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Database: PDB
Entry: 5IJ7
LinkDB: 5IJ7
Original site: 5IJ7 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-MAR-16   5IJ7              
TITLE     STRUCTURE OF HS/ACPRC2 IN COMPLEX WITH A PYRIDONE INHIBITOR           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENHANCER OF ZESTE HOMOLOG 2 (EZH2),HISTONE-LYSINE N-       
COMPND   3 METHYLTRANSFERASE EZH2;                                              
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: ENX-1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE
COMPND   6 6;                                                                   
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: POLYCOMB PROTEIN EED;                                      
COMPND  11 CHAIN: E, F;                                                         
COMPND  12 SYNONYM: HEED,WD PROTEIN ASSOCIATING WITH INTEGRIN CYTOPLASMIC TAILS 
COMPND  13 1,WAIT-1;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: POLYCOMB PROTEIN SUZ12;                                    
COMPND  17 CHAIN: S, T;                                                         
COMPND  18 SYNONYM: CHROMATIN PRECIPITATED E2F TARGET 9 PROTEIN,CHET 9 PROTEIN, 
COMPND  19 JOINED TO JAZF1 PROTEIN,SUPPRESSOR OF ZESTE 12 PROTEIN HOMOLOG;      
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANOLIS CAROLINENSIS, HOMO SAPIENS;              
SOURCE   3 ORGANISM_COMMON: GREEN ANOLE, HUMAN;                                 
SOURCE   4 ORGANISM_TAXID: 28377, 9606;                                         
SOURCE   5 GENE: EZH2, EZH2, KMT6;                                              
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
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: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
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: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    LYSINE METHYLTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.S.GAJIWALA,A.BROOUN,Y.-L.DENG,W.LIU                                 
REVDAT   3   22-NOV-17 5IJ7    1       REMARK                                   
REVDAT   2   11-MAY-16 5IJ7    1       JRNL                                     
REVDAT   1   04-MAY-16 5IJ7    0                                                
JRNL        AUTH   A.BROOUN,K.S.GAJIWALA,Y.L.DENG,W.LIU,B.BOLANOS,P.BINGHAM,    
JRNL        AUTH 2 Y.A.HE,W.DIEHL,N.GRABLE,P.P.KUNG,S.SUTTON,K.A.MAEGLEY,X.YU,  
JRNL        AUTH 3 A.E.STEWART                                                  
JRNL        TITL   POLYCOMB REPRESSIVE COMPLEX 2 STRUCTURE WITH INHIBITOR       
JRNL        TITL 2 REVEALS A MECHANISM OF ACTIVATION AND DRUG RESISTANCE.       
JRNL        REF    NAT COMMUN                    V.   7 11384 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27122193                                                     
JRNL        DOI    10.1038/NCOMMS11384                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 70532                          
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)  : 0.194                          
REMARK   3   R VALUE            (WORKING SET)  : 0.191                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.090                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3591                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.62                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.60                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5242                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2347                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4977                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2318                   
REMARK   3   BIN FREE R VALUE                        : 0.2868                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.06                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 265                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15510                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 73.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.67040                                            
REMARK   3    B22 (A**2) : 18.30440                                             
REMARK   3    B33 (A**2) : -3.63400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.33620                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.331               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.581               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.282               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.701               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.293               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 15954  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 21519  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5716   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 448    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2312   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 15954  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 15     ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 2018   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 17737  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.00                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.00                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IJ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218785.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 98                                 
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC, AIMLESS                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70687                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 149.390                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24.0 %W/V PEG MONOMETHYL ETHER 2000,     
REMARK 280  0.0050 M TCEP HYDROCHLORIDE, 0.1 M BIS_TRIS (PH 6.60), VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 286K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       57.52100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, 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     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     SER A    73                                                      
REMARK 465     VAL A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     SER A    76                                                      
REMARK 465     LEU A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     THR A    80                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     THR A   126                                                      
REMARK 465     VAL A   127                                                      
REMARK 465     LEU A   128                                                      
REMARK 465     HIS A   129                                                      
REMARK 465     ASN A   130                                                      
REMARK 465     ILE A   131                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     TYR A   133                                                      
REMARK 465     MET A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     ASP A   136                                                      
REMARK 465     GLU A   137                                                      
REMARK 465     VAL A   138                                                      
REMARK 465     LEU A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     GLN A   141                                                      
REMARK 465     ASP A   142                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     THR A   144                                                      
REMARK 465     PHE A   145                                                      
REMARK 465     ILE A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     ILE A   150                                                      
REMARK 465     LYS A   151                                                      
REMARK 465     ASN A   152                                                      
REMARK 465     TYR A   153                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     LYS A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     HIS A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     CYS A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     PHE A   165                                                      
REMARK 465     GLN A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     GLU A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     ASN A   206                                                      
REMARK 465     GLN A   207                                                      
REMARK 465     ILE A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     PRO A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     ARG A   216                                                      
REMARK 465     LYS A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     THR A   248                                                      
REMARK 465     GLU A   249                                                      
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   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     ASN A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     MET A   400                                                      
REMARK 465     ALA A   401                                                      
REMARK 465     ILE A   402                                                      
REMARK 465     ASP A   403                                                      
REMARK 465     ASN A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     CYS A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     PRO A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     CYS A   411                                                      
REMARK 465     TYR A   412                                                      
REMARK 465     GLN A   413                                                      
REMARK 465     HIS A   414                                                      
REMARK 465     LEU A   415                                                      
REMARK 465     GLU A   416                                                      
REMARK 465     GLY A   417                                                      
REMARK 465     ALA A   418                                                      
REMARK 465     LYS A   419                                                      
REMARK 465     GLU A   420                                                      
REMARK 465     PHE A   421                                                      
REMARK 465     ALA A   422                                                      
REMARK 465     ALA A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     LEU A   425                                                      
REMARK 465     THR A   426                                                      
REMARK 465     ALA A   427                                                      
REMARK 465     GLU A   428                                                      
REMARK 465     ASN A   429                                                      
REMARK 465     VAL A   430                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     GLU A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 465     SER A   479                                                      
REMARK 465     ILE A   480                                                      
REMARK 465     ILE A   481                                                      
REMARK 465     ALA A   482                                                      
REMARK 465     PRO A   483                                                      
REMARK 465     ALA A   484                                                      
REMARK 465     PRO A   485                                                      
REMARK 465     ALA A   486                                                      
REMARK 465     GLU A   487                                                      
REMARK 465     ASP A   488                                                      
REMARK 465     VAL A   489                                                      
REMARK 465     ASP A   490                                                      
REMARK 465     THR A   491                                                      
REMARK 465     LEU A   492                                                      
REMARK 465     GLY A   493                                                      
REMARK 465     GLY A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     GLY A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     GLY A   498                                                      
REMARK 465     GLY A   499                                                      
REMARK 465     GLY A   500                                                      
REMARK 465     GLY A   501                                                      
REMARK 465     SER A   502                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     ALA A   508                                                      
REMARK 465     ALA A   509                                                      
REMARK 465     ALA 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     HIS A   516                                                      
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     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     SER B    73                                                      
REMARK 465     VAL B    74                                                      
REMARK 465     SER B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     LEU B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     THR B    80                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     THR B   126                                                      
REMARK 465     VAL B   127                                                      
REMARK 465     LEU B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     ASN B   130                                                      
REMARK 465     ILE B   131                                                      
REMARK 465     PRO B   132                                                      
REMARK 465     TYR B   133                                                      
REMARK 465     MET B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     ASP B   136                                                      
REMARK 465     GLU B   137                                                      
REMARK 465     VAL B   138                                                      
REMARK 465     LEU B   139                                                      
REMARK 465     ASP B   140                                                      
REMARK 465     GLN B   141                                                      
REMARK 465     ASP B   142                                                      
REMARK 465     GLY B   143                                                      
REMARK 465     THR B   144                                                      
REMARK 465     PHE B   145                                                      
REMARK 465     ILE B   146                                                      
REMARK 465     GLU B   147                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     LEU B   149                                                      
REMARK 465     ILE B   150                                                      
REMARK 465     LYS B   151                                                      
REMARK 465     ASN B   152                                                      
REMARK 465     TYR B   153                                                      
REMARK 465     ASP B   154                                                      
REMARK 465     GLY B   155                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     VAL B   157                                                      
REMARK 465     HIS B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     ARG B   161                                                      
REMARK 465     GLU B   162                                                      
REMARK 465     CYS B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     PHE B   165                                                      
REMARK 465     GLN B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ASN B   202                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     GLU B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     ASN B   206                                                      
REMARK 465     GLN B   207                                                      
REMARK 465     ILE B   208                                                      
REMARK 465     ASP B   209                                                      
REMARK 465     LYS B   210                                                      
REMARK 465     GLU B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     PRO B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     ARG B   216                                                      
REMARK 465     LYS B   217                                                      
REMARK 465     PHE B   218                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     GLN B   250                                                      
REMARK 465     GLN B   251                                                      
REMARK 465     LEU B   252                                                      
REMARK 465     PRO B   253                                                      
REMARK 465     GLY B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     LEU B   256                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     LYS B   396                                                      
REMARK 465     ASN B   397                                                      
REMARK 465     THR B   398                                                      
REMARK 465     GLU B   399                                                      
REMARK 465     MET B   400                                                      
REMARK 465     ALA B   401                                                      
REMARK 465     ILE B   402                                                      
REMARK 465     ASP B   403                                                      
REMARK 465     ASN B   404                                                      
REMARK 465     LYS B   405                                                      
REMARK 465     PRO B   406                                                      
REMARK 465     CYS B   407                                                      
REMARK 465     GLY B   408                                                      
REMARK 465     PRO B   409                                                      
REMARK 465     HIS B   410                                                      
REMARK 465     CYS B   411                                                      
REMARK 465     TYR B   412                                                      
REMARK 465     GLN B   413                                                      
REMARK 465     HIS B   414                                                      
REMARK 465     LEU B   415                                                      
REMARK 465     GLU B   416                                                      
REMARK 465     GLY B   417                                                      
REMARK 465     ALA B   418                                                      
REMARK 465     LYS B   419                                                      
REMARK 465     GLU B   420                                                      
REMARK 465     PHE B   421                                                      
REMARK 465     ALA B   422                                                      
REMARK 465     ALA B   423                                                      
REMARK 465     ALA B   424                                                      
REMARK 465     LEU B   425                                                      
REMARK 465     THR B   426                                                      
REMARK 465     ALA B   427                                                      
REMARK 465     GLU B   428                                                      
REMARK 465     ASN B   429                                                      
REMARK 465     GLU B   477                                                      
REMARK 465     SER B   478                                                      
REMARK 465     SER B   479                                                      
REMARK 465     ILE B   480                                                      
REMARK 465     ILE B   481                                                      
REMARK 465     ALA B   482                                                      
REMARK 465     PRO B   483                                                      
REMARK 465     ALA B   484                                                      
REMARK 465     PRO B   485                                                      
REMARK 465     ALA B   486                                                      
REMARK 465     GLU B   487                                                      
REMARK 465     ASP B   488                                                      
REMARK 465     VAL B   489                                                      
REMARK 465     ASP B   490                                                      
REMARK 465     THR B   491                                                      
REMARK 465     LEU B   492                                                      
REMARK 465     GLY B   493                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     GLY B   495                                                      
REMARK 465     GLY B   496                                                      
REMARK 465     SER B   497                                                      
REMARK 465     GLY B   498                                                      
REMARK 465     GLY B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     GLY B   501                                                      
REMARK 465     SER B   502                                                      
REMARK 465     GLY B   503                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     GLY B   505                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     ALA B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     ALA B   510                                                      
REMARK 465     ASP B   511                                                      
REMARK 465     GLY B   512                                                      
REMARK 465     SER B   513                                                      
REMARK 465     SER B   514                                                      
REMARK 465     ASN B   515                                                      
REMARK 465     HIS B   516                                                      
REMARK 465     LEU B   734                                                      
REMARK 465     LYS B   735                                                      
REMARK 465     TYR B   736                                                      
REMARK 465     VAL B   737                                                      
REMARK 465     GLY B   738                                                      
REMARK 465     ILE B   739                                                      
REMARK 465     GLU B   740                                                      
REMARK 465     ARG B   741                                                      
REMARK 465     GLU B   742                                                      
REMARK 465     MET B   743                                                      
REMARK 465     GLU B   744                                                      
REMARK 465     ILE B   745                                                      
REMARK 465     PRO B   746                                                      
REMARK 465     MET E    66                                                      
REMARK 465     ASP E   381                                                      
REMARK 465     PRO E   382                                                      
REMARK 465     HIS E   383                                                      
REMARK 465     LYS E   384                                                      
REMARK 465     ALA E   385                                                      
REMARK 465     ARG E   427                                                      
REMARK 465     MET F    66                                                      
REMARK 465     ARG F   427                                                      
REMARK 465     MET S   535                                                      
REMARK 465     ASP S   536                                                      
REMARK 465     TYR S   537                                                      
REMARK 465     LYS S   538                                                      
REMARK 465     ASP S   539                                                      
REMARK 465     ASP S   540                                                      
REMARK 465     ASP S   541                                                      
REMARK 465     ASP S   542                                                      
REMARK 465     LYS S   543                                                      
REMARK 465     GLY S   544                                                      
REMARK 465     GLU S   545                                                      
REMARK 465     SER S   546                                                      
REMARK 465     GLU S   547                                                      
REMARK 465     ASP S   548                                                      
REMARK 465     GLY S   549                                                      
REMARK 465     GLU S   550                                                      
REMARK 465     VAL S   551                                                      
REMARK 465     GLU S   552                                                      
REMARK 465     GLN S   553                                                      
REMARK 465     GLN S   554                                                      
REMARK 465     ARG S   555                                                      
REMARK 465     THR S   556                                                      
REMARK 465     TYR S   557                                                      
REMARK 465     SER S   558                                                      
REMARK 465     SER S   559                                                      
REMARK 465     GLY S   560                                                      
REMARK 465     HIS S   561                                                      
REMARK 465     GLU S   689                                                      
REMARK 465     LYS S   690                                                      
REMARK 465     GLY S   691                                                      
REMARK 465     GLU S   692                                                      
REMARK 465     SER S   693                                                      
REMARK 465     ALA S   694                                                      
REMARK 465     SER S   695                                                      
REMARK 465     PRO S   696                                                      
REMARK 465     ALA S   697                                                      
REMARK 465     ASN S   698                                                      
REMARK 465     GLU S   699                                                      
REMARK 465     GLU S   700                                                      
REMARK 465     ILE S   701                                                      
REMARK 465     THR S   702                                                      
REMARK 465     GLU S   703                                                      
REMARK 465     GLU S   704                                                      
REMARK 465     GLN S   705                                                      
REMARK 465     ASN S   706                                                      
REMARK 465     GLY S   707                                                      
REMARK 465     THR S   708                                                      
REMARK 465     ALA S   709                                                      
REMARK 465     ASN S   710                                                      
REMARK 465     GLY S   711                                                      
REMARK 465     PHE S   712                                                      
REMARK 465     SER S   713                                                      
REMARK 465     GLU S   714                                                      
REMARK 465     ILE S   715                                                      
REMARK 465     ASN S   716                                                      
REMARK 465     SER S   717                                                      
REMARK 465     LYS S   718                                                      
REMARK 465     GLU S   719                                                      
REMARK 465     LYS S   720                                                      
REMARK 465     ALA S   721                                                      
REMARK 465     LEU S   722                                                      
REMARK 465     GLU S   723                                                      
REMARK 465     THR S   724                                                      
REMARK 465     ASP S   725                                                      
REMARK 465     MET T   535                                                      
REMARK 465     ASP T   536                                                      
REMARK 465     TYR T   537                                                      
REMARK 465     LYS T   538                                                      
REMARK 465     ASP T   539                                                      
REMARK 465     ASP T   540                                                      
REMARK 465     ASP T   541                                                      
REMARK 465     ASP T   542                                                      
REMARK 465     LYS T   543                                                      
REMARK 465     GLY T   544                                                      
REMARK 465     GLU T   545                                                      
REMARK 465     SER T   546                                                      
REMARK 465     GLU T   547                                                      
REMARK 465     ASP T   548                                                      
REMARK 465     GLY T   549                                                      
REMARK 465     GLU T   550                                                      
REMARK 465     VAL T   551                                                      
REMARK 465     GLU T   552                                                      
REMARK 465     GLN T   553                                                      
REMARK 465     GLN T   554                                                      
REMARK 465     ARG T   555                                                      
REMARK 465     THR T   556                                                      
REMARK 465     TYR T   557                                                      
REMARK 465     SER T   558                                                      
REMARK 465     SER T   559                                                      
REMARK 465     GLY T   560                                                      
REMARK 465     GLU T   689                                                      
REMARK 465     LYS T   690                                                      
REMARK 465     GLY T   691                                                      
REMARK 465     GLU T   692                                                      
REMARK 465     SER T   693                                                      
REMARK 465     ALA T   694                                                      
REMARK 465     SER T   695                                                      
REMARK 465     PRO T   696                                                      
REMARK 465     ALA T   697                                                      
REMARK 465     ASN T   698                                                      
REMARK 465     GLU T   699                                                      
REMARK 465     GLU T   700                                                      
REMARK 465     ILE T   701                                                      
REMARK 465     THR T   702                                                      
REMARK 465     GLU T   703                                                      
REMARK 465     GLU T   704                                                      
REMARK 465     GLN T   705                                                      
REMARK 465     ASN T   706                                                      
REMARK 465     GLY T   707                                                      
REMARK 465     THR T   708                                                      
REMARK 465     ALA T   709                                                      
REMARK 465     ASN T   710                                                      
REMARK 465     GLY T   711                                                      
REMARK 465     PHE T   712                                                      
REMARK 465     SER T   713                                                      
REMARK 465     GLU T   714                                                      
REMARK 465     ILE T   715                                                      
REMARK 465     ASN T   716                                                      
REMARK 465     SER T   717                                                      
REMARK 465     LYS T   718                                                      
REMARK 465     GLU T   719                                                      
REMARK 465     LYS T   720                                                      
REMARK 465     ALA T   721                                                      
REMARK 465     LEU T   722                                                      
REMARK 465     GLU T   723                                                      
REMARK 465     THR T   724                                                      
REMARK 465     ASP T   725                                                      
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    GLU A 198       99.90    -66.18                                   
REMARK 500    ALA A 269      104.88    -51.88                                   
REMARK 500    TYR A 306       49.49   -100.20                                   
REMARK 500    TYR A 448      -57.42     -9.08                                   
REMARK 500    ASP A 449       12.94   -140.20                                   
REMARK 500    CYS A 463      -38.22    -37.33                                   
REMARK 500    ASP A 531     -161.47   -108.42                                   
REMARK 500    GLN A 565      -82.76     77.69                                   
REMARK 500    HIS A 593       73.29     37.45                                   
REMARK 500    CYS A 604       26.08   -145.98                                   
REMARK 500    VAL A 621      -82.99   -111.00                                   
REMARK 500    ILE A 638      -62.07   -100.50                                   
REMARK 500    ALA B 269      105.06    -51.08                                   
REMARK 500    TYR B 306       49.38    -99.10                                   
REMARK 500    THR B 446      -67.58    -96.40                                   
REMARK 500    TYR B 448      -74.38    -94.57                                   
REMARK 500    ASP B 531     -162.19   -108.26                                   
REMARK 500    GLN B 565      -82.79     77.60                                   
REMARK 500    HIS B 593       73.32     38.22                                   
REMARK 500    CYS B 604       26.75   -146.73                                   
REMARK 500    VAL B 621      -84.66   -111.89                                   
REMARK 500    ILE B 638      -62.28   -100.45                                   
REMARK 500    SER E 104     -140.07     53.69                                   
REMARK 500    LEU E 121      -63.68    -91.59                                   
REMARK 500    ASN E 143      -74.36    -74.49                                   
REMARK 500    HIS E 199       -5.41     93.49                                   
REMARK 500    PHE E 285      148.85    175.40                                   
REMARK 500    SER E 309     -157.54   -131.27                                   
REMARK 500    CYS E 347       53.70   -144.81                                   
REMARK 500    VAL E 379       57.77   -114.24                                   
REMARK 500    SER F 104     -140.57     54.91                                   
REMARK 500    LEU F 121      -63.79    -91.42                                   
REMARK 500    ASN F 143      -75.80    -74.22                                   
REMARK 500    HIS F 199       -7.09     94.38                                   
REMARK 500    PHE F 285      147.27    176.85                                   
REMARK 500    SER F 309     -157.72   -132.42                                   
REMARK 500    CYS F 347       54.17   -144.53                                   
REMARK 500    GLU F 378       57.48    -97.13                                   
REMARK 500    LYS F 384       33.07    -95.29                                   
REMARK 500    MET S 579       71.43     44.34                                   
REMARK 500    GLU S 584       39.39    -82.32                                   
REMARK 500    ASN S 651       72.02     53.64                                   
REMARK 500    ASN T 562      -30.44   -144.08                                   
REMARK 500    MET T 579       99.75     -6.03                                   
REMARK 500    GLU T 580       37.36   -152.02                                   
REMARK 500    ASP T 582       74.34   -118.36                                   
REMARK 500    ASP T 583       45.55   -103.84                                   
REMARK 500    GLU T 584       45.92    -93.06                                   
REMARK 500    ASN T 651       72.81     53.25                                   
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 A9008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 286   SG                                                     
REMARK 620 2 CYS A 289   SG  106.9                                              
REMARK 620 3 CYS A 294   SG  110.1 104.0                                        
REMARK 620 4 HIS A 297   ND1 102.3 122.7 110.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 CYS A 536   SG  113.6                                              
REMARK 620 3 CYS A 543   SG  108.5 112.4                                        
REMARK 620 4 CYS A 547   SG  107.3 108.4 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 HIS A 525   NE2 102.4                                              
REMARK 620 3 CYS A 530   SG  107.7 105.6                                        
REMARK 620 4 CYS A 534   SG  121.8 109.8 108.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 530   SG                                                     
REMARK 620 2 CYS A 543   SG   98.8                                              
REMARK 620 3 CYS A 549   SG  112.7 110.2                                        
REMARK 620 4 CYS A 553   SG  108.1 116.8 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 562   SG  103.4                                              
REMARK 620 3 CYS A 566   SG  106.5 108.8                                        
REMARK 620 4 CYS A 571   SG  109.7 110.7 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 573   SG  102.0                                              
REMARK 620 3 CYS A 580   SG  103.8 114.8                                        
REMARK 620 4 CYS A 585   SG  109.7 104.5 120.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 566   SG                                                     
REMARK 620 2 CYS A 580   SG  104.4                                              
REMARK 620 3 CYS A 588   SG  104.6 110.1                                        
REMARK 620 4 CYS A 601   SG  118.3 109.8 109.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 286   SG                                                     
REMARK 620 2 CYS B 289   SG  103.5                                              
REMARK 620 3 CYS B 294   SG  109.4 107.2                                        
REMARK 620 4 HIS B 297   ND1  97.5 125.3 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 523   SG                                                     
REMARK 620 2 CYS B 536   SG  112.1                                              
REMARK 620 3 CYS B 543   SG  107.7 117.7                                        
REMARK 620 4 CYS B 547   SG  102.1 109.3 106.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 523   SG                                                     
REMARK 620 2 HIS B 525   NE2  98.7                                              
REMARK 620 3 CYS B 530   SG  111.7 103.8                                        
REMARK 620 4 CYS B 534   SG  123.5 103.5 112.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 530   SG                                                     
REMARK 620 2 CYS B 543   SG   99.0                                              
REMARK 620 3 CYS B 549   SG  112.6 111.7                                        
REMARK 620 4 CYS B 553   SG  106.8 116.7 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 560   SG                                                     
REMARK 620 2 CYS B 562   SG   98.6                                              
REMARK 620 3 CYS B 566   SG  105.5 106.9                                        
REMARK 620 4 CYS B 571   SG  111.7 108.7 122.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 560   SG                                                     
REMARK 620 2 CYS B 573   SG  103.0                                              
REMARK 620 3 CYS B 580   SG  104.2 115.9                                        
REMARK 620 4 CYS B 585   SG  109.0 106.8 116.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 566   SG                                                     
REMARK 620 2 CYS B 580   SG   99.7                                              
REMARK 620 3 CYS B 588   SG  105.8 112.9                                        
REMARK 620 4 CYS B 601   SG  119.2 115.9 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BN A 9001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BN B 9001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9008                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IJ8   RELATED DB: PDB                                   
DBREF  5IJ7 A    1   428  UNP    G1KPH4   G1KPH4_ANOCA     4    332             
DBREF  5IJ7 A  429   746  UNP    Q15910   EZH2_HUMAN     390    707             
DBREF  5IJ7 B    1   428  UNP    G1KPH4   G1KPH4_ANOCA     4    332             
DBREF  5IJ7 B  429   746  UNP    Q15910   EZH2_HUMAN     390    707             
DBREF  5IJ7 E   67   427  UNP    O75530   EED_HUMAN       81    441             
DBREF  5IJ7 F   67   427  UNP    O75530   EED_HUMAN       81    441             
DBREF  5IJ7 S  545   725  UNP    Q15022   SUZ12_HUMAN    545    725             
DBREF  5IJ7 T  545   725  UNP    Q15022   SUZ12_HUMAN    545    725             
SEQADV 5IJ7     A       UNP  Q15910    PRO   449 LINKER                         
SEQADV 5IJ7     A       UNP  Q15910    PRO   450 LINKER                         
SEQADV 5IJ7     A       UNP  Q15910    ARG   451 LINKER                         
SEQADV 5IJ7     A       UNP  Q15910    LYS   452 LINKER                         
SEQADV 5IJ7 LEU A  492  UNP  Q15910    LYS   453 LINKER                         
SEQADV 5IJ7 GLY A  493  UNP  Q15910    LYS   454 LINKER                         
SEQADV 5IJ7 GLY A  494  UNP  Q15910    ARG   455 LINKER                         
SEQADV 5IJ7 GLY A  495  UNP  Q15910    LYS   456 LINKER                         
SEQADV 5IJ7 GLY A  496  UNP  Q15910    HIS   457 LINKER                         
SEQADV 5IJ7 SER A  497  UNP  Q15910    ARG   458 LINKER                         
SEQADV 5IJ7 GLY A  498  UNP  Q15910    LEU   459 LINKER                         
SEQADV 5IJ7 GLY A  499  UNP  Q15910    TRP   460 LINKER                         
SEQADV 5IJ7 GLY A  500  UNP  Q15910    ALA   461 LINKER                         
SEQADV 5IJ7 GLY A  501  UNP  Q15910    ALA   462 LINKER                         
SEQADV 5IJ7 SER A  502  UNP  Q15910    HIS   463 LINKER                         
SEQADV 5IJ7 GLY A  503  UNP  Q15910    CYS   464 LINKER                         
SEQADV 5IJ7 GLY A  504  UNP  Q15910    ARG   465 LINKER                         
SEQADV 5IJ7 GLY A  505  UNP  Q15910    LYS   466 LINKER                         
SEQADV 5IJ7 GLY A  506  UNP  Q15910    ILE   467 LINKER                         
SEQADV 5IJ7 SER A  507  UNP  Q15910    GLN   468 LINKER                         
SEQADV 5IJ7 ALA A  508  UNP  Q15910    LEU   469 LINKER                         
SEQADV 5IJ7 ALA A  509  UNP  Q15910    LYS   470 LINKER                         
SEQADV 5IJ7 ALA A  510  UNP  Q15910    LYS   471 LINKER                         
SEQADV 5IJ7 ASN A  532  UNP  Q15910    SER   493 ENGINEERED MUTATION            
SEQADV 5IJ7     B       UNP  Q15910    PRO   449 LINKER                         
SEQADV 5IJ7     B       UNP  Q15910    PRO   450 LINKER                         
SEQADV 5IJ7     B       UNP  Q15910    ARG   451 LINKER                         
SEQADV 5IJ7     B       UNP  Q15910    LYS   452 LINKER                         
SEQADV 5IJ7 LEU B  492  UNP  Q15910    LYS   453 LINKER                         
SEQADV 5IJ7 GLY B  493  UNP  Q15910    LYS   454 LINKER                         
SEQADV 5IJ7 GLY B  494  UNP  Q15910    ARG   455 LINKER                         
SEQADV 5IJ7 GLY B  495  UNP  Q15910    LYS   456 LINKER                         
SEQADV 5IJ7 GLY B  496  UNP  Q15910    HIS   457 LINKER                         
SEQADV 5IJ7 SER B  497  UNP  Q15910    ARG   458 LINKER                         
SEQADV 5IJ7 GLY B  498  UNP  Q15910    LEU   459 LINKER                         
SEQADV 5IJ7 GLY B  499  UNP  Q15910    TRP   460 LINKER                         
SEQADV 5IJ7 GLY B  500  UNP  Q15910    ALA   461 LINKER                         
SEQADV 5IJ7 GLY B  501  UNP  Q15910    ALA   462 LINKER                         
SEQADV 5IJ7 SER B  502  UNP  Q15910    HIS   463 LINKER                         
SEQADV 5IJ7 GLY B  503  UNP  Q15910    CYS   464 LINKER                         
SEQADV 5IJ7 GLY B  504  UNP  Q15910    ARG   465 LINKER                         
SEQADV 5IJ7 GLY B  505  UNP  Q15910    LYS   466 LINKER                         
SEQADV 5IJ7 GLY B  506  UNP  Q15910    ILE   467 LINKER                         
SEQADV 5IJ7 SER B  507  UNP  Q15910    GLN   468 LINKER                         
SEQADV 5IJ7 ALA B  508  UNP  Q15910    LEU   469 LINKER                         
SEQADV 5IJ7 ALA B  509  UNP  Q15910    LYS   470 LINKER                         
SEQADV 5IJ7 ALA B  510  UNP  Q15910    LYS   471 LINKER                         
SEQADV 5IJ7 ASN B  532  UNP  Q15910    SER   493 ENGINEERED MUTATION            
SEQADV 5IJ7 MET E   66  UNP  O75530              INITIATING METHIONINE          
SEQADV 5IJ7 MET F   66  UNP  O75530              INITIATING METHIONINE          
SEQADV 5IJ7 MET S  535  UNP  Q15022              INITIATING METHIONINE          
SEQADV 5IJ7 ASP S  536  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 TYR S  537  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 LYS S  538  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP S  539  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP S  540  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP S  541  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP S  542  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 LYS S  543  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 GLY S  544  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP S  583  UNP  Q15022    SER   583 ENGINEERED MUTATION            
SEQADV 5IJ7 MET T  535  UNP  Q15022              INITIATING METHIONINE          
SEQADV 5IJ7 ASP T  536  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 TYR T  537  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 LYS T  538  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP T  539  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP T  540  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP T  541  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP T  542  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 LYS T  543  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 GLY T  544  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5IJ7 ASP T  583  UNP  Q15022    SER   583 ENGINEERED MUTATION            
SEQRES   1 A  643  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO ILE          
SEQRES   2 A  643  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 A  643  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 A  643  SER MET PHE ASN SER ASN ARG GLN LYS ILE GLN GLU ARG          
SEQRES   5 A  643  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 A  643  GLN PRO VAL HIS ILE MET THR SER VAL SER SER LEU ARG          
SEQRES   7 A  643  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 A  643  PRO LYS GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 A  643  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 A  643  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 A  643  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 A  643  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 A  643  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 A  643  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN LEU ASP          
SEQRES  15 A  643  ARG ARG ASP GLU LYS GLN LYS ASN GLN GLU SER ASN GLN          
SEQRES  16 A  643  ILE ASP LYS GLU SER HIS PRO PRO ARG LYS PHE PRO SER          
SEQRES  17 A  643  ASP LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP          
SEQRES  18 A  643  LYS GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU          
SEQRES  19 A  643  LEU THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU          
SEQRES  20 A  643  CYS THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL          
SEQRES  21 A  643  GLN ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE          
SEQRES  22 A  643  CYS ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO          
SEQRES  23 A  643  PHE HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR          
SEQRES  24 A  643  GLU MET ALA ILE ASP ASN LYS PRO CYS GLY PRO HIS CYS          
SEQRES  25 A  643  TYR GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA          
SEQRES  26 A  643  LEU THR ALA GLU ASN VAL GLU TRP SER GLY ALA GLU ALA          
SEQRES  27 A  643  SER MET PHE ARG VAL LEU ILE GLY THR TYR TYR ASP ASN          
SEQRES  28 A  643  PHE CYS ALA ILE ALA ARG LEU ILE GLY THR LYS THR CYS          
SEQRES  29 A  643  ARG GLN VAL TYR GLU PHE ARG VAL LYS GLU SER SER ILE          
SEQRES  30 A  643  ILE ALA PRO ALA PRO ALA GLU ASP VAL ASP THR LEU GLY          
SEQRES  31 A  643  GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  32 A  643  SER ALA ALA ALA ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  33 A  643  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP ASN          
SEQRES  34 A  643  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  35 A  643  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  36 A  643  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  37 A  643  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  38 A  643  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  39 A  643  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  40 A  643  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  41 A  643  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  42 A  643  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  43 A  643  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  44 A  643  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  45 A  643  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  46 A  643  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  47 A  643  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  48 A  643  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  49 A  643  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  50 A  643  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 B  643  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO ILE          
SEQRES   2 B  643  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 B  643  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 B  643  SER MET PHE ASN SER ASN ARG GLN LYS ILE GLN GLU ARG          
SEQRES   5 B  643  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 B  643  GLN PRO VAL HIS ILE MET THR SER VAL SER SER LEU ARG          
SEQRES   7 B  643  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 B  643  PRO LYS GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 B  643  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 B  643  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 B  643  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 B  643  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 B  643  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 B  643  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN LEU ASP          
SEQRES  15 B  643  ARG ARG ASP GLU LYS GLN LYS ASN GLN GLU SER ASN GLN          
SEQRES  16 B  643  ILE ASP LYS GLU SER HIS PRO PRO ARG LYS PHE PRO SER          
SEQRES  17 B  643  ASP LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP          
SEQRES  18 B  643  LYS GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU          
SEQRES  19 B  643  LEU THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU          
SEQRES  20 B  643  CYS THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL          
SEQRES  21 B  643  GLN ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE          
SEQRES  22 B  643  CYS ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO          
SEQRES  23 B  643  PHE HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR          
SEQRES  24 B  643  GLU MET ALA ILE ASP ASN LYS PRO CYS GLY PRO HIS CYS          
SEQRES  25 B  643  TYR GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA          
SEQRES  26 B  643  LEU THR ALA GLU ASN VAL GLU TRP SER GLY ALA GLU ALA          
SEQRES  27 B  643  SER MET PHE ARG VAL LEU ILE GLY THR TYR TYR ASP ASN          
SEQRES  28 B  643  PHE CYS ALA ILE ALA ARG LEU ILE GLY THR LYS THR CYS          
SEQRES  29 B  643  ARG GLN VAL TYR GLU PHE ARG VAL LYS GLU SER SER ILE          
SEQRES  30 B  643  ILE ALA PRO ALA PRO ALA GLU ASP VAL ASP THR LEU GLY          
SEQRES  31 B  643  GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  32 B  643  SER ALA ALA ALA ASP GLY SER SER ASN HIS VAL TYR ASN          
SEQRES  33 B  643  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP ASN          
SEQRES  34 B  643  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES  35 B  643  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES  36 B  643  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES  37 B  643  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES  38 B  643  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES  39 B  643  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES  40 B  643  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES  41 B  643  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  42 B  643  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  43 B  643  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  44 B  643  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  45 B  643  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  46 B  643  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  47 B  643  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  48 B  643  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  49 B  643  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  50 B  643  ARG GLU MET GLU ILE PRO                                      
SEQRES   1 E  362  MET SER PHE LYS CYS VAL ASN SER LEU LYS GLU ASP HIS          
SEQRES   2 E  362  ASN GLN PRO LEU PHE GLY VAL GLN PHE ASN TRP HIS SER          
SEQRES   3 E  362  LYS GLU GLY ASP PRO LEU VAL PHE ALA THR VAL GLY SER          
SEQRES   4 E  362  ASN ARG VAL THR LEU TYR GLU CYS HIS SER GLN GLY GLU          
SEQRES   5 E  362  ILE ARG LEU LEU GLN SER TYR VAL ASP ALA ASP ALA ASP          
SEQRES   6 E  362  GLU ASN PHE TYR THR CYS ALA TRP THR TYR ASP SER ASN          
SEQRES   7 E  362  THR SER HIS PRO LEU LEU ALA VAL ALA GLY SER ARG GLY          
SEQRES   8 E  362  ILE ILE ARG ILE ILE ASN PRO ILE THR MET GLN CYS ILE          
SEQRES   9 E  362  LYS HIS TYR VAL GLY HIS GLY ASN ALA ILE ASN GLU LEU          
SEQRES  10 E  362  LYS PHE HIS PRO ARG ASP PRO ASN LEU LEU LEU SER VAL          
SEQRES  11 E  362  SER LYS ASP HIS ALA LEU ARG LEU TRP ASN ILE GLN THR          
SEQRES  12 E  362  ASP THR LEU VAL ALA ILE PHE GLY GLY VAL GLU GLY HIS          
SEQRES  13 E  362  ARG ASP GLU VAL LEU SER ALA ASP TYR ASP LEU LEU GLY          
SEQRES  14 E  362  GLU LYS ILE MET SER CYS GLY MET ASP HIS SER LEU LYS          
SEQRES  15 E  362  LEU TRP ARG ILE ASN SER LYS ARG MET MET ASN ALA ILE          
SEQRES  16 E  362  LYS GLU SER TYR ASP TYR ASN PRO ASN LYS THR ASN ARG          
SEQRES  17 E  362  PRO PHE ILE SER GLN LYS ILE HIS PHE PRO ASP PHE SER          
SEQRES  18 E  362  THR ARG ASP ILE HIS ARG ASN TYR VAL ASP CYS VAL ARG          
SEQRES  19 E  362  TRP LEU GLY ASP LEU ILE LEU SER LYS SER CYS GLU ASN          
SEQRES  20 E  362  ALA ILE VAL CYS TRP LYS PRO GLY LYS MET GLU ASP ASP          
SEQRES  21 E  362  ILE ASP LYS ILE LYS PRO SER GLU SER ASN VAL THR ILE          
SEQRES  22 E  362  LEU GLY ARG PHE ASP TYR SER GLN CYS ASP ILE TRP TYR          
SEQRES  23 E  362  MET ARG PHE SER MET ASP PHE TRP GLN LYS MET LEU ALA          
SEQRES  24 E  362  LEU GLY ASN GLN VAL GLY LYS LEU TYR VAL TRP ASP LEU          
SEQRES  25 E  362  GLU VAL GLU ASP PRO HIS LYS ALA LYS CYS THR THR LEU          
SEQRES  26 E  362  THR HIS HIS LYS CYS GLY ALA ALA ILE ARG GLN THR SER          
SEQRES  27 E  362  PHE SER ARG ASP SER SER ILE LEU ILE ALA VAL CYS ASP          
SEQRES  28 E  362  ASP ALA SER ILE TRP ARG TRP ASP ARG LEU ARG                  
SEQRES   1 F  362  MET SER PHE LYS CYS VAL ASN SER LEU LYS GLU ASP HIS          
SEQRES   2 F  362  ASN GLN PRO LEU PHE GLY VAL GLN PHE ASN TRP HIS SER          
SEQRES   3 F  362  LYS GLU GLY ASP PRO LEU VAL PHE ALA THR VAL GLY SER          
SEQRES   4 F  362  ASN ARG VAL THR LEU TYR GLU CYS HIS SER GLN GLY GLU          
SEQRES   5 F  362  ILE ARG LEU LEU GLN SER TYR VAL ASP ALA ASP ALA ASP          
SEQRES   6 F  362  GLU ASN PHE TYR THR CYS ALA TRP THR TYR ASP SER ASN          
SEQRES   7 F  362  THR SER HIS PRO LEU LEU ALA VAL ALA GLY SER ARG GLY          
SEQRES   8 F  362  ILE ILE ARG ILE ILE ASN PRO ILE THR MET GLN CYS ILE          
SEQRES   9 F  362  LYS HIS TYR VAL GLY HIS GLY ASN ALA ILE ASN GLU LEU          
SEQRES  10 F  362  LYS PHE HIS PRO ARG ASP PRO ASN LEU LEU LEU SER VAL          
SEQRES  11 F  362  SER LYS ASP HIS ALA LEU ARG LEU TRP ASN ILE GLN THR          
SEQRES  12 F  362  ASP THR LEU VAL ALA ILE PHE GLY GLY VAL GLU GLY HIS          
SEQRES  13 F  362  ARG ASP GLU VAL LEU SER ALA ASP TYR ASP LEU LEU GLY          
SEQRES  14 F  362  GLU LYS ILE MET SER CYS GLY MET ASP HIS SER LEU LYS          
SEQRES  15 F  362  LEU TRP ARG ILE ASN SER LYS ARG MET MET ASN ALA ILE          
SEQRES  16 F  362  LYS GLU SER TYR ASP TYR ASN PRO ASN LYS THR ASN ARG          
SEQRES  17 F  362  PRO PHE ILE SER GLN LYS ILE HIS PHE PRO ASP PHE SER          
SEQRES  18 F  362  THR ARG ASP ILE HIS ARG ASN TYR VAL ASP CYS VAL ARG          
SEQRES  19 F  362  TRP LEU GLY ASP LEU ILE LEU SER LYS SER CYS GLU ASN          
SEQRES  20 F  362  ALA ILE VAL CYS TRP LYS PRO GLY LYS MET GLU ASP ASP          
SEQRES  21 F  362  ILE ASP LYS ILE LYS PRO SER GLU SER ASN VAL THR ILE          
SEQRES  22 F  362  LEU GLY ARG PHE ASP TYR SER GLN CYS ASP ILE TRP TYR          
SEQRES  23 F  362  MET ARG PHE SER MET ASP PHE TRP GLN LYS MET LEU ALA          
SEQRES  24 F  362  LEU GLY ASN GLN VAL GLY LYS LEU TYR VAL TRP ASP LEU          
SEQRES  25 F  362  GLU VAL GLU ASP PRO HIS LYS ALA LYS CYS THR THR LEU          
SEQRES  26 F  362  THR HIS HIS LYS CYS GLY ALA ALA ILE ARG GLN THR SER          
SEQRES  27 F  362  PHE SER ARG ASP SER SER ILE LEU ILE ALA VAL CYS ASP          
SEQRES  28 F  362  ASP ALA SER ILE TRP ARG TRP ASP ARG LEU ARG                  
SEQRES   1 S  191  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU SER GLU          
SEQRES   2 S  191  ASP GLY GLU VAL GLU GLN GLN ARG THR TYR SER SER GLY          
SEQRES   3 S  191  HIS ASN ARG LEU TYR PHE HIS SER ASP THR CYS LEU PRO          
SEQRES   4 S  191  LEU ARG PRO GLN GLU MET GLU VAL ASP ASP GLU ASP GLU          
SEQRES   5 S  191  LYS ASP PRO GLU TRP LEU ARG GLU LYS THR ILE THR GLN          
SEQRES   6 S  191  ILE GLU GLU PHE SER ASP VAL ASN GLU GLY GLU LYS GLU          
SEQRES   7 S  191  VAL MET LYS LEU TRP ASN LEU HIS VAL MET LYS HIS GLY          
SEQRES   8 S  191  PHE ILE ALA ASP ASN GLN MET ASN HIS ALA CYS MET LEU          
SEQRES   9 S  191  PHE VAL GLU ASN TYR GLY GLN LYS ILE ILE LYS LYS ASN          
SEQRES  10 S  191  LEU CYS ARG ASN PHE MET LEU HIS LEU VAL SER MET HIS          
SEQRES  11 S  191  ASP PHE ASN LEU ILE SER ILE MET SER ILE ASP LYS ALA          
SEQRES  12 S  191  VAL THR LYS LEU ARG GLU MET GLN GLN LYS LEU GLU LYS          
SEQRES  13 S  191  GLY GLU SER ALA SER PRO ALA ASN GLU GLU ILE THR GLU          
SEQRES  14 S  191  GLU GLN ASN GLY THR ALA ASN GLY PHE SER GLU ILE ASN          
SEQRES  15 S  191  SER LYS GLU LYS ALA LEU GLU THR ASP                          
SEQRES   1 T  191  MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU SER GLU          
SEQRES   2 T  191  ASP GLY GLU VAL GLU GLN GLN ARG THR TYR SER SER GLY          
SEQRES   3 T  191  HIS ASN ARG LEU TYR PHE HIS SER ASP THR CYS LEU PRO          
SEQRES   4 T  191  LEU ARG PRO GLN GLU MET GLU VAL ASP ASP GLU ASP GLU          
SEQRES   5 T  191  LYS ASP PRO GLU TRP LEU ARG GLU LYS THR ILE THR GLN          
SEQRES   6 T  191  ILE GLU GLU PHE SER ASP VAL ASN GLU GLY GLU LYS GLU          
SEQRES   7 T  191  VAL MET LYS LEU TRP ASN LEU HIS VAL MET LYS HIS GLY          
SEQRES   8 T  191  PHE ILE ALA ASP ASN GLN MET ASN HIS ALA CYS MET LEU          
SEQRES   9 T  191  PHE VAL GLU ASN TYR GLY GLN LYS ILE ILE LYS LYS ASN          
SEQRES  10 T  191  LEU CYS ARG ASN PHE MET LEU HIS LEU VAL SER MET HIS          
SEQRES  11 T  191  ASP PHE ASN LEU ILE SER ILE MET SER ILE ASP LYS ALA          
SEQRES  12 T  191  VAL THR LYS LEU ARG GLU MET GLN GLN LYS LEU GLU LYS          
SEQRES  13 T  191  GLY GLU SER ALA SER PRO ALA ASN GLU GLU ILE THR GLU          
SEQRES  14 T  191  GLU GLN ASN GLY THR ALA ASN GLY PHE SER GLU ILE ASN          
SEQRES  15 T  191  SER LYS GLU LYS ALA LEU GLU THR ASP                          
HET    6BN  A9001      36                                                       
HET     ZN  A9002       1                                                       
HET     ZN  A9003       1                                                       
HET     ZN  A9004       1                                                       
HET     ZN  A9005       1                                                       
HET     ZN  A9006       1                                                       
HET     ZN  A9007       1                                                       
HET     ZN  A9008       1                                                       
HET    6BN  B9001      36                                                       
HET     ZN  B9002       1                                                       
HET     ZN  B9003       1                                                       
HET     ZN  B9004       1                                                       
HET     ZN  B9005       1                                                       
HET     ZN  B9006       1                                                       
HET     ZN  B9007       1                                                       
HET     ZN  B9008       1                                                       
HETNAM     6BN 5,8-DICHLORO-2-[(4-ETHYL-6-METHYL-2-OXO-1,2-                     
HETNAM   2 6BN  DIHYDROPYRIDIN-3-YL)METHYL]-7-({1-[(2R)-2-                      
HETNAM   3 6BN  HYDROXYPROPANOYL]PIPERIDIN-4-YL}OXY)-3,4-                       
HETNAM   4 6BN  DIHYDROISOQUINOLIN-1(2H)-ONE                                    
HETNAM      ZN ZINC ION                                                         
FORMUL   7  6BN    2(C26 H31 CL2 N3 O5)                                         
FORMUL   8   ZN    14(ZN 2+)                                                    
FORMUL  23  HOH   *36(H2 O)                                                     
HELIX    1 AA1 GLY A   11  GLN A   62  1                                  52    
HELIX    2 AA2 ASN A  167  GLU A  198  1                                  20    
HELIX    3 AA3 SER A  220  PHE A  231  1                                  12    
HELIX    4 AA4 PRO A  232  GLY A  235  5                                   4    
HELIX    5 AA5 THR A  236  LYS A  245  1                                  10    
HELIX    6 AA6 GLN A  273  LEU A  284  1                                  12    
HELIX    7 AA7 THR A  302  LYS A  307  5                                   6    
HELIX    8 AA8 SER A  433  ILE A  444  1                                  12    
HELIX    9 AA9 ASN A  450  GLY A  459  1                                  10    
HELIX   10 AB1 THR A  462  LYS A  472  1                                  11    
HELIX   11 AB2 CYS A  534  ALA A  539  1                                   6    
HELIX   12 AB3 CYS A  571  ALA A  576  1                                   6    
HELIX   13 AB4 CYS A  604  GLY A  609  1                                   6    
HELIX   14 AB5 GLN A  648  TYR A  661  1                                  14    
HELIX   15 AB6 LYS A  683  ALA A  687  5                                   5    
HELIX   16 AB7 ASP A  725  ALA A  731  1                                   7    
HELIX   17 AB8 GLY B   11  GLN B   62  1                                  52    
HELIX   18 AB9 ASN B  167  ASP B  197  1                                  19    
HELIX   19 AC1 SER B  220  PHE B  231  1                                  12    
HELIX   20 AC2 THR B  236  THR B  248  1                                  13    
HELIX   21 AC3 GLN B  273  LEU B  284  1                                  12    
HELIX   22 AC4 THR B  302  LYS B  307  5                                   6    
HELIX   23 AC5 SER B  433  TYR B  447  1                                  15    
HELIX   24 AC6 ASN B  450  GLY B  459  1                                  10    
HELIX   25 AC7 THR B  462  LYS B  472  1                                  11    
HELIX   26 AC8 CYS B  534  ALA B  539  1                                   6    
HELIX   27 AC9 CYS B  571  ALA B  576  1                                   6    
HELIX   28 AD1 CYS B  604  GLY B  609  1                                   6    
HELIX   29 AD2 GLN B  648  TYR B  661  1                                  14    
HELIX   30 AD3 LYS B  683  ALA B  687  5                                   5    
HELIX   31 AD4 ASP B  725  ALA B  731  1                                   7    
HELIX   32 AD5 SER E  253  TYR E  266  1                                  14    
HELIX   33 AD6 ASP E  325  ILE E  329  5                                   5    
HELIX   34 AD7 SER F  253  TYR F  266  1                                  14    
HELIX   35 AD8 ASP F  325  ILE F  329  5                                   5    
HELIX   36 AD9 ARG S  575  MET S  579  5                                   5    
HELIX   37 AE1 PRO S  589  GLU S  602  1                                  14    
HELIX   38 AE2 ASN S  607  GLY S  625  1                                  19    
HELIX   39 AE3 ALA S  628  ASN S  630  5                                   3    
HELIX   40 AE4 GLN S  631  LYS S  650  1                                  20    
HELIX   41 AE5 LEU S  652  PHE S  666  1                                  15    
HELIX   42 AE6 SER S  670  LYS S  687  1                                  18    
HELIX   43 AE7 ARG T  575  MET T  579  5                                   5    
HELIX   44 AE8 PRO T  589  GLU T  602  1                                  14    
HELIX   45 AE9 ASN T  607  GLY T  625  1                                  19    
HELIX   46 AF1 ALA T  628  ASN T  630  5                                   3    
HELIX   47 AF2 GLN T  631  LYS T  650  1                                  20    
HELIX   48 AF3 LEU T  652  PHE T  666  1                                  15    
HELIX   49 AF4 SER T  670  LYS T  687  1                                  18    
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 E  68  GLU E  76 -1  O  LYS E  75   N  THR A  86           
SHEET    4 AA1 6 SER E 419  ARG E 425 -1  O  ARG E 422   N  ASN E  72           
SHEET    5 AA1 6 ILE E 410  CYS E 415 -1  N  ALA E 413   O  TRP E 421           
SHEET    6 AA1 6 ILE E 399  PHE E 404 -1  N  SER E 403   O  ILE E 412           
SHEET    1 AA2 5 LYS A  99  LEU A 101  0                                        
SHEET    2 AA2 5 ILE E 118  ASP E 126  1  O  VAL E 125   N  LEU A 101           
SHEET    3 AA2 5 ARG E 106  CYS E 112 -1  N  GLU E 111   O  ARG E 119           
SHEET    4 AA2 5 VAL E  98  GLY E 103 -1  N  GLY E 103   O  ARG E 106           
SHEET    5 AA2 5 LEU E  82  PHE E  87 -1  N  GLN E  86   O  ALA E 100           
SHEET    1 AA3 4 SER A 114  PRO A 115  0                                        
SHEET    2 AA3 4 PHE A 673  GLY A 681  1  O  GLY A 681   N  SER A 114           
SHEET    3 AA3 4 GLY A 643  SER A 647 -1  N  ILE A 646   O  VAL A 674           
SHEET    4 AA3 4 PHE A 120  MET A 121  1  N  PHE A 120   O  GLY A 643           
SHEET    1 AA4 3 SER A 114  PRO A 115  0                                        
SHEET    2 AA4 3 PHE A 673  GLY A 681  1  O  GLY A 681   N  SER A 114           
SHEET    3 AA4 3 LEU A 666  ASN A 668 -1  N  PHE A 667   O  VAL A 675           
SHEET    1 AA5 2 PHE A 285  CYS A 286  0                                        
SHEET    2 AA5 2 LYS A 291  TYR A 292 -1  O  LYS A 291   N  CYS A 286           
SHEET    1 AA6 2 LEU A 614  PRO A 618  0                                        
SHEET    2 AA6 2 TRP A 624  ILE A 628 -1  O  PHE A 627   N  LEU A 615           
SHEET    1 AA7 3 PHE A 637  GLU A 640  0                                        
SHEET    2 AA7 3 ASP A 705  ALA A 712 -1  O  ILE A 710   N  ILE A 638           
SHEET    3 AA7 3 CYS A 695  VAL A 702 -1  N  VAL A 702   O  ASP A 705           
SHEET    1 AA8 2 ASN A 688  HIS A 689  0                                        
SHEET    2 AA8 2 PHE A 723  PHE A 724  1  O  PHE A 724   N  ASN A 688           
SHEET    1 AA9 6 GLN B  94  PRO B  97  0                                        
SHEET    2 AA9 6 GLU B  82  SER B  87 -1  N  CYS B  83   O  ILE B  96           
SHEET    3 AA9 6 PHE F  68  GLU F  76 -1  O  LYS F  75   N  THR B  86           
SHEET    4 AA9 6 SER F 419  ARG F 425 -1  O  ARG F 422   N  ASN F  72           
SHEET    5 AA9 6 ILE F 410  CYS F 415 -1  N  ALA F 413   O  TRP F 421           
SHEET    6 AA9 6 ILE F 399  PHE F 404 -1  N  SER F 403   O  ILE F 412           
SHEET    1 AB1 5 LYS B  99  LEU B 101  0                                        
SHEET    2 AB1 5 ILE F 118  ASP F 126  1  O  VAL F 125   N  LEU B 101           
SHEET    3 AB1 5 ARG F 106  CYS F 112 -1  N  GLU F 111   O  ARG F 119           
SHEET    4 AB1 5 VAL F  98  GLY F 103 -1  N  PHE F  99   O  TYR F 110           
SHEET    5 AB1 5 LEU F  82  PHE F  87 -1  N  GLN F  86   O  ALA F 100           
SHEET    1 AB2 4 SER B 114  PRO B 115  0                                        
SHEET    2 AB2 4 PHE B 673  GLY B 681  1  O  GLY B 681   N  SER B 114           
SHEET    3 AB2 4 GLY B 643  SER B 647 -1  N  ILE B 646   O  VAL B 674           
SHEET    4 AB2 4 PHE B 120  MET B 121  1  N  PHE B 120   O  GLY B 643           
SHEET    1 AB3 3 SER B 114  PRO B 115  0                                        
SHEET    2 AB3 3 PHE B 673  GLY B 681  1  O  GLY B 681   N  SER B 114           
SHEET    3 AB3 3 LEU B 666  ASN B 668 -1  N  PHE B 667   O  VAL B 675           
SHEET    1 AB4 2 PHE B 285  CYS B 286  0                                        
SHEET    2 AB4 2 LYS B 291  TYR B 292 -1  O  LYS B 291   N  CYS B 286           
SHEET    1 AB5 2 LEU B 614  PRO B 618  0                                        
SHEET    2 AB5 2 TRP B 624  ILE B 628 -1  O  PHE B 627   N  LEU B 615           
SHEET    1 AB6 3 PHE B 637  GLU B 640  0                                        
SHEET    2 AB6 3 ASP B 705  ALA B 712 -1  O  ILE B 710   N  ILE B 638           
SHEET    3 AB6 3 CYS B 695  VAL B 702 -1  N  VAL B 702   O  ASP B 705           
SHEET    1 AB7 2 ASN B 688  HIS B 689  0                                        
SHEET    2 AB7 2 PHE B 723  PHE B 724  1  O  PHE B 724   N  ASN B 688           
SHEET    1 AB8 4 PHE E 133  TYR E 140  0                                        
SHEET    2 AB8 4 PRO E 147  GLY E 153 -1  O  ALA E 150   N  ALA E 137           
SHEET    3 AB8 4 ILE E 158  ASN E 162 -1  O  ILE E 161   N  LEU E 149           
SHEET    4 AB8 4 GLN E 167  TYR E 172 -1  O  GLN E 167   N  ASN E 162           
SHEET    1 AB9 5 ILE E 179  PHE E 184  0                                        
SHEET    2 AB9 5 LEU E 191  SER E 196 -1  O  LEU E 193   N  LYS E 183           
SHEET    3 AB9 5 LEU E 201  ASN E 205 -1  O  TRP E 204   N  LEU E 192           
SHEET    4 AB9 5 THR E 210  PHE E 215 -1  O  THR E 210   N  ASN E 205           
SHEET    5 AB9 5 GLN E 278  ILE E 280  1  O  GLN E 278   N  ILE E 214           
SHEET    1 AC1 4 VAL E 225  TYR E 230  0                                        
SHEET    2 AC1 4 LYS E 236  GLY E 241 -1  O  CYS E 240   N  SER E 227           
SHEET    3 AC1 4 LEU E 246  ARG E 250 -1  O  LYS E 247   N  SER E 239           
SHEET    4 AC1 4 PHE E 285  THR E 287 -1  O  PHE E 285   N  LEU E 248           
SHEET    1 AC2 4 CYS E 297  LEU E 301  0                                        
SHEET    2 AC2 4 LEU E 304  LYS E 308 -1  O  LEU E 306   N  ARG E 299           
SHEET    3 AC2 4 ALA E 313  PRO E 319 -1  O  VAL E 315   N  SER E 307           
SHEET    4 AC2 4 VAL E 336  ASP E 343 -1  O  GLY E 340   N  CYS E 316           
SHEET    1 AC3 4 SER E 355  MET E 356  0                                        
SHEET    2 AC3 4 MET E 362  GLY E 366 -1  O  ALA E 364   N  SER E 355           
SHEET    3 AC3 4 LEU E 372  ASP E 376 -1  O  TYR E 373   N  LEU E 365           
SHEET    4 AC3 4 CYS E 387  LEU E 390 -1  O  LEU E 390   N  LEU E 372           
SHEET    1 AC4 4 PHE F 133  TYR F 140  0                                        
SHEET    2 AC4 4 PRO F 147  GLY F 153 -1  O  ALA F 150   N  ALA F 137           
SHEET    3 AC4 4 ILE F 158  ASN F 162 -1  O  ILE F 161   N  LEU F 149           
SHEET    4 AC4 4 GLN F 167  TYR F 172 -1  O  LYS F 170   N  ILE F 160           
SHEET    1 AC5 5 ILE F 179  PHE F 184  0                                        
SHEET    2 AC5 5 LEU F 191  SER F 196 -1  O  LEU F 193   N  LYS F 183           
SHEET    3 AC5 5 LEU F 201  ASN F 205 -1  O  TRP F 204   N  LEU F 192           
SHEET    4 AC5 5 THR F 210  PHE F 215 -1  O  THR F 210   N  ASN F 205           
SHEET    5 AC5 5 GLN F 278  ILE F 280  1  O  GLN F 278   N  ILE F 214           
SHEET    1 AC6 4 VAL F 225  TYR F 230  0                                        
SHEET    2 AC6 4 LYS F 236  GLY F 241 -1  O  CYS F 240   N  SER F 227           
SHEET    3 AC6 4 LEU F 246  ARG F 250 -1  O  LYS F 247   N  SER F 239           
SHEET    4 AC6 4 PHE F 285  THR F 287 -1  O  PHE F 285   N  LEU F 248           
SHEET    1 AC7 4 CYS F 297  LEU F 301  0                                        
SHEET    2 AC7 4 LEU F 304  LYS F 308 -1  O  LEU F 306   N  ARG F 299           
SHEET    3 AC7 4 ALA F 313  PRO F 319 -1  O  VAL F 315   N  SER F 307           
SHEET    4 AC7 4 VAL F 336  ASP F 343 -1  O  GLY F 340   N  CYS F 316           
SHEET    1 AC8 4 SER F 355  MET F 356  0                                        
SHEET    2 AC8 4 MET F 362  GLY F 366 -1  O  ALA F 364   N  SER F 355           
SHEET    3 AC8 4 LEU F 372  ASP F 376 -1  O  TYR F 373   N  LEU F 365           
SHEET    4 AC8 4 CYS F 387  LEU F 390 -1  O  LEU F 390   N  LEU F 372           
SSBOND   1 CYS B  452    CYS B  463                          1555   1555  2.71  
LINK         SG  CYS A 286                ZN    ZN A9008     1555   1555  2.15  
LINK         SG  CYS A 289                ZN    ZN A9008     1555   1555  2.33  
LINK         SG  CYS A 294                ZN    ZN A9008     1555   1555  2.27  
LINK         ND1 HIS A 297                ZN    ZN A9008     1555   1555  1.92  
LINK         SG  CYS A 523                ZN    ZN A9003     1555   1555  2.48  
LINK         SG  CYS A 523                ZN    ZN A9004     1555   1555  2.20  
LINK         NE2 HIS A 525                ZN    ZN A9004     1555   1555  1.94  
LINK         SG  CYS A 530                ZN    ZN A9002     1555   1555  2.28  
LINK         SG  CYS A 530                ZN    ZN A9004     1555   1555  2.25  
LINK         SG  CYS A 534                ZN    ZN A9004     1555   1555  2.14  
LINK         SG  CYS A 536                ZN    ZN A9003     1555   1555  2.34  
LINK         SG  CYS A 543                ZN    ZN A9002     1555   1555  2.43  
LINK         SG  CYS A 543                ZN    ZN A9003     1555   1555  2.35  
LINK         SG  CYS A 547                ZN    ZN A9003     1555   1555  2.26  
LINK         SG  CYS A 549                ZN    ZN A9002     1555   1555  2.17  
LINK         SG  CYS A 553                ZN    ZN A9002     1555   1555  2.22  
LINK         SG  CYS A 560                ZN    ZN A9007     1555   1555  2.30  
LINK         SG  CYS A 560                ZN    ZN A9005     1555   1555  2.49  
LINK         SG  CYS A 562                ZN    ZN A9007     1555   1555  2.47  
LINK         SG  CYS A 566                ZN    ZN A9007     1555   1555  2.23  
LINK         SG  CYS A 566                ZN    ZN A9006     1555   1555  2.28  
LINK         SG  CYS A 571                ZN    ZN A9007     1555   1555  2.22  
LINK         SG  CYS A 573                ZN    ZN A9005     1555   1555  2.26  
LINK         SG  CYS A 580                ZN    ZN A9005     1555   1555  2.11  
LINK         SG  CYS A 580                ZN    ZN A9006     1555   1555  2.42  
LINK         SG  CYS A 585                ZN    ZN A9005     1555   1555  2.15  
LINK         SG  CYS A 588                ZN    ZN A9006     1555   1555  2.40  
LINK         SG  CYS A 601                ZN    ZN A9006     1555   1555  2.17  
LINK         SG  CYS B 286                ZN    ZN B9008     1555   1555  2.22  
LINK         SG  CYS B 289                ZN    ZN B9008     1555   1555  2.31  
LINK         SG  CYS B 294                ZN    ZN B9008     1555   1555  2.23  
LINK         ND1 HIS B 297                ZN    ZN B9008     1555   1555  1.95  
LINK         SG  CYS B 523                ZN    ZN B9003     1555   1555  2.57  
LINK         SG  CYS B 523                ZN    ZN B9002     1555   1555  2.17  
LINK         NE2 HIS B 525                ZN    ZN B9002     1555   1555  2.10  
LINK         SG  CYS B 530                ZN    ZN B9002     1555   1555  2.18  
LINK         SG  CYS B 530                ZN    ZN B9004     1555   1555  2.30  
LINK         SG  CYS B 534                ZN    ZN B9002     1555   1555  2.16  
LINK         SG  CYS B 536                ZN    ZN B9003     1555   1555  2.25  
LINK         SG  CYS B 543                ZN    ZN B9003     1555   1555  2.31  
LINK         SG  CYS B 543                ZN    ZN B9004     1555   1555  2.39  
LINK         SG  CYS B 547                ZN    ZN B9003     1555   1555  2.31  
LINK         SG  CYS B 549                ZN    ZN B9004     1555   1555  2.18  
LINK         SG  CYS B 553                ZN    ZN B9004     1555   1555  2.25  
LINK         SG  CYS B 560                ZN    ZN B9005     1555   1555  2.30  
LINK         SG  CYS B 560                ZN    ZN B9007     1555   1555  2.50  
LINK         SG  CYS B 562                ZN    ZN B9005     1555   1555  2.60  
LINK         SG  CYS B 566                ZN    ZN B9005     1555   1555  2.19  
LINK         SG  CYS B 566                ZN    ZN B9006     1555   1555  2.40  
LINK         SG  CYS B 571                ZN    ZN B9005     1555   1555  2.13  
LINK         SG  CYS B 573                ZN    ZN B9007     1555   1555  2.17  
LINK         SG  CYS B 580                ZN    ZN B9006     1555   1555  2.40  
LINK         SG  CYS B 580                ZN    ZN B9007     1555   1555  2.16  
LINK         SG  CYS B 585                ZN    ZN B9007     1555   1555  2.14  
LINK         SG  CYS B 588                ZN    ZN B9006     1555   1555  2.27  
LINK         SG  CYS B 601                ZN    ZN B9006     1555   1555  2.09  
CISPEP   1 MET T  579    GLU T  580          0        -1.57                     
SITE     1 AC1 15 ILE A 109  MET A 110  TYR A 111  GLY A 623                    
SITE     2 AC1 15 TRP A 624  VAL A 657  TYR A 658  TYR A 661                    
SITE     3 AC1 15 PHE A 665  ARG A 685  PHE A 686  ASN A 688                    
SITE     4 AC1 15 HOH A9101  ARG E 222  ASP E 223                               
SITE     1 AC2  4 CYS A 530  CYS A 543  CYS A 549  CYS A 553                    
SITE     1 AC3  5 CYS A 523  CYS A 536  CYS A 543  CYS A 547                    
SITE     2 AC3  5  ZN A9004                                                     
SITE     1 AC4  5 CYS A 523  HIS A 525  CYS A 530  CYS A 534                    
SITE     2 AC4  5  ZN A9003                                                     
SITE     1 AC5  4 CYS A 560  CYS A 573  CYS A 580  CYS A 585                    
SITE     1 AC6  4 CYS A 566  CYS A 580  CYS A 588  CYS A 601                    
SITE     1 AC7  4 CYS A 560  CYS A 562  CYS A 566  CYS A 571                    
SITE     1 AC8  4 CYS A 286  CYS A 289  CYS A 294  HIS A 297                    
SITE     1 AC9 14 ILE B 109  MET B 110  TYR B 111  GLY B 623                    
SITE     2 AC9 14 TRP B 624  VAL B 657  TYR B 658  TYR B 661                    
SITE     3 AC9 14 PHE B 665  ARG B 685  PHE B 686  ASN B 688                    
SITE     4 AC9 14 ARG F 222  ASP F 223                                          
SITE     1 AD1  5 CYS B 523  HIS B 525  CYS B 530  CYS B 534                    
SITE     2 AD1  5  ZN B9003                                                     
SITE     1 AD2  5 CYS B 523  CYS B 536  CYS B 543  CYS B 547                    
SITE     2 AD2  5  ZN B9002                                                     
SITE     1 AD3  4 CYS B 530  CYS B 543  CYS B 549  CYS B 553                    
SITE     1 AD4  4 CYS B 560  CYS B 562  CYS B 566  CYS B 571                    
SITE     1 AD5  4 CYS B 566  CYS B 580  CYS B 588  CYS B 601                    
SITE     1 AD6  4 CYS B 560  CYS B 573  CYS B 580  CYS B 585                    
SITE     1 AD7  4 CYS B 286  CYS B 289  CYS B 294  HIS B 297                    
CRYST1   69.575  115.042  153.033  90.00 102.53  90.00 P 1 21 1      4          
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      0.014373  0.000000  0.003194        0.00000                         
SCALE2      0.000000  0.008692  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006694        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system