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Database: PDB
Entry: 5LS6
LinkDB: 5LS6
Original site: 5LS6 
HEADER    TRANSFERASE/INHIBITOR                   22-AUG-16   5LS6              
TITLE     STRUCTURE OF HUMAN POLYCOMB REPRESSIVE COMPLEX 2 (PRC2) WITH INHIBITOR
CAVEAT     5LS6    74D A 809 HAS WRONG CHIRALITY AT ATOM CAC 74D D 809 HAS      
CAVEAT   2 5LS6    WRONG CHIRALITY AT ATOM CAC 74D G 809 HAS WRONG CHIRALITY    
CAVEAT   3 5LS6    AT ATOM CAC 74D J 809 HAS WRONG CHIRALITY AT ATOM CAC        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EZH2,HISTONE-LYSINE N-  
COMPND   3 METHYLTRANSFERASE EZH2,HISTONE-LYSINE N-METHYLTRANSFERASE EZH2;      
COMPND   4 CHAIN: A, D, G, J;                                                   
COMPND   5 SYNONYM: ENX-1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE
COMPND   6 6,ENX-1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE 6,ENX-
COMPND   7 1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE 6;          
COMPND   8 EC: 2.1.1.43,2.1.1.43,2.1.1.43;                                      
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: POLYCOMB PROTEIN EED;                                      
COMPND  12 CHAIN: B, E, H, K;                                                   
COMPND  13 SYNONYM: HEED,WD PROTEIN ASSOCIATING WITH INTEGRIN CYTOPLASMIC TAILS 
COMPND  14 1,WAIT-1;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: POLYCOMB PROTEIN SUZ12;                                    
COMPND  18 CHAIN: C, F, I, L;                                                   
COMPND  19 SYNONYM: CHROMATIN PRECIPITATED E2F TARGET 9 PROTEIN,CHET 9 PROTEIN, 
COMPND  20 JOINED TO JAZF1 PROTEIN,SUPPRESSOR OF ZESTE 12 PROTEIN HOMOLOG;      
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: JARID2 K116ME3;                                            
COMPND  24 CHAIN: Q, R, S, T;                                                   
COMPND  25 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EZH2, KMT6;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: EED;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: SUZ12, CHET9, JJAZ1, KIAA0160;                                 
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 SYNTHETIC: YES;                                                      
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606                                                 
KEYWDS    HUMAN PRC2, INHIBITOR, H3K27, TRANSFERASE-INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,N.JUSTIN,S.CHEN,J.WILSON,S.GAMBLIN                            
REVDAT   2   20-FEB-19 5LS6    1       REMARK LINK                              
REVDAT   1   22-FEB-17 5LS6    0                                                
JRNL        AUTH   R.G.VASWANI,V.S.GEHLING,L.A.DAKIN,A.S.COOK,C.G.NASVESCHUK,   
JRNL        AUTH 2 M.DUPLESSIS,P.IYER,S.BALASUBRAMANIAN,F.ZHAO,A.C.GOOD,        
JRNL        AUTH 3 R.CAMPBELL,C.LEE,N.CANTONE,R.T.CUMMINGS,E.NORMANT,           
JRNL        AUTH 4 S.F.BELLON,B.K.ALBRECHT,J.C.HARMANGE,P.TROJER,J.E.AUDIA,     
JRNL        AUTH 5 Y.ZHANG,N.JUSTIN,S.CHEN,J.R.WILSON,S.J.GAMBLIN               
JRNL        TITL   IDENTIFICATION OF                                            
JRNL        TITL 2 (R)-N-((4-METHOXY-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-3-YL)    
JRNL        TITL 3 METHYL)-2-METHYL-1-(1-(1-(2,2,2-TRIFLUOROETHYL)              
JRNL        TITL 4 PIPERIDIN-4-YL)ETHYL)-1H-INDOLE-3-CARBOXAMIDE (CPI-1205), A  
JRNL        TITL 5 POTENT AND SELECTIVE INHIBITOR OF HISTONE METHYLTRANSFERASE  
JRNL        TITL 6 EZH2, SUITABLE FOR PHASE I CLINICAL TRIALS FOR B-CELL        
JRNL        TITL 7 LYMPHOMAS.                                                   
JRNL        REF    J. MED. CHEM.                 V.  59  9928 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27739677                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01315                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 68.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 76561                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3952                            
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) : 3.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5594                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 280                          
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 34711                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 104.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.66000                                             
REMARK   3    B22 (A**2) : 7.94000                                              
REMARK   3    B33 (A**2) : -6.28000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.712         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.715         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.578        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35667 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 33400 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 48152 ; 1.599 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 76964 ; 1.101 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4246 ; 8.063 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1801 ;35.857 ;24.048       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6315 ;17.322 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   252 ;16.574 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5102 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 40260 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  8584 ; 0.002 ; 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): 17092 ; 6.024 ;10.403       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 17091 ; 6.024 ;10.402       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21302 ;10.070 ;15.573       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 21303 ;10.070 ;15.573       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 18575 ; 4.985 ;10.585       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 18575 ; 4.985 ;10.585       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 26851 ; 8.777 ;15.777       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 39765 ;14.592 ;80.434       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 39766 ;14.591 ;80.436       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LS6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001270.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5-6.75                           
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76561                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.30000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.81000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5HYN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350, 400MM AMMONIAN CITRATE      
REMARK 280  PH6.67, VAPOR DIFFUSION, SITTING DROP, 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       65.65500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      137.77000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.13500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      137.77000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.65500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.13500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, Q                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, R                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, S                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, T                            
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     GLU A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     ALA A    -5                                                      
REMARK 465     GLU A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     LYS A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     LYS A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     PRO A   219                                                      
REMARK 465     GLN A   250                                                      
REMARK 465     GLN A   251                                                      
REMARK 465     LEU A   252                                                      
REMARK 465     PRO A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     PRO A   380                                                      
REMARK 465     LYS A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     ARG A   386                                                      
REMARK 465     ARG A   387                                                      
REMARK 465     ARG A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     ARG A   390                                                      
REMARK 465     LEU A   391                                                      
REMARK 465     PRO A   392                                                      
REMARK 465     ASN A   393                                                      
REMARK 465     ASN A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     SER A   396                                                      
REMARK 465     ARG A   397                                                      
REMARK 465     PRO A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     THR A   400                                                      
REMARK 465     PRO A   401                                                      
REMARK 465     THR A   402                                                      
REMARK 465     ILE A   403                                                      
REMARK 465     ASN A   404                                                      
REMARK 465     VAL A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     GLU A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     ASP A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     ASP A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     ASP A   414                                                      
REMARK 465     ARG A   415                                                      
REMARK 465     GLU A   416                                                      
REMARK 465     ALA A   417                                                      
REMARK 465     GLY A   418                                                      
REMARK 465     PRO A   419                                                      
REMARK 465     GLY A   420                                                      
REMARK 465     LYS A   421                                                      
REMARK 465     PRO A   481                                                      
REMARK 465     ALA A   482                                                      
REMARK 465     GLU A   483                                                      
REMARK 465     ASP A   484                                                      
REMARK 465     VAL A   485                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     THR A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     PRO A   489                                                      
REMARK 465     ARG A   490                                                      
REMARK 465     LYS A   491                                                      
REMARK 465     LYS A   492                                                      
REMARK 465     LYS A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     LYS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     ARG A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     TRP A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     CYS A   503                                                      
REMARK 465     ARG A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ILE A   506                                                      
REMARK 465     GLN A   507                                                      
REMARK 465     LEU A   508                                                      
REMARK 465     LYS A   509                                                      
REMARK 465     LYS A   510                                                      
REMARK 465     ASP A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     ASN A   515                                                      
REMARK 465     SER A   729                                                      
REMARK 465     GLN A   730                                                      
REMARK 465     ALA A   731                                                      
REMARK 465     ASP A   732                                                      
REMARK 465     ALA A   733                                                      
REMARK 465     LEU A   734                                                      
REMARK 465     LYS A   735                                                      
REMARK 465     TYR A   736                                                      
REMARK 465     VAL A   737                                                      
REMARK 465     GLY A   738                                                      
REMARK 465     ILE A   739                                                      
REMARK 465     GLU A   740                                                      
REMARK 465     ARG A   741                                                      
REMARK 465     GLU A   742                                                      
REMARK 465     MET A   743                                                      
REMARK 465     GLU A   744                                                      
REMARK 465     ILE A   745                                                      
REMARK 465     PRO A   746                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     GLY C   557                                                      
REMARK 465     SER C   558                                                      
REMARK 465     SER C   559                                                      
REMARK 465     GLY C   560                                                      
REMARK 465     GLU D    -9                                                      
REMARK 465     THR D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     ALA D    -5                                                      
REMARK 465     GLU D    -4                                                      
REMARK 465     GLU D    -3                                                      
REMARK 465     LYS D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     THR D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     GLU D     9                                                      
REMARK 465     LYS D   217                                                      
REMARK 465     PHE D   218                                                      
REMARK 465     PRO D   219                                                      
REMARK 465     GLN D   250                                                      
REMARK 465     GLN D   251                                                      
REMARK 465     LEU D   252                                                      
REMARK 465     PRO D   253                                                      
REMARK 465     GLY D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     LEU D   256                                                      
REMARK 465     PRO D   379                                                      
REMARK 465     PRO D   380                                                      
REMARK 465     LYS D   381                                                      
REMARK 465     ARG D   382                                                      
REMARK 465     PRO D   383                                                      
REMARK 465     GLY D   384                                                      
REMARK 465     GLY D   385                                                      
REMARK 465     ARG D   386                                                      
REMARK 465     ARG D   387                                                      
REMARK 465     ARG D   388                                                      
REMARK 465     GLY D   389                                                      
REMARK 465     ARG D   390                                                      
REMARK 465     LEU D   391                                                      
REMARK 465     PRO D   392                                                      
REMARK 465     ASN D   393                                                      
REMARK 465     ASN D   394                                                      
REMARK 465     SER D   395                                                      
REMARK 465     SER D   396                                                      
REMARK 465     ARG D   397                                                      
REMARK 465     PRO D   398                                                      
REMARK 465     SER D   399                                                      
REMARK 465     THR D   400                                                      
REMARK 465     PRO D   401                                                      
REMARK 465     THR D   402                                                      
REMARK 465     ILE D   403                                                      
REMARK 465     ASN D   404                                                      
REMARK 465     VAL D   405                                                      
REMARK 465     LEU D   406                                                      
REMARK 465     GLU D   407                                                      
REMARK 465     SER D   408                                                      
REMARK 465     LYS D   409                                                      
REMARK 465     ASP D   410                                                      
REMARK 465     THR D   411                                                      
REMARK 465     ASP D   412                                                      
REMARK 465     SER D   413                                                      
REMARK 465     ASP D   414                                                      
REMARK 465     ARG D   415                                                      
REMARK 465     GLU D   416                                                      
REMARK 465     ALA D   417                                                      
REMARK 465     GLY D   418                                                      
REMARK 465     PRO D   419                                                      
REMARK 465     GLY D   420                                                      
REMARK 465     LYS D   421                                                      
REMARK 465     PRO D   481                                                      
REMARK 465     ALA D   482                                                      
REMARK 465     GLU D   483                                                      
REMARK 465     ASP D   484                                                      
REMARK 465     VAL D   485                                                      
REMARK 465     ASP D   486                                                      
REMARK 465     THR D   487                                                      
REMARK 465     PRO D   488                                                      
REMARK 465     PRO D   489                                                      
REMARK 465     ARG D   490                                                      
REMARK 465     LYS D   491                                                      
REMARK 465     LYS D   492                                                      
REMARK 465     LYS D   493                                                      
REMARK 465     ARG D   494                                                      
REMARK 465     LYS D   495                                                      
REMARK 465     HIS D   496                                                      
REMARK 465     ARG D   497                                                      
REMARK 465     LEU D   498                                                      
REMARK 465     TRP D   499                                                      
REMARK 465     ALA D   500                                                      
REMARK 465     ALA D   501                                                      
REMARK 465     HIS D   502                                                      
REMARK 465     CYS D   503                                                      
REMARK 465     ARG D   504                                                      
REMARK 465     LYS D   505                                                      
REMARK 465     ILE D   506                                                      
REMARK 465     GLN D   507                                                      
REMARK 465     LEU D   508                                                      
REMARK 465     LYS D   509                                                      
REMARK 465     LYS D   510                                                      
REMARK 465     ASP D   511                                                      
REMARK 465     GLY D   512                                                      
REMARK 465     SER D   513                                                      
REMARK 465     SER D   514                                                      
REMARK 465     ASN D   515                                                      
REMARK 465     SER D   729                                                      
REMARK 465     GLN D   730                                                      
REMARK 465     ALA D   731                                                      
REMARK 465     ASP D   732                                                      
REMARK 465     ALA D   733                                                      
REMARK 465     LEU D   734                                                      
REMARK 465     LYS D   735                                                      
REMARK 465     TYR D   736                                                      
REMARK 465     VAL D   737                                                      
REMARK 465     GLY D   738                                                      
REMARK 465     ILE D   739                                                      
REMARK 465     GLU D   740                                                      
REMARK 465     ARG D   741                                                      
REMARK 465     GLU D   742                                                      
REMARK 465     MET D   743                                                      
REMARK 465     GLU D   744                                                      
REMARK 465     ILE D   745                                                      
REMARK 465     PRO D   746                                                      
REMARK 465     GLY E    75                                                      
REMARK 465     SER E    76                                                      
REMARK 465     GLY F   557                                                      
REMARK 465     SER F   558                                                      
REMARK 465     SER F   559                                                      
REMARK 465     GLY F   560                                                      
REMARK 465     GLU G    -9                                                      
REMARK 465     THR G    -8                                                      
REMARK 465     SER G    -7                                                      
REMARK 465     LEU G    -6                                                      
REMARK 465     ALA G    -5                                                      
REMARK 465     GLU G    -4                                                      
REMARK 465     GLU G    -3                                                      
REMARK 465     LYS G    -2                                                      
REMARK 465     LEU G    -1                                                      
REMARK 465     THR G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     GLN G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     GLY G     5                                                      
REMARK 465     LYS G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     SER G     8                                                      
REMARK 465     GLU G     9                                                      
REMARK 465     LYS G   217                                                      
REMARK 465     PHE G   218                                                      
REMARK 465     PRO G   219                                                      
REMARK 465     GLN G   250                                                      
REMARK 465     GLN G   251                                                      
REMARK 465     LEU G   252                                                      
REMARK 465     PRO G   253                                                      
REMARK 465     GLY G   254                                                      
REMARK 465     ALA G   255                                                      
REMARK 465     LEU G   256                                                      
REMARK 465     PRO G   379                                                      
REMARK 465     PRO G   380                                                      
REMARK 465     LYS G   381                                                      
REMARK 465     ARG G   382                                                      
REMARK 465     PRO G   383                                                      
REMARK 465     GLY G   384                                                      
REMARK 465     GLY G   385                                                      
REMARK 465     ARG G   386                                                      
REMARK 465     ARG G   387                                                      
REMARK 465     ARG G   388                                                      
REMARK 465     GLY G   389                                                      
REMARK 465     ARG G   390                                                      
REMARK 465     LEU G   391                                                      
REMARK 465     PRO G   392                                                      
REMARK 465     ASN G   393                                                      
REMARK 465     ASN G   394                                                      
REMARK 465     SER G   395                                                      
REMARK 465     SER G   396                                                      
REMARK 465     ARG G   397                                                      
REMARK 465     PRO G   398                                                      
REMARK 465     SER G   399                                                      
REMARK 465     THR G   400                                                      
REMARK 465     PRO G   401                                                      
REMARK 465     THR G   402                                                      
REMARK 465     ILE G   403                                                      
REMARK 465     ASN G   404                                                      
REMARK 465     VAL G   405                                                      
REMARK 465     LEU G   406                                                      
REMARK 465     GLU G   407                                                      
REMARK 465     SER G   408                                                      
REMARK 465     LYS G   409                                                      
REMARK 465     ASP G   410                                                      
REMARK 465     THR G   411                                                      
REMARK 465     ASP G   412                                                      
REMARK 465     SER G   413                                                      
REMARK 465     ASP G   414                                                      
REMARK 465     ARG G   415                                                      
REMARK 465     GLU G   416                                                      
REMARK 465     ALA G   417                                                      
REMARK 465     GLY G   418                                                      
REMARK 465     PRO G   419                                                      
REMARK 465     GLY G   420                                                      
REMARK 465     LYS G   421                                                      
REMARK 465     PRO G   481                                                      
REMARK 465     ALA G   482                                                      
REMARK 465     GLU G   483                                                      
REMARK 465     ASP G   484                                                      
REMARK 465     VAL G   485                                                      
REMARK 465     ASP G   486                                                      
REMARK 465     THR G   487                                                      
REMARK 465     PRO G   488                                                      
REMARK 465     PRO G   489                                                      
REMARK 465     ARG G   490                                                      
REMARK 465     LYS G   491                                                      
REMARK 465     LYS G   492                                                      
REMARK 465     LYS G   493                                                      
REMARK 465     ARG G   494                                                      
REMARK 465     LYS G   495                                                      
REMARK 465     HIS G   496                                                      
REMARK 465     ARG G   497                                                      
REMARK 465     LEU G   498                                                      
REMARK 465     TRP G   499                                                      
REMARK 465     ALA G   500                                                      
REMARK 465     ALA G   501                                                      
REMARK 465     HIS G   502                                                      
REMARK 465     CYS G   503                                                      
REMARK 465     ARG G   504                                                      
REMARK 465     LYS G   505                                                      
REMARK 465     ILE G   506                                                      
REMARK 465     GLN G   507                                                      
REMARK 465     LEU G   508                                                      
REMARK 465     LYS G   509                                                      
REMARK 465     LYS G   510                                                      
REMARK 465     ASP G   511                                                      
REMARK 465     GLY G   512                                                      
REMARK 465     SER G   513                                                      
REMARK 465     SER G   514                                                      
REMARK 465     ASN G   515                                                      
REMARK 465     ALA G   731                                                      
REMARK 465     ASP G   732                                                      
REMARK 465     ALA G   733                                                      
REMARK 465     LEU G   734                                                      
REMARK 465     LYS G   735                                                      
REMARK 465     TYR G   736                                                      
REMARK 465     VAL G   737                                                      
REMARK 465     GLY G   738                                                      
REMARK 465     ILE G   739                                                      
REMARK 465     GLU G   740                                                      
REMARK 465     ARG G   741                                                      
REMARK 465     GLU G   742                                                      
REMARK 465     MET G   743                                                      
REMARK 465     GLU G   744                                                      
REMARK 465     ILE G   745                                                      
REMARK 465     PRO G   746                                                      
REMARK 465     GLY H    75                                                      
REMARK 465     SER H    76                                                      
REMARK 465     GLY I   557                                                      
REMARK 465     SER I   558                                                      
REMARK 465     SER I   559                                                      
REMARK 465     GLY I   560                                                      
REMARK 465     GLU J    -9                                                      
REMARK 465     THR J    -8                                                      
REMARK 465     SER J    -7                                                      
REMARK 465     LEU J    -6                                                      
REMARK 465     ALA J    -5                                                      
REMARK 465     GLU J    -4                                                      
REMARK 465     GLU J    -3                                                      
REMARK 465     LYS J    -2                                                      
REMARK 465     LEU J    -1                                                      
REMARK 465     THR J     0                                                      
REMARK 465     MET J     1                                                      
REMARK 465     GLY J     2                                                      
REMARK 465     GLN J     3                                                      
REMARK 465     THR J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     LYS J     6                                                      
REMARK 465     LYS J     7                                                      
REMARK 465     SER J     8                                                      
REMARK 465     GLU J     9                                                      
REMARK 465     LYS J   217                                                      
REMARK 465     PHE J   218                                                      
REMARK 465     PRO J   219                                                      
REMARK 465     GLN J   250                                                      
REMARK 465     GLN J   251                                                      
REMARK 465     LEU J   252                                                      
REMARK 465     PRO J   253                                                      
REMARK 465     GLY J   254                                                      
REMARK 465     ALA J   255                                                      
REMARK 465     LEU J   256                                                      
REMARK 465     PRO J   379                                                      
REMARK 465     PRO J   380                                                      
REMARK 465     LYS J   381                                                      
REMARK 465     ARG J   382                                                      
REMARK 465     PRO J   383                                                      
REMARK 465     GLY J   384                                                      
REMARK 465     GLY J   385                                                      
REMARK 465     ARG J   386                                                      
REMARK 465     ARG J   387                                                      
REMARK 465     ARG J   388                                                      
REMARK 465     GLY J   389                                                      
REMARK 465     ARG J   390                                                      
REMARK 465     LEU J   391                                                      
REMARK 465     PRO J   392                                                      
REMARK 465     ASN J   393                                                      
REMARK 465     ASN J   394                                                      
REMARK 465     SER J   395                                                      
REMARK 465     SER J   396                                                      
REMARK 465     ARG J   397                                                      
REMARK 465     PRO J   398                                                      
REMARK 465     SER J   399                                                      
REMARK 465     THR J   400                                                      
REMARK 465     PRO J   401                                                      
REMARK 465     THR J   402                                                      
REMARK 465     ILE J   403                                                      
REMARK 465     ASN J   404                                                      
REMARK 465     VAL J   405                                                      
REMARK 465     LEU J   406                                                      
REMARK 465     GLU J   407                                                      
REMARK 465     SER J   408                                                      
REMARK 465     LYS J   409                                                      
REMARK 465     ASP J   410                                                      
REMARK 465     THR J   411                                                      
REMARK 465     ASP J   412                                                      
REMARK 465     SER J   413                                                      
REMARK 465     ASP J   414                                                      
REMARK 465     ARG J   415                                                      
REMARK 465     GLU J   416                                                      
REMARK 465     ALA J   417                                                      
REMARK 465     GLY J   418                                                      
REMARK 465     PRO J   419                                                      
REMARK 465     GLY J   420                                                      
REMARK 465     LYS J   421                                                      
REMARK 465     PRO J   481                                                      
REMARK 465     ALA J   482                                                      
REMARK 465     GLU J   483                                                      
REMARK 465     ASP J   484                                                      
REMARK 465     VAL J   485                                                      
REMARK 465     ASP J   486                                                      
REMARK 465     THR J   487                                                      
REMARK 465     PRO J   488                                                      
REMARK 465     PRO J   489                                                      
REMARK 465     ARG J   490                                                      
REMARK 465     LYS J   491                                                      
REMARK 465     LYS J   492                                                      
REMARK 465     LYS J   493                                                      
REMARK 465     ARG J   494                                                      
REMARK 465     LYS J   495                                                      
REMARK 465     HIS J   496                                                      
REMARK 465     ARG J   497                                                      
REMARK 465     LEU J   498                                                      
REMARK 465     TRP J   499                                                      
REMARK 465     ALA J   500                                                      
REMARK 465     ALA J   501                                                      
REMARK 465     HIS J   502                                                      
REMARK 465     CYS J   503                                                      
REMARK 465     ARG J   504                                                      
REMARK 465     LYS J   505                                                      
REMARK 465     ILE J   506                                                      
REMARK 465     GLN J   507                                                      
REMARK 465     LEU J   508                                                      
REMARK 465     LYS J   509                                                      
REMARK 465     LYS J   510                                                      
REMARK 465     ASP J   511                                                      
REMARK 465     GLY J   512                                                      
REMARK 465     SER J   513                                                      
REMARK 465     SER J   514                                                      
REMARK 465     ASN J   515                                                      
REMARK 465     SER J   729                                                      
REMARK 465     GLN J   730                                                      
REMARK 465     ALA J   731                                                      
REMARK 465     ASP J   732                                                      
REMARK 465     ALA J   733                                                      
REMARK 465     LEU J   734                                                      
REMARK 465     LYS J   735                                                      
REMARK 465     TYR J   736                                                      
REMARK 465     VAL J   737                                                      
REMARK 465     GLY J   738                                                      
REMARK 465     ILE J   739                                                      
REMARK 465     GLU J   740                                                      
REMARK 465     ARG J   741                                                      
REMARK 465     GLU J   742                                                      
REMARK 465     MET J   743                                                      
REMARK 465     GLU J   744                                                      
REMARK 465     ILE J   745                                                      
REMARK 465     PRO J   746                                                      
REMARK 465     GLY K    75                                                      
REMARK 465     SER K    76                                                      
REMARK 465     GLY L   557                                                      
REMARK 465     SER L   558                                                      
REMARK 465     SER L   559                                                      
REMARK 465     GLY L   560                                                      
REMARK 465     ARG Q     1                                                      
REMARK 465     ARG R     1                                                      
REMARK 465     ARG S     1                                                      
REMARK 465     ARG T     1                                                      
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   CD1  PHE A   667     OH   TYR A   728              0.84            
REMARK 500   CE1  PHE A   667     OH   TYR A   728              1.50            
REMARK 500   SG   CYS J   588    ZN     ZN J   806              1.51            
REMARK 500   CD1  PHE A   667     CZ   TYR A   728              1.75            
REMARK 500   CD2  PHE A   667     CD1  ILE A   708              2.00            
REMARK 500   CE2  PHE A   667     CD1  ILE A   708              2.07            
REMARK 500   CG   PHE A   667     OH   TYR A   728              2.17            
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    GLN A  66       42.63     35.89                                   
REMARK 500    VAL A  68       19.78     99.28                                   
REMARK 500    ALA A 103      115.82     -0.53                                   
REMARK 500    ASN A 119     -176.01    -65.72                                   
REMARK 500    GLU A 259       52.22   -103.29                                   
REMARK 500    PRO A 262     -179.96    -68.33                                   
REMARK 500    PHE A 290       31.91     80.41                                   
REMARK 500    ASP A 293       71.11     48.98                                   
REMARK 500    ALA A 314       68.55     60.86                                   
REMARK 500    GLN A 323       61.39    -62.26                                   
REMARK 500    GLU A 329      127.02    -37.05                                   
REMARK 500    ALA A 331      -84.40    -59.08                                   
REMARK 500    ASN A 423       64.88     76.32                                   
REMARK 500    GLU A 428      153.83    -48.66                                   
REMARK 500    TYR A 448       77.64     44.17                                   
REMARK 500    ASP A 449       -0.39     66.85                                   
REMARK 500    ASP A 524       72.29   -164.79                                   
REMARK 500    SER A 532       -7.01    -57.31                                   
REMARK 500    LYS A 545      -38.56    -36.43                                   
REMARK 500    SER A 550      144.92    -38.77                                   
REMARK 500    GLU A 552       50.28   -108.46                                   
REMARK 500    ALA A 564     -139.91   -142.79                                   
REMARK 500    GLN A 565      -39.57    -25.81                                   
REMARK 500    CYS A 580      170.19    -53.97                                   
REMARK 500    HIS A 593      125.21    -20.63                                   
REMARK 500    SER A 596       81.03    -68.62                                   
REMARK 500    LYS A 602       54.82   -117.98                                   
REMARK 500    ASN A 603       41.43   -146.97                                   
REMARK 500    VAL A 621      -56.88   -120.79                                   
REMARK 500    ILE A 638      -60.11    -99.63                                   
REMARK 500    THR A 678      -73.64    -58.24                                   
REMARK 500    ARG A 714      154.87    177.66                                   
REMARK 500    ASN B  93      -16.17     80.37                                   
REMARK 500    SER B 118     -139.46     43.70                                   
REMARK 500    ASN B 119       48.11   -102.87                                   
REMARK 500    GLU B 145      154.14    -38.41                                   
REMARK 500    ASN B 157      -76.01    -76.20                                   
REMARK 500    PRO B 203        1.56    -68.97                                   
REMARK 500    HIS B 213       -4.14     90.33                                   
REMARK 500    ASP B 237     -153.13   -133.42                                   
REMARK 500    ASP B 257        8.46    -53.13                                   
REMARK 500    HIS B 258        1.65     81.32                                   
REMARK 500    TYR B 365       45.62     70.41                                   
REMARK 500    ASP B 395      164.68     68.80                                   
REMARK 500    HIS B 397       72.36     31.93                                   
REMARK 500    LYS B 398     -109.61     42.35                                   
REMARK 500    ARG B 420      -70.59    -58.71                                   
REMARK 500    CYS C 571       15.83    -61.92                                   
REMARK 500    GLU C 590      -62.01    -21.12                                   
REMARK 500    ASP C 605       -4.20     96.94                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     193 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 MET A  134     GLY A  135                 -142.36                    
REMARK 500 THR A  311     GLU A  312                   33.48                    
REMARK 500 GLN A  326     HIS A  327                  -39.05                    
REMARK 500 HIS C  561     ASN C  562                  -30.67                    
REMARK 500 MET C  579     GLU C  580                  -31.34                    
REMARK 500 LYS C  587     ASP C  588                  148.10                    
REMARK 500 PRO D   67     VAL D   68                  149.40                    
REMARK 500 MET D  134     GLY D  135                 -144.05                    
REMARK 500 ASP D  595     SER D  596                  148.10                    
REMARK 500 MET F  579     GLU F  580                  -33.44                    
REMARK 500 MET G  134     GLY G  135                 -149.02                    
REMARK 500 HIS G  525     PRO G  526                 -148.61                    
REMARK 500 MET J  134     GLY J  135                 -148.31                    
REMARK 500 HIS J  525     PRO J  526                 -144.34                    
REMARK 500 MET L  579     GLU L  580                  -32.01                    
REMARK 500 PHE L  603     SER L  604                  149.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 286   SG                                                     
REMARK 620 2 CYS A 294   SG   93.5                                              
REMARK 620 3 HIS A 297   ND1  93.6 106.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 320   SG                                                     
REMARK 620 2 CYS A 452   SG   99.9                                              
REMARK 620 3 CYS A 463   SG  100.5 136.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 HIS A 525   NE2 117.0                                              
REMARK 620 3 CYS A 530   SG  123.7 115.9                                        
REMARK 620 4 CYS A 534   SG   93.5  74.6 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 CYS A 536   SG   98.7                                              
REMARK 620 3 CYS A 543   SG  105.9 121.4                                        
REMARK 620 4 CYS A 547   SG   97.4 115.3 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 530   SG                                                     
REMARK 620 2 CYS A 543   SG  104.1                                              
REMARK 620 3 CYS A 549   SG  108.2 115.4                                        
REMARK 620 4 CYS A 553   SG  100.8 111.9 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 808  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 562   SG  108.2                                              
REMARK 620 3 CYS A 566   SG  113.6 125.0                                        
REMARK 620 4 CYS A 571   SG  111.6  92.9 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 573   SG  131.5                                              
REMARK 620 3 CYS A 580   SG   96.5 114.3                                        
REMARK 620 4 CYS A 585   SG  103.0 104.7 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 566   SG                                                     
REMARK 620 2 CYS A 580   SG   94.0                                              
REMARK 620 3 CYS A 588   SG  144.1 117.1                                        
REMARK 620 4 CYS A 601   SG   90.2  93.0 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 286   SG                                                     
REMARK 620 2 CYS D 289   SG  118.8                                              
REMARK 620 3 CYS D 294   SG  100.7 113.8                                        
REMARK 620 4 HIS D 297   ND1 105.1 113.1 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 320   SG                                                     
REMARK 620 2 CYS D 452   SG  111.0                                              
REMARK 620 3 CYS D 463   SG  115.8 110.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 523   SG                                                     
REMARK 620 2 HIS D 525   NE2 116.2                                              
REMARK 620 3 CYS D 530   SG  119.1 113.5                                        
REMARK 620 4 CYS D 534   SG   99.6  82.3 120.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 523   SG                                                     
REMARK 620 2 CYS D 536   SG   99.4                                              
REMARK 620 3 CYS D 543   SG  105.4 111.9                                        
REMARK 620 4 CYS D 547   SG  102.5 115.7 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 530   SG                                                     
REMARK 620 2 CYS D 543   SG  107.0                                              
REMARK 620 3 CYS D 549   SG   99.0 115.4                                        
REMARK 620 4 CYS D 553   SG   97.5 121.7 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 560   SG                                                     
REMARK 620 2 CYS D 573   SG  125.3                                              
REMARK 620 3 CYS D 580   SG   97.2 119.1                                        
REMARK 620 4 CYS D 585   SG  109.9 100.0 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 808  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 560   SG                                                     
REMARK 620 2 CYS D 562   SG  111.8                                              
REMARK 620 3 CYS D 566   SG  110.9 121.1                                        
REMARK 620 4 CYS D 571   SG  100.7  98.0 111.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 566   SG                                                     
REMARK 620 2 CYS D 580   SG  111.1                                              
REMARK 620 3 CYS D 588   SG  133.1 113.3                                        
REMARK 620 4 CYS D 601   SG   90.7  99.6  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 286   SG                                                     
REMARK 620 2 CYS G 289   SG  102.8                                              
REMARK 620 3 CYS G 294   SG  107.3 119.7                                        
REMARK 620 4 HIS G 297   ND1  84.7 118.3 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 324   SG                                                     
REMARK 620 2 CYS G 452   SG  109.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 523   SG                                                     
REMARK 620 2 HIS G 525   NE2 124.2                                              
REMARK 620 3 CYS G 530   SG  110.8 114.6                                        
REMARK 620 4 CYS G 534   SG  102.2  98.7 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 523   SG                                                     
REMARK 620 2 CYS G 536   SG  113.5                                              
REMARK 620 3 CYS G 543   SG  101.0 106.4                                        
REMARK 620 4 CYS G 547   SG  115.5 114.0 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 530   SG                                                     
REMARK 620 2 CYS G 543   SG  101.7                                              
REMARK 620 3 CYS G 549   SG  111.3 103.1                                        
REMARK 620 4 CYS G 553   SG  113.8 115.0 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 808  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 560   SG                                                     
REMARK 620 2 CYS G 562   SG  101.4                                              
REMARK 620 3 CYS G 566   SG  117.5 126.1                                        
REMARK 620 4 CYS G 571   SG  104.8  95.9 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 560   SG                                                     
REMARK 620 2 CYS G 573   SG  132.1                                              
REMARK 620 3 CYS G 580   SG   96.6 126.4                                        
REMARK 620 4 CYS G 585   SG  100.2  92.4 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 566   SG                                                     
REMARK 620 2 CYS G 580   SG  103.0                                              
REMARK 620 3 CYS G 601   SG   87.4  99.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 286   SG                                                     
REMARK 620 2 CYS J 289   SG  103.7                                              
REMARK 620 3 CYS J 294   SG  112.4 122.8                                        
REMARK 620 4 HIS J 297   ND1  86.1 115.9 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 320   SG                                                     
REMARK 620 2 CYS J 324   SG  119.2                                              
REMARK 620 3 CYS J 463   SG  129.8 101.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 523   SG                                                     
REMARK 620 2 CYS J 536   SG  116.7                                              
REMARK 620 3 CYS J 547   SG   97.6 130.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 523   SG                                                     
REMARK 620 2 HIS J 525   NE2 115.1                                              
REMARK 620 3 CYS J 530   SG  110.5 115.8                                        
REMARK 620 4 CYS J 534   SG  110.0  86.0 117.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 530   SG                                                     
REMARK 620 2 CYS J 543   SG   88.5                                              
REMARK 620 3 CYS J 549   SG   98.4 114.6                                        
REMARK 620 4 CYS J 553   SG  117.3  93.2 135.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 808  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 560   SG                                                     
REMARK 620 2 CYS J 562   SG  103.8                                              
REMARK 620 3 CYS J 566   SG  114.0 129.1                                        
REMARK 620 4 CYS J 571   SG  110.1  92.5 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 560   SG                                                     
REMARK 620 2 CYS J 573   SG  125.7                                              
REMARK 620 3 CYS J 580   SG   95.4 124.7                                        
REMARK 620 4 CYS J 585   SG   99.8  99.8 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 566   SG                                                     
REMARK 620 2 CYS J 580   SG   90.9                                              
REMARK 620 3 CYS J 601   SG   91.3 101.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 808                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 74D A 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 808                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 74D D 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 808                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 74D G 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 808                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 74D J 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG Q 6 and M3L Q 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L Q 7 and PHE Q 8    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG R 6 and M3L R 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L R 7 and PHE R 8    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG S 6 and M3L S 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L S 7 and PHE S 8    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG T 6 and M3L T 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L T 7 and PHE T 8    
DBREF  5LS6 A    1   182  UNP    Q15910   EZH2_HUMAN       1    182             
DBREF  5LS6 A  211   418  UNP    Q15910   EZH2_HUMAN     211    385             
DBREF  5LS6 A  421   746  UNP    Q15910   EZH2_HUMAN     421    746             
DBREF  5LS6 B   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5LS6 C  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5LS6 D    1   182  UNP    Q15910   EZH2_HUMAN       1    182             
DBREF  5LS6 D  211   418  UNP    Q15910   EZH2_HUMAN     211    385             
DBREF  5LS6 D  421   746  UNP    Q15910   EZH2_HUMAN     421    746             
DBREF  5LS6 E   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5LS6 F  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5LS6 G    1   182  UNP    Q15910   EZH2_HUMAN       1    182             
DBREF  5LS6 G  211   418  UNP    Q15910   EZH2_HUMAN     211    385             
DBREF  5LS6 G  421   746  UNP    Q15910   EZH2_HUMAN     421    746             
DBREF  5LS6 H   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5LS6 I  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5LS6 J    1   182  UNP    Q15910   EZH2_HUMAN       1    182             
DBREF  5LS6 J  211   418  UNP    Q15910   EZH2_HUMAN     211    385             
DBREF  5LS6 J  421   746  UNP    Q15910   EZH2_HUMAN     421    746             
DBREF  5LS6 K   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5LS6 L  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5LS6 Q    1    11  PDB    5LS6     5LS6             1     11             
DBREF  5LS6 R    1    11  PDB    5LS6     5LS6             1     11             
DBREF  5LS6 S    1    11  PDB    5LS6     5LS6             1     11             
DBREF  5LS6 T    1    11  PDB    5LS6     5LS6             1     11             
SEQADV 5LS6 GLU A   -9  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR A   -8  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 SER A   -7  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU A   -6  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 ALA A   -5  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU A   -4  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU A   -3  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LYS A   -2  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU A   -1  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR A    0  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLN A  249  UNP  Q15910    GLU   249 CONFLICT                       
SEQADV 5LS6 PRO A  419  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY A  420  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY B   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 SER B   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 GLY C  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5LS6 GLU D   -9  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR D   -8  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 SER D   -7  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU D   -6  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 ALA D   -5  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU D   -4  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU D   -3  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LYS D   -2  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU D   -1  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR D    0  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLN D  249  UNP  Q15910    GLU   249 CONFLICT                       
SEQADV 5LS6 PRO D  419  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY D  420  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY E   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 SER E   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 GLY F  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5LS6 GLU G   -9  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR G   -8  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 SER G   -7  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU G   -6  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 ALA G   -5  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU G   -4  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU G   -3  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LYS G   -2  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU G   -1  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR G    0  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLN G  249  UNP  Q15910    GLU   249 CONFLICT                       
SEQADV 5LS6 PRO G  419  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY G  420  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY H   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 SER H   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 GLY I  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5LS6 GLU J   -9  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR J   -8  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 SER J   -7  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU J   -6  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 ALA J   -5  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU J   -4  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLU J   -3  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LYS J   -2  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 LEU J   -1  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 THR J    0  UNP  Q15910              EXPRESSION TAG                 
SEQADV 5LS6 GLN J  249  UNP  Q15910    GLU   249 CONFLICT                       
SEQADV 5LS6 PRO J  419  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY J  420  UNP  Q15910              LINKER                         
SEQADV 5LS6 GLY K   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 SER K   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5LS6 GLY L  557  UNP  Q15022              EXPRESSION TAG                 
SEQRES   1 A  695  GLU THR SER LEU ALA GLU GLU LYS LEU THR MET GLY GLN          
SEQRES   2 A  695  THR GLY LYS LYS SER GLU LYS GLY PRO VAL CYS TRP ARG          
SEQRES   3 A  695  LYS ARG VAL LYS SER GLU TYR MET ARG LEU ARG GLN LEU          
SEQRES   4 A  695  LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS SER MET PHE          
SEQRES   5 A  695  SER SER ASN ARG GLN LYS ILE LEU GLU ARG THR GLU ILE          
SEQRES   6 A  695  LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE GLN PRO VAL          
SEQRES   7 A  695  HIS ILE LEU THR SER VAL SER SER LEU ARG GLY THR ARG          
SEQRES   8 A  695  GLU CYS SER VAL THR SER ASP LEU ASP PHE PRO THR GLN          
SEQRES   9 A  695  VAL ILE PRO LEU LYS THR LEU ASN ALA VAL ALA SER VAL          
SEQRES  10 A  695  PRO ILE MET TYR SER TRP SER PRO LEU GLN GLN ASN PHE          
SEQRES  11 A  695  MET VAL GLU ASP GLU THR VAL LEU HIS ASN ILE PRO TYR          
SEQRES  12 A  695  MET GLY ASP GLU VAL LEU ASP GLN ASP GLY THR PHE ILE          
SEQRES  13 A  695  GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS VAL HIS GLY          
SEQRES  14 A  695  ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU ILE PHE VAL          
SEQRES  15 A  695  GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN GLU SER ARG          
SEQRES  16 A  695  PRO PRO ARG LYS PHE PRO SER ASP LYS ILE PHE GLU ALA          
SEQRES  17 A  695  ILE SER SER MET PHE PRO ASP LYS GLY THR ALA GLU GLU          
SEQRES  18 A  695  LEU LYS GLU LYS TYR LYS GLU LEU THR GLN GLN GLN LEU          
SEQRES  19 A  695  PRO GLY ALA LEU PRO PRO GLU CYS THR PRO ASN ILE ASP          
SEQRES  20 A  695  GLY PRO ASN ALA LYS SER VAL GLN ARG GLU GLN SER LEU          
SEQRES  21 A  695  HIS SER PHE HIS THR LEU PHE CYS ARG ARG CYS PHE LYS          
SEQRES  22 A  695  TYR ASP CYS PHE LEU HIS PRO PHE HIS ALA THR PRO ASN          
SEQRES  23 A  695  THR TYR LYS ARG LYS ASN THR GLU THR ALA LEU ASP ASN          
SEQRES  24 A  695  LYS PRO CYS GLY PRO GLN CYS TYR GLN HIS LEU GLU GLY          
SEQRES  25 A  695  ALA LYS GLU PHE ALA ALA ALA LEU THR ALA GLU ARG ILE          
SEQRES  26 A  695  LYS THR PRO PRO LYS ARG PRO GLY GLY ARG ARG ARG GLY          
SEQRES  27 A  695  ARG LEU PRO ASN ASN SER SER ARG PRO SER THR PRO THR          
SEQRES  28 A  695  ILE ASN VAL LEU GLU SER LYS ASP THR ASP SER ASP ARG          
SEQRES  29 A  695  GLU ALA GLY PRO GLY LYS PRO ASN ILE GLU PRO PRO GLU          
SEQRES  30 A  695  ASN VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG          
SEQRES  31 A  695  VAL LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE          
SEQRES  32 A  695  ALA ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR          
SEQRES  33 A  695  GLU PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA          
SEQRES  34 A  695  PRO ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS          
SEQRES  35 A  695  ARG LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE          
SEQRES  36 A  695  GLN LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  37 A  695  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER          
SEQRES  38 A  695  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  39 A  695  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  40 A  695  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  41 A  695  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  42 A  695  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  43 A  695  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  44 A  695  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  45 A  695  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  46 A  695  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  47 A  695  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  48 A  695  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  49 A  695  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  50 A  695  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  51 A  695  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  52 A  695  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  53 A  695  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  54 A  695  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 B  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 B  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 B  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 B  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 B  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 B  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 B  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 B  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 B  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 B  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 B  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 B  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 B  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 B  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 B  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 B  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 B  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 B  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 B  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 B  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 B  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 B  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 B  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 B  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 B  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 B  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 B  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 B  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 B  367  ARG LEU ARG                                                  
SEQRES   1 C  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 C  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 C  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 C  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 C  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 C  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 C  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 C  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 C  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 C  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 D  695  GLU THR SER LEU ALA GLU GLU LYS LEU THR MET GLY GLN          
SEQRES   2 D  695  THR GLY LYS LYS SER GLU LYS GLY PRO VAL CYS TRP ARG          
SEQRES   3 D  695  LYS ARG VAL LYS SER GLU TYR MET ARG LEU ARG GLN LEU          
SEQRES   4 D  695  LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS SER MET PHE          
SEQRES   5 D  695  SER SER ASN ARG GLN LYS ILE LEU GLU ARG THR GLU ILE          
SEQRES   6 D  695  LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE GLN PRO VAL          
SEQRES   7 D  695  HIS ILE LEU THR SER VAL SER SER LEU ARG GLY THR ARG          
SEQRES   8 D  695  GLU CYS SER VAL THR SER ASP LEU ASP PHE PRO THR GLN          
SEQRES   9 D  695  VAL ILE PRO LEU LYS THR LEU ASN ALA VAL ALA SER VAL          
SEQRES  10 D  695  PRO ILE MET TYR SER TRP SER PRO LEU GLN GLN ASN PHE          
SEQRES  11 D  695  MET VAL GLU ASP GLU THR VAL LEU HIS ASN ILE PRO TYR          
SEQRES  12 D  695  MET GLY ASP GLU VAL LEU ASP GLN ASP GLY THR PHE ILE          
SEQRES  13 D  695  GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS VAL HIS GLY          
SEQRES  14 D  695  ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU ILE PHE VAL          
SEQRES  15 D  695  GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN GLU SER ARG          
SEQRES  16 D  695  PRO PRO ARG LYS PHE PRO SER ASP LYS ILE PHE GLU ALA          
SEQRES  17 D  695  ILE SER SER MET PHE PRO ASP LYS GLY THR ALA GLU GLU          
SEQRES  18 D  695  LEU LYS GLU LYS TYR LYS GLU LEU THR GLN GLN GLN LEU          
SEQRES  19 D  695  PRO GLY ALA LEU PRO PRO GLU CYS THR PRO ASN ILE ASP          
SEQRES  20 D  695  GLY PRO ASN ALA LYS SER VAL GLN ARG GLU GLN SER LEU          
SEQRES  21 D  695  HIS SER PHE HIS THR LEU PHE CYS ARG ARG CYS PHE LYS          
SEQRES  22 D  695  TYR ASP CYS PHE LEU HIS PRO PHE HIS ALA THR PRO ASN          
SEQRES  23 D  695  THR TYR LYS ARG LYS ASN THR GLU THR ALA LEU ASP ASN          
SEQRES  24 D  695  LYS PRO CYS GLY PRO GLN CYS TYR GLN HIS LEU GLU GLY          
SEQRES  25 D  695  ALA LYS GLU PHE ALA ALA ALA LEU THR ALA GLU ARG ILE          
SEQRES  26 D  695  LYS THR PRO PRO LYS ARG PRO GLY GLY ARG ARG ARG GLY          
SEQRES  27 D  695  ARG LEU PRO ASN ASN SER SER ARG PRO SER THR PRO THR          
SEQRES  28 D  695  ILE ASN VAL LEU GLU SER LYS ASP THR ASP SER ASP ARG          
SEQRES  29 D  695  GLU ALA GLY PRO GLY LYS PRO ASN ILE GLU PRO PRO GLU          
SEQRES  30 D  695  ASN VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG          
SEQRES  31 D  695  VAL LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE          
SEQRES  32 D  695  ALA ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR          
SEQRES  33 D  695  GLU PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA          
SEQRES  34 D  695  PRO ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS          
SEQRES  35 D  695  ARG LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE          
SEQRES  36 D  695  GLN LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  37 D  695  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER          
SEQRES  38 D  695  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  39 D  695  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  40 D  695  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  41 D  695  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  42 D  695  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  43 D  695  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  44 D  695  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  45 D  695  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  46 D  695  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  47 D  695  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  48 D  695  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  49 D  695  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  50 D  695  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  51 D  695  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  52 D  695  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  53 D  695  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  54 D  695  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 E  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 E  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 E  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 E  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 E  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 E  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 E  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 E  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 E  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 E  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 E  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 E  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 E  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 E  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 E  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 E  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 E  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 E  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 E  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 E  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 E  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 E  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 E  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 E  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 E  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 E  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 E  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 E  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 E  367  ARG LEU ARG                                                  
SEQRES   1 F  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 F  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 F  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 F  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 F  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 F  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 F  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 F  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 F  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 F  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 G  695  GLU THR SER LEU ALA GLU GLU LYS LEU THR MET GLY GLN          
SEQRES   2 G  695  THR GLY LYS LYS SER GLU LYS GLY PRO VAL CYS TRP ARG          
SEQRES   3 G  695  LYS ARG VAL LYS SER GLU TYR MET ARG LEU ARG GLN LEU          
SEQRES   4 G  695  LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS SER MET PHE          
SEQRES   5 G  695  SER SER ASN ARG GLN LYS ILE LEU GLU ARG THR GLU ILE          
SEQRES   6 G  695  LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE GLN PRO VAL          
SEQRES   7 G  695  HIS ILE LEU THR SER VAL SER SER LEU ARG GLY THR ARG          
SEQRES   8 G  695  GLU CYS SER VAL THR SER ASP LEU ASP PHE PRO THR GLN          
SEQRES   9 G  695  VAL ILE PRO LEU LYS THR LEU ASN ALA VAL ALA SER VAL          
SEQRES  10 G  695  PRO ILE MET TYR SER TRP SER PRO LEU GLN GLN ASN PHE          
SEQRES  11 G  695  MET VAL GLU ASP GLU THR VAL LEU HIS ASN ILE PRO TYR          
SEQRES  12 G  695  MET GLY ASP GLU VAL LEU ASP GLN ASP GLY THR PHE ILE          
SEQRES  13 G  695  GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS VAL HIS GLY          
SEQRES  14 G  695  ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU ILE PHE VAL          
SEQRES  15 G  695  GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN GLU SER ARG          
SEQRES  16 G  695  PRO PRO ARG LYS PHE PRO SER ASP LYS ILE PHE GLU ALA          
SEQRES  17 G  695  ILE SER SER MET PHE PRO ASP LYS GLY THR ALA GLU GLU          
SEQRES  18 G  695  LEU LYS GLU LYS TYR LYS GLU LEU THR GLN GLN GLN LEU          
SEQRES  19 G  695  PRO GLY ALA LEU PRO PRO GLU CYS THR PRO ASN ILE ASP          
SEQRES  20 G  695  GLY PRO ASN ALA LYS SER VAL GLN ARG GLU GLN SER LEU          
SEQRES  21 G  695  HIS SER PHE HIS THR LEU PHE CYS ARG ARG CYS PHE LYS          
SEQRES  22 G  695  TYR ASP CYS PHE LEU HIS PRO PHE HIS ALA THR PRO ASN          
SEQRES  23 G  695  THR TYR LYS ARG LYS ASN THR GLU THR ALA LEU ASP ASN          
SEQRES  24 G  695  LYS PRO CYS GLY PRO GLN CYS TYR GLN HIS LEU GLU GLY          
SEQRES  25 G  695  ALA LYS GLU PHE ALA ALA ALA LEU THR ALA GLU ARG ILE          
SEQRES  26 G  695  LYS THR PRO PRO LYS ARG PRO GLY GLY ARG ARG ARG GLY          
SEQRES  27 G  695  ARG LEU PRO ASN ASN SER SER ARG PRO SER THR PRO THR          
SEQRES  28 G  695  ILE ASN VAL LEU GLU SER LYS ASP THR ASP SER ASP ARG          
SEQRES  29 G  695  GLU ALA GLY PRO GLY LYS PRO ASN ILE GLU PRO PRO GLU          
SEQRES  30 G  695  ASN VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG          
SEQRES  31 G  695  VAL LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE          
SEQRES  32 G  695  ALA ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR          
SEQRES  33 G  695  GLU PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA          
SEQRES  34 G  695  PRO ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS          
SEQRES  35 G  695  ARG LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE          
SEQRES  36 G  695  GLN LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  37 G  695  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER          
SEQRES  38 G  695  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  39 G  695  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  40 G  695  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  41 G  695  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  42 G  695  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  43 G  695  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  44 G  695  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  45 G  695  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  46 G  695  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  47 G  695  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  48 G  695  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  49 G  695  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  50 G  695  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  51 G  695  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  52 G  695  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  53 G  695  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  54 G  695  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 H  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 H  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 H  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 H  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 H  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 H  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 H  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 H  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 H  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 H  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 H  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 H  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 H  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 H  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 H  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 H  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 H  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 H  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 H  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 H  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 H  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 H  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 H  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 H  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 H  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 H  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 H  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 H  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 H  367  ARG LEU ARG                                                  
SEQRES   1 I  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 I  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 I  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 I  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 I  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 I  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 I  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 I  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 I  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 I  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 J  695  GLU THR SER LEU ALA GLU GLU LYS LEU THR MET GLY GLN          
SEQRES   2 J  695  THR GLY LYS LYS SER GLU LYS GLY PRO VAL CYS TRP ARG          
SEQRES   3 J  695  LYS ARG VAL LYS SER GLU TYR MET ARG LEU ARG GLN LEU          
SEQRES   4 J  695  LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS SER MET PHE          
SEQRES   5 J  695  SER SER ASN ARG GLN LYS ILE LEU GLU ARG THR GLU ILE          
SEQRES   6 J  695  LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE GLN PRO VAL          
SEQRES   7 J  695  HIS ILE LEU THR SER VAL SER SER LEU ARG GLY THR ARG          
SEQRES   8 J  695  GLU CYS SER VAL THR SER ASP LEU ASP PHE PRO THR GLN          
SEQRES   9 J  695  VAL ILE PRO LEU LYS THR LEU ASN ALA VAL ALA SER VAL          
SEQRES  10 J  695  PRO ILE MET TYR SER TRP SER PRO LEU GLN GLN ASN PHE          
SEQRES  11 J  695  MET VAL GLU ASP GLU THR VAL LEU HIS ASN ILE PRO TYR          
SEQRES  12 J  695  MET GLY ASP GLU VAL LEU ASP GLN ASP GLY THR PHE ILE          
SEQRES  13 J  695  GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS VAL HIS GLY          
SEQRES  14 J  695  ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU ILE PHE VAL          
SEQRES  15 J  695  GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN GLU SER ARG          
SEQRES  16 J  695  PRO PRO ARG LYS PHE PRO SER ASP LYS ILE PHE GLU ALA          
SEQRES  17 J  695  ILE SER SER MET PHE PRO ASP LYS GLY THR ALA GLU GLU          
SEQRES  18 J  695  LEU LYS GLU LYS TYR LYS GLU LEU THR GLN GLN GLN LEU          
SEQRES  19 J  695  PRO GLY ALA LEU PRO PRO GLU CYS THR PRO ASN ILE ASP          
SEQRES  20 J  695  GLY PRO ASN ALA LYS SER VAL GLN ARG GLU GLN SER LEU          
SEQRES  21 J  695  HIS SER PHE HIS THR LEU PHE CYS ARG ARG CYS PHE LYS          
SEQRES  22 J  695  TYR ASP CYS PHE LEU HIS PRO PHE HIS ALA THR PRO ASN          
SEQRES  23 J  695  THR TYR LYS ARG LYS ASN THR GLU THR ALA LEU ASP ASN          
SEQRES  24 J  695  LYS PRO CYS GLY PRO GLN CYS TYR GLN HIS LEU GLU GLY          
SEQRES  25 J  695  ALA LYS GLU PHE ALA ALA ALA LEU THR ALA GLU ARG ILE          
SEQRES  26 J  695  LYS THR PRO PRO LYS ARG PRO GLY GLY ARG ARG ARG GLY          
SEQRES  27 J  695  ARG LEU PRO ASN ASN SER SER ARG PRO SER THR PRO THR          
SEQRES  28 J  695  ILE ASN VAL LEU GLU SER LYS ASP THR ASP SER ASP ARG          
SEQRES  29 J  695  GLU ALA GLY PRO GLY LYS PRO ASN ILE GLU PRO PRO GLU          
SEQRES  30 J  695  ASN VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG          
SEQRES  31 J  695  VAL LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE          
SEQRES  32 J  695  ALA ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR          
SEQRES  33 J  695  GLU PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA          
SEQRES  34 J  695  PRO ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS          
SEQRES  35 J  695  ARG LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE          
SEQRES  36 J  695  GLN LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  37 J  695  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER          
SEQRES  38 J  695  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  39 J  695  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  40 J  695  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  41 J  695  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  42 J  695  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  43 J  695  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  44 J  695  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  45 J  695  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  46 J  695  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  47 J  695  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  48 J  695  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  49 J  695  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  50 J  695  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  51 J  695  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  52 J  695  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  53 J  695  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  54 J  695  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 K  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 K  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 K  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 K  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 K  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 K  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 K  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 K  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 K  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 K  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 K  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 K  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 K  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 K  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 K  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 K  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 K  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 K  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 K  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 K  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 K  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 K  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 K  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 K  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 K  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 K  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 K  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 K  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 K  367  ARG LEU ARG                                                  
SEQRES   1 L  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 L  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 L  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 L  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 L  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 L  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 L  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 L  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 L  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 L  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 Q   11  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER                  
SEQRES   1 R   11  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER                  
SEQRES   1 S   11  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER                  
SEQRES   1 T   11  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER                  
HET    M3L  Q   7      12                                                       
HET    M3L  R   7      12                                                       
HET    M3L  S   7      12                                                       
HET    M3L  T   7      12                                                       
HET     ZN  A 801       1                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET     ZN  A 804       1                                                       
HET     ZN  A 805       1                                                       
HET     ZN  A 806       1                                                       
HET     ZN  A 807       1                                                       
HET     ZN  A 808       1                                                       
HET    74D  A 809      37                                                       
HET     ZN  D 801       1                                                       
HET     ZN  D 802       1                                                       
HET     ZN  D 803       1                                                       
HET     ZN  D 804       1                                                       
HET     ZN  D 805       1                                                       
HET     ZN  D 806       1                                                       
HET     ZN  D 807       1                                                       
HET     ZN  D 808       1                                                       
HET    74D  D 809      37                                                       
HET     ZN  G 801       1                                                       
HET     ZN  G 802       1                                                       
HET     ZN  G 803       1                                                       
HET     ZN  G 804       1                                                       
HET     ZN  G 805       1                                                       
HET     ZN  G 806       1                                                       
HET     ZN  G 807       1                                                       
HET     ZN  G 808       1                                                       
HET    74D  G 809      37                                                       
HET     ZN  J 801       1                                                       
HET     ZN  J 802       1                                                       
HET     ZN  J 803       1                                                       
HET     ZN  J 804       1                                                       
HET     ZN  J 805       1                                                       
HET     ZN  J 806       1                                                       
HET     ZN  J 807       1                                                       
HET     ZN  J 808       1                                                       
HET    74D  J 809      37                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     74D 1-[(1~{R})-1-[1-[2,2-BIS(FLUORANYL)PROPYL]PIPERIDIN-4-           
HETNAM   2 74D  YL]ETHYL]-~{N}-[(4-METHOXY-6-METHYL-2-OXIDANYLIDENE-            
HETNAM   3 74D  3~{H}-PYRIDIN-3-YL)METHYL]-2-METHYL-INDOLE-3-                   
HETNAM   4 74D  CARBOXAMIDE                                                     
FORMUL  13  M3L    4(C9 H21 N2 O2 1+)                                           
FORMUL  17   ZN    32(ZN 2+)                                                    
FORMUL  25  74D    4(C28 H36 F2 N4 O3)                                          
HELIX    1 AA1 GLY A   11  GLN A   62  1                                  52    
HELIX    2 AA2 MET A  134  LEU A  139  1                                   6    
HELIX    3 AA3 GLY A  143  ASN A  152  1                                  10    
HELIX    4 AA4 ASN A  167  ASN A  182  1                                  16    
HELIX    5 AA5 LYS A  222  MET A  230  1                                   9    
HELIX    6 AA6 THR A  236  THR A  248  1                                  13    
HELIX    7 AA7 GLN A  273  LEU A  278  1                                   6    
HELIX    8 AA8 LEU A  278  PHE A  285  1                                   8    
HELIX    9 AA9 PRO A  303  LYS A  307  5                                   5    
HELIX   10 AB1 ALA A  331  LYS A  344  1                                  14    
HELIX   11 AB2 SER A  433  TYR A  448  1                                  16    
HELIX   12 AB3 ASN A  450  GLY A  459  1                                  10    
HELIX   13 AB4 THR A  462  ILE A  476  1                                  15    
HELIX   14 AB5 CYS A  534  ALA A  539  1                                   6    
HELIX   15 AB6 CYS A  571  ALA A  576  1                                   6    
HELIX   16 AB7 CYS A  604  GLY A  609  1                                   6    
HELIX   17 AB8 GLN A  648  TYR A  661  1                                  14    
HELIX   18 AB9 ASN A  682  ALA A  687  5                                   6    
HELIX   19 AC1 SER B  267  TYR B  280  1                                  14    
HELIX   20 AC2 ASP B  339  ILE B  343  5                                   5    
HELIX   21 AC3 ARG C  575  MET C  579  5                                   5    
HELIX   22 AC4 PRO C  589  GLU C  602  1                                  14    
HELIX   23 AC5 GLY C  609  GLY C  625  1                                  17    
HELIX   24 AC6 ALA C  628  ASN C  630  5                                   3    
HELIX   25 AC7 GLN C  631  TYR C  643  1                                  13    
HELIX   26 AC8 TYR C  643  LYS C  650  1                                   8    
HELIX   27 AC9 LEU C  652  PHE C  666  1                                  15    
HELIX   28 AD1 SER C  670  GLN C  685  1                                  16    
HELIX   29 AD2 GLY D   11  GLN D   62  1                                  52    
HELIX   30 AD3 MET D  134  LEU D  139  1                                   6    
HELIX   31 AD4 GLY D  143  ASN D  152  1                                  10    
HELIX   32 AD5 ASN D  167  GLN D  180  1                                  14    
HELIX   33 AD6 LYS D  222  PHE D  231  1                                  10    
HELIX   34 AD7 THR D  236  LEU D  247  1                                  12    
HELIX   35 AD8 GLN D  273  PHE D  285  1                                  13    
HELIX   36 AD9 PHE D  334  LYS D  344  1                                  11    
HELIX   37 AE1 SER D  433  TYR D  448  1                                  16    
HELIX   38 AE2 ASN D  450  GLY D  459  1                                  10    
HELIX   39 AE3 THR D  462  ILE D  476  1                                  15    
HELIX   40 AE4 CYS D  534  ALA D  539  1                                   6    
HELIX   41 AE5 CYS D  571  ALA D  576  1                                   6    
HELIX   42 AE6 CYS D  604  GLY D  609  1                                   6    
HELIX   43 AE7 ASP D  649  TYR D  661  1                                  13    
HELIX   44 AE8 LYS D  683  ALA D  687  5                                   5    
HELIX   45 AE9 SER E  267  TYR E  280  1                                  14    
HELIX   46 AF1 ARG F  575  MET F  579  5                                   5    
HELIX   47 AF2 PRO F  589  GLU F  602  1                                  14    
HELIX   48 AF3 GLY F  609  GLY F  625  1                                  17    
HELIX   49 AF4 GLN F  631  TYR F  643  1                                  13    
HELIX   50 AF5 TYR F  643  ASN F  651  1                                   9    
HELIX   51 AF6 LEU F  652  PHE F  666  1                                  15    
HELIX   52 AF7 SER F  670  GLU F  683  1                                  14    
HELIX   53 AF8 VAL G   13  GLN G   62  1                                  50    
HELIX   54 AF9 GLY G  143  ASN G  152  1                                  10    
HELIX   55 AG1 ASN G  167  ASN G  182  1                                  16    
HELIX   56 AG2 LYS G  222  PHE G  231  1                                  10    
HELIX   57 AG3 THR G  236  THR G  248  1                                  13    
HELIX   58 AG4 GLN G  273  LEU G  278  1                                   6    
HELIX   59 AG5 LEU G  278  PHE G  285  1                                   8    
HELIX   60 AG6 GLY G  330  LYS G  344  1                                  15    
HELIX   61 AG7 SER G  433  TYR G  448  1                                  16    
HELIX   62 AG8 ASN G  450  GLY G  459  1                                  10    
HELIX   63 AG9 THR G  462  ILE G  476  1                                  15    
HELIX   64 AH1 CYS G  534  GLN G  540  1                                   7    
HELIX   65 AH2 CYS G  571  ALA G  576  1                                   6    
HELIX   66 AH3 CYS G  604  GLY G  609  1                                   6    
HELIX   67 AH4 SER G  647  TYR G  661  1                                  15    
HELIX   68 AH5 LYS G  683  ALA G  687  5                                   5    
HELIX   69 AH6 SER H  267  TYR H  280  1                                  14    
HELIX   70 AH7 ARG I  575  MET I  579  5                                   5    
HELIX   71 AH8 PRO I  589  GLU I  602  1                                  14    
HELIX   72 AH9 GLY I  609  GLY I  625  1                                  17    
HELIX   73 AI1 GLN I  631  ASN I  642  1                                  12    
HELIX   74 AI2 TYR I  643  ASN I  651  1                                   9    
HELIX   75 AI3 LEU I  652  PHE I  666  1                                  15    
HELIX   76 AI4 ILE I  671  GLU I  683  1                                  13    
HELIX   77 AI5 GLY J   11  GLN J   62  1                                  52    
HELIX   78 AI6 MET J  134  LEU J  139  1                                   6    
HELIX   79 AI7 GLY J  143  ASN J  152  1                                  10    
HELIX   80 AI8 ASN J  167  ASN J  182  1                                  16    
HELIX   81 AI9 LYS J  222  MET J  230  1                                   9    
HELIX   82 AJ1 THR J  236  THR J  248  1                                  13    
HELIX   83 AJ2 GLN J  273  LEU J  278  1                                   6    
HELIX   84 AJ3 LEU J  278  PHE J  285  1                                   8    
HELIX   85 AJ4 PRO J  303  LYS J  307  5                                   5    
HELIX   86 AJ5 GLY J  330  LYS J  344  1                                  15    
HELIX   87 AJ6 SER J  433  TYR J  447  1                                  15    
HELIX   88 AJ7 ASN J  450  GLY J  459  1                                  10    
HELIX   89 AJ8 THR J  462  ILE J  476  1                                  15    
HELIX   90 AJ9 CYS J  534  ALA J  539  1                                   6    
HELIX   91 AK1 CYS J  571  ALA J  576  1                                   6    
HELIX   92 AK2 GLN J  648  TYR J  661  1                                  14    
HELIX   93 AK3 LYS J  683  ALA J  687  5                                   5    
HELIX   94 AK4 SER K  267  TYR K  280  1                                  14    
HELIX   95 AK5 ASP K  339  ILE K  343  5                                   5    
HELIX   96 AK6 ARG L  575  MET L  579  5                                   5    
HELIX   97 AK7 PRO L  589  GLU L  602  1                                  14    
HELIX   98 AK8 GLU L  610  GLY L  625  1                                  16    
HELIX   99 AK9 GLN L  631  ASN L  642  1                                  12    
HELIX  100 AL1 TYR L  643  LYS L  650  1                                   8    
HELIX  101 AL2 ARG L  654  PHE L  666  1                                  13    
HELIX  102 AL3 ILE L  671  GLU L  683  1                                  13    
SHEET    1 AA1 6 GLN A  94  PRO A  97  0                                        
SHEET    2 AA1 6 GLU A  82  SER A  87 -1  N  CYS A  83   O  ILE A  96           
SHEET    3 AA1 6 PHE B  82  GLU B  90 -1  O  LYS B  89   N  THR A  86           
SHEET    4 AA1 6 SER B 433  ARG B 439 -1  O  ILE B 434   N  LEU B  88           
SHEET    5 AA1 6 ILE B 424  CYS B 429 -1  N  LEU B 425   O  TRP B 437           
SHEET    6 AA1 6 ILE B 413  PHE B 418 -1  N  SER B 417   O  ILE B 426           
SHEET    1 AA2 5 LYS A  99  LEU A 101  0                                        
SHEET    2 AA2 5 ILE B 132  ASP B 140  1  O  VAL B 139   N  LYS A  99           
SHEET    3 AA2 5 ARG B 120  CYS B 126 -1  N  VAL B 121   O  TYR B 138           
SHEET    4 AA2 5 VAL B 112  GLY B 117 -1  N  PHE B 113   O  TYR B 124           
SHEET    5 AA2 5 LEU B  96  PHE B 101 -1  N  GLY B  98   O  VAL B 116           
SHEET    1 AA3 2 SER A 114  PRO A 115  0                                        
SHEET    2 AA3 2 LYS A 680  GLY A 681  1  O  GLY A 681   N  SER A 114           
SHEET    1 AA4 4 PHE A 120  MET A 121  0                                        
SHEET    2 AA4 4 GLU A 644  SER A 647  1  O  ILE A 645   N  PHE A 120           
SHEET    3 AA4 4 PHE A 673  ASP A 676 -1  O  VAL A 674   N  ILE A 646           
SHEET    4 AA4 4 LEU A 666  ASN A 668 -1  N  PHE A 667   O  VAL A 675           
SHEET    1 AA5 3 LEU A 614  PRO A 618  0                                        
SHEET    2 AA5 3 TRP A 624  ILE A 628 -1  O  PHE A 627   N  LEU A 615           
SHEET    3 AA5 3 GLU A 721  LEU A 722 -1  O  LEU A 722   N  ILE A 626           
SHEET    1 AA6 3 PHE A 637  SER A 639  0                                        
SHEET    2 AA6 3 ASP A 705  ALA A 712 -1  O  ILE A 710   N  SER A 639           
SHEET    3 AA6 3 CYS A 695  VAL A 702 -1  N  VAL A 702   O  ASP A 705           
SHEET    1 AA7 4 PHE B 147  TYR B 154  0                                        
SHEET    2 AA7 4 PRO B 161  GLY B 167 -1  O  ALA B 166   N  THR B 149           
SHEET    3 AA7 4 ILE B 172  ASN B 176 -1  O  ARG B 173   N  VAL B 165           
SHEET    4 AA7 4 GLN B 181  TYR B 186 -1  O  LYS B 184   N  ILE B 174           
SHEET    1 AA8 5 ILE B 193  PHE B 198  0                                        
SHEET    2 AA8 5 LEU B 205  SER B 210 -1  O  LEU B 207   N  LYS B 197           
SHEET    3 AA8 5 ARG B 216  ASN B 219 -1  O  TRP B 218   N  LEU B 206           
SHEET    4 AA8 5 THR B 224  PHE B 229 -1  O  ALA B 227   N  LEU B 217           
SHEET    5 AA8 5 GLN B 292  ILE B 294  1  O  GLN B 292   N  ILE B 228           
SHEET    1 AA9 4 VAL B 239  TYR B 244  0                                        
SHEET    2 AA9 4 LYS B 250  GLY B 255 -1  O  CYS B 254   N  SER B 241           
SHEET    3 AA9 4 LEU B 260  ARG B 264 -1  O  LYS B 261   N  SER B 253           
SHEET    4 AA9 4 PHE B 299  THR B 301 -1  O  PHE B 299   N  LEU B 262           
SHEET    1 AB1 4 CYS B 311  LEU B 315  0                                        
SHEET    2 AB1 4 LEU B 318  SER B 323 -1  O  LEU B 320   N  ARG B 313           
SHEET    3 AB1 4 ALA B 327  PRO B 333 -1  O  TRP B 331   N  ILE B 319           
SHEET    4 AB1 4 VAL B 350  PHE B 356 -1  O  PHE B 356   N  ILE B 328           
SHEET    1 AB2 4 PHE B 368  MET B 370  0                                        
SHEET    2 AB2 4 MET B 376  GLY B 380 -1  O  ALA B 378   N  SER B 369           
SHEET    3 AB2 4 LEU B 386  ASP B 390 -1  O  TRP B 389   N  LEU B 377           
SHEET    4 AB2 4 THR B 402  LEU B 404 -1  O  LEU B 404   N  LEU B 386           
SHEET    1 AB3 6 GLN D  94  PRO D  97  0                                        
SHEET    2 AB3 6 GLU D  82  SER D  87 -1  N  VAL D  85   O  GLN D  94           
SHEET    3 AB3 6 LYS E  83  GLU E  90 -1  O  LYS E  89   N  THR D  86           
SHEET    4 AB3 6 SER E 433  ASP E 438 -1  O  ILE E 434   N  LEU E  88           
SHEET    5 AB3 6 ILE E 424  VAL E 428 -1  N  ALA E 427   O  TRP E 435           
SHEET    6 AB3 6 THR E 416  PHE E 418 -1  N  SER E 417   O  ILE E 426           
SHEET    1 AB4 5 LYS D  99  LEU D 101  0                                        
SHEET    2 AB4 5 ILE E 132  ASP E 140  1  O  VAL E 139   N  LEU D 101           
SHEET    3 AB4 5 ARG E 120  CYS E 126 -1  N  LEU E 123   O  GLN E 136           
SHEET    4 AB4 5 VAL E 112  GLY E 117 -1  N  PHE E 113   O  TYR E 124           
SHEET    5 AB4 5 LEU E  96  PHE E 101 -1  N  GLN E 100   O  ALA E 114           
SHEET    1 AB5 4 SER D 114  PRO D 115  0                                        
SHEET    2 AB5 4 VAL D 674  GLY D 681  1  O  ARG D 679   N  SER D 114           
SHEET    3 AB5 4 GLY D 643  ILE D 646 -1  N  ILE D 646   O  VAL D 674           
SHEET    4 AB5 4 PHE D 120  MET D 121  1  N  PHE D 120   O  ILE D 645           
SHEET    1 AB6 3 SER D 114  PRO D 115  0                                        
SHEET    2 AB6 3 VAL D 674  GLY D 681  1  O  ARG D 679   N  SER D 114           
SHEET    3 AB6 3 LEU D 666  ASN D 668 -1  N  PHE D 667   O  VAL D 675           
SHEET    1 AB7 4 LEU D 614  PRO D 618  0                                        
SHEET    2 AB7 4 TRP D 624  ILE D 628 -1  O  PHE D 627   N  LEU D 615           
SHEET    3 AB7 4 GLU D 720  PHE D 724 -1  O  LEU D 722   N  ILE D 626           
SHEET    4 AB7 4 ASN D 688  HIS D 689  1  N  ASN D 688   O  PHE D 724           
SHEET    1 AB8 3 PHE D 637  TYR D 641  0                                        
SHEET    2 AB8 3 ASP D 705  ALA D 712 -1  O  ILE D 710   N  ILE D 638           
SHEET    3 AB8 3 CYS D 695  VAL D 702 -1  N  VAL D 702   O  ASP D 705           
SHEET    1 AB9 4 PHE E 147  TYR E 154  0                                        
SHEET    2 AB9 4 PRO E 161  GLY E 167 -1  O  LEU E 162   N  THR E 153           
SHEET    3 AB9 4 ILE E 172  ASN E 176 -1  O  ARG E 173   N  VAL E 165           
SHEET    4 AB9 4 GLN E 181  TYR E 186 -1  O  LYS E 184   N  ILE E 174           
SHEET    1 AC1 5 ILE E 193  HIS E 199  0                                        
SHEET    2 AC1 5 ASP E 202  SER E 210 -1  O  LEU E 207   N  LYS E 197           
SHEET    3 AC1 5 LEU E 215  ASN E 219 -1  O  TRP E 218   N  LEU E 206           
SHEET    4 AC1 5 THR E 224  PHE E 229 -1  O  THR E 224   N  ASN E 219           
SHEET    5 AC1 5 GLN E 292  ILE E 294  1  O  GLN E 292   N  ILE E 228           
SHEET    1 AC2 4 VAL E 239  TYR E 244  0                                        
SHEET    2 AC2 4 LYS E 250  GLY E 255 -1  O  CYS E 254   N  SER E 241           
SHEET    3 AC2 4 LEU E 260  ARG E 264 -1  O  LYS E 261   N  SER E 253           
SHEET    4 AC2 4 SER E 300  THR E 301 -1  O  THR E 301   N  LEU E 260           
SHEET    1 AC3 4 CYS E 311  LEU E 315  0                                        
SHEET    2 AC3 4 LEU E 318  LYS E 322 -1  O  LEU E 318   N  LEU E 315           
SHEET    3 AC3 4 ALA E 327  PRO E 333 -1  O  VAL E 329   N  SER E 321           
SHEET    4 AC3 4 VAL E 350  ASP E 357 -1  O  PHE E 356   N  ILE E 328           
SHEET    1 AC4 4 PHE E 368  MET E 370  0                                        
SHEET    2 AC4 4 MET E 376  GLY E 380 -1  O  ALA E 378   N  SER E 369           
SHEET    3 AC4 4 LEU E 386  ASP E 390 -1  O  TRP E 389   N  LEU E 377           
SHEET    4 AC4 4 THR E 402  LEU E 404 -1  O  THR E 402   N  VAL E 388           
SHEET    1 AC5 7 LEU H  88  LYS H  89  0                                        
SHEET    2 AC5 7 ARG G  81  SER G  87 -1  N  THR G  86   O  LYS H  89           
SHEET    3 AC5 7 GLN G  94  LEU G 101 -1  O  LEU G  98   N  ARG G  81           
SHEET    4 AC5 7 ILE H 132  ASP H 140  1  O  VAL H 139   N  LEU G 101           
SHEET    5 AC5 7 ARG H 120  CYS H 126 -1  N  GLU H 125   O  ARG H 133           
SHEET    6 AC5 7 LEU H 111  GLY H 117 -1  N  PHE H 113   O  TYR H 124           
SHEET    7 AC5 7 LEU H  96  PHE H 101 -1  N  GLN H 100   O  ALA H 114           
SHEET    1 AC6 4 SER G 114  PRO G 115  0                                        
SHEET    2 AC6 4 VAL G 674  GLY G 681  1  O  GLY G 681   N  SER G 114           
SHEET    3 AC6 4 GLY G 643  ILE G 646 -1  N  ILE G 646   O  VAL G 674           
SHEET    4 AC6 4 PHE G 120  MET G 121  1  N  PHE G 120   O  ILE G 645           
SHEET    1 AC7 3 SER G 114  PRO G 115  0                                        
SHEET    2 AC7 3 VAL G 674  GLY G 681  1  O  GLY G 681   N  SER G 114           
SHEET    3 AC7 3 LEU G 666  ASN G 668 -1  N  PHE G 667   O  VAL G 675           
SHEET    1 AC8 2 LEU G 614  PRO G 618  0                                        
SHEET    2 AC8 2 TRP G 624  ILE G 628 -1  O  PHE G 627   N  LEU G 615           
SHEET    1 AC9 3 PHE G 637  TYR G 641  0                                        
SHEET    2 AC9 3 ASP G 705  ALA G 712 -1  O  ILE G 710   N  SER G 639           
SHEET    3 AC9 3 CYS G 695  VAL G 702 -1  N  VAL G 702   O  ASP G 705           
SHEET    1 AD1 4 PHE H  82  ASN H  86  0                                        
SHEET    2 AD1 4 ARG H 436  ARG H 439 -1  O  ARG H 436   N  ASN H  86           
SHEET    3 AD1 4 ILE H 424  CYS H 429 -1  N  LEU H 425   O  TRP H 437           
SHEET    4 AD1 4 ILE H 413  PHE H 418 -1  N  SER H 417   O  ILE H 426           
SHEET    1 AD2 4 PHE H 147  ASP H 155  0                                        
SHEET    2 AD2 4 HIS H 160  GLY H 167 -1  O  LEU H 162   N  THR H 153           
SHEET    3 AD2 4 ILE H 172  ILE H 175 -1  O  ILE H 175   N  LEU H 163           
SHEET    4 AD2 4 CYS H 182  TYR H 186 -1  O  LYS H 184   N  ILE H 174           
SHEET    1 AD3 5 ILE H 193  PHE H 198  0                                        
SHEET    2 AD3 5 LEU H 205  SER H 210 -1  O  LEU H 207   N  LYS H 197           
SHEET    3 AD3 5 LEU H 215  ASN H 219 -1  O  ARG H 216   N  SER H 208           
SHEET    4 AD3 5 THR H 224  PHE H 229 -1  O  ALA H 227   N  LEU H 217           
SHEET    5 AD3 5 GLN H 292  ILE H 294  1  O  ILE H 294   N  ILE H 228           
SHEET    1 AD4 4 VAL H 239  TYR H 244  0                                        
SHEET    2 AD4 4 LYS H 250  GLY H 255 -1  O  MET H 252   N  ASP H 243           
SHEET    3 AD4 4 LEU H 260  ARG H 264 -1  O  TRP H 263   N  ILE H 251           
SHEET    4 AD4 4 PHE H 299  THR H 301 -1  O  THR H 301   N  LEU H 260           
SHEET    1 AD5 4 CYS H 311  LEU H 315  0                                        
SHEET    2 AD5 4 LEU H 318  LYS H 322 -1  O  LEU H 318   N  LEU H 315           
SHEET    3 AD5 4 ALA H 327  PRO H 333 -1  O  VAL H 329   N  SER H 321           
SHEET    4 AD5 4 VAL H 350  ASP H 357 -1  O  LEU H 353   N  CYS H 330           
SHEET    1 AD6 4 PHE H 368  MET H 370  0                                        
SHEET    2 AD6 4 MET H 376  GLY H 380 -1  O  ALA H 378   N  SER H 369           
SHEET    3 AD6 4 LEU H 386  ASP H 390 -1  O  TYR H 387   N  LEU H 379           
SHEET    4 AD6 4 THR H 402  LEU H 404 -1  O  THR H 402   N  VAL H 388           
SHEET    1 AD7 6 GLN J  94  PRO J  97  0                                        
SHEET    2 AD7 6 GLU J  82  SER J  87 -1  N  VAL J  85   O  GLN J  94           
SHEET    3 AD7 6 PHE K  82  LYS K  89 -1  O  LYS K  89   N  THR J  86           
SHEET    4 AD7 6 SER K 433  ARG K 439 -1  O  ILE K 434   N  LEU K  88           
SHEET    5 AD7 6 ILE K 424  CYS K 429 -1  N  LEU K 425   O  TRP K 437           
SHEET    6 AD7 6 ILE K 413  PHE K 418 -1  N  SER K 417   O  ILE K 426           
SHEET    1 AD8 5 LYS J  99  LEU J 101  0                                        
SHEET    2 AD8 5 GLU K 131  ASP K 140  1  O  VAL K 139   N  LEU J 101           
SHEET    3 AD8 5 ARG K 120  HIS K 127 -1  N  GLU K 125   O  ARG K 133           
SHEET    4 AD8 5 LEU K 111  GLY K 117 -1  N  PHE K 113   O  TYR K 124           
SHEET    5 AD8 5 LEU K  96  PHE K 101 -1  N  GLN K 100   O  ALA K 114           
SHEET    1 AD9 4 SER J 114  PRO J 115  0                                        
SHEET    2 AD9 4 PHE J 673  GLY J 681  1  O  ARG J 679   N  SER J 114           
SHEET    3 AD9 4 GLY J 643  SER J 647 -1  N  GLU J 644   O  ASP J 676           
SHEET    4 AD9 4 PHE J 120  MET J 121  1  N  PHE J 120   O  ILE J 645           
SHEET    1 AE1 3 SER J 114  PRO J 115  0                                        
SHEET    2 AE1 3 PHE J 673  GLY J 681  1  O  ARG J 679   N  SER J 114           
SHEET    3 AE1 3 LEU J 666  ASN J 668 -1  N  PHE J 667   O  VAL J 675           
SHEET    1 AE2 3 LEU J 614  PRO J 618  0                                        
SHEET    2 AE2 3 TRP J 624  ILE J 628 -1  O  PHE J 627   N  LEU J 615           
SHEET    3 AE2 3 GLU J 720  GLU J 721 -1  O  GLU J 720   N  ILE J 628           
SHEET    1 AE3 3 PHE J 637  GLU J 640  0                                        
SHEET    2 AE3 3 ASP J 705  ALA J 712 -1  O  ILE J 710   N  ILE J 638           
SHEET    3 AE3 3 CYS J 695  VAL J 702 -1  N  LYS J 698   O  GLY J 709           
SHEET    1 AE4 2 ASN J 688  HIS J 689  0                                        
SHEET    2 AE4 2 PHE J 723  PHE J 724  1  O  PHE J 724   N  ASN J 688           
SHEET    1 AE5 4 PHE K 147  ASP K 155  0                                        
SHEET    2 AE5 4 HIS K 160  GLY K 167 -1  O  LEU K 162   N  THR K 153           
SHEET    3 AE5 4 ILE K 172  ASN K 176 -1  O  ILE K 175   N  LEU K 163           
SHEET    4 AE5 4 GLN K 181  TYR K 186 -1  O  TYR K 186   N  ILE K 172           
SHEET    1 AE6 5 ILE K 193  PHE K 198  0                                        
SHEET    2 AE6 5 LEU K 205  SER K 210 -1  O  LEU K 207   N  LYS K 197           
SHEET    3 AE6 5 LEU K 215  ASN K 219 -1  O  TRP K 218   N  LEU K 206           
SHEET    4 AE6 5 THR K 224  PHE K 229 -1  O  PHE K 229   N  LEU K 215           
SHEET    5 AE6 5 GLN K 292  ILE K 294  1  O  ILE K 294   N  ILE K 228           
SHEET    1 AE7 4 VAL K 239  TYR K 244  0                                        
SHEET    2 AE7 4 LYS K 250  GLY K 255 -1  O  MET K 252   N  ASP K 243           
SHEET    3 AE7 4 LEU K 260  ARG K 264 -1  O  TRP K 263   N  ILE K 251           
SHEET    4 AE7 4 PHE K 299  THR K 301 -1  O  PHE K 299   N  LEU K 262           
SHEET    1 AE8 4 CYS K 311  LEU K 315  0                                        
SHEET    2 AE8 4 LEU K 318  LYS K 322 -1  O  LEU K 320   N  ARG K 313           
SHEET    3 AE8 4 ALA K 327  PRO K 333 -1  O  VAL K 329   N  SER K 321           
SHEET    4 AE8 4 VAL K 350  ASP K 357 -1  O  PHE K 356   N  ILE K 328           
SHEET    1 AE9 2 MET K 376  GLY K 380  0                                        
SHEET    2 AE9 2 LEU K 386  ASP K 390 -1  O  TRP K 389   N  LEU K 377           
LINK         SG  CYS A 286                ZN    ZN A 801     1555   1555  2.33  
LINK         SG  CYS A 294                ZN    ZN A 801     1555   1555  2.50  
LINK         ND1 HIS A 297                ZN    ZN A 801     1555   1555  2.17  
LINK         SG  CYS A 320                ZN    ZN A 802     1555   1555  2.82  
LINK         SG  CYS A 452                ZN    ZN A 802     1555   1555  2.37  
LINK         SG  CYS A 463                ZN    ZN A 802     1555   1555  1.93  
LINK         SG  CYS A 523                ZN    ZN A 804     1555   1555  2.21  
LINK         SG  CYS A 523                ZN    ZN A 805     1555   1555  2.31  
LINK         NE2 HIS A 525                ZN    ZN A 804     1555   1555  2.39  
LINK         SG  CYS A 530                ZN    ZN A 803     1555   1555  1.92  
LINK         SG  CYS A 530                ZN    ZN A 804     1555   1555  2.46  
LINK         SG  CYS A 534                ZN    ZN A 804     1555   1555  2.35  
LINK         SG  CYS A 536                ZN    ZN A 805     1555   1555  2.42  
LINK         SG  CYS A 543                ZN    ZN A 803     1555   1555  2.47  
LINK         SG  CYS A 543                ZN    ZN A 805     1555   1555  2.27  
LINK         SG  CYS A 547                ZN    ZN A 805     1555   1555  2.25  
LINK         SG  CYS A 549                ZN    ZN A 803     1555   1555  2.32  
LINK         SG  CYS A 553                ZN    ZN A 803     1555   1555  2.63  
LINK         SG  CYS A 560                ZN    ZN A 808     1555   1555  2.28  
LINK         SG  CYS A 560                ZN    ZN A 807     1555   1555  2.49  
LINK         SG  CYS A 562                ZN    ZN A 808     1555   1555  2.47  
LINK         SG  CYS A 566                ZN    ZN A 808     1555   1555  2.88  
LINK         SG  CYS A 566                ZN    ZN A 806     1555   1555  2.39  
LINK         SG  CYS A 571                ZN    ZN A 808     1555   1555  2.33  
LINK         SG  CYS A 573                ZN    ZN A 807     1555   1555  2.16  
LINK         SG  CYS A 580                ZN    ZN A 806     1555   1555  2.40  
LINK         SG  CYS A 580                ZN    ZN A 807     1555   1555  2.76  
LINK         SG  CYS A 585                ZN    ZN A 807     1555   1555  2.11  
LINK         SG  CYS A 588                ZN    ZN A 806     1555   1555  2.12  
LINK         SG  CYS A 601                ZN    ZN A 806     1555   1555  2.80  
LINK         SG  CYS D 286                ZN    ZN D 801     1555   1555  2.33  
LINK         SG  CYS D 289                ZN    ZN D 801     1555   1555  2.12  
LINK         SG  CYS D 294                ZN    ZN D 801     1555   1555  2.06  
LINK         ND1 HIS D 297                ZN    ZN D 801     1555   1555  2.08  
LINK         SG  CYS D 320                ZN    ZN D 802     1555   1555  2.12  
LINK         SG  CYS D 452                ZN    ZN D 802     1555   1555  2.12  
LINK         SG  CYS D 463                ZN    ZN D 802     1555   1555  2.54  
LINK         SG  CYS D 523                ZN    ZN D 804     1555   1555  2.42  
LINK         SG  CYS D 523                ZN    ZN D 805     1555   1555  2.41  
LINK         NE2 HIS D 525                ZN    ZN D 804     1555   1555  2.29  
LINK         SG  CYS D 530                ZN    ZN D 804     1555   1555  2.32  
LINK         SG  CYS D 530                ZN    ZN D 803     1555   1555  2.20  
LINK         SG  CYS D 534                ZN    ZN D 804     1555   1555  2.29  
LINK         SG  CYS D 536                ZN    ZN D 805     1555   1555  2.24  
LINK         SG  CYS D 543                ZN    ZN D 805     1555   1555  2.35  
LINK         SG  CYS D 543                ZN    ZN D 803     1555   1555  2.35  
LINK         SG  CYS D 547                ZN    ZN D 805     1555   1555  2.22  
LINK         SG  CYS D 549                ZN    ZN D 803     1555   1555  2.32  
LINK         SG  CYS D 553                ZN    ZN D 803     1555   1555  2.45  
LINK         SG  CYS D 560                ZN    ZN D 807     1555   1555  1.99  
LINK         SG  CYS D 560                ZN    ZN D 808     1555   1555  2.39  
LINK         SG  CYS D 562                ZN    ZN D 808     1555   1555  2.43  
LINK         SG  CYS D 566                ZN    ZN D 806     1555   1555  2.23  
LINK         SG  CYS D 566                ZN    ZN D 808     1555   1555  2.93  
LINK         SG  CYS D 571                ZN    ZN D 808     1555   1555  2.07  
LINK         SG  CYS D 573                ZN    ZN D 807     1555   1555  2.35  
LINK         SG  CYS D 580                ZN    ZN D 806     1555   1555  2.16  
LINK         SG  CYS D 580                ZN    ZN D 807     1555   1555  2.59  
LINK         SG  CYS D 585                ZN    ZN D 807     1555   1555  2.15  
LINK         SG  CYS D 588                ZN    ZN D 806     1555   1555  2.35  
LINK         SG  CYS D 601                ZN    ZN D 806     1555   1555  2.50  
LINK         SG  CYS G 286                ZN    ZN G 801     1555   1555  2.55  
LINK         SG  CYS G 289                ZN    ZN G 801     1555   1555  2.26  
LINK         SG  CYS G 294                ZN    ZN G 801     1555   1555  2.22  
LINK         ND1 HIS G 297                ZN    ZN G 801     1555   1555  2.13  
LINK         SG  CYS G 324                ZN    ZN G 802     1555   1555  2.58  
LINK         SG  CYS G 452                ZN    ZN G 802     1555   1555  2.70  
LINK         SG  CYS G 523                ZN    ZN G 804     1555   1555  2.20  
LINK         SG  CYS G 523                ZN    ZN G 805     1555   1555  2.04  
LINK         NE2 HIS G 525                ZN    ZN G 804     1555   1555  2.38  
LINK         SG  CYS G 530                ZN    ZN G 803     1555   1555  2.01  
LINK         SG  CYS G 530                ZN    ZN G 804     1555   1555  2.32  
LINK         SG  CYS G 534                ZN    ZN G 804     1555   1555  2.27  
LINK         SG  CYS G 536                ZN    ZN G 805     1555   1555  2.21  
LINK         SG  CYS G 543                ZN    ZN G 803     1555   1555  2.32  
LINK         SG  CYS G 543                ZN    ZN G 805     1555   1555  2.70  
LINK         SG  CYS G 547                ZN    ZN G 805     1555   1555  2.32  
LINK         SG  CYS G 549                ZN    ZN G 803     1555   1555  2.40  
LINK         SG  CYS G 553                ZN    ZN G 803     1555   1555  2.12  
LINK         SG  CYS G 560                ZN    ZN G 808     1555   1555  2.42  
LINK         SG  CYS G 560                ZN    ZN G 807     1555   1555  2.37  
LINK         SG  CYS G 562                ZN    ZN G 808     1555   1555  2.64  
LINK         SG  CYS G 566                ZN    ZN G 806     1555   1555  2.53  
LINK         SG  CYS G 566                ZN    ZN G 808     1555   1555  2.91  
LINK         SG  CYS G 571                ZN    ZN G 808     1555   1555  2.66  
LINK         SG  CYS G 573                ZN    ZN G 807     1555   1555  2.57  
LINK         SG  CYS G 580                ZN    ZN G 806     1555   1555  2.25  
LINK         SG  CYS G 580                ZN    ZN G 807     1555   1555  2.45  
LINK         SG  CYS G 585                ZN    ZN G 807     1555   1555  2.28  
LINK         SG  CYS G 601                ZN    ZN G 806     1555   1555  2.37  
LINK         SG  CYS J 286                ZN    ZN J 801     1555   1555  2.54  
LINK         SG  CYS J 289                ZN    ZN J 801     1555   1555  1.99  
LINK         SG  CYS J 294                ZN    ZN J 801     1555   1555  2.13  
LINK         ND1 HIS J 297                ZN    ZN J 801     1555   1555  2.04  
LINK         SG  CYS J 320                ZN    ZN J 802     1555   1555  2.09  
LINK         SG  CYS J 324                ZN    ZN J 802     1555   1555  2.90  
LINK         SG  CYS J 463                ZN    ZN J 802     1555   1555  2.77  
LINK         SG  CYS J 523                ZN    ZN J 805     1555   1555  2.10  
LINK         SG  CYS J 523                ZN    ZN J 804     1555   1555  2.51  
LINK         NE2 HIS J 525                ZN    ZN J 804     1555   1555  2.69  
LINK         SG  CYS J 530                ZN    ZN J 803     1555   1555  2.32  
LINK         SG  CYS J 530                ZN    ZN J 804     1555   1555  2.02  
LINK         SG  CYS J 534                ZN    ZN J 804     1555   1555  2.09  
LINK         SG  CYS J 536                ZN    ZN J 805     1555   1555  2.06  
LINK         SG  CYS J 543                ZN    ZN J 803     1555   1555  2.79  
LINK         SG  CYS J 547                ZN    ZN J 805     1555   1555  2.47  
LINK         SG  CYS J 549                ZN    ZN J 803     1555   1555  2.18  
LINK         SG  CYS J 553                ZN    ZN J 803     1555   1555  2.25  
LINK         SG  CYS J 560                ZN    ZN J 808     1555   1555  2.26  
LINK         SG  CYS J 560                ZN    ZN J 807     1555   1555  2.41  
LINK         SG  CYS J 562                ZN    ZN J 808     1555   1555  2.26  
LINK         SG  CYS J 566                ZN    ZN J 806     1555   1555  2.43  
LINK         SG  CYS J 566                ZN    ZN J 808     1555   1555  2.91  
LINK         SG  CYS J 571                ZN    ZN J 808     1555   1555  2.78  
LINK         SG  CYS J 573                ZN    ZN J 807     1555   1555  2.43  
LINK         SG  CYS J 580                ZN    ZN J 806     1555   1555  2.51  
LINK         SG  CYS J 580                ZN    ZN J 807     1555   1555  2.20  
LINK         SG  CYS J 585                ZN    ZN J 807     1555   1555  2.08  
LINK         SG  CYS J 601                ZN    ZN J 806     1555   1555  2.48  
LINK         C   ARG Q   6                 N   M3L Q   7     1555   1555  1.33  
LINK         C   M3L Q   7                 N   PHE Q   8     1555   1555  1.33  
LINK         C   ARG R   6                 N   M3L R   7     1555   1555  1.34  
LINK         C   M3L R   7                 N   PHE R   8     1555   1555  1.33  
LINK         C   ARG S   6                 N   M3L S   7     1555   1555  1.33  
LINK         C   M3L S   7                 N   PHE S   8     1555   1555  1.33  
LINK         C   ARG T   6                 N   M3L T   7     1555   1555  1.34  
LINK         C   M3L T   7                 N   PHE T   8     1555   1555  1.34  
CISPEP   1 SER A   73    VAL A   74          0        11.62                     
CISPEP   2 GLN A  141    ASP A  142          0        -3.38                     
CISPEP   3 HIS A  158    GLY A  159          0         9.56                     
CISPEP   4 SER A  212    ARG A  213          0         9.70                     
CISPEP   5 PRO A  214    PRO A  215          0        -8.62                     
CISPEP   6 GLY A  235    THR A  236          0        15.16                     
CISPEP   7 PRO A  258    GLU A  259          0        13.08                     
CISPEP   8 THR A  302    PRO A  303          0       -19.58                     
CISPEP   9 GLU A  312    THR A  313          0        -7.06                     
CISPEP  10 LYS A  318    PRO A  319          0        -4.56                     
CISPEP  11 CYS A  320    GLY A  321          0         2.28                     
CISPEP  12 GLY A  321    PRO A  322          0       -11.64                     
CISPEP  13 LYS B   79    TYR B   80          0         7.03                     
CISPEP  14 SER B  128    GLN B  129          0       -12.81                     
CISPEP  15 PRO B  396    HIS B  397          0        19.30                     
CISPEP  16 HIS B  397    LYS B  398          0        -3.09                     
CISPEP  17 ALA B  399    LYS B  400          0       -22.22                     
CISPEP  18 VAL C  581    ASP C  582          0        -2.54                     
CISPEP  19 GLU C  586    LYS C  587          0        -2.42                     
CISPEP  20 GLU C  608    GLY C  609          0         2.46                     
CISPEP  21 SER D   73    VAL D   74          0         7.32                     
CISPEP  22 GLN D  141    ASP D  142          0         4.48                     
CISPEP  23 HIS D  158    GLY D  159          0         5.31                     
CISPEP  24 SER D  212    ARG D  213          0        -1.33                     
CISPEP  25 PRO D  214    PRO D  215          0       -13.32                     
CISPEP  26 GLY D  235    THR D  236          0         9.65                     
CISPEP  27 PRO D  258    GLU D  259          0       -10.37                     
CISPEP  28 THR D  302    PRO D  303          0       -18.03                     
CISPEP  29 THR D  311    GLU D  312          0        22.59                     
CISPEP  30 GLU D  312    THR D  313          0         3.31                     
CISPEP  31 LYS D  318    PRO D  319          0        -7.32                     
CISPEP  32 CYS D  320    GLY D  321          0       -11.53                     
CISPEP  33 GLY D  321    PRO D  322          0       -12.23                     
CISPEP  34 GLN D  326    HIS D  327          0       -28.31                     
CISPEP  35 LYS E   79    TYR E   80          0        -1.53                     
CISPEP  36 SER E  128    GLN E  129          0        -8.42                     
CISPEP  37 PRO E  396    HIS E  397          0        23.57                     
CISPEP  38 HIS E  397    LYS E  398          0        -2.82                     
CISPEP  39 ALA E  399    LYS E  400          0       -11.12                     
CISPEP  40 HIS F  561    ASN F  562          0       -27.90                     
CISPEP  41 VAL F  581    ASP F  582          0        -0.07                     
CISPEP  42 GLU F  586    LYS F  587          0         1.06                     
CISPEP  43 GLU F  608    GLY F  609          0        12.76                     
CISPEP  44 SER G   73    VAL G   74          0        -0.18                     
CISPEP  45 GLN G  141    ASP G  142          0         6.90                     
CISPEP  46 HIS G  158    GLY G  159          0       -10.08                     
CISPEP  47 SER G  212    ARG G  213          0        -3.13                     
CISPEP  48 PRO G  214    PRO G  215          0       -12.88                     
CISPEP  49 GLY G  235    THR G  236          0        17.22                     
CISPEP  50 PRO G  258    GLU G  259          0        10.57                     
CISPEP  51 THR G  302    PRO G  303          0        -6.95                     
CISPEP  52 THR G  311    GLU G  312          0        20.16                     
CISPEP  53 GLU G  312    THR G  313          0        -6.11                     
CISPEP  54 LYS G  318    PRO G  319          0        -4.73                     
CISPEP  55 CYS G  320    GLY G  321          0        -5.06                     
CISPEP  56 GLY G  321    PRO G  322          0         7.93                     
CISPEP  57 GLN G  326    HIS G  327          0       -24.36                     
CISPEP  58 SER G  729    GLN G  730          0        -6.40                     
CISPEP  59 LYS H   79    TYR H   80          0         1.92                     
CISPEP  60 SER H  128    GLN H  129          0        -1.01                     
CISPEP  61 PRO H  396    HIS H  397          0        17.29                     
CISPEP  62 HIS H  397    LYS H  398          0       -10.34                     
CISPEP  63 ALA H  399    LYS H  400          0        -8.82                     
CISPEP  64 HIS I  561    ASN I  562          0       -21.65                     
CISPEP  65 MET I  579    GLU I  580          0       -23.94                     
CISPEP  66 VAL I  581    ASP I  582          0        -1.33                     
CISPEP  67 GLU I  586    LYS I  587          0        -1.16                     
CISPEP  68 GLU I  608    GLY I  609          0        14.27                     
CISPEP  69 SER J   73    VAL J   74          0         7.35                     
CISPEP  70 GLN J  141    ASP J  142          0        -0.63                     
CISPEP  71 HIS J  158    GLY J  159          0        -4.41                     
CISPEP  72 SER J  212    ARG J  213          0         4.91                     
CISPEP  73 PRO J  214    PRO J  215          0        -7.19                     
CISPEP  74 GLY J  235    THR J  236          0        17.66                     
CISPEP  75 PRO J  258    GLU J  259          0         0.00                     
CISPEP  76 THR J  302    PRO J  303          0       -11.01                     
CISPEP  77 THR J  311    GLU J  312          0        20.25                     
CISPEP  78 GLU J  312    THR J  313          0        -9.78                     
CISPEP  79 LYS J  318    PRO J  319          0         3.52                     
CISPEP  80 CYS J  320    GLY J  321          0        -2.86                     
CISPEP  81 GLY J  321    PRO J  322          0       -11.77                     
CISPEP  82 GLN J  326    HIS J  327          0       -27.29                     
CISPEP  83 LYS K   79    TYR K   80          0         0.41                     
CISPEP  84 SER K  128    GLN K  129          0        -2.68                     
CISPEP  85 PRO K  396    HIS K  397          0        23.46                     
CISPEP  86 HIS K  397    LYS K  398          0       -12.33                     
CISPEP  87 ALA K  399    LYS K  400          0       -13.15                     
CISPEP  88 HIS L  561    ASN L  562          0       -22.62                     
CISPEP  89 VAL L  581    ASP L  582          0        -5.02                     
CISPEP  90 GLU L  586    LYS L  587          0        -5.85                     
CISPEP  91 GLU L  608    GLY L  609          0        17.53                     
CISPEP  92 ALA Q    9    GLN Q   10          0       -14.15                     
CISPEP  93 GLN R   10    SER R   11          0        -1.57                     
CISPEP  94 ALA S    9    GLN S   10          0        -3.97                     
CISPEP  95 ALA T    9    GLN T   10          0         9.14                     
CISPEP  96 GLN T   10    SER T   11          0        -4.72                     
SITE     1 AC1  4 CYS A 286  CYS A 289  CYS A 294  HIS A 297                    
SITE     1 AC2  4 CYS A 320  CYS A 324  CYS A 452  CYS A 463                    
SITE     1 AC3  5 CYS A 530  CYS A 543  CYS A 549  CYS A 553                    
SITE     2 AC3  5  ZN A 804                                                     
SITE     1 AC4  6 CYS A 523  HIS A 525  CYS A 530  CYS A 534                    
SITE     2 AC4  6  ZN A 803   ZN A 805                                          
SITE     1 AC5  5 CYS A 523  CYS A 536  CYS A 543  CYS A 547                    
SITE     2 AC5  5  ZN A 804                                                     
SITE     1 AC6  6 CYS A 560  CYS A 566  CYS A 580  CYS A 588                    
SITE     2 AC6  6 CYS A 601   ZN A 808                                          
SITE     1 AC7  4 CYS A 560  CYS A 573  CYS A 580  CYS A 585                    
SITE     1 AC8  5 CYS A 560  CYS A 562  CYS A 566  CYS A 571                    
SITE     2 AC8  5  ZN A 806                                                     
SITE     1 AC9 10 ILE A 109  TYR A 111  TRP A 624  TYR A 658                    
SITE     2 AC9 10 CYS A 663  PHE A 665  PHE A 686  ASN A 688                    
SITE     3 AC9 10 ARG B 236  ASP B 237                                          
SITE     1 AD1  4 CYS D 286  CYS D 289  CYS D 294  HIS D 297                    
SITE     1 AD2  4 CYS D 320  CYS D 324  CYS D 452  CYS D 463                    
SITE     1 AD3  5 CYS D 530  CYS D 543  CYS D 549  CYS D 553                    
SITE     2 AD3  5  ZN D 804                                                     
SITE     1 AD4  5 CYS D 523  HIS D 525  CYS D 530  CYS D 534                    
SITE     2 AD4  5  ZN D 803                                                     
SITE     1 AD5  4 CYS D 523  CYS D 536  CYS D 543  CYS D 547                    
SITE     1 AD6  6 CYS D 560  CYS D 566  CYS D 580  CYS D 588                    
SITE     2 AD6  6 CYS D 601   ZN D 808                                          
SITE     1 AD7  4 CYS D 560  CYS D 573  CYS D 580  CYS D 585                    
SITE     1 AD8  5 CYS D 560  CYS D 562  CYS D 566  CYS D 571                    
SITE     2 AD8  5  ZN D 806                                                     
SITE     1 AD9 13 ILE D 109  MET D 110  TYR D 111  GLY D 623                    
SITE     2 AD9 13 TRP D 624  TYR D 658  TYR D 661  CYS D 663                    
SITE     3 AD9 13 PHE D 665  ARG D 685  PHE D 686  ASN D 688                    
SITE     4 AD9 13 ASP E 237                                                     
SITE     1 AE1  4 CYS G 286  CYS G 289  CYS G 294  HIS G 297                    
SITE     1 AE2  5 CYS G 320  CYS G 324  TYR G 325  CYS G 452                    
SITE     2 AE2  5 CYS G 463                                                     
SITE     1 AE3  4 CYS G 530  CYS G 543  CYS G 549  CYS G 553                    
SITE     1 AE4  4 CYS G 523  HIS G 525  CYS G 530  CYS G 534                    
SITE     1 AE5  4 CYS G 523  CYS G 536  CYS G 543  CYS G 547                    
SITE     1 AE6  5 CYS G 566  CYS G 580  CYS G 588  CYS G 601                    
SITE     2 AE6  5  ZN G 808                                                     
SITE     1 AE7  5 CYS G 560  CYS G 573  CYS G 580  CYS G 585                    
SITE     2 AE7  5  ZN G 808                                                     
SITE     1 AE8  6 CYS G 560  CYS G 562  CYS G 566  CYS G 571                    
SITE     2 AE8  6  ZN G 806   ZN G 807                                          
SITE     1 AE9 12 MET G 110  TYR G 111  PRO G 132  TRP G 624                    
SITE     2 AE9 12 VAL G 657  TYR G 661  CYS G 663  PHE G 665                    
SITE     3 AE9 12 THR G 678  ARG G 685  PHE G 686  ASN G 688                    
SITE     1 AF1  4 CYS J 286  CYS J 289  CYS J 294  HIS J 297                    
SITE     1 AF2  4 CYS J 320  CYS J 324  CYS J 452  CYS J 463                    
SITE     1 AF3  4 CYS J 530  CYS J 543  CYS J 549  CYS J 553                    
SITE     1 AF4  4 CYS J 523  HIS J 525  CYS J 530  CYS J 534                    
SITE     1 AF5  4 CYS J 523  CYS J 536  CYS J 543  CYS J 547                    
SITE     1 AF6  6 CYS J 560  CYS J 566  CYS J 580  CYS J 588                    
SITE     2 AF6  6 CYS J 601   ZN J 808                                          
SITE     1 AF7  5 CYS J 560  CYS J 573  CYS J 580  CYS J 585                    
SITE     2 AF7  5  ZN J 808                                                     
SITE     1 AF8  6 CYS J 560  CYS J 562  CYS J 566  CYS J 571                    
SITE     2 AF8  6  ZN J 806   ZN J 807                                          
SITE     1 AF9 10 MET J 110  TYR J 111  GLY J 623  TRP J 624                    
SITE     2 AF9 10 TYR J 661  CYS J 663  PHE J 665  ARG J 685                    
SITE     3 AF9 10 PHE J 686  ASP K 237                                          
SITE     1 AG1 11 ASP A 136  ASP A 140  PHE B  97  TYR B 148                    
SITE     2 AG1 11 ILE B 363  TRP B 364  TYR B 365  ARG B 414                    
SITE     3 AG1 11 GLN Q   3  GLN Q   5  PHE Q   8                               
SITE     1 AG2  9 ASP A 136  PHE B  97  TYR B 148  ILE B 363                    
SITE     2 AG2  9 TRP B 364  TYR B 365  ARG B 414  ARG Q   6                    
SITE     3 AG2  9 ALA Q   9                                                     
SITE     1 AG3 11 ASP D 136  TYR E 148  ILE E 363  TRP E 364                    
SITE     2 AG3 11 ARG E 414  LYS K 408  GLN R   3  ALA R   4                    
SITE     3 AG3 11 GLN R   5  PHE R   8  GLN R  10                               
SITE     1 AG4  7 ASP D 136  TYR E 148  ILE E 363  TRP E 364                    
SITE     2 AG4  7 ARG E 414  ARG R   6  ALA R   9                               
SITE     1 AG5 10 ASP G 136  PHE H  97  ILE H 363  TRP H 364                    
SITE     2 AG5 10 TYR H 365  ARG H 414  GLN S   3  ALA S   4                    
SITE     3 AG5 10 GLN S   5  PHE S   8                                          
SITE     1 AG6  9 ASP G 136  PHE H  97  ILE H 363  TRP H 364                    
SITE     2 AG6  9 TYR H 365  ARG H 414  ASP H 430  ARG S   6                    
SITE     3 AG6  9 ALA S   9                                                     
SITE     1 AG7 11 ASP J 136  ASP J 140  PHE K  97  TYR K 148                    
SITE     2 AG7 11 ILE K 363  TRP K 364  TYR K 365  ARG K 414                    
SITE     3 AG7 11 GLN T   5  PHE T   8  ALA T   9                               
SITE     1 AG8  9 ASP J 136  PHE K  97  TYR K 148  ILE K 363                    
SITE     2 AG8  9 TRP K 364  TYR K 365  ARG K 414  ARG T   6                    
SITE     3 AG8  9 ALA T   9                                                     
CRYST1  131.310  170.270  275.540  90.00  90.00  90.00 P 21 21 21   16          
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      0.007616  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003629        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system