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Database: PDB
Entry: 5LF6
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HEADER    HYDROLASE                               30-JUN-16   5LF6              
TITLE     HUMAN 20S PROTEASOME COMPLEX WITH Z-LLY-KETOALDEHYDE AT 2.1 ANGSTROM  
CAVEAT     5LF6    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: LLY-KETOALDEHYDE PEPTIDE;                                  
COMPND  64 CHAIN: c, d;                                                         
COMPND  65 ENGINEERED: YES;                                                     
COMPND  66 MOL_ID: 12;                                                          
COMPND  67 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  68 CHAIN: K, Y;                                                         
COMPND  69 SYNONYM: MACROPAIN EPSILON CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  70 EPSILON CHAIN,PROTEASOME CHAIN 6,PROTEASOME EPSILON CHAIN,PROTEASOME 
COMPND  71 SUBUNIT MB1,PROTEASOME SUBUNIT X;                                    
COMPND  72 EC: 3.4.25.1;                                                        
COMPND  73 MOL_ID: 13;                                                          
COMPND  74 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  75 CHAIN: L, Z;                                                         
COMPND  76 SYNONYM: MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  77 SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN;           
COMPND  78 EC: 3.4.25.1;                                                        
COMPND  79 MOL_ID: 14;                                                          
COMPND  80 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  81 CHAIN: M, a;                                                         
COMPND  82 SYNONYM: 26 KDA PROSOMAL PROTEIN,PROS-26,MACROPAIN BETA CHAIN,       
COMPND  83 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN,PROTEASOME BETA      
COMPND  84 CHAIN,PROTEASOME CHAIN 3,HSN3;                                       
COMPND  85 EC: 3.4.25.1;                                                        
COMPND  86 MOL_ID: 15;                                                          
COMPND  87 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  88 CHAIN: N, b;                                                         
COMPND  89 SYNONYM: MACROPAIN DELTA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  90 DELTA CHAIN,PROTEASOME DELTA CHAIN,PROTEASOME SUBUNIT Y;             
COMPND  91 EC: 3.4.25.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HELA;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: HELA;                                                     
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: HELA;                                                     
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: HELA;                                                     
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 CELL_LINE: HELA;                                                     
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 CELL_LINE: HELA;                                                     
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 CELL_LINE: HELA;                                                     
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 CELL_LINE: HELA;                                                     
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 CELL_LINE: HELA;                                                     
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606;                                                
SOURCE  50 CELL_LINE: HELA;                                                     
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 SYNTHETIC: YES;                                                      
SOURCE  53 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  54 ORGANISM_COMMON: HUMAN;                                              
SOURCE  55 ORGANISM_TAXID: 9606;                                                
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 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  73 ORGANISM_COMMON: HUMAN;                                              
SOURCE  74 ORGANISM_TAXID: 9606;                                                
SOURCE  75 CELL_LINE: HELA                                                      
KEYWDS    PROTEASOME, MULTICATALYTIC PROTEINASE, NTN-HYDROLASE, HYDROLASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHRADER,F.HENNEBERG,R.MATA,K.TITTMANN,T.R.SCHNEIDER,H.STARK,       
AUTHOR   2 G.BOURENKOV,A.CHARI                                                  
REVDAT   2   06-SEP-17 5LF6    1       REMARK                                   
REVDAT   1   17-AUG-16 5LF6    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.    2.07 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) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 171.02                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 403247                         
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 21152                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 16897                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 893                          
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 47933                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 3501                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.35000                                             
REMARK   3    B22 (A**2) : 1.13000                                              
REMARK   3    B33 (A**2) : 1.21000                                              
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): 0.205         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.503        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 49344 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 46892 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 66756 ; 1.743 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):107642 ; 1.281 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6303 ; 7.205 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2126 ;35.042 ;23.711       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8271 ;15.522 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   340 ;17.679 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7541 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 56166 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11214 ; 0.004 ; 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): 25033 ; 1.664 ; 2.885       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25032 ; 1.664 ; 2.885       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31274 ; 2.755 ; 4.318       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31275 ; 2.755 ; 4.318       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 24311 ; 2.249 ; 3.137       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 24311 ; 2.249 ; 3.137       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 35442 ; 3.484 ; 4.597       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 57201 ; 8.994 ;24.415       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 57202 ; 8.994 ;24.416       
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   25942  0.07  0.05     
REMARK   3    2     B     2    249       P     2    249   27828  0.08  0.05     
REMARK   3    3     C     2    237       Q     2    237   25130  0.10  0.05     
REMARK   3    4     D     9    241       R     9    241   26352  0.08  0.05     
REMARK   3    5     E     4    236       S     4    236   27320  0.08  0.05     
REMARK   3    6     F     6    243       T     6    243   28024  0.08  0.05     
REMARK   3    7     G     2    245       U     2    245   26430  0.08  0.05     
REMARK   3    8     H     1    220       V     1    220   24744  0.06  0.05     
REMARK   3    9     I     1    204       W     1    204   25698  0.07  0.05     
REMARK   3   10     J     1    196       X     1    196   24512  0.08  0.05     
REMARK   3   11     K     1    199       Y     1    199   23284  0.09  0.05     
REMARK   3   12     L     1    213       Z     1    213   24754  0.07  0.05     
REMARK   3   13     M     1    216       a     1    216   24916  0.07  0.05     
REMARK   3   14     N     1    201       b     1    201   22966  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):  76.9060 206.7490   1.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4575 T22:   0.2226                                     
REMARK   3      T33:   0.0896 T12:   0.1246                                     
REMARK   3      T13:   0.0672 T23:   0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5522 L22:   0.7489                                     
REMARK   3      L33:   0.4515 L12:   0.2411                                     
REMARK   3      L13:   0.1751 L23:  -0.0154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0101 S12:   0.0310 S13:   0.0020                       
REMARK   3      S21:  -0.1218 S22:  -0.0800 S23:  -0.1316                       
REMARK   3      S31:   0.1879 S32:   0.2237 S33:   0.0700                       
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):  64.8610 177.8030  -0.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7796 T22:   0.0505                                     
REMARK   3      T33:   0.0504 T12:   0.1621                                     
REMARK   3      T13:   0.0698 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3979 L22:   0.3775                                     
REMARK   3      L33:   0.3907 L12:   0.0097                                     
REMARK   3      L13:   0.0603 L23:  -0.2964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0312 S12:   0.0454 S13:  -0.0593                       
REMARK   3      S21:  -0.2233 S22:  -0.0360 S23:  -0.0365                       
REMARK   3      S31:   0.3403 S32:   0.0661 S33:   0.0672                       
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):  34.1560 169.7140  -3.9070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9418 T22:   0.0384                                     
REMARK   3      T33:   0.1068 T12:  -0.1026                                     
REMARK   3      T13:  -0.1059 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0043 L22:   0.1946                                     
REMARK   3      L33:   0.2534 L12:  -0.2168                                     
REMARK   3      L13:  -0.0315 L23:   0.0471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0172 S12:  -0.0172 S13:  -0.2427                       
REMARK   3      S21:  -0.0849 S22:   0.0514 S23:  -0.0032                       
REMARK   3      S31:   0.2301 S32:  -0.0643 S33:  -0.0686                       
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):  10.3650 188.5980  -7.8440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7092 T22:   0.2070                                     
REMARK   3      T33:   0.0709 T12:  -0.2317                                     
REMARK   3      T13:  -0.2117 T23:   0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3954 L22:   0.9688                                     
REMARK   3      L33:   0.5370 L12:  -0.0670                                     
REMARK   3      L13:  -0.2196 L23:  -0.2417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:   0.0810 S13:  -0.0044                       
REMARK   3      S21:  -0.2645 S22:   0.1177 S23:   0.1291                       
REMARK   3      S31:   0.2981 S32:  -0.3120 S33:  -0.1283                       
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:   0.4614 T22:   0.2088                                     
REMARK   3      T33:   0.1164 T12:  -0.0663                                     
REMARK   3      T13:  -0.0639 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4469 L22:   0.2980                                     
REMARK   3      L33:   0.8203 L12:  -0.2788                                     
REMARK   3      L13:   0.0454 L23:   0.1030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:  -0.0063 S13:  -0.1503                       
REMARK   3      S21:  -0.0349 S22:  -0.0157 S23:   0.0687                       
REMARK   3      S31:   0.1291 S32:  -0.2754 S33:  -0.0335                       
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:   0.4619 T22:   0.1104                                     
REMARK   3      T33:   0.1380 T12:   0.0076                                     
REMARK   3      T13:  -0.0280 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6129 L22:   0.2728                                     
REMARK   3      L33:   0.2957 L12:  -0.0981                                     
REMARK   3      L13:   0.0731 L23:  -0.0563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0130 S12:   0.0277 S13:   0.0856                       
REMARK   3      S21:  -0.0353 S22:  -0.0214 S23:   0.0310                       
REMARK   3      S31:   0.0142 S32:  -0.0148 S33:   0.0084                       
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:   0.4557 T22:   0.1799                                     
REMARK   3      T33:   0.1278 T12:   0.0154                                     
REMARK   3      T13:   0.0236 T23:   0.0849                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3007 L22:   0.6606                                     
REMARK   3      L33:   0.2691 L12:   0.0235                                     
REMARK   3      L13:  -0.0566 L23:   0.1804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0571 S12:   0.0726 S13:   0.0847                       
REMARK   3      S21:  -0.0915 S22:  -0.0942 S23:  -0.0404                       
REMARK   3      S31:   0.0174 S32:   0.1175 S33:   0.0371                       
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:   0.4075 T22:   0.2484                                     
REMARK   3      T33:   0.1145 T12:  -0.0036                                     
REMARK   3      T13:   0.0334 T23:   0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0088 L22:   0.3745                                     
REMARK   3      L33:   0.3924 L12:   0.0162                                     
REMARK   3      L13:  -0.0051 L23:  -0.2637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:  -0.0065 S13:  -0.0033                       
REMARK   3      S21:  -0.0450 S22:  -0.0936 S23:   0.0154                       
REMARK   3      S31:   0.0028 S32:   0.2642 S33:   0.0872                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5710 186.5180  39.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5046 T22:   0.1708                                     
REMARK   3      T33:   0.0898 T12:   0.1047                                     
REMARK   3      T13:   0.0484 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2689 L22:   0.2960                                     
REMARK   3      L33:   0.9610 L12:   0.1261                                     
REMARK   3      L13:   0.0030 L23:  -0.4276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0012 S12:  -0.0163 S13:   0.0106                       
REMARK   3      S21:  -0.1114 S22:  -0.0981 S23:   0.0042                       
REMARK   3      S31:   0.2063 S32:   0.2391 S33:   0.0993                       
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:   0.6561 T22:   0.0113                                     
REMARK   3      T33:   0.1014 T12:  -0.0120                                     
REMARK   3      T13:  -0.0226 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4307 L22:   0.1949                                     
REMARK   3      L33:   1.2045 L12:   0.0585                                     
REMARK   3      L13:  -0.2559 L23:  -0.0713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0440 S12:   0.0334 S13:  -0.0366                       
REMARK   3      S21:  -0.1367 S22:   0.0036 S23:   0.0669                       
REMARK   3      S31:   0.3738 S32:  -0.0167 S33:   0.0404                       
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:   0.5206 T22:   0.1919                                     
REMARK   3      T33:   0.1280 T12:  -0.2185                                     
REMARK   3      T13:  -0.1291 T23:   0.1204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1724 L22:   0.5859                                     
REMARK   3      L33:   1.0406 L12:  -0.0190                                     
REMARK   3      L13:  -0.1979 L23:   0.0914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0371 S12:   0.0306 S13:  -0.0056                       
REMARK   3      S21:  -0.1503 S22:   0.1063 S23:   0.0754                       
REMARK   3      S31:   0.3082 S32:  -0.2790 S33:  -0.1434                       
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:   0.3602 T22:   0.3626                                     
REMARK   3      T33:   0.1312 T12:  -0.0865                                     
REMARK   3      T13:  -0.0858 T23:   0.1938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1656 L22:   0.4475                                     
REMARK   3      L33:   0.6985 L12:   0.0635                                     
REMARK   3      L13:  -0.1739 L23:   0.0939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0265 S12:  -0.0041 S13:   0.0013                       
REMARK   3      S21:  -0.1160 S22:   0.1564 S23:   0.0782                       
REMARK   3      S31:   0.0364 S32:  -0.3027 S33:  -0.1829                       
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:   0.4398 T22:   0.1945                                     
REMARK   3      T33:   0.1457 T12:   0.0649                                     
REMARK   3      T13:   0.0156 T23:   0.0756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1244 L22:   0.2149                                     
REMARK   3      L33:   0.8443 L12:  -0.0254                                     
REMARK   3      L13:  -0.1129 L23:  -0.2119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:   0.0255 S13:   0.0130                       
REMARK   3      S21:   0.0310 S22:   0.1381 S23:   0.0298                       
REMARK   3      S31:  -0.1575 S32:  -0.1786 S33:  -0.1340                       
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:   0.4949 T22:   0.0959                                     
REMARK   3      T33:   0.1202 T12:  -0.0480                                     
REMARK   3      T13:   0.0057 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3007 L22:   0.2961                                     
REMARK   3      L33:   0.8874 L12:  -0.0135                                     
REMARK   3      L13:  -0.0515 L23:  -0.2220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:   0.0557 S13:   0.0042                       
REMARK   3      S21:   0.0436 S22:  -0.0356 S23:   0.0096                       
REMARK   3      S31:  -0.1715 S32:   0.0645 S33:  -0.0032                       
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:   0.4214 T22:   0.3645                                     
REMARK   3      T33:   0.1544 T12:   0.2550                                     
REMARK   3      T13:   0.2082 T23:   0.1425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3827 L22:   1.1783                                     
REMARK   3      L33:   0.4386 L12:   0.1767                                     
REMARK   3      L13:   0.1202 L23:   0.1894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0325 S12:  -0.0794 S13:   0.0611                       
REMARK   3      S21:   0.1297 S22:   0.0409 S23:   0.2960                       
REMARK   3      S31:  -0.2227 S32:  -0.2936 S33:  -0.0733                       
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):  -8.1010 194.5600 104.9280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3261 T22:   0.4471                                     
REMARK   3      T33:   0.1867 T12:  -0.0131                                     
REMARK   3      T13:   0.1276 T23:   0.2333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0886 L22:   0.7411                                     
REMARK   3      L33:   0.4118 L12:  -0.0257                                     
REMARK   3      L13:   0.0514 L23:   0.1472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:  -0.0329 S13:  -0.0304                       
REMARK   3      S21:   0.1244 S22:   0.1443 S23:   0.2018                       
REMARK   3      S31:  -0.0106 S32:  -0.3029 S33:  -0.1367                       
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):  15.7790 174.6050 109.6110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4811 T22:   0.1730                                     
REMARK   3      T33:   0.2085 T12:  -0.0717                                     
REMARK   3      T13:  -0.0072 T23:   0.0984                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4203 L22:   0.1872                                     
REMARK   3      L33:   0.5324 L12:  -0.0514                                     
REMARK   3      L13:   0.1947 L23:   0.1100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0978 S12:  -0.0123 S13:  -0.3715                       
REMARK   3      S21:   0.1121 S22:   0.0832 S23:   0.0360                       
REMARK   3      S31:   0.1404 S32:  -0.1542 S33:  -0.1811                       
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):  45.9470 181.8370 112.7750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4609 T22:   0.1599                                     
REMARK   3      T33:   0.0972 T12:   0.0082                                     
REMARK   3      T13:   0.0433 T23:   0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4192 L22:   0.2747                                     
REMARK   3      L33:   0.6483 L12:  -0.1667                                     
REMARK   3      L13:  -0.0781 L23:  -0.2191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0640 S12:  -0.0466 S13:  -0.0621                       
REMARK   3      S21:  -0.0185 S22:   0.0699 S23:   0.0381                       
REMARK   3      S31:   0.1157 S32:   0.0882 S33:  -0.0058                       
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):  59.0710 210.3000 113.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4782 T22:   0.2514                                     
REMARK   3      T33:   0.0524 T12:  -0.0834                                     
REMARK   3      T13:   0.0042 T23:   0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3875 L22:   0.4307                                     
REMARK   3      L33:   0.7279 L12:  -0.0856                                     
REMARK   3      L13:   0.0875 L23:  -0.2945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0174 S12:  -0.0692 S13:  -0.0457                       
REMARK   3      S21:   0.1017 S22:  -0.0607 S23:  -0.0093                       
REMARK   3      S31:  -0.1813 S32:   0.2860 S33:   0.0781                       
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):  46.6700 237.8720 111.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7893 T22:   0.0707                                     
REMARK   3      T33:   0.0318 T12:  -0.0951                                     
REMARK   3      T13:   0.0814 T23:  -0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0092 L22:   0.3170                                     
REMARK   3      L33:   0.5637 L12:   0.0362                                     
REMARK   3      L13:  -0.2514 L23:   0.0192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0997 S12:  -0.1746 S13:   0.0459                       
REMARK   3      S21:   0.0770 S22:  -0.0371 S23:   0.0284                       
REMARK   3      S31:  -0.4682 S32:   0.0627 S33:  -0.0626                       
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):  16.2340 244.6230 107.3910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8141 T22:   0.1722                                     
REMARK   3      T33:   0.0936 T12:   0.2389                                     
REMARK   3      T13:   0.1535 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7734 L22:   0.3664                                     
REMARK   3      L33:   0.0968 L12:   0.1629                                     
REMARK   3      L13:  -0.0611 L23:  -0.0044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:  -0.1391 S13:   0.1484                       
REMARK   3      S21:   0.0950 S22:   0.0169 S23:   0.0334                       
REMARK   3      S31:  -0.2062 S32:  -0.1006 S33:  -0.0199                       
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):   1.1830 230.2430  64.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4223 T22:   0.3549                                     
REMARK   3      T33:   0.1536 T12:   0.1735                                     
REMARK   3      T13:   0.1121 T23:   0.1644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1695 L22:   0.5534                                     
REMARK   3      L33:   0.3962 L12:   0.2401                                     
REMARK   3      L13:   0.0574 L23:   0.0912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0212 S12:   0.0199 S13:   0.0076                       
REMARK   3      S21:   0.0726 S22:   0.1358 S23:   0.0707                       
REMARK   3      S31:  -0.2079 S32:  -0.3205 S33:  -0.1570                       
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):  -6.2100 202.9450  65.0870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2897 T22:   0.4303                                     
REMARK   3      T33:   0.1696 T12:  -0.0274                                     
REMARK   3      T13:   0.0316 T23:   0.2226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0860 L22:   0.4953                                     
REMARK   3      L33:   1.3325 L12:  -0.1122                                     
REMARK   3      L13:   0.0284 L23:   0.2887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0271 S12:  -0.0312 S13:   0.0123                       
REMARK   3      S21:   0.0403 S22:   0.1803 S23:   0.0467                       
REMARK   3      S31:   0.0247 S32:  -0.4457 S33:  -0.2074                       
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):  11.6500 176.6690  68.7380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4371 T22:   0.1702                                     
REMARK   3      T33:   0.1521 T12:  -0.1416                                     
REMARK   3      T13:  -0.0249 T23:   0.0989                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2238 L22:   0.3951                                     
REMARK   3      L33:   0.8638 L12:  -0.0264                                     
REMARK   3      L13:  -0.1551 L23:  -0.0358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0292 S12:  -0.0441 S13:   0.0159                       
REMARK   3      S21:  -0.0288 S22:   0.0998 S23:   0.0419                       
REMARK   3      S31:   0.2276 S32:  -0.1623 S33:  -0.0706                       
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):  44.1640 172.9570  72.7160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5061 T22:   0.0940                                     
REMARK   3      T33:   0.1000 T12:   0.0146                                     
REMARK   3      T13:   0.0033 T23:   0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4505 L22:   0.4627                                     
REMARK   3      L33:   0.9868 L12:   0.1578                                     
REMARK   3      L13:  -0.1972 L23:  -0.1531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0198 S12:  -0.0875 S13:   0.0327                       
REMARK   3      S21:  -0.0460 S22:  -0.0322 S23:   0.0116                       
REMARK   3      S31:   0.2350 S32:   0.0668 S33:   0.0124                       
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):  65.4290 195.8260  73.7670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4188 T22:   0.2351                                     
REMARK   3      T33:   0.1108 T12:   0.0060                                     
REMARK   3      T13:   0.0052 T23:   0.0502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1608 L22:   0.4193                                     
REMARK   3      L33:   0.6216 L12:  -0.1410                                     
REMARK   3      L13:  -0.1261 L23:  -0.2145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0353 S12:  -0.0364 S13:   0.0106                       
REMARK   3      S21:   0.0127 S22:  -0.1060 S23:   0.0230                       
REMARK   3      S31:   0.0340 S32:   0.2253 S33:   0.0708                       
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):  60.6350 228.5340  70.9650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4818 T22:   0.1665                                     
REMARK   3      T33:   0.0910 T12:  -0.0979                                     
REMARK   3      T13:  -0.0087 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2015 L22:   0.2138                                     
REMARK   3      L33:   0.9104 L12:  -0.0439                                     
REMARK   3      L13:  -0.0949 L23:  -0.2485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0057 S12:  -0.0263 S13:  -0.0018                       
REMARK   3      S21:   0.1084 S22:  -0.0520 S23:   0.0299                       
REMARK   3      S31:  -0.2218 S32:   0.1952 S33:   0.0463                       
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):  32.6690 245.3540  67.9690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6033 T22:   0.0461                                     
REMARK   3      T33:   0.0892 T12:   0.0460                                     
REMARK   3      T13:   0.0553 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2509 L22:   0.2839                                     
REMARK   3      L33:   1.0569 L12:   0.0115                                     
REMARK   3      L13:   0.0020 L23:  -0.1601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:  -0.0214 S13:  -0.0099                       
REMARK   3      S21:   0.1070 S22:   0.0389 S23:   0.0370                       
REMARK   3      S31:  -0.3229 S32:  -0.0803 S33:  -0.0410                       
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 5LF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : CRL TRANSFOCATOR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 403247                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 171.020                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 6.920                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.3                               
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         : 0.600                              
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       56.93500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      157.81500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.74000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      157.81500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.93500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.74000            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: 30-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 30-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 128080 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 209550 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1109.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: c, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U, V, W, X, d, Y, Z, a,         
REMARK 350                    AND CHAINS: b                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     LYS B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     LYS B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     GLN B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C   239                                                      
REMARK 465     GLU C   240                                                      
REMARK 465     LYS C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     LYS C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     ALA C   247                                                      
REMARK 465     SER C   248                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PHE D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PHE E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     GLU E   238                                                      
REMARK 465     ARG E   239                                                      
REMARK 465     PRO E   240                                                      
REMARK 465     GLN E   241                                                      
REMARK 465     ARG E   242                                                      
REMARK 465     LYS E   243                                                      
REMARK 465     ALA E   244                                                      
REMARK 465     GLN E   245                                                      
REMARK 465     PRO E   246                                                      
REMARK 465     ALA E   247                                                      
REMARK 465     GLN E   248                                                      
REMARK 465     PRO E   249                                                      
REMARK 465     ALA E   250                                                      
REMARK 465     ASP E   251                                                      
REMARK 465     GLU E   252                                                      
REMARK 465     PRO E   253                                                      
REMARK 465     ALA E   254                                                      
REMARK 465     GLU E   255                                                      
REMARK 465     LYS E   256                                                      
REMARK 465     ALA E   257                                                      
REMARK 465     ASP E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     PRO E   260                                                      
REMARK 465     MET E   261                                                      
REMARK 465     GLU E   262                                                      
REMARK 465     HIS E   263                                                      
REMARK 465     MET F     0                                                      
REMARK 465     SER F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ILE F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F   245                                                      
REMARK 465     GLU F   246                                                      
REMARK 465     ASP F   247                                                      
REMARK 465     GLU F   248                                                      
REMARK 465     SER F   249                                                      
REMARK 465     ASP F   250                                                      
REMARK 465     ASP F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     ASN F   253                                                      
REMARK 465     MET F   254                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ASP G   246                                                      
REMARK 465     ILE H   221                                                      
REMARK 465     GLU H   222                                                      
REMARK 465     VAL H   223                                                      
REMARK 465     LEU H   224                                                      
REMARK 465     GLU H   225                                                      
REMARK 465     GLU H   226                                                      
REMARK 465     THR H   227                                                      
REMARK 465     VAL H   228                                                      
REMARK 465     GLN H   229                                                      
REMARK 465     THR H   230                                                      
REMARK 465     MET H   231                                                      
REMARK 465     ASP H   232                                                      
REMARK 465     THR H   233                                                      
REMARK 465     SER H   234                                                      
REMARK 465     MET I     0                                                      
REMARK 465     PRO J   197                                                      
REMARK 465     LYS J   198                                                      
REMARK 465     GLN J   199                                                      
REMARK 465     GLY J   200                                                      
REMARK 465     SER J   201                                                      
REMARK 465     GLY K   205                                                      
REMARK 465     SER K   206                                                      
REMARK 465     THR K   207                                                      
REMARK 465     PRO K   208                                                      
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     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   241                                                      
REMARK 465     LYS Q   242                                                      
REMARK 465     LYS Q   243                                                      
REMARK 465     GLN Q   244                                                      
REMARK 465     LYS Q   245                                                      
REMARK 465     LYS Q   246                                                      
REMARK 465     ALA Q   247                                                      
REMARK 465     SER Q   248                                                      
REMARK 465     MET R     1                                                      
REMARK 465     PHE R     2                                                      
REMARK 465     LEU R     3                                                      
REMARK 465     THR R     4                                                      
REMARK 465     ARG R     5                                                      
REMARK 465     SER R     6                                                      
REMARK 465     GLU R     7                                                      
REMARK 465     TYR R     8                                                      
REMARK 465     MET S     1                                                      
REMARK 465     PRO S   240                                                      
REMARK 465     GLN S   241                                                      
REMARK 465     ARG S   242                                                      
REMARK 465     LYS S   243                                                      
REMARK 465     ALA S   244                                                      
REMARK 465     GLN S   245                                                      
REMARK 465     PRO S   246                                                      
REMARK 465     ALA S   247                                                      
REMARK 465     GLN S   248                                                      
REMARK 465     PRO S   249                                                      
REMARK 465     ALA S   250                                                      
REMARK 465     ASP S   251                                                      
REMARK 465     GLU S   252                                                      
REMARK 465     PRO S   253                                                      
REMARK 465     ALA S   254                                                      
REMARK 465     GLU S   255                                                      
REMARK 465     LYS S   256                                                      
REMARK 465     ALA S   257                                                      
REMARK 465     ASP S   258                                                      
REMARK 465     GLU S   259                                                      
REMARK 465     PRO S   260                                                      
REMARK 465     MET S   261                                                      
REMARK 465     GLU S   262                                                      
REMARK 465     HIS S   263                                                      
REMARK 465     MET T     0                                                      
REMARK 465     SER T     1                                                      
REMARK 465     SER T     2                                                      
REMARK 465     ILE T     3                                                      
REMARK 465     GLY T     4                                                      
REMARK 465     GLU T   245                                                      
REMARK 465     GLU T   246                                                      
REMARK 465     ASP T   247                                                      
REMARK 465     GLU T   248                                                      
REMARK 465     SER T   249                                                      
REMARK 465     ASP T   250                                                      
REMARK 465     ASP T   251                                                      
REMARK 465     ASP T   252                                                      
REMARK 465     ASN T   253                                                      
REMARK 465     MET T   254                                                      
REMARK 465     MET U     1                                                      
REMARK 465     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   207                                                      
REMARK 465     THR Y   208                                                      
REMARK 465     PRO Y   209                                                      
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     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  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 110    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     LEU N 202    CG   CD1  CD2                                       
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     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 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   516     O    HOH Y   537              1.99            
REMARK 500   O    HOH D   411     O    HOH D   446              2.05            
REMARK 500   OD1  ASN P   155     OG1  THR Q    77              2.06            
REMARK 500   ND2  ASN S   152     O    HOH S   401              2.07            
REMARK 500   O    HOH E   441     O    HOH E   531              2.09            
REMARK 500   NZ   LYS J   185     O    HOH J   401              2.10            
REMARK 500   O    HOH E   477     O    HOH E   519              2.15            
REMARK 500   O    HOH G   520     O    HOH N   518              2.18            
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 G 108   CD    GLU G 108   OE1     0.105                       
REMARK 500    ASP Q  13   CB    ASP Q  13   CG      0.141                       
REMARK 500    GLU b  92   CD    GLU b  92   OE2     0.087                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP D   9   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG F  85   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG F  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    MET F 117   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    VAL F 190   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    CYS G  78   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG G 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG H  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG H  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASN I  17   C   -  N   -  CA  ANGL. DEV. =  22.1 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG I  69   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG I  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG J  86   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG J  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG K 124   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG K 161   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG K 162   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG L  99   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG L  99   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    MET L 172   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    LEU O 181   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ARG P  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG Q  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP R   9   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU R 121   C   -  N   -  CA  ANGL. DEV. =  27.2 DEGREES          
REMARK 500    GLY T   6   N   -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    MET T  27   CG  -  SD  -  CE  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ASP T 113   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG T 114   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    MET T 117   CG  -  SD  -  CE  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG U  11   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP U  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG U  88   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG U 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP V 104   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASN W  17   C   -  N   -  CA  ANGL. DEV. =  21.5 DEGREES          
REMARK 500    ARG W  25   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG W  69   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG W  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG X  86   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG X  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    MET Y  50   CG  -  SD  -  CE  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ARG Y 125   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG Y 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG Y 162   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG Y 162   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 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       55.80    -69.54                                   
REMARK 500    LYS A  52     -130.14    -65.30                                   
REMARK 500    SER A  53      127.77     -7.31                                   
REMARK 500    GLN A 122      -38.42   -139.60                                   
REMARK 500    LYS A 175       47.81   -100.04                                   
REMARK 500    ARG A 176      -25.01   -176.30                                   
REMARK 500    PHE A 198      -70.34    -69.94                                   
REMARK 500    GLU A 199      101.42     66.73                                   
REMARK 500    GLN A 201      117.20     75.38                                   
REMARK 500    ARG B   8       66.83     65.04                                   
REMARK 500    LEU B  55        0.96    -69.53                                   
REMARK 500    GLU B  58       97.58     68.08                                   
REMARK 500    VAL B  59      -33.44   -135.07                                   
REMARK 500    ASN B  69     -166.29   -169.55                                   
REMARK 500    MET B 201       60.99   -102.19                                   
REMARK 500    ASP B 202       39.15    -81.02                                   
REMARK 500    VAL B 203       62.93   -162.37                                   
REMARK 500    SER B 204      -89.22   -145.24                                   
REMARK 500    GLU B 248      -60.63    -99.24                                   
REMARK 500    ASP C  39       33.49   -140.12                                   
REMARK 500    LYS C  47     -117.87     58.21                                   
REMARK 500    VAL C  50     -139.73     76.74                                   
REMARK 500    ALA C  51       99.93     95.67                                   
REMARK 500    ASP C  55       98.98    -69.88                                   
REMARK 500    GLN C 200      -82.53    -36.56                                   
REMARK 500    LYS C 204      -91.97     88.22                                   
REMARK 500    ASP C 214       -5.14     67.91                                   
REMARK 500    SER C 216      170.33     60.78                                   
REMARK 500    GLU C 237      -54.62   -134.62                                   
REMARK 500    ARG D  53       70.56     73.72                                   
REMARK 500    GLU D 126       34.50   -160.67                                   
REMARK 500    ALA D 128     -162.84   -105.87                                   
REMARK 500    GLU D 175      -78.23    -54.26                                   
REMARK 500    PHE D 226      125.05    -34.83                                   
REMARK 500    SER E  40     -166.15   -115.85                                   
REMARK 500    HIS E  59      127.71    126.78                                   
REMARK 500    ALA E 151       -0.32     80.04                                   
REMARK 500    ASP E 226     -118.08     57.74                                   
REMARK 500    LEU E 236       75.60    -59.35                                   
REMARK 500    ARG G   3       78.27     67.52                                   
REMARK 500    VAL G  56       74.85   -118.63                                   
REMARK 500    TRP G 189       50.44     34.68                                   
REMARK 500    GLU G 192      -35.57   -132.71                                   
REMARK 500    GLN G 193       78.44   -106.01                                   
REMARK 500    ASP G 209       87.36     60.86                                   
REMARK 500    ASN H  30       55.44   -141.50                                   
REMARK 500    SER H 171     -127.79     67.39                                   
REMARK 500    ARG H 203       90.62    -69.58                                   
REMARK 500    GLN I  30     -117.67     47.80                                   
REMARK 500    ASP I  37       42.59   -141.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     137 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 D  175     GLY D  176                 -141.39                    
REMARK 500 GLU D  175     GLY D  176                  137.55                    
REMARK 500 GLY I   78     ARG I   79                 -135.95                    
REMARK 500 MET J    1     GLU J    2                 -142.91                    
REMARK 500 MET J    1     GLU J    2                 -143.81                    
REMARK 500 ASP P  202     VAL P  203                  147.04                    
REMARK 500 VAL P  203     SER P  204                 -143.64                    
REMARK 500 GLU P  244     ALA P  245                 -146.21                    
REMARK 500 ALA P  245     LYS P  246                   47.93                    
REMARK 500 LYS Q   47     LYS Q   48                 -136.40                    
REMARK 500 SER Q   49     VAL Q   50                 -142.06                    
REMARK 500 PRO R  130     GLY R  131                  146.56                    
REMARK 500 GLY R  223     GLN R  224                 -148.96                    
REMARK 500 THR T    5     GLY T    6                 -148.45                    
REMARK 500 GLY W   78     ARG W   79                 -135.55                    
REMARK 500 MET X    1     GLU X    2                 -140.55                    
REMARK 500 ILE a  215     SER a  216                 -127.41                    
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 E 536        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH E 537        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH G 590        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH I 556        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH I 557        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH J 533        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH O 489        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH Q 471        DISTANCE =  6.44 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    91.3                                              
REMARK 620 3 ASN G 128   O    80.2  91.8                                        
REMARK 620 4 MET G 131   O   160.7 108.0  98.6                                  
REMARK 620 5 HOH G 468   O    74.4 154.6 105.9  87.6                            
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 466   O    79.7                                              
REMARK 620 3 HOH N 409   O    87.9  89.3                                        
REMARK 620 4 HOH H 520   O   101.6  92.3 170.5                                  
REMARK 620 5 HOH N 432   O   162.2  82.6  91.0  79.9                            
REMARK 620 6 HOH N 489   O   106.1 172.8  86.7  90.7  91.6                      
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   111.1                                              
REMARK 620 3 SER H 169   O    99.5  90.5                                        
REMARK 620 4 ASP Z 213   O   109.0 136.7  98.6                                  
REMARK 620 5 HOH H 460   O    82.8  88.9 177.7  80.3                            
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    86.6                                              
REMARK 620 3 SER I 180   O   104.1  92.2                                        
REMARK 620 4 HOH I 412   O    84.0 166.2  99.9                                  
REMARK 620 5 HOH I 465   O   157.5  88.3  98.0  96.4                            
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 169   O   109.2                                              
REMARK 620 3 ASP Y 172   O   140.1 104.8                                        
REMARK 620 4 SER Y 175   O    99.0 103.9  92.6                                  
REMARK 620 5 HOH Y 479   O    83.1  77.1  84.6 177.2                            
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 168   O                                                      
REMARK 620 2 ASP K 171   O   103.0                                              
REMARK 620 3 SER K 174   O   106.5  93.1                                        
REMARK 620 4 ASP W 204   O   107.8 139.2 102.9                                  
REMARK 620 5 HOH K 467   O    77.7  87.0 175.7  74.5                            
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    99.6                                              
REMARK 620 3 THR L 189   O    99.7  83.5                                        
REMARK 620 4 HOH L 461   O    88.4 166.6  84.6                                  
REMARK 620 5 HOH V 454   O   134.7  95.6 124.3  86.1                            
REMARK 620 6 HOH L 423   O    54.1 126.5 139.9  66.9  82.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 213   O                                                      
REMARK 620 2 ILE V 163   O   107.5                                              
REMARK 620 3 ASP V 166   O   137.4 112.3                                        
REMARK 620 4 SER V 169   O    98.9  97.9  90.3                                  
REMARK 620 5 HOH V 461   O    77.7  85.9  90.4 175.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K N 306   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET N 164   O                                                      
REMARK 620 2 ASP N 167   O    92.5                                              
REMARK 620 3 SER N 170   O    98.4  71.2                                        
REMARK 620 4 HOH N 536   O    88.0 167.2  96.1                                  
REMARK 620 5 HOH N 478   O    89.7  84.3 154.3 108.5                            
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    91.8                                              
REMARK 620 3 ASN U 128   O    82.0  94.3                                        
REMARK 620 4 MET U 131   O   160.2 107.5 100.5                                  
REMARK 620 5 HOH U 447   O    74.3 150.1 109.4  86.4                            
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 450   O    86.8                                              
REMARK 620 3 HOH V 465   O    88.8  96.7                                        
REMARK 620 4 HOH b 406   O    90.5 165.2  97.7                                  
REMARK 620 5 HOH b 434   O   175.0  95.0  86.3  88.9                            
REMARK 620 6 HOH b 422   O    99.0  86.7 171.7  79.3  85.8                      
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    88.1                                              
REMARK 620 3 SER W 180   O   108.3  94.6                                        
REMARK 620 4 HOH W 444   O   156.6  87.7  95.1                                  
REMARK 620 5 HOH W 468   O    86.2 165.9  99.4  92.4                            
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    98.7                                              
REMARK 620 3 THR Z 189   O   100.3  84.3                                        
REMARK 620 4 HOH Z 446   O   133.9  98.2 123.9                                  
REMARK 620 5 HOH H 452   O    61.3 126.2 144.5  74.2                            
REMARK 620 6 HOH Z 452   O    95.5 163.6  85.0  77.6  68.3                      
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    92.2                                              
REMARK 620 3 SER b 170   O    98.1  70.3                                        
REMARK 620 4 HOH b 438   O   144.8 117.6 108.9                                  
REMARK 620 5 HOH b 455   O    89.6  84.1 153.5  76.3                            
REMARK 620 6 HOH b 493   O    95.2 166.3  97.2  60.1 107.4                      
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 402   O                                                      
REMARK 620 2 HOH J 445   O    93.4                                              
REMARK 620 3 HOH J 513   O    86.5  97.9                                        
REMARK 620 4 HOH J 525   O    84.2 173.3  88.1                                  
REMARK 620 5 HOH K 472   O   174.9  88.9  97.8  93.0                            
REMARK 620 6 HOH J 458   O    81.2  94.0 163.3  79.5  94.0                      
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 407   O                                                      
REMARK 620 2 HOH X 435   O    79.9                                              
REMARK 620 3 HOH X 517   O    86.4  87.5                                        
REMARK 620 4 HOH Y 515   O   169.1  89.3  92.1                                  
REMARK 620 5 HOH X 444   O    93.1  94.1 178.3  88.7                            
REMARK 620 6 HOH X 503   O    88.9 166.6  84.4 101.6  93.9                      
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 MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHQ c 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE M 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE N 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K N 306                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K U 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL W 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE W 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE Z 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K Z 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE a 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE b 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K b 305                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6V1 E 148         
REMARK 800  through PRO E 149 bound to THR E 147                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VF c 4 through   
REMARK 800  LEU c 3 bound to THR K 5                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VF c 4 bound to THR K 5   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6V1 S 148         
REMARK 800  through PRO S 149 bound to THR S 147                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VF d 4 through   
REMARK 800  LEU d 3 bound to THR Y 6                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VF d 4 bound to THR Y 6   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PHQ d 101 and LEU d    
REMARK 800  2                                                                   
DBREF  5LF6 A    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LF6 B    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LF6 C    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LF6 D    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LF6 E    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LF6 F    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LF6 G    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LF6 H    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LF6 I    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LF6 J    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LF6 c    2     4  PDB    5LF6     5LF6             2      4             
DBREF  5LF6 K    5   208  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LF6 L    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LF6 M    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LF6 N    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LF6 O    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LF6 P    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LF6 Q    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LF6 R    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LF6 S    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LF6 T    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LF6 U    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LF6 V    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LF6 W    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LF6 X    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LF6 d    2     4  PDB    5LF6     5LF6             2      4             
DBREF  5LF6 Y    6   209  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LF6 Z    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LF6 a    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LF6 b    1   205  UNP    P28072   PSB6_HUMAN      35    239             
SEQADV 5LF6 6V1 E  148  UNP  P25786    CYS   148 MODIFIED RESIDUE               
SEQADV 5LF6 6V1 S  148  UNP  P25786    CYS   148 MODIFIED RESIDUE               
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 c    3  LEU LEU 6VF                                                  
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 d    3  LEU LEU 6VF                                                  
SEQRES   1 Y  204  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 Y  204  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 Y  204  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  204  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  204  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 Y  204  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  204  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 Y  204  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 Y  204  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 Y  204  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 Y  204  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 Y  204  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 Y  204  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 Y  204  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 Y  204  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 Y  204  HIS GLU LYS TYR SER GLY SER THR PRO                          
SEQRES   1 Z  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 Z  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 Z  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 Z  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 Z  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 Z  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 Z  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 Z  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 Z  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 Z  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 Z  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 Z  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 Z  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 Z  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 Z  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 Z  213  SER LEU ARG LYS ASP                                          
SEQRES   1 a  219  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 a  219  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 a  219  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 a  219  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 a  219  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 a  219  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 a  219  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 a  219  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 a  219  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 a  219  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 a  219  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 a  219  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 a  219  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 a  219  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 a  219  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 a  219  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 a  219  TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU                  
SEQRES   1 b  205  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 b  205  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 b  205  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 b  205  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  205  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 b  205  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 b  205  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 b  205  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 b  205  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 b  205  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 b  205  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 b  205  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 b  205  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 b  205  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 b  205  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 b  205  LYS PHE ALA VAL ALA THR LEU PRO PRO ALA                      
MODRES 5LF6 YCM C   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 6V1 G   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 YCM G  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 6V1 G  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 6V1 J   91  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 YCM Q   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 6V1 U   47  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 YCM U  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 6V1 U  161  CYS  MODIFIED RESIDUE                                   
MODRES 5LF6 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    6VF  c   4      14                                                       
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    6VF  d   4      14                                                       
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     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    PHQ  c 101      10                                                       
HET     MG  K 301       1                                                       
HET     CL  K 302       1                                                       
HET     CL  K 303       1                                                       
HET     CL  K 304       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    1PE  M 304      16                                                       
HET     CL  N 301       1                                                       
HET     CL  N 302       1                                                       
HET     CL  N 303       1                                                       
HET     CL  N 304       1                                                       
HET    1PE  N 305      16                                                       
HET      K  N 306       1                                                       
HET     CL  O 301       1                                                       
HET     CL  O 302       1                                                       
HET     CL  O 303       1                                                       
HET     CL  O 304       1                                                       
HET     CL  P 301       1                                                       
HET     CL  Q 301       1                                                       
HET     CL  Q 302       1                                                       
HET     CL  R 301       1                                                       
HET     CL  R 302       1                                                       
HET     CL  S 301       1                                                       
HET     CL  S 302       1                                                       
HET     CL  S 303       1                                                       
HET     CL  U 301       1                                                       
HET      K  U 302       1                                                       
HET     MG  V 301       1                                                       
HET     CL  V 302       1                                                       
HET     CL  V 303       1                                                       
HET     MG  W 301       1                                                       
HET     CL  W 302       1                                                       
HET    1PE  W 303      16                                                       
HET     MG  X 301       1                                                       
HET    PHQ  d 101      10                                                       
HET     CL  Y 301       1                                                       
HET     CL  Y 302       1                                                       
HET     CL  Y 303       1                                                       
HET     CL  Y 304       1                                                       
HET    1PE  Z 301      16                                                       
HET      K  Z 302       1                                                       
HET     CL  a 301       1                                                       
HET     CL  a 302       1                                                       
HET     CL  a 303       1                                                       
HET    1PE  a 304      16                                                       
HET     CL  b 301       1                                                       
HET     CL  b 302       1                                                       
HET     CL  b 303       1                                                       
HET    1PE  b 304      16                                                       
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     6VF (2~{R},3~{S})-3-AZANYL-4-(4-HYDROXYPHENYL)BUTANE-1,2-            
HETNAM   2 6VF  DIOL                                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     PHQ BENZYL CHLOROCARBONATE                                           
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  11  6VF    2(C10 H15 N O3)                                              
FORMUL  31   CL    55(CL 1-)                                                    
FORMUL  47    K    6(K 1+)                                                      
FORMUL  48   MG    10(MG 2+)                                                    
FORMUL  54  1PE    9(C10 H22 O6)                                                
FORMUL  58  PHQ    2(C8 H7 CL O2)                                               
FORMUL  13  HOH   *3501(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  GLU A  196  1                                  15    
HELIX    7 AA7 THR A  221  ALA A  231  1                                  11    
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  LYS B  246  1                                  18    
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 LEU D   81  ASN D  104  1                                  24    
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  GLN E   31  1                                  13    
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  GLN E  121  5                                   3    
HELIX   34 AD7 ARG E  164  MET E  176  1                                  13    
HELIX   35 AD8 SER E  177  CYS E  182  5                                   6    
HELIX   36 AD9 ASN E  183  GLU E  197  1                                  15    
HELIX   37 AE1 VAL E  229  GLU E  234  1                                   6    
HELIX   38 AE2 VAL F   20  ASN F   32  1                                  13    
HELIX   39 AE3 LEU F   80  GLY F  103  1                                  24    
HELIX   40 AE4 PRO F  107  TYR F  122  1                                  16    
HELIX   41 AE5 ALA F  168  GLU F  177  1                                  10    
HELIX   42 AE6 LYS F  178  LEU F  179  5                                   2    
HELIX   43 AE7 GLN F  180  MET F  184  5                                   5    
HELIX   44 AE8 THR F  185  HIS F  201  1                                  17    
HELIX   45 AE9 LEU F  219  ASN F  221  5                                   3    
HELIX   46 AF1 PRO F  228  LYS F  244  1                                  17    
HELIX   47 AF2 LEU G   22  GLY G   35  1                                  14    
HELIX   48 AF3 ASP G   62  VAL G   66  5                                   5    
HELIX   49 AF4 MET G   83  GLY G  106  1                                  24    
HELIX   50 AF5 PRO G  110  ASN G  128  1                                  19    
HELIX   51 AF6 LYS G  171  LYS G  186  1                                  16    
HELIX   52 AF7 PHE G  187  THR G  190  5                                   4    
HELIX   53 AF8 GLN G  193  SER G  207  1                                  15    
HELIX   54 AF9 THR G  231  GLU G  244  1                                  14    
HELIX   55 AG1 THR H   48  GLY H   71  1                                  24    
HELIX   56 AG2 ARG H   75  TYR H   90  1                                  16    
HELIX   57 AG3 GLY H  130  PHE H  142  1                                  13    
HELIX   58 AG4 GLU H  147  ASP H  166  1                                  20    
HELIX   59 AG5 SER I    1  TYR I    5  5                                   5    
HELIX   60 AG6 LEU I   55  GLU I   77  1                                  23    
HELIX   61 AG7 LYS I   82  GLU I   96  1                                  15    
HELIX   62 AG8 CYS I  141  TRP I  153  1                                  13    
HELIX   63 AG9 ASP I  158  ASP I  175  1                                  18    
HELIX   64 AH1 GLY J   51  GLY J   72  1                                  22    
HELIX   65 AH2 SER J   76  ARG J   93  1                                  18    
HELIX   66 AH3 GLY J  135  TYR J  147  1                                  13    
HELIX   67 AH4 SER J  152  PHE J  171  1                                  20    
HELIX   68 AH5 GLY K   52  LYS K   75  1                                  24    
HELIX   69 AH6 SER K   79  GLN K   93  1                                  15    
HELIX   70 AH7 GLY K  135  TYR K  147  1                                  13    
HELIX   71 AH8 GLU K  152  ASP K  171  1                                  20    
HELIX   72 AH9 VAL K  196  SER K  204  1                                   9    
HELIX   73 AI1 PHE L   57  ASN L   80  1                                  24    
HELIX   74 AI2 THR L   84  ARG L   99  1                                  16    
HELIX   75 AI3 ALA L  141  VAL L  153  1                                  13    
HELIX   76 AI4 SER L  167  ASP L  186  1                                  20    
HELIX   77 AI5 TYR M   57  LEU M   77  1                                  21    
HELIX   78 AI6 SER M   84  LYS M  102  1                                  19    
HELIX   79 AI7 TYR M  141  ALA M  146  1                                   6    
HELIX   80 AI8 ALA M  146  GLN M  157  1                                  12    
HELIX   81 AI9 SER M  161  ASP M  180  1                                  20    
HELIX   82 AJ1 TRP M  209  MET M  214  5                                   6    
HELIX   83 AJ2 SER N   48  ASN N   71  1                                  24    
HELIX   84 AJ3 LEU N   75  TYR N   90  1                                  16    
HELIX   85 AJ4 ARG N   91  LEU N   94  5                                   4    
HELIX   86 AJ5 GLY N  129  TYR N  134  5                                   6    
HELIX   87 AJ6 ILE N  135  TYR N  143  1                                   9    
HELIX   88 AJ7 THR N  148  ASP N  167  1                                  20    
HELIX   89 AJ8 LEU N  190  ILE N  194  5                                   5    
HELIX   90 AJ9 LEU O   18  GLY O   30  1                                  13    
HELIX   91 AK1 ASP O   57  VAL O   61  5                                   5    
HELIX   92 AK2 MET O   78  GLN O  101  1                                  24    
HELIX   93 AK3 PRO O  105  TYR O  120  1                                  16    
HELIX   94 AK4 ASN O  165  LYS O  175  1                                  11    
HELIX   95 AK5 GLU O  182  GLU O  196  1                                  15    
HELIX   96 AK6 THR O  221  ALA O  230  1                                  10    
HELIX   97 AK7 LEU P   18  ALA P   31  1                                  14    
HELIX   98 AK8 ILE P   79  GLN P  102  1                                  24    
HELIX   99 AK9 PRO P  106  PHE P  124  1                                  19    
HELIX  100 AL1 ASN P  167  TYR P  179  1                                  13    
HELIX  101 AL2 THR P  185  MET P  201  1                                  17    
HELIX  102 AL3 SER P  207  GLU P  209  5                                   3    
HELIX  103 AL4 LYS P  229  GLU P  244  1                                  16    
HELIX  104 AL5 LEU Q   16  LYS Q   28  1                                  13    
HELIX  105 AL6 ASP Q   55  ARG Q   60  5                                   6    
HELIX  106 AL7 LEU Q   76  GLU Q   99  1                                  24    
HELIX  107 AL8 THR Q  103  TYR Q  118  1                                  16    
HELIX  108 AL9 GLY Q  164  TYR Q  176  1                                  13    
HELIX  109 AM1 THR Q  183  GLU Q  197  1                                  15    
HELIX  110 AM2 ASN Q  221  LYS Q  234  1                                  14    
HELIX  111 AM3 LYS Q  234  ASN Q  239  1                                   6    
HELIX  112 AM4 LEU R   21  LYS R   32  1                                  12    
HELIX  113 AM5 GLU R   60  ILE R   64  5                                   5    
HELIX  114 AM6 LEU R   81  ASN R  104  1                                  24    
HELIX  115 AM7 THR R  108  ASN R  118  1                                  11    
HELIX  116 AM8 ALA R  173  TYR R  185  1                                  13    
HELIX  117 AM9 THR R  190  MET R  206  1                                  17    
HELIX  118 AN1 THR R  230  LYS R  239  1                                  10    
HELIX  119 AN2 ARG S    3  ASP S    7  5                                   5    
HELIX  120 AN3 ILE S   19  GLN S   31  1                                  13    
HELIX  121 AN4 LEU S   77  ASP S  100  1                                  24    
HELIX  122 AN5 PRO S  104  ILE S  118  1                                  15    
HELIX  123 AN6 PRO S  119  GLN S  121  5                                   3    
HELIX  124 AN7 ARG S  164  MET S  176  1                                  13    
HELIX  125 AN8 SER S  177  CYS S  182  5                                   6    
HELIX  126 AN9 ASN S  183  GLU S  197  1                                  15    
HELIX  127 AO1 VAL S  229  GLU S  234  1                                   6    
HELIX  128 AO2 VAL T   20  ASN T   32  1                                  13    
HELIX  129 AO3 LEU T   80  GLY T  103  1                                  24    
HELIX  130 AO4 PRO T  107  TYR T  122  1                                  16    
HELIX  131 AO5 ALA T  168  LYS T  178  1                                  11    
HELIX  132 AO6 LEU T  179  MET T  184  5                                   6    
HELIX  133 AO7 THR T  185  HIS T  201  1                                  17    
HELIX  134 AO8 LEU T  219  ASN T  221  5                                   3    
HELIX  135 AO9 PRO T  228  LYS T  244  1                                  17    
HELIX  136 AP1 LEU U   22  GLY U   35  1                                  14    
HELIX  137 AP2 ASP U   62  VAL U   66  5                                   5    
HELIX  138 AP3 MET U   83  GLY U  106  1                                  24    
HELIX  139 AP4 PRO U  110  ASN U  128  1                                  19    
HELIX  140 AP5 LYS U  171  LYS U  184  1                                  14    
HELIX  141 AP6 THR U  194  SER U  207  1                                  14    
HELIX  142 AP7 THR U  231  GLU U  244  1                                  14    
HELIX  143 AP8 THR V   48  GLY V   71  1                                  24    
HELIX  144 AP9 ARG V   75  TYR V   90  1                                  16    
HELIX  145 AQ1 GLY V  130  PHE V  142  1                                  13    
HELIX  146 AQ2 GLU V  147  ASP V  166  1                                  20    
HELIX  147 AQ3 SER W    1  TYR W    5  5                                   5    
HELIX  148 AQ4 LEU W   55  GLU W   77  1                                  23    
HELIX  149 AQ5 LYS W   82  GLU W   96  1                                  15    
HELIX  150 AQ6 CYS W  141  TRP W  153  1                                  13    
HELIX  151 AQ7 ASP W  158  ASP W  175  1                                  18    
HELIX  152 AQ8 GLY X   51  GLY X   72  1                                  22    
HELIX  153 AQ9 SER X   76  ARG X   93  1                                  18    
HELIX  154 AR1 GLY X  135  TYR X  147  1                                  13    
HELIX  155 AR2 SER X  152  PHE X  171  1                                  20    
HELIX  156 AR3 GLY Y   53  LYS Y   76  1                                  24    
HELIX  157 AR4 SER Y   80  GLN Y   94  1                                  15    
HELIX  158 AR5 GLY Y  136  TYR Y  148  1                                  13    
HELIX  159 AR6 GLU Y  153  ASP Y  172  1                                  20    
HELIX  160 AR7 VAL Y  197  TYR Y  204  1                                   8    
HELIX  161 AR8 PHE Z   57  ASN Z   80  1                                  24    
HELIX  162 AR9 THR Z   84  ARG Z   99  1                                  16    
HELIX  163 AS1 ALA Z  141  VAL Z  153  1                                  13    
HELIX  164 AS2 SER Z  167  ASP Z  186  1                                  20    
HELIX  165 AS3 TYR a   57  GLY a   78  1                                  22    
HELIX  166 AS4 SER a   84  LYS a  102  1                                  19    
HELIX  167 AS5 TYR a  141  ALA a  146  1                                   6    
HELIX  168 AS6 ALA a  146  GLN a  157  1                                  12    
HELIX  169 AS7 SER a  161  ASP a  180  1                                  20    
HELIX  170 AS8 TRP a  209  MET a  214  5                                   6    
HELIX  171 AS9 SER b   48  ASN b   71  1                                  24    
HELIX  172 AT1 LEU b   75  TYR b   90  1                                  16    
HELIX  173 AT2 ARG b   91  LEU b   94  5                                   4    
HELIX  174 AT3 GLY b  129  TYR b  134  5                                   6    
HELIX  175 AT4 ILE b  135  TYR b  143  1                                   9    
HELIX  176 AT5 THR b  148  ASP b  167  1                                  20    
HELIX  177 AT6 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  ALA A  39 -1  N  GLY A  36   O  THR A 160           
SHEET    3 AA1 5 GLY A  42  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  PRO A  66  0                                        
SHEET    2 AA2 5 ILE A  71  GLY A  77 -1  O  LEU A  73   N  GLU A  65           
SHEET    3 AA2 5 VAL A 131  ASN A 139 -1  O  CYS A 136   N  GLY A  72           
SHEET    4 AA2 5 ARG A 142  SER A 148 -1  O  PHE A 146   N  ILE A 135           
SHEET    5 AA2 5 TYR A 154  ALA A 156 -1  O  PHE A 155   N  GLN A 147           
SHEET    1 AA3 5 ALA B 161  ILE B 164  0                                        
SHEET    2 AA3 5 CYS B  34  ALA B  39 -1  N  CYS B  34   O  ILE B 164           
SHEET    3 AA3 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  LEU B  35           
SHEET    4 AA3 5 VAL B 211  GLU B 219 -1  O  GLU B 212   N  ALA B  47           
SHEET    5 AA3 5 LYS B 222  VAL B 227 -1  O  VAL B 224   N  THR B 217           
SHEET    1 AA4 5 ILE B  65  ASN B  69  0                                        
SHEET    2 AA4 5 MET B  72  GLY B  78 -1  O  CYS B  74   N  TYR B  66           
SHEET    3 AA4 5 VAL B 132  ASP B 140 -1  O  ILE B 137   N  ALA B  73           
SHEET    4 AA4 5 GLY B 144  SER B 150 -1  O  TYR B 148   N  TYR B 136           
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  ALA C 209   N  LEU C  43           
SHEET    5 AA5 5 SER C 216  ILE C 219 -1  O  LYS C 218   N  VAL C 210           
SHEET    1 AA6 5 ILE C  62  ASP C  66  0                                        
SHEET    2 AA6 5 VAL C  69  GLY C  75 -1  O  MET C  71   N  YCM C  63           
SHEET    3 AA6 5 ILE C 129  PHE C 136 -1  O  LEU C 132   N  ALA C  72           
SHEET    4 AA6 5 PRO C 142  THR C 147 -1  O  TYR C 145   N  ILE C 133           
SHEET    5 AA6 5 TYR C 153  ALA C 155 -1  O  HIS C 154   N  GLN C 146           
SHEET    1 AA7 5 ALA D 167  ILE D 170  0                                        
SHEET    2 AA7 5 ALA D  37  THR D  42 -1  N  GLY D  39   O  ARG D 168           
SHEET    3 AA7 5 GLY D  45  GLU D  51 -1  O  ALA D  49   N  ILE D  38           
SHEET    4 AA7 5 ILE D 215  VAL D 220 -1  O  ALA D 218   N  LEU D  48           
SHEET    5 AA7 5 HIS D 227  MET D 228 -1  O  HIS D 227   N  THR D 219           
SHEET    1 AA8 5 ILE D  67  ASP D  71  0                                        
SHEET    2 AA8 5 ILE D  74  GLY D  80 -1  O  ILE D  74   N  ILE D  70           
SHEET    3 AA8 5 VAL D 139  ASP D 147 -1  O  GLY D 144   N  GLY D  75           
SHEET    4 AA8 5 GLY D 150  MET D 156 -1  O  GLN D 152   N  GLY D 145           
SHEET    5 AA8 5 PHE D 162  GLN D 164 -1  O  VAL D 163   N  HIS D 155           
SHEET    1 AA9 5 ALA E 158  ILE E 161  0                                        
SHEET    2 AA9 5 THR E  35  LYS E  39 -1  N  GLY E  37   O  MET E 159           
SHEET    3 AA9 5 HIS E  43  LEU E  49 -1  O  VAL E  45   N  LEU E  38           
SHEET    4 AA9 5 VAL E 210  GLY E 216 -1  O  SER E 211   N  ALA E  48           
SHEET    5 AA9 5 LEU E 219  ASP E 225 -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  LEU E 133   N  SER E  73           
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  ASP E 155 -1  O  PHE E 154   N  GLN E 146           
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  ILE F 151   N  PHE F 135           
SHEET    5 AB3 5 SER F 157  GLY F 159 -1  O  TYR F 158   N  MET F 150           
SHEET    1 AB4 5 ALA G 165  GLY G 169  0                                        
SHEET    2 AB4 5 THR G  38  ARG G  43 -1  N  ALA G  41   O  THR G 166           
SHEET    3 AB4 5 6V1 G  47  GLN G  53 -1  O  VAL G  51   N  VAL G  40           
SHEET    4 AB4 5 ILE G 215  THR G 221 -1  O  GLY G 218   N  ILE G  50           
SHEET    5 AB4 5 ARG G 228  ILE G 229 -1  O  ARG G 228   N  VAL G 219           
SHEET    1 AB5 5 LEU G  69  THR G  73  0                                        
SHEET    2 AB5 5 ILE G  76  GLY G  82 -1  O  ILE G  76   N  ILE G  72           
SHEET    3 AB5 5 CYS G 136  ASP G 144 -1  O  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  PHE G 163 -1  O  PHE G 163   N  VAL G 151           
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  ILE I 194   N  THR H 217           
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  GLY I  15 -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  THR I 132 -1  O  MET I 130   N  SER I 122           
SHEET    1 AC3 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC3 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC3 5 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  ASN J 101   N  VAL J  47           
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 129  VAL K 132  0                                        
SHEET    2 AC7 5 THR K   7  PHE K  12 -1  N  THR K   7   O  VAL K 132           
SHEET    3 AC7 5 GLY K  15  ALA K  20 -1  O  ALA K  19   N  LEU K   8           
SHEET    4 AC7 5 ALA K 177  ARG K 184 -1  O  VAL K 183   N  VAL K  16           
SHEET    5 AC7 5 GLY K 187  ASN K 195 -1  O  SER K 192   N  LEU K 180           
SHEET    1 AC8 2 ALA K  24  ALA K  26  0                                        
SHEET    2 AC8 2 TYR K  29  SER K  32 -1  O  TYR K  29   N  ALA K  26           
SHEET    1 AC9 4 VAL K  38  ASN K  42  0                                        
SHEET    2 AC9 4 LEU K  45  THR K  48 -1  O  GLY K  47   N  ILE K  39           
SHEET    3 AC9 4 MET K 101  ASP K 109 -1  O  CYS K 106   N  LEU K  46           
SHEET    4 AC9 4 ALA K  50  GLY K  51 -1  N  ALA K  50   O  GLY K 102           
SHEET    1 AD1 5 VAL K  38  ASN K  42  0                                        
SHEET    2 AD1 5 LEU K  45  THR K  48 -1  O  GLY K  47   N  ILE K  39           
SHEET    3 AD1 5 MET K 101  ASP K 109 -1  O  CYS K 106   N  LEU K  46           
SHEET    4 AD1 5 GLY K 112  ASP K 119 -1  O  VAL K 118   N  THR K 103           
SHEET    5 AD1 5 ARG K 124  SER K 126 -1  O  ILE K 125   N  TYR K 117           
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  VAL L 198   N  ALA L  21           
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  ILE L 109   N  GLY L  53           
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  GLY M 113   N  MET M  50           
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  VAL N  13   N  VAL N   6           
SHEET    4 AD8 5 ILE N 174  ALA N 180 -1  O  ILE N 179   N  VAL N  12           
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  ALA N 101   N  PHE N  42           
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  ALA O  39 -1  N  GLY O  36   O  THR O 160           
SHEET    3 AE2 5 GLY O  42  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  PRO O  66  0                                        
SHEET    2 AE3 5 ILE O  71  GLY O  77 -1  O  LEU O  73   N  GLU O  65           
SHEET    3 AE3 5 VAL O 131  ASN O 139 -1  O  CYS O 136   N  GLY O  72           
SHEET    4 AE3 5 ARG O 142  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  TYR P 148   N  TYR P 136           
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  ALA Q 209   N  LEU Q  43           
SHEET    5 AE6 5 SER Q 216  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  LEU Q 132   N  ALA Q  72           
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  GLY R  39   O  ARG R 168           
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  ASP S 225 -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  ASP S 155 -1  O  PHE S 154   N  GLN S 146           
SHEET    1 AF3 5 GLY T 162  ILE T 165  0                                        
SHEET    2 AF3 5 ALA T  36  CYS T  41 -1  N  GLY T  38   O  CYS T 163           
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  ILE T 151   N  PHE T 135           
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  PHE U 163 -1  O  PHE U 163   N  VAL U 151           
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  VAL V  25   N  GLU V  22           
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  ALA V  97   N  ALA V  46           
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  GLY W  15 -1  N  MET W  13   O  ALA W  20           
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  PRO W  43  0                                        
SHEET    2 AG3 5 LEU W  48  GLY W  54 -1  O  ILE W  50   N  PHE W  42           
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  CYS W 121   N  ILE W 108           
SHEET    5 AG3 5 PRO W 129  THR W 132 -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 TYR X  12  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 TYR X  12  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  LEU X  44   N  PHE X  36           
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  ALA X 114   N  GLY X 106           
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 130  VAL Y 133  0                                        
SHEET    2 AG8 5 THR Y   8  PHE Y  13 -1  N  THR Y   8   O  VAL Y 133           
SHEET    3 AG8 5 GLY Y  16  ALA Y  21 -1  O  ALA Y  20   N  LEU Y   9           
SHEET    4 AG8 5 ALA Y 178  ARG Y 185 -1  O  VAL Y 184   N  VAL Y  17           
SHEET    5 AG8 5 GLY Y 188  ASN Y 196 -1  O  SER Y 193   N  LEU Y 181           
SHEET    1 AG9 2 ALA Y  25  ALA Y  27  0                                        
SHEET    2 AG9 2 TYR Y  30  SER Y  33 -1  O  TYR Y  30   N  ALA Y  27           
SHEET    1 AH1 4 VAL Y  39  ASN Y  43  0                                        
SHEET    2 AH1 4 LEU Y  46  THR Y  49 -1  O  GLY Y  48   N  ILE Y  40           
SHEET    3 AH1 4 MET Y 102  ASP Y 110 -1  O  CYS Y 107   N  LEU Y  47           
SHEET    4 AH1 4 ALA Y  51  GLY Y  52 -1  N  ALA Y  51   O  GLY Y 103           
SHEET    1 AH2 5 VAL Y  39  ASN Y  43  0                                        
SHEET    2 AH2 5 LEU Y  46  THR Y  49 -1  O  GLY Y  48   N  ILE Y  40           
SHEET    3 AH2 5 MET Y 102  ASP Y 110 -1  O  CYS Y 107   N  LEU Y  47           
SHEET    4 AH2 5 GLY Y 113  ASP Y 120 -1  O  VAL Y 119   N  THR Y 104           
SHEET    5 AH2 5 ARG Y 125  SER Y 127 -1  O  ILE Y 126   N  TYR Y 118           
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  ILE Z 109   N  GLY Z  53           
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  GLY a 113   N  MET a  50           
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  ALA b 101   N  PHE b  42           
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  1.34  
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  2.78  
LINK         C   ASP G  46                 N   6V1 G  47     1555   1555  1.33  
LINK         C   6V1 G  47                 N   ALA G  48     1555   1555  1.34  
LINK         O   TYR G 125                 K     K G 303     1555   1555  2.57  
LINK         O   ASN G 128                 K     K G 303     1555   1555  2.59  
LINK         O   MET G 131                 K     K G 303     1555   1555  2.51  
LINK         C   CYS G 136                 N   YCM G 137     1555   1555  1.31  
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  1.33  
LINK         OE1 GLN H  91                MG    MG H 301     1555   1555  2.19  
LINK         O   ILE H 163                MG    MG H 302     1555   1555  2.18  
LINK         O   ASP H 166                MG    MG H 302     1555   1555  2.19  
LINK         O   SER H 169                MG    MG H 302     1555   1555  2.20  
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  2.23  
LINK         O   ASP I 204                MG    MG I 305     1555   1555  2.16  
LINK         C   ASP J  90                 N   6V1 J  91     1555   1555  1.34  
LINK         C   6V1 J  91                 N   LEU J  92     1555   1555  1.35  
LINK         N   LEU c   2                 C1  PHQ c 101     1555   1555  1.33  
LINK         C   LEU c   3                 N4  6VF c   4     1555   1555  1.33  
LINK         C22 6VF c   4                 N   THR K   5     1555   1555  1.49  
LINK         C1  6VF c   4                 OG1 THR K   5     1555   1555  1.44  
LINK         O   THR K 168                MG    MG K 301     1555   1555  2.22  
LINK         O   ASP K 171                MG    MG K 301     1555   1555  2.18  
LINK         O   SER K 174                MG    MG K 301     1555   1555  2.21  
LINK         O   ALA L 183                 K     K L 302     1555   1555  2.60  
LINK         O   ASP L 186                 K     K L 302     1555   1555  2.63  
LINK         O   THR L 189                 K     K L 302     1555   1555  2.62  
LINK         O   ASP L 213                MG    MG L 303     1555   1555  2.19  
LINK         O   MET N 164                 K     K N 306     1555   1555  2.54  
LINK         O   ASP N 167                 K     K N 306     1555   1555  2.61  
LINK         O   SER N 170                 K     K N 306     1555   1555  2.60  
LINK         C   ILE Q  62                 N   YCM Q  63     1555   1555  1.34  
LINK         C   YCM Q  63                 N   ALA Q  64     1555   1555  1.34  
LINK         C   THR S 147                 N   6V1 S 148     1555   1555  1.33  
LINK         C   6V1 S 148                 N   PRO S 149     1555   1555  1.34  
LINK         OG1 THR U  14                 K     K U 302     1555   1555  2.77  
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  2.56  
LINK         O   ASN U 128                 K     K U 302     1555   1555  2.55  
LINK         O   MET U 131                 K     K U 302     1555   1555  2.53  
LINK         C   CYS U 136                 N   YCM U 137     1555   1555  1.34  
LINK         C   YCM U 137                 N   MET U 138     1555   1555  1.33  
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  2.18  
LINK         O   ILE V 163                MG    MG L 303     1555   1555  2.19  
LINK         O   ASP V 166                MG    MG L 303     1555   1555  2.19  
LINK         O   SER V 169                MG    MG L 303     1555   1555  2.20  
LINK         O   VAL W 174                MG    MG W 301     1555   1555  2.20  
LINK         O   ASP W 177                MG    MG W 301     1555   1555  2.20  
LINK         O   SER W 180                MG    MG W 301     1555   1555  2.19  
LINK         O   ASP W 204                MG    MG K 301     1555   1555  2.18  
LINK         C   ASP X  90                 N   6V1 X  91     1555   1555  1.34  
LINK         C   6V1 X  91                 N   LEU X  92     1555   1555  1.34  
LINK         N   LEU d   2                 C1  PHQ d 101     1555   1555  1.32  
LINK         C   LEU d   3                 N4  6VF d   4     1555   1555  1.35  
LINK         C22 6VF d   4                 N   THR Y   6     1555   1555  1.47  
LINK         C1  6VF d   4                 OG1 THR Y   6     1555   1555  1.42  
LINK         O   THR Y 169                MG    MG I 305     1555   1555  2.21  
LINK         O   ASP Y 172                MG    MG I 305     1555   1555  2.17  
LINK         O   SER Y 175                MG    MG I 305     1555   1555  2.25  
LINK         O   ALA Z 183                 K     K Z 302     1555   1555  2.61  
LINK         O   ASP Z 186                 K     K Z 302     1555   1555  2.62  
LINK         O   THR Z 189                 K     K Z 302     1555   1555  2.61  
LINK         O   ASP Z 213                MG    MG H 302     1555   1555  2.20  
LINK         O   MET b 164                 K     K b 305     1555   1555  2.55  
LINK         O   ASP b 167                 K     K b 305     1555   1555  2.66  
LINK         O   SER b 170                 K     K b 305     1555   1555  2.59  
LINK         K     K G 303                 O   HOH G 468     1555   1555  2.62  
LINK        MG    MG H 301                 O   HOH H 466     1555   1555  2.19  
LINK        MG    MG H 301                 O   HOH N 409     1555   1555  2.25  
LINK        MG    MG H 301                 O   HOH H 520     1555   1555  1.92  
LINK        MG    MG H 301                 O   HOH N 432     1555   1555  2.52  
LINK        MG    MG H 301                 O   HOH N 489     1555   1555  2.27  
LINK        MG    MG H 302                 O   HOH H 460     1555   1555  2.72  
LINK        MG    MG I 301                 O   HOH I 412     1555   1555  2.52  
LINK        MG    MG I 301                 O   HOH I 465     1555   1555  2.14  
LINK        MG    MG I 305                 O   HOH Y 479     1555   1555  2.64  
LINK        MG    MG J 301                 O   HOH J 402     1555   1555  2.27  
LINK        MG    MG J 301                 O   HOH J 445     1555   1555  2.08  
LINK        MG    MG J 301                 O   HOH J 513     1555   1555  1.93  
LINK        MG    MG J 301                 O   HOH J 525     1555   1555  2.07  
LINK        MG    MG J 301                 O   HOH K 472     1555   1555  2.01  
LINK        MG    MG J 301                 O   HOH J 458     1555   1555  2.20  
LINK        MG    MG K 301                 O   HOH K 467     1555   1555  2.83  
LINK         K     K L 302                 O   HOH L 461     1555   1555  2.67  
LINK         K     K L 302                 O   HOH V 454     1555   1555  3.29  
LINK         K     K L 302                 O   HOH L 423     1555   1555  3.15  
LINK        MG    MG L 303                 O   HOH V 461     1555   1555  2.76  
LINK         K     K N 306                 O   HOH N 536     1555   1555  2.39  
LINK         K     K N 306                 O   HOH N 478     1555   1555  2.55  
LINK         K     K U 302                 O   HOH U 447     1555   1555  2.73  
LINK        MG    MG V 301                 O   HOH V 450     1555   1555  1.94  
LINK        MG    MG V 301                 O   HOH V 465     1555   1555  1.99  
LINK        MG    MG V 301                 O   HOH b 406     1555   1555  2.22  
LINK        MG    MG V 301                 O   HOH b 434     1555   1555  2.24  
LINK        MG    MG V 301                 O   HOH b 422     1555   1555  2.41  
LINK        MG    MG W 301                 O   HOH W 444     1555   1555  2.21  
LINK        MG    MG W 301                 O   HOH W 468     1555   1555  2.28  
LINK        MG    MG X 301                 O   HOH X 407     1555   1555  2.01  
LINK        MG    MG X 301                 O   HOH X 435     1555   1555  2.06  
LINK        MG    MG X 301                 O   HOH X 517     1555   1555  2.25  
LINK        MG    MG X 301                 O   HOH Y 515     1555   1555  2.17  
LINK        MG    MG X 301                 O   HOH X 444     1555   1555  2.16  
LINK        MG    MG X 301                 O   HOH X 503     1555   1555  2.13  
LINK         K     K Z 302                 O   HOH Z 446     1555   1555  3.17  
LINK         K     K Z 302                 O   HOH H 452     1555   1555  3.17  
LINK         K     K Z 302                 O   HOH Z 452     1555   1555  2.56  
LINK         K     K b 305                 O   HOH b 438     1555   1555  3.23  
LINK         K     K b 305                 O   HOH b 455     1555   1555  2.62  
LINK         K     K b 305                 O   HOH b 493     1555   1555  2.74  
CISPEP   1 VAL B  203    SER B  204          0        12.28                     
CISPEP   2 LYS C   47    LYS C   48          0        11.41                     
CISPEP   3 GLY C  202    GLY C  203          0         2.18                     
CISPEP   4 GLY C  203    LYS C  204          0        17.81                     
CISPEP   5 ARG H  187    PRO H  188          0        -7.45                     
CISPEP   6 ARG H  187    PRO H  188          0        -7.47                     
CISPEP   7 GLY M  201    PRO M  202          0        -2.63                     
CISPEP   8 ILE P   52    HIS P   53          0       -13.13                     
CISPEP   9 LYS Q  204    ASN Q  205          0       -10.34                     
CISPEP  10 LEU Q  220    ASN Q  221          0        29.14                     
CISPEP  11 GLU S  234    GLY S  235          0       -28.13                     
CISPEP  12 GLU S  238    ARG S  239          0       -16.25                     
CISPEP  13 GLY T    6    TYR T    7          0       -13.51                     
CISPEP  14 ARG V  187    PRO V  188          0        -4.88                     
CISPEP  15 TYR Y  204    SER Y  205          0       -10.16                     
CISPEP  16 GLY a  201    PRO a  202          0        -4.06                     
CISPEP  17 GLY a  201    PRO a  202          0        -5.32                     
SITE     1 AC1  4 SER A   6  HOH A 483  ARG C   5  HOH C 418                    
SITE     1 AC2  1 ARG A 219                                                     
SITE     1 AC3  2 HIS A  87  ARG A  90                                          
SITE     1 AC4  2 THR A  68  HOH A 461                                          
SITE     1 AC5  5 ASN B  69  GLU B  70  GLN B  95   CL B 302                    
SITE     2 AC5  5 HOH B 501                                                     
SITE     1 AC6  2  CL B 301  HOH B 446                                          
SITE     1 AC7  1 GLY C 162                                                     
SITE     1 AC8  3 ARG C  86  ARG C 117  HOH C 440                               
SITE     1 AC9  3 ILE D  31  GLY D 171  SER D 174                               
SITE     1 AD1  4 THR D 161  HOH D 427  LEU E  77  THR E  78                    
SITE     1 AD2  5 6V1 E 148  ILE E 161  GLY E 162  SER E 165                    
SITE     2 AD2  5 HOH E 473                                                     
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 461                                          
SITE     1 AD6  4 LYS G 102  HOH G 413  HOH G 561  HOH N 420                    
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 468                                                     
SITE     1 AD9  7 GLN H  91  HOH H 466  HOH H 520  ASP N  51                    
SITE     2 AD9  7 HOH N 409  HOH N 432  HOH N 489                               
SITE     1 AE1  5 ILE H 163  ASP H 166  SER H 169  HOH H 460                    
SITE     2 AE1  5 ASP Z 213                                                     
SITE     1 AE2  3 THR H   1  GLY H 128  SER H 129                               
SITE     1 AE3  3 ASN H  80  ARG H  81  HOH H 524                               
SITE     1 AE4  5 VAL I 174  ASP I 177  SER I 180  HOH I 412                    
SITE     2 AE4  5 HOH I 465                                                     
SITE     1 AE5  2 ARG I  65  ARG I  69                                          
SITE     1 AE6  3 GLU I  96  LYS I  97  ASP J  90                               
SITE     1 AE7  4 LEU H  58  TYR H  90  TYR I  95  HOH I 496                    
SITE     1 AE8  5 ASP I 204  THR Y 169  ASP Y 172  SER Y 175                    
SITE     2 AE8  5 HOH Y 479                                                     
SITE     1 AE9  6 HOH J 402  HOH J 445  HOH J 458  HOH J 513                    
SITE     2 AE9  6 HOH J 525  HOH K 472                                          
SITE     1 AF1  4 HOH K 403  HOH K 453  ASP L 125  LEU c   2                    
SITE     1 AF2  5 THR K 168  ASP K 171  SER K 174  HOH K 467                    
SITE     2 AF2  5 ASP W 204                                                     
SITE     1 AF3  2 LYS K  36  ASN K 179                                          
SITE     1 AF4  3 TYR K  70  ARG K  73  HOH K 429                               
SITE     1 AF5  2 ILE K 125  SER K 126                                          
SITE     1 AF6  5 PHE K  58  SER L  98  PHE L 101  HOH L 486                    
SITE     2 AF6  5 HOH L 506                                                     
SITE     1 AF7  4 ALA L 183  ASP L 186  THR L 189  HOH L 461                    
SITE     1 AF8  5 ASP L 213  ILE V 163  ASP V 166  SER V 169                    
SITE     2 AF8  5 HOH V 461                                                     
SITE     1 AF9  5 PHE M  36  ARG M  37  ASN M  38  HOH M 521                    
SITE     2 AF9  5 HOH N 502                                                     
SITE     1 AG1  5 TYR M  30  ARG M  35  PRO N 115  MET N 116                    
SITE     2 AG1  5  CL N 303                                                     
SITE     1 AG2  1 ARG M  44                                                     
SITE     1 AG3  4 PHE L  33  TYR M 141  TYR M 144  THR b  22                    
SITE     1 AG4  5 HOH H 406  THR N  31  ARG N  45  ALA N  49                    
SITE     2 AG4  5 GLN N  53                                                     
SITE     1 AG5  3 THR N   1  GLY N 129  SER N 130                               
SITE     1 AG6  6 ARG M  35   CL M 302  SER N  46  GLY N  97                    
SITE     2 AG6  6 GLY N 128  GLY N 129                                          
SITE     1 AG7  5 ARG N  19  ARG N  29  GLY N 171  GLY N 172                    
SITE     2 AG7  5 HOH a 438                                                     
SITE     1 AG8  6 TYR G 103  GLN H  91  TYR N  90  HOH N 411                    
SITE     2 AG8  6 HOH N 487  HOH N 494                                          
SITE     1 AG9  6 ARG N  19  MET N 164  ASP N 167  SER N 170                    
SITE     2 AG9  6 HOH N 478  HOH N 536                                          
SITE     1 AH1  3 SER O   6  ARG Q   5  HOH Q 440                               
SITE     1 AH2  1 TYR O 100                                                     
SITE     1 AH3  2 ARG O 218  ARG O 219                                          
SITE     1 AH4  2 HIS O  87  ARG O  90                                          
SITE     1 AH5  3 GLU P  70  GLN P  95  HOH P 502                               
SITE     1 AH6  2 ARG Q  95  GLU Q  99                                          
SITE     1 AH7  3 VAL Q  26  GLY Q 162  HOH Q 417                               
SITE     1 AH8  6 ILE R  31  ILE R 170  GLY R 171  SER R 174                    
SITE     2 AH8  6 HOH R 455  HOH R 486                                          
SITE     1 AH9  3 THR R 161  HOH R 442  THR S  78                               
SITE     1 AI1  4 ILE S 161  GLY S 162  SER S 165  HOH S 495                    
SITE     1 AI2  3 6V1 S 148  SER S 150  ASN S 152                               
SITE     1 AI3  5 GLY S  32  SER S  33  LYS S  62  ALA S  75                    
SITE     2 AI3  5 GLY S  76                                                     
SITE     1 AI4  4 LYS U 102  HOH U 411  HOH U 481  HOH b 415                    
SITE     1 AI5  5 THR U  14  TYR U 125  ASN U 128  MET U 131                    
SITE     2 AI5  5 HOH U 447                                                     
SITE     1 AI6  8 GLN V  91  HOH V 450  HOH V 465  ASP b  51                    
SITE     2 AI6  8 ASP b  93  HOH b 406  HOH b 422  HOH b 434                    
SITE     1 AI7  3 THR V   1  GLY V 128  SER V 129                               
SITE     1 AI8  2 ASN V  80  ARG V  81                                          
SITE     1 AI9  5 VAL W 174  ASP W 177  SER W 180  HOH W 444                    
SITE     2 AI9  5 HOH W 468                                                     
SITE     1 AJ1  2 ARG W  65  ARG W  69                                          
SITE     1 AJ2  4 GLU W  96  LYS W  97  HOH W 451  ASP X  90                    
SITE     1 AJ3  6 HOH X 407  HOH X 435  HOH X 444  HOH X 503                    
SITE     2 AJ3  6 HOH X 517  HOH Y 515                                          
SITE     1 AJ4  3 TYR Y  71  ARG Y  74  HOH Y 497                               
SITE     1 AJ5  2 LYS Y  37  ASN Y 180                                          
SITE     1 AJ6  2 ILE Y 126  SER Y 127                                          
SITE     1 AJ7  3 ASP Y 159  LEU Y 160  HOH Y 503                               
SITE     1 AJ8  4 TYR Z  97  SER Z  98  PHE Z 101  HOH Z 436                    
SITE     1 AJ9  4 ALA Z 183  ASP Z 186  THR Z 189  HOH Z 452                    
SITE     1 AK1  4 PHE a  36  ARG a  37  ASN a  38  HOH b 467                    
SITE     1 AK2  5 TYR a  30  ARG a  35  PRO b 115  MET b 116                    
SITE     2 AK2  5  CL b 302                                                     
SITE     1 AK3  2 MET a  43  ARG a  44                                          
SITE     1 AK4  4 SER H 129  PHE Z  33  TYR a 141  HOH a 504                    
SITE     1 AK5  2 GLY b 129  SER b 130                                          
SITE     1 AK6  6 ARG a  35   CL a 302  SER b  46  GLY b  97                    
SITE     2 AK6  6 GLY b 128  GLY b 129                                          
SITE     1 AK7  5 HOH M 430  ARG b  19  ARG b  29  GLY b 171                    
SITE     2 AK7  5 GLY b 172                                                     
SITE     1 AK8  6 TYR U 103  PHE V  88  ARG V  89  GLN V  91                    
SITE     2 AK8  6 TYR b  61  HOH b 509                                          
SITE     1 AK9  6 ARG b  19  MET b 164  ASP b 167  SER b 170                    
SITE     2 AK9  6 HOH b 455  HOH b 493                                          
SITE     1 AL1 16 ALA E  25  VAL E  29  PRO E 127  TYR E 128                    
SITE     2 AL1 16 VAL E 130  GLN E 146  THR E 147  SER E 150                    
SITE     3 AL1 16 ALA E 151  ASN E 152  PHE E 154   CL E 301                    
SITE     4 AL1 16  CL E 302  HOH E 434  HOH E 454  HOH E 479                    
SITE     1 AL2 15 THR K   5  ARG K  23  ALA K  24  THR K  25                    
SITE     2 AL2 15 VAL K  35  LYS K  37  GLY K  51  ALA K  53                    
SITE     3 AL2 15 TYR K 173  HOH K 409  SER L 129  LEU c   2                    
SITE     4 AL2 15 HOH c 201  HOH c 202  HOH c 203                               
SITE     1 AL3 13 THR K   5  ARG K  23  VAL K  35  LYS K  37                    
SITE     2 AL3 13 GLY K  51  ALA K  53  TYR K 173  HOH K 409                    
SITE     3 AL3 13 SER L 129  LEU c   3  HOH c 201  HOH c 202                    
SITE     4 AL3 13 HOH c 203                                                     
SITE     1 AL4 13 VAL S  29  PRO S 127  TYR S 128  VAL S 130                    
SITE     2 AL4 13 GLN S 146  THR S 147  SER S 150  ALA S 151                    
SITE     3 AL4 13 ASN S 152   CL S 302  HOH S 459  HOH S 466                    
SITE     4 AL4 13 HOH S 470                                                     
SITE     1 AL5 15 THR Y   6  ARG Y  24  ALA Y  25  THR Y  26                    
SITE     2 AL5 15 VAL Y  36  LYS Y  38  GLY Y  52  ALA Y  54                    
SITE     3 AL5 15 TYR Y 174  HOH Y 407  HOH Y 433  HOH Z 437                    
SITE     4 AL5 15 LEU d   2  HOH d 201  HOH d 202                               
SITE     1 AL6 13 THR Y   6  ARG Y  24  VAL Y  36  LYS Y  38                    
SITE     2 AL6 13 GLY Y  52  ALA Y  54  TYR Y 174  HOH Y 407                    
SITE     3 AL6 13 HOH Y 433  HOH Z 437  LEU d   3  HOH d 201                    
SITE     4 AL6 13 HOH d 202                                                     
SITE     1 AL7  9 THR Y  26  ALA Y  32  ALA Y  54  HOH Y 408                    
SITE     2 AL7  9 HOH Y 474  ASP Z 125  SER Z 129  HOH Z 416                    
SITE     3 AL7  9 LEU d   3                                                     
CRYST1  113.870  203.480  315.630  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      0.008782  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004914  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003168        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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