 121           
SHEET    1 AD5 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AD5 5 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD5 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD5 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD5 5 ILE M  42  ASN M  46 -1  N  MET M  43   O  LEU M  51           
SHEET    1 AD6 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AD6 7 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD6 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD6 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD6 7 ASN M 108  ALA M 116 -1  O  THR M 109   N  SER M  54           
SHEET    6 AD6 7 GLU M 119  VAL M 125 -1  O  VAL M 125   N  MET M 110           
SHEET    7 AD6 7 ALA M 131  GLU M 133 -1  O  TYR M 132   N  TYR M 124           
SHEET    1 AD7 5 SER M 136  ALA M 138  0                                        
SHEET    2 AD7 5 VAL M  11  PHE M  16 -1  N  GLY M  13   O  LEU M 137           
SHEET    3 AD7 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  PHE M  16           
SHEET    4 AD7 5 PHE M 187  THR M 193 -1  O  ALA M 190   N  ILE M  22           
SHEET    5 AD7 5 GLY M 196  LEU M 203 -1  O  GLU M 200   N  ILE M 189           
SHEET    1 AD8 5 PHE N 125  GLY N 128  0                                        
SHEET    2 AD8 5 ILE N   3  PHE N   8 -1  N  ALA N   5   O  ALA N 126           
SHEET    3 AD8 5 GLY N  11  ALA N  16 -1  O  GLY N  15   N  MET N   4           
SHEET    4 AD8 5 ILE N 174  ALA N 180 -1  O  ARG N 175   N  ALA N  16           
SHEET    5 AD8 5 GLY N 183  LEU N 189 -1  O  LEU N 189   N  ILE N 174           
SHEET    1 AD9 2 THR N  20  THR N  22  0                                        
SHEET    2 AD9 2 TYR N  25  ASN N  28 -1  O  ASN N  28   N  THR N  20           
SHEET    1 AE1 5 LEU N  34  HIS N  38  0                                        
SHEET    2 AE1 5 ILE N  41  GLY N  47 -1  O  ILE N  41   N  ILE N  37           
SHEET    3 AE1 5 ALA N  96  ASP N 104 -1  O  ILE N  99   N  CYS N  44           
SHEET    4 AE1 5 GLY N 108  VAL N 114 -1  O  TYR N 112   N  ILE N 100           
SHEET    5 AE1 5 VAL N 121  ARG N 122 -1  O  VAL N 121   N  SER N 113           
SHEET    1 AE2 5 ALA O 159  MET O 162  0                                        
SHEET    2 AE2 5 SER O  34  LYS O  38 -1  N  SER O  34   O  MET O 162           
SHEET    3 AE2 5 VAL O  43  GLU O  48 -1  O  ALA O  46   N  VAL O  35           
SHEET    4 AE2 5 ILE O 207  ASN O 213 -1  O  GLY O 210   N  LEU O  45           
SHEET    5 AE2 5 GLY O 216  ARG O 219 -1  O  ARG O 218   N  ILE O 211           
SHEET    1 AE3 5 GLU O  65  THR O  68  0                                        
SHEET    2 AE3 5 ILE O  71  GLY O  77 -1  O  ILE O  71   N  ILE O  67           
SHEET    3 AE3 5 VAL O 131  TRP O 138 -1  O  CYS O 136   N  GLY O  72           
SHEET    4 AE3 5 PRO O 143  SER O 148 -1  O  PHE O 146   N  ILE O 135           
SHEET    5 AE3 5 TYR O 154  ALA O 156 -1  O  PHE O 155   N  GLN O 147           
SHEET    1 AE4 5 ALA P 161  ILE P 164  0                                        
SHEET    2 AE4 5 CYS P  34  ALA P  39 -1  N  CYS P  34   O  ILE P 164           
SHEET    3 AE4 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  LEU P  35           
SHEET    4 AE4 5 VAL P 211  GLU P 219 -1  O  GLU P 212   N  ALA P  47           
SHEET    5 AE4 5 LYS P 222  VAL P 227 -1  O  VAL P 224   N  THR P 217           
SHEET    1 AE5 5 ILE P  65  ASN P  69  0                                        
SHEET    2 AE5 5 MET P  72  GLY P  78 -1  O  CYS P  74   N  TYR P  66           
SHEET    3 AE5 5 VAL P 132  ASP P 140 -1  O  ILE P 137   N  ALA P  73           
SHEET    4 AE5 5 GLY P 144  SER P 150 -1  O  GLN P 146   N  GLY P 138           
SHEET    5 AE5 5 TYR P 156  GLY P 158 -1  O  GLY P 157   N  GLN P 149           
SHEET    1 AE6 5 ALA Q 158  ILE Q 161  0                                        
SHEET    2 AE6 5 ALA Q  32  ARG Q  36 -1  N  ALA Q  32   O  ILE Q 161           
SHEET    3 AE6 5 ILE Q  40  VAL Q  45 -1  O  GLY Q  44   N  VAL Q  33           
SHEET    4 AE6 5 GLU Q 207  ARG Q 212 -1  O  GLU Q 207   N  VAL Q  45           
SHEET    5 AE6 5 LYS Q 218  LEU Q 220 -1  O  LYS Q 218   N  VAL Q 210           
SHEET    1 AE7 5 ILE Q  62  ASP Q  66  0                                        
SHEET    2 AE7 5 VAL Q  69  GLY Q  75 -1  O  MET Q  71   N  YCM Q  63           
SHEET    3 AE7 5 ILE Q 129  PHE Q 136 -1  O  VAL Q 134   N  CYS Q  70           
SHEET    4 AE7 5 PRO Q 142  THR Q 147 -1  O  TYR Q 145   N  ILE Q 133           
SHEET    5 AE7 5 TYR Q 153  ALA Q 155 -1  O  HIS Q 154   N  GLN Q 146           
SHEET    1 AE8 5 ALA R 167  ILE R 170  0                                        
SHEET    2 AE8 5 ALA R  37  THR R  42 -1  N  ALA R  37   O  ILE R 170           
SHEET    3 AE8 5 GLY R  45  GLU R  51 -1  O  ALA R  49   N  ILE R  38           
SHEET    4 AE8 5 ILE R 215  VAL R 220 -1  O  ALA R 218   N  LEU R  48           
SHEET    5 AE8 5 HIS R 227  MET R 228 -1  O  HIS R 227   N  THR R 219           
SHEET    1 AE9 5 ILE R  67  ASP R  71  0                                        
SHEET    2 AE9 5 ILE R  74  GLY R  80 -1  O  ILE R  74   N  ILE R  70           
SHEET    3 AE9 5 VAL R 139  ASP R 147 -1  O  GLY R 144   N  GLY R  75           
SHEET    4 AE9 5 GLY R 150  MET R 156 -1  O  GLN R 152   N  GLY R 145           
SHEET    5 AE9 5 PHE R 162  GLN R 164 -1  O  VAL R 163   N  HIS R 155           
SHEET    1 AF1 5 ALA S 158  ILE S 161  0                                        
SHEET    2 AF1 5 THR S  35  LYS S  39 -1  N  GLY S  37   O  MET S 159           
SHEET    3 AF1 5 HIS S  43  LEU S  49 -1  O  VAL S  45   N  LEU S  38           
SHEET    4 AF1 5 VAL S 210  GLY S 216 -1  O  VAL S 215   N  ALA S  44           
SHEET    5 AF1 5 LEU S 219  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF2 5 ILE S  63  ASP S  67  0                                        
SHEET    2 AF2 5 ILE S  70  GLY S  76 -1  O  ILE S  72   N  LEU S  64           
SHEET    3 AF2 5 VAL S 130  ASP S 138 -1  O  ALA S 135   N  GLY S  71           
SHEET    4 AF2 5 GLY S 141  THR S 147 -1  O  PHE S 145   N  ILE S 134           
SHEET    5 AF2 5 TYR S 153  CYS S 156 -1  O  CYS S 156   N  ILE S 144           
SHEET    1 AF3 5 GLY T 162  ILE T 165  0                                        
SHEET    2 AF3 5 ALA T  36  CYS T  41 -1  N  ALA T  36   O  ILE T 165           
SHEET    3 AF3 5 GLY T  44  LEU T  52 -1  O  GLY T  44   N  CYS T  41           
SHEET    4 AF3 5 PHE T 209  GLY T 217 -1  O  SER T 214   N  PHE T  47           
SHEET    5 AF3 5 GLU T 225  ILE T 226 -1  O  GLU T 225   N  TRP T 215           
SHEET    1 AF4 5 LEU T  66  ASP T  70  0                                        
SHEET    2 AF4 5 VAL T  73  GLY T  79 -1  O  MET T  75   N  PHE T  67           
SHEET    3 AF4 5 CYS T 133  SER T 141 -1  O  MET T 136   N  ALA T  76           
SHEET    4 AF4 5 GLY T 145  ILE T 151 -1  O  GLN T 147   N  SER T 139           
SHEET    5 AF4 5 SER T 157  GLY T 159 -1  O  TYR T 158   N  MET T 150           
SHEET    1 AF5 5 ALA U 165  GLY U 169  0                                        
SHEET    2 AF5 5 THR U  38  ARG U  43 -1  N  ALA U  41   O  THR U 166           
SHEET    3 AF5 5 6V1 U  47  GLN U  53 -1  O  VAL U  51   N  VAL U  40           
SHEET    4 AF5 5 ILE U 215  THR U 221 -1  O  GLY U 218   N  ILE U  50           
SHEET    5 AF5 5 ARG U 228  ILE U 229 -1  O  ARG U 228   N  VAL U 219           
SHEET    1 AF6 5 LEU U  69  THR U  73  0                                        
SHEET    2 AF6 5 ILE U  76  GLY U  82 -1  O  ILE U  76   N  ILE U  72           
SHEET    3 AF6 5 CYS U 136  ASP U 144 -1  O  YCM U 137   N  THR U  81           
SHEET    4 AF6 5 GLY U 148  CYS U 154 -1  O  TYR U 152   N  LEU U 140           
SHEET    5 AF6 5 TYR U 160  GLY U 162 -1  O  6V1 U 161   N  LYS U 153           
SHEET    1 AF7 5 TYR V 124  MET V 127  0                                        
SHEET    2 AF7 5 ILE V   3  TYR V   8 -1  N  ILE V   3   O  MET V 127           
SHEET    3 AF7 5 GLY V  11  ASP V  17 -1  O  GLY V  15   N  ALA V   4           
SHEET    4 AF7 5 ILE V 173  SER V 179 -1  O  ASP V 174   N  ALA V  16           
SHEET    5 AF7 5 LEU V 183  THR V 190 -1  O  TYR V 189   N  ILE V 173           
SHEET    1 AF8 2 ALA V  20  GLU V  22  0                                        
SHEET    2 AF8 2 VAL V  25  ASP V  28 -1  O  ASP V  28   N  ALA V  20           
SHEET    1 AF9 5 ILE V  34  SER V  38  0                                        
SHEET    2 AF9 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF9 5 ALA V  96  ASP V 104 -1  O  GLY V 101   N  TYR V  42           
SHEET    4 AF9 5 GLY V 107  ILE V 113 -1  O  TYR V 111   N  LEU V 100           
SHEET    5 AF9 5 THR V 119  LYS V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AG1 6 VAL V 211  PRO V 218  0                                        
SHEET    2 AG1 6 LYS W 193  LEU W 199 -1  O  ILE W 194   N  THR V 217           
SHEET    3 AG1 6 VAL W 184  GLU W 190 -1  N  ILE W 188   O  THR W 195           
SHEET    4 AG1 6 CYS W  18  ASP W  24 -1  N  VAL W  19   O  ILE W 189           
SHEET    5 AG1 6 ALA W   9  LYS W  14 -1  N  MET W  11   O  ALA W  22           
SHEET    6 AG1 6 PHE W 135  GLY W 139 -1  O  SER W 138   N  VAL W  10           
SHEET    1 AG2 2 PHE W  27  ILE W  29  0                                        
SHEET    2 AG2 2 GLN W  32  THR W  35 -1  O  VAL W  34   N  PHE W  27           
SHEET    1 AG3 5 ILE W  41  GLY W  45  0                                        
SHEET    2 AG3 5 LEU W  48  GLY W  54 -1  O  LEU W  48   N  MET W  44           
SHEET    3 AG3 5 THR W 104  LEU W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG3 5 PRO W 118  LEU W 123 -1  O  PHE W 119   N  GLY W 110           
SHEET    5 AG3 5 PRO W 129  VAL W 131 -1  O  MET W 130   N  SER W 122           
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 GLY X 187  ASP X 190 -1  O  HIS X 189   N  ILE X 182           
SHEET    1 AG5 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG5 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG5 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG5 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG5 5 ILE X 194  SER X 195 -1  O  ILE X 194   N  PHE X 178           
SHEET    1 AG6 2 ALA X  21  SER X  23  0                                        
SHEET    2 AG6 2 VAL X  26  LYS X  29 -1  O  MET X  28   N  ALA X  21           
SHEET    1 AG7 5 MET X  35  SER X  39  0                                        
SHEET    2 AG7 5 ILE X  42  GLY X  48 -1  O  ILE X  42   N  MET X  38           
SHEET    3 AG7 5 VAL X 100  ASP X 108 -1  O  LEU X 103   N  LEU X  45           
SHEET    4 AG7 5 GLY X 112  MET X 118 -1  O  MET X 118   N  LEU X 102           
SHEET    5 AG7 5 LEU X 124  LYS X 126 -1  O  ALA X 125   N  TYR X 117           
SHEET    1 AG8 5 THR Y 125  VAL Y 128  0                                        
SHEET    2 AG8 5 THR Y   3  PHE Y   8 -1  N  ALA Y   5   O  PHE Y 126           
SHEET    3 AG8 5 GLY Y  11  ALA Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4 AG8 5 ALA Y 173  ARG Y 180 -1  O  VAL Y 179   N  VAL Y  12           
SHEET    5 AG8 5 GLY Y 183  ASN Y 191 -1  O  ASP Y 190   N  VAL Y 174           
SHEET    1 AG9 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG9 2 TYR Y  25  SER Y  28 -1  O  SER Y  28   N  ALA Y  20           
SHEET    1 AH1 4 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AH1 4 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AH1 4 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AH1 4 ALA Y  46  GLY Y  47 -1  N  ALA Y  46   O  GLY Y  98           
SHEET    1 AH2 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AH2 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AH2 5 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AH2 5 GLY Y 108  ASP Y 115 -1  O  VAL Y 114   N  THR Y  99           
SHEET    5 AH2 5 ARG Y 120  SER Y 122 -1  O  ILE Y 121   N  TYR Y 113           
SHEET    1 AH3 5 PHE Z 135  GLY Z 139  0                                        
SHEET    2 AH3 5 THR Z  11  ALA Z  16 -1  N  ILE Z  12   O  GLY Z 138           
SHEET    3 AH3 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AH3 5 ALA Z 192  THR Z 199 -1  O  ARG Z 194   N  SER Z  25           
SHEET    5 AH3 5 GLY Z 202  SER Z 209 -1  O  GLU Z 206   N  ILE Z 195           
SHEET    1 AH4 2 LEU Z  29  GLU Z  31  0                                        
SHEET    2 AH4 2 SER Z  34  THR Z  37 -1  O  HIS Z  36   N  LEU Z  29           
SHEET    1 AH5 5 CYS Z  43  THR Z  47  0                                        
SHEET    2 AH5 5 THR Z  50  GLY Z  56 -1  O  THR Z  50   N  LEU Z  46           
SHEET    3 AH5 5 VAL Z 106  LEU Z 113 -1  O  GLY Z 111   N  VAL Z  51           
SHEET    4 AH5 5 GLY Z 119  PHE Z 124 -1  O  TYR Z 122   N  ILE Z 110           
SHEET    5 AH5 5 TYR Z 130  ASP Z 133 -1  O  ASP Z 133   N  VAL Z 121           
SHEET    1 AH6 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH6 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH6 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH6 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH6 5 ILE a  42  ASN a  46 -1  N  MET a  43   O  LEU a  51           
SHEET    1 AH7 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH7 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH7 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH7 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH7 7 ASN a 108  ALA a 116 -1  O  THR a 109   N  SER a  54           
SHEET    6 AH7 7 GLU a 119  VAL a 125 -1  O  VAL a 125   N  MET a 110           
SHEET    7 AH7 7 ALA a 131  GLU a 133 -1  O  TYR a 132   N  TYR a 124           
SHEET    1 AH8 5 SER a 136  ALA a 138  0                                        
SHEET    2 AH8 5 VAL a  11  PHE a  16 -1  N  GLY a  13   O  LEU a 137           
SHEET    3 AH8 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  PHE a  16           
SHEET    4 AH8 5 PHE a 187  THR a 193 -1  O  ALA a 190   N  ILE a  22           
SHEET    5 AH8 5 GLY a 196  LEU a 203 -1  O  GLU a 200   N  ILE a 189           
SHEET    1 AH9 5 PHE b 125  GLY b 128  0                                        
SHEET    2 AH9 5 ILE b   3  PHE b   8 -1  N  ALA b   5   O  ALA b 126           
SHEET    3 AH9 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4 AH9 5 ILE b 174  ALA b 180 -1  O  ARG b 175   N  ALA b  16           
SHEET    5 AH9 5 GLY b 183  LEU b 189 -1  O  LEU b 189   N  ILE b 174           
SHEET    1 AI1 2 THR b  20  THR b  22  0                                        
SHEET    2 AI1 2 TYR b  25  ASN b  28 -1  O  ASN b  28   N  THR b  20           
SHEET    1 AI2 5 LEU b  34  HIS b  38  0                                        
SHEET    2 AI2 5 ILE b  41  GLY b  47 -1  O  ILE b  41   N  ILE b  37           
SHEET    3 AI2 5 ALA b  96  ASP b 104 -1  O  GLY b  97   N  SER b  46           
SHEET    4 AI2 5 GLY b 108  VAL b 114 -1  O  TYR b 112   N  ILE b 100           
SHEET    5 AI2 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  1.33  
LINK         C   THR E 147                 N   6V1 E 148     1555   1555  1.33  
LINK         C   6V1 E 148                 N   PRO E 149     1555   1555  1.34  
LINK         OG1 THR G  14                 K     K G 303     1555   1555  2.77  
LINK         C   ASP G  46                 N   6V1 G  47     1555   1555  1.33  
LINK         C   6V1 G  47                 N   ALA G  48     1555   1555  1.31  
LINK         O   TYR G 125                 K     K G 303     1555   1555  2.56  
LINK         O   ASN G 128                 K     K G 303     1555   1555  2.58  
LINK         O   MET G 131                 K     K G 303     1555   1555  2.51  
LINK         C   CYS G 136                 N   YCM G 137     1555   1555  1.30  
LINK         C   YCM G 137                 N   MET G 138     1555   1555  1.32  
LINK         C   TYR G 160                 N   6V1 G 161     1555   1555  1.32  
LINK         C   6V1 G 161                 N   GLY G 162     1555   1555  1.31  
LINK         OE1 GLN H  91                MG    MG H 301     1555   1555  2.18  
LINK         O   ILE H 163                MG    MG H 302     1555   1555  2.19  
LINK         O   ASP H 166                MG    MG H 302     1555   1555  2.22  
LINK         O   SER H 169                MG    MG H 302     1555   1555  2.22  
LINK         O   VAL I 174                MG    MG I 301     1555   1555  2.22  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.21  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.22  
LINK         O   ASP I 204                MG    MG I 305     1555   1555  2.14  
LINK         C   ASP J  90                 N   6V1 J  91     1555   1555  1.34  
LINK         C   6V1 J  91                 N   LEU J  92     1555   1555  1.33  
LINK         N   THR K   1                 C23 6VA c   4     1555   1555  1.52  
LINK         OG1 THR K   1                 C21 6VA c   4     1555   1555  1.44  
LINK         O   THR K 164                MG    MG K 301     1555   1555  2.21  
LINK         O   ASP K 167                MG    MG K 301     1555   1555  2.16  
LINK         O   SER K 170                MG    MG K 301     1555   1555  2.22  
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 304     1555   1555  2.53  
LINK         O   ASP N 167                 K     K N 304     1555   1555  2.62  
LINK         O   SER N 170                 K     K N 304     1555   1555  2.56  
LINK         C   ILE Q  62                 N   YCM Q  63     1555   1555  1.34  
LINK         C   YCM Q  63                 N   ALA Q  64     1555   1555  1.33  
LINK         C   THR S 147                 N   6V1 S 148     1555   1555  1.34  
LINK         C   6V1 S 148                 N   PRO S 149     1555   1555  1.34  
LINK         OG1 THR U  14                 K     K U 302     1555   1555  2.75  
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  2.55  
LINK         O   ASN U 128                 K     K U 302     1555   1555  2.55  
LINK         O   MET U 131                 K     K U 302     1555   1555  2.51  
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  1.32  
LINK         C   6V1 U 161                 N   GLY U 162     1555   1555  1.33  
LINK         OE1 GLN V  91                MG    MG V 301     1555   1555  2.17  
LINK         O   ILE V 163                MG    MG L 303     1555   1555  2.20  
LINK         O   ASP V 166                MG    MG L 303     1555   1555  2.19  
LINK         O   SER V 169                MG    MG L 303     1555   1555  2.21  
LINK         O   VAL W 174                MG    MG W 301     1555   1555  2.23  
LINK         O   ASP W 177                MG    MG W 301     1555   1555  2.25  
LINK         O   SER W 180                MG    MG W 301     1555   1555  2.21  
LINK         O   ASP W 204                MG    MG K 301     1555   1555  2.17  
LINK         C   ASP X  90                 N   6V1 X  91     1555   1555  1.32  
LINK         C   6V1 X  91                 N   LEU X  92     1555   1555  1.32  
LINK         N   THR Y   1                 C23 6VA d   4     1555   1555  1.49  
LINK         OG1 THR Y   1                 C21 6VA d   4     1555   1555  1.42  
LINK         O   THR Y 164                MG    MG I 305     1555   1555  2.18  
LINK         O   ASP Y 167                MG    MG I 305     1555   1555  2.16  
LINK         O   SER Y 170                MG    MG I 305     1555   1555  2.25  
LINK         O   ALA Z 183                 K     K Z 302     1555   1555  2.62  
LINK         O   ASP Z 186                 K     K Z 302     1555   1555  2.63  
LINK         O   THR Z 189                 K     K Z 302     1555   1555  2.59  
LINK         O   ASP Z 213                MG    MG H 302     1555   1555  2.19  
LINK         O   MET b 164                 K     K b 305     1555   1555  2.53  
LINK         O   ASP b 167                 K     K b 305     1555   1555  2.62  
LINK         O   SER b 170                 K     K b 305     1555   1555  2.59  
LINK         C4  6V9 c   1                 N   OAS c   2     1555   1555  1.32  
LINK         C   OAS c   2                 N   OAS c   3     1555   1555  1.32  
LINK         C   OAS c   3                 N3  6VA c   4     1555   1555  1.32  
LINK         C4  6V9 d   1                 N   OAS d   2     1555   1555  1.32  
LINK         C   OAS d   2                 N   OAS d   3     1555   1555  1.36  
LINK         C   OAS d   3                 N3  6VA d   4     1555   1555  1.34  
LINK         K     K G 303                 O   HOH G 462     1555   1555  2.72  
LINK        MG    MG H 301                 O   HOH H 465     1555   1555  2.27  
LINK        MG    MG H 301                 O   HOH N 417     1555   1555  2.16  
LINK        MG    MG H 301                 O   HOH H 511     1555   1555  1.95  
LINK        MG    MG H 301                 O   HOH N 405     1555   1555  2.58  
LINK        MG    MG H 301                 O   HOH N 490     1555   1555  2.30  
LINK        MG    MG H 302                 O   HOH H 484     1555   1555  2.66  
LINK        MG    MG I 301                 O   HOH I 404     1555   1555  2.59  
LINK        MG    MG I 301                 O   HOH I 492     1555   1555  2.15  
LINK        MG    MG I 305                 O   HOH Y 479     1555   1555  2.70  
LINK        MG    MG J 301                 O   HOH J 409     1555   1555  2.26  
LINK        MG    MG J 301                 O   HOH J 449     1555   1555  2.21  
LINK        MG    MG J 301                 O   HOH J 468     1555   1555  2.12  
LINK        MG    MG J 301                 O   HOH J 512     1555   1555  1.93  
LINK        MG    MG J 301                 O   HOH J 527     1555   1555  2.03  
LINK        MG    MG J 301                 O   HOH K 486     1555   1555  1.97  
LINK        MG    MG K 301                 O   HOH K 462     1555   1555  2.72  
LINK         K     K L 302                 O   HOH L 472     1555   1555  2.53  
LINK         K     K L 302                 O   HOH L 457     1555   1555  3.16  
LINK        MG    MG L 303                 O   HOH V 473     1555   1555  2.66  
LINK         K     K N 304                 O   HOH N 543     1555   1555  2.40  
LINK         K     K N 304                 O   HOH N 472     1555   1555  2.50  
LINK         K     K U 302                 O   HOH U 463     1555   1555  2.75  
LINK        MG    MG V 301                 O   HOH V 462     1555   1555  1.94  
LINK        MG    MG V 301                 O   HOH V 470     1555   1555  2.01  
LINK        MG    MG V 301                 O   HOH b 412     1555   1555  2.10  
LINK        MG    MG V 301                 O   HOH b 441     1555   1555  2.17  
LINK        MG    MG V 301                 O   HOH b 425     1555   1555  2.43  
LINK        MG    MG W 301                 O   HOH W 455     1555   1555  2.31  
LINK        MG    MG W 301                 O   HOH W 459     1555   1555  2.11  
LINK        MG    MG X 301                 O   HOH X 409     1555   1555  2.04  
LINK        MG    MG X 301                 O   HOH X 440     1555   1555  2.07  
LINK        MG    MG X 301                 O   HOH X 519     1555   1555  2.14  
LINK        MG    MG X 301                 O   HOH Y 509     1555   1555  2.15  
LINK        MG    MG X 301                 O   HOH X 441     1555   1555  2.19  
LINK        MG    MG X 301                 O   HOH X 509     1555   1555  2.19  
LINK         K     K Z 302                 O   HOH Z 461     1555   1555  3.26  
LINK         K     K Z 302                 O   HOH H 464     1555   1555  3.13  
LINK         K     K Z 302                 O   HOH Z 473     1555   1555  2.55  
LINK         K     K b 305                 O   HOH b 468     1555   1555  2.54  
LINK         K     K b 305                 O   HOH b 470     1555   1555  3.46  
LINK         K     K b 305                 O   HOH b 508     1555   1555  2.39  
CISPEP   1 VAL B  203    SER B  204          0        17.26                     
CISPEP   2 LYS C   47    LYS C   48          0         5.20                     
CISPEP   3 GLY C  202    GLY C  203          0        -5.05                     
CISPEP   4 GLY C  203    LYS C  204          0        29.19                     
CISPEP   5 ARG H  187    PRO H  188          0        -6.04                     
CISPEP   6 ARG H  187    PRO H  188          0        -5.99                     
CISPEP   7 GLY M  201    PRO M  202          0        -5.11                     
CISPEP   8 ILE P   52    HIS P   53          0       -20.75                     
CISPEP   9 LYS Q  204    ASN Q  205          0        -6.75                     
CISPEP  10 LEU Q  220    ASN Q  221          0         1.29                     
CISPEP  11 GLU S  234    GLY S  235          0        -8.17                     
CISPEP  12 GLU S  238    ARG S  239          0       -11.98                     
CISPEP  13 GLY T    6    TYR T    7          0       -24.68                     
CISPEP  14 ARG V  187    PRO V  188          0        -5.46                     
CISPEP  15 GLY a  201    PRO a  202          0        -3.88                     
CISPEP  16 GLY a  201    PRO a  202          0        -1.44                     
SITE     1 AC1  4 SER A   6  HOH A 435  ARG C   5  HOH C 419                    
SITE     1 AC2  1 ARG A 219                                                     
SITE     1 AC3  2 HIS A  87  ARG A  90                                          
SITE     1 AC4  3 THR A  68  HOH A 453  HOH A 470                               
SITE     1 AC5  6 ASN B  69  GLU B  70  GLN B  95   CL B 302                    
SITE     2 AC5  6 HOH B 495  HOH I 544                                          
SITE     1 AC6  2  CL B 301  HOH B 453                                          
SITE     1 AC7  1 GLY C 162                                                     
SITE     1 AC8  3 ARG C  86  ARG C 117  HOH C 446                               
SITE     1 AC9  4 ILE D  31  ILE D 170  GLY D 171  SER D 174                    
SITE     1 AD1  4 THR D 161  LEU E  77  THR E  78  HOH E 464                    
SITE     1 AD2  6 LYS E  30  6V1 E 148  ILE E 161  GLY E 162                    
SITE     2 AD2  6 SER E 165  HOH E 517                                          
SITE     1 AD3  2 6V1 E 148  SER E 150                                          
SITE     1 AD4  4 GLY E  32  SER E  33  LYS E  62  GLY E  76                    
SITE     1 AD5  6 VAL F  30  ILE F 165  GLY F 166  ARG F 169                    
SITE     2 AD5  6 HOH F 401  HOH F 452                                          
SITE     1 AD6  3 HOH G 427  HOH G 440  HOH N 418                               
SITE     1 AD7  4 LYS G 186  GLU G 192  GLN G 193  THR G 197                    
SITE     1 AD8  5 THR G  14  TYR G 125  ASN G 128  MET G 131                    
SITE     2 AD8  5 HOH G 462                                                     
SITE     1 AD9  7 GLN H  91  HOH H 465  HOH H 511  ASP N  51                    
SITE     2 AD9  7 HOH N 405  HOH N 417  HOH N 490                               
SITE     1 AE1  5 ILE H 163  ASP H 166  SER H 169  HOH H 484                    
SITE     2 AE1  5 ASP Z 213                                                     
SITE     1 AE2  3 GLY H 128  SER H 129  HOH H 542                               
SITE     1 AE3  3 ASN H  80  ARG H  81  HOH H 521                               
SITE     1 AE4  7 TYR G 103  PHE H  88  GLN H  91  HOH H 436                    
SITE     2 AE4  7 HOH H 442  HOH H 479  TYR N  90                               
SITE     1 AE5  3 SER H 129  HOH H 473  THR N  22                               
SITE     1 AE6  5 VAL I 174  ASP I 177  SER I 180  HOH I 404                    
SITE     2 AE6  5 HOH I 492                                                     
SITE     1 AE7  2 ARG I  65  ARG I  69                                          
SITE     1 AE8  3 GLU I  96  LYS I  97  ASP J  90                               
SITE     1 AE9  3 LEU H  58  TYR H  90  TYR I  95                               
SITE     1 AF1  5 ASP I 204  THR Y 164  ASP Y 167  SER Y 170                    
SITE     2 AF1  5 HOH Y 479                                                     
SITE     1 AF2  6 HOH J 409  HOH J 449  HOH J 468  HOH J 512                    
SITE     2 AF2  6 HOH J 527  HOH K 486                                          
SITE     1 AF3  5 THR K 164  ASP K 167  SER K 170  HOH K 462                    
SITE     2 AF3  5 ASP W 204                                                     
SITE     1 AF4  3 GLY K 129  SER K 130  6VA c   4                               
SITE     1 AF5  2 LYS K  32  ASN K 175                                          
SITE     1 AF6  3 TYR K  66  ARG K  69  HOH K 445                               
SITE     1 AF7  2 ILE K 121  SER K 122                                          
SITE     1 AF8  4 PHE K  54  SER L  98  PHE L 101  HOH L 452                    
SITE     1 AF9  4 ALA L 183  ASP L 186  THR L 189  HOH L 472                    
SITE     1 AG1  5 ASP L 213  ILE V 163  ASP V 166  SER V 169                    
SITE     2 AG1  5 HOH V 473                                                     
SITE     1 AG2  4 PHE M  36  ARG M  37  ASN M  38  HOH N 493                    
SITE     1 AG3  6 ARG M  35   CL M 303  SER N  46  GLY N  97                    
SITE     2 AG3  6 GLY N 128  GLY N 129                                          
SITE     1 AG4  5 TYR M  30  ARG M  35   CL M 302  PRO N 115                    
SITE     2 AG4  5 MET N 116                                                     
SITE     1 AG5  1 ARG M  44                                                     
SITE     1 AG6  3 TYR M 144  SER V 129  THR b  22                               
SITE     1 AG7  3 THR N  31  ARG N  45  GLN N  53                               
SITE     1 AG8  3 THR N   1  GLY N 129  SER N 130                               
SITE     1 AG9  5 ARG N  19  ARG N  29  GLY N 171  GLY N 172                    
SITE     2 AG9  5 HOH a 438                                                     
SITE     1 AH1  5 MET N 164  ASP N 167  SER N 170  HOH N 472                    
SITE     2 AH1  5 HOH N 543                                                     
SITE     1 AH2  4 SER O   6  PHE O   7  ARG Q   5  HOH Q 440                    
SITE     1 AH3  1 TYR O 100                                                     
SITE     1 AH4  2 ARG O 218  ARG O 219                                          
SITE     1 AH5  2 HIS O  87  ARG O  90                                          
SITE     1 AH6  4 ASN P  69  GLU P  70  GLN P  95  HOH P 507                    
SITE     1 AH7  1 ARG Q  95                                                     
SITE     1 AH8  3 ILE Q 161  GLY Q 162  HOH Q 408                               
SITE     1 AH9  6 ILE R  31  ILE R 170  GLY R 171  SER R 174                    
SITE     2 AH9  6 HOH R 453  HOH R 506                                          
SITE     1 AI1  3 THR R 161  HOH R 446  THR S  78                               
SITE     1 AI2  4 ILE S 161  GLY S 162  SER S 165  HOH S 503                    
SITE     1 AI3  3 SER S 150  ASN S 152  HOH S 401                               
SITE     1 AI4  5 GLY S  32  SER S  33  LYS S  62  ALA S  75                    
SITE     2 AI4  5 GLY S  76                                                     
SITE     1 AI5  4 LYS U 102  HOH U 429  HOH U 434  HOH b 424                    
SITE     1 AI6  5 THR U  14  TYR U 125  ASN U 128  MET U 131                    
SITE     2 AI6  5 HOH U 463                                                     
SITE     1 AI7  7 GLN V  91  HOH V 462  HOH V 470  ASP b  93                    
SITE     2 AI7  7 HOH b 412  HOH b 425  HOH b 441                               
SITE     1 AI8  2 GLY V 128  SER V 129                                          
SITE     1 AI9  2 ASN V  80  ARG V  81                                          
SITE     1 AJ1  5 TYR U 103  ARG V  89  GLN V  91  HOH V 499                    
SITE     2 AJ1  5 TYR b  61                                                     
SITE     1 AJ2  5 VAL W 174  ASP W 177  SER W 180  HOH W 455                    
SITE     2 AJ2  5 HOH W 459                                                     
SITE     1 AJ3  2 ARG W  65  ARG W  69                                          
SITE     1 AJ4  4 GLU W  96  LYS W  97  HOH W 462  ASP X  90                    
SITE     1 AJ5  6 HOH X 409  HOH X 440  HOH X 441  HOH X 509                    
SITE     2 AJ5  6 HOH X 519  HOH Y 509                                          
SITE     1 AJ6  3 GLY Y 129  SER Y 130  6VA d   4                               
SITE     1 AJ7  3 TYR Y  66  ARG Y  69  HOH Y 498                               
SITE     1 AJ8  2 LYS Y  32  ASN Y 175                                          
SITE     1 AJ9  2 ILE Y 121  SER Y 122                                          
SITE     1 AK1  3 ASP Y 154  LEU Y 155  HOH Y 486                               
SITE     1 AK2  6 HOH R 490  PHE Y  54  TYR Z  97  SER Z  98                    
SITE     2 AK2  6 PHE Z 101  HOH Z 468                                          
SITE     1 AK3  4 ALA Z 183  ASP Z 186  THR Z 189  HOH Z 473                    
SITE     1 AK4  5 PHE a  36  ARG a  37  ASN a  38  ILE a  39                    
SITE     2 AK4  5 HOH b 499                                                     
SITE     1 AK5  5 TYR a  30  ARG a  35  PRO b 115  MET b 116                    
SITE     2 AK5  5  CL b 302                                                     
SITE     1 AK6  2 MET a  43  ARG a  44                                          
SITE     1 AK7  3 THR b   1  GLY b 129  SER b 130                               
SITE     1 AK8  5 ARG a  35   CL a 302  SER b  46  GLY b 128                    
SITE     2 AK8  5 GLY b 129                                                     
SITE     1 AK9  4 HOH M 437  ARG b  19  ARG b  29  GLY b 172                    
SITE     1 AL1  4 HOH V 461  THR b  31  ARG b  45  GLN b  53                    
SITE     1 AL2  5 MET b 164  ASP b 167  SER b 170  HOH b 468                    
SITE     2 AL2  5 HOH b 508                                                     
SITE     1 AL3 16 THR K   1  ARG K  19  ALA K  20  THR K  21                    
SITE     2 AL3 16 VAL K  31  MET K  45  GLY K  47  ALA K  49                    
SITE     3 AL3 16 SER K 130  TYR K 169   CL K 302  HOH K 406                    
SITE     4 AL3 16 ASP L 125  VAL L 127  HOH L 415  HOH c 101                    
SITE     1 AL4 11 THR K   1  ARG K  19  VAL K  31  MET K  45                    
SITE     2 AL4 11 GLY K  47  ALA K  49  SER K 130  TYR K 169                    
SITE     3 AL4 11  CL K 302  HOH K 406  OAS c   3                               
SITE     1 AL5 16 THR Y   1  ARG Y  19  ALA Y  20  THR Y  21                    
SITE     2 AL5 16 VAL Y  31  MET Y  45  GLY Y  47  ALA Y  49                    
SITE     3 AL5 16 SER Y 130  TYR Y 169   CL Y 301  HOH Y 444                    
SITE     4 AL5 16 HOH Y 470  ASP Z 125  PRO Z 126  HOH Z 417                    
SITE     1 AL6 11 THR Y   1  ARG Y  19  VAL Y  31  MET Y  45                    
SITE     2 AL6 11 GLY Y  47  ALA Y  49  SER Y 130  TYR Y 169                    
SITE     3 AL6 11  CL Y 301  HOH Y 444  OAS d   3                               
CRYST1  113.390  202.650  315.140  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      0.008819  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004935  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003173        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system