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Database: PDB
Entry: 5T0K
LinkDB: 5T0K
Original site: 5T0K 
HEADER    TRANSFERASE                             16-AUG-16   5T0K              
TITLE     STRUCTURE OF G9A SET-DOMAIN WITH H3K9M MUTANT PEPTIDE AND SAM         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-     
COMPND   5 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-     
COMPND   6 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;                  
COMPND   7 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: H3K9 MUTANT PEPTIDE;                                       
COMPND  11 CHAIN: P, Q;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EHMT2, BAT8, C6ORF30, G9A, KMT1C, NG36;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    HISTONE METHYLTRANSFERASE, SET DOMAIN, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.XU,L.TONG                                                           
REVDAT   2   20-SEP-17 5T0K    1       REMARK                                   
REVDAT   1   05-OCT-16 5T0K    0                                                
JRNL        AUTH   C.M.SHAN,J.WANG,K.XU,H.CHEN,J.X.YUE,S.ANDREWS,J.J.MORESCO,   
JRNL        AUTH 2 J.R.YATES,P.L.NAGY,L.TONG,S.JIA                              
JRNL        TITL   A HISTONE H3K9M MUTATION TRAPS HISTONE METHYLTRANSFERASE     
JRNL        TITL 2 CLR4 TO PREVENT HETEROCHROMATIN SPREADING.                   
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27648579                                                     
JRNL        DOI    10.7554/ELIFE.17903                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 71258                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.4117 -  4.0927    0.98     5160   147  0.1510 0.1732        
REMARK   3     2  4.0927 -  3.2487    0.99     5022   144  0.1477 0.1877        
REMARK   3     3  3.2487 -  2.8381    1.00     5014   147  0.1692 0.1938        
REMARK   3     4  2.8381 -  2.5786    0.99     4993   143  0.1706 0.1695        
REMARK   3     5  2.5786 -  2.3938    0.99     4947   144  0.1666 0.1836        
REMARK   3     6  2.3938 -  2.2526    1.00     4980   143  0.1665 0.2191        
REMARK   3     7  2.2526 -  2.1398    0.99     4947   144  0.1667 0.1868        
REMARK   3     8  2.1398 -  2.0467    0.99     4922   141  0.1727 0.2136        
REMARK   3     9  2.0467 -  1.9679    1.00     4952   139  0.1704 0.2084        
REMARK   3    10  1.9679 -  1.9000    1.00     4903   144  0.1729 0.2029        
REMARK   3    11  1.9000 -  1.8406    1.00     4962   143  0.1848 0.2044        
REMARK   3    12  1.8406 -  1.7880    1.00     4951   146  0.1872 0.2277        
REMARK   3    13  1.7880 -  1.7409    1.00     4921   135  0.1938 0.2325        
REMARK   3    14  1.7409 -  1.6984    0.93     4588   136  0.2052 0.2276        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.940           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4584                                  
REMARK   3   ANGLE     :  1.037           6198                                  
REMARK   3   CHIRALITY :  0.045            662                                  
REMARK   3   PLANARITY :  0.004            810                                  
REMARK   3   DIHEDRAL  : 14.460           1724                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5T0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223419.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 704U                      
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 704U                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692                                       
REMARK 200 STARTING MODEL: 2O8J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE (PH 7.5), 18%     
REMARK 280  (W/V) PEG3350, 0.2 M NAF, AND 5% (V/V) ETHYLENE GLYCOL, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.55050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.57150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.15350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.57150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.55050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.15350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASN A   913                                                      
REMARK 465     ARG A   914                                                      
REMARK 465     ALA A   915                                                      
REMARK 465     ILE A   916                                                      
REMARK 465     ARG A   917                                                      
REMARK 465     THR A   918                                                      
REMARK 465     GLU A   919                                                      
REMARK 465     ASN A  1091                                                      
REMARK 465     LYS A  1092                                                      
REMARK 465     ASP A  1093                                                      
REMARK 465     GLY A  1094                                                      
REMARK 465     ARG A  1188                                                      
REMARK 465     LEU A  1189                                                      
REMARK 465     ALA A  1190                                                      
REMARK 465     ARG A  1191                                                      
REMARK 465     LEU A  1192                                                      
REMARK 465     ASP A  1193                                                      
REMARK 465     ASN B   913                                                      
REMARK 465     ARG B   914                                                      
REMARK 465     ALA B   915                                                      
REMARK 465     ILE B   916                                                      
REMARK 465     ARG B   917                                                      
REMARK 465     THR B   918                                                      
REMARK 465     GLU B   919                                                      
REMARK 465     LYS B   920                                                      
REMARK 465     GLN B  1004                                                      
REMARK 465     GLU B  1005                                                      
REMARK 465     PHE B  1006                                                      
REMARK 465     ASN B  1007                                                      
REMARK 465     LYS B  1008                                                      
REMARK 465     ILE B  1009                                                      
REMARK 465     GLU B  1010                                                      
REMARK 465     ASP B  1193                                                      
REMARK 465     ALA P     1                                                      
REMARK 465     ARG P     2                                                      
REMARK 465     GLY P    13                                                      
REMARK 465     LYS P    14                                                      
REMARK 465     ALA P    15                                                      
REMARK 465     ALA Q     1                                                      
REMARK 465     ARG Q     2                                                      
REMARK 465     GLY Q    13                                                      
REMARK 465     LYS Q    14                                                      
REMARK 465     ALA Q    15                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY P  12    CA   C    O                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1724     O    HOH A  1725              1.88            
REMARK 500   O    HOH B  1739     O    HOH B  1740              1.95            
REMARK 500   O    HOH A  1648     O    HOH A  1664              1.96            
REMARK 500   O    HOH A  1471     O    HOH A  1637              1.97            
REMARK 500   O    HOH B  1544     O    HOH B  1591              1.99            
REMARK 500   O    HOH A  1405     O    HOH A  1439              2.01            
REMARK 500   O    HOH A  1411     O    HOH A  1655              2.02            
REMARK 500   O    HOH A  1684     O    HOH A  1716              2.02            
REMARK 500   O    HOH A  1671     O    HOH A  1722              2.03            
REMARK 500   N    THR Q     3     O    HOH Q   101              2.06            
REMARK 500   NH2  ARG B   924     O    HOH B  1401              2.08            
REMARK 500   O    HOH B  1681     O    HOH B  1697              2.09            
REMARK 500   O    HOH B  1664     O    HOH B  1691              2.10            
REMARK 500   O    ASP A  1090     O    HOH A  1401              2.10            
REMARK 500   O    HOH B  1706     O    HOH B  1730              2.11            
REMARK 500   N    GLY P    12     O    HOH P   101              2.12            
REMARK 500   N    LYS A   920     O    HOH A  1402              2.12            
REMARK 500   NH1  ARG B   924     O    HOH B  1402              2.13            
REMARK 500   NE2  GLN B  1019     O    HOH B  1403              2.13            
REMARK 500   OD1  ASP B   999     O    HOH B  1404              2.14            
REMARK 500   O    HOH B  1634     O    HOH Q   107              2.14            
REMARK 500   O    THR P     3     O    HOH P   102              2.14            
REMARK 500   O    HOH A  1582     O    HOH B  1504              2.15            
REMARK 500   O    HOH A  1524     O    HOH A  1700              2.17            
REMARK 500   O    HOH A  1614     O    HOH A  1689              2.18            
REMARK 500   O    HOH A  1485     O    HOH A  1513              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  1456     O    HOH B  1524     4455     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 949       32.56    -92.83                                   
REMARK 500    ASP A 978     -149.51   -116.09                                   
REMARK 500    ILE A 992      -59.80     77.81                                   
REMARK 500    ASN A1029       47.58   -106.41                                   
REMARK 500    ARG A1030       40.34   -144.34                                   
REMARK 500    ILE A1064      -63.42   -101.95                                   
REMARK 500    ASN A1106     -161.99   -113.45                                   
REMARK 500    ASP A1116       73.95   -111.42                                   
REMARK 500    MET A1126      -91.14   -129.36                                   
REMARK 500    ASP B 925      102.60   -167.07                                   
REMARK 500    ASP B 978     -134.28   -142.71                                   
REMARK 500    ILE B 992      -52.34     68.82                                   
REMARK 500    ILE B1064      -61.13   -109.22                                   
REMARK 500    ASN B1106     -162.07   -110.89                                   
REMARK 500    ASP B1116       73.52   -114.29                                   
REMARK 500    MET B1126      -96.07   -128.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1725        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A1726        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A1727        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH B1744        DISTANCE =  5.81 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 987   SG  113.9                                              
REMARK 620 3 CYS A1017   SG  109.0 113.1                                        
REMARK 620 4 CYS A1021   SG  106.1  98.6 115.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 976   SG  106.2                                              
REMARK 620 3 CYS A 980   SG  107.9 107.5                                        
REMARK 620 4 CYS A 985   SG  110.7 108.6 115.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 980   SG                                                     
REMARK 620 2 CYS A1017   SG  111.5                                              
REMARK 620 3 CYS A1023   SG  105.2 107.8                                        
REMARK 620 4 CYS A1027   SG  112.4 106.7 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1115   SG                                                     
REMARK 620 2 CYS A1168   SG  114.2                                              
REMARK 620 3 CYS A1170   SG  107.3 105.4                                        
REMARK 620 4 CYS A1175   SG  105.2 108.9 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 976   SG  107.2                                              
REMARK 620 3 CYS B 980   SG  107.7 103.9                                        
REMARK 620 4 CYS B 985   SG  112.1 110.7 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 987   SG  112.0                                              
REMARK 620 3 CYS B1017   SG  109.3 114.2                                        
REMARK 620 4 CYS B1021   SG  105.9  98.8 116.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 980   SG                                                     
REMARK 620 2 CYS B1017   SG  111.8                                              
REMARK 620 3 CYS B1023   SG  102.9 106.7                                        
REMARK 620 4 CYS B1027   SG  112.3 106.6 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1115   SG                                                     
REMARK 620 2 CYS B1168   SG  112.8                                              
REMARK 620 3 CYS B1170   SG  107.8 105.1                                        
REMARK 620 4 CYS B1175   SG  105.5 110.5 115.3                                  
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 ZN A 1300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1304                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5T0M   RELATED DB: PDB                                   
DBREF  5T0K A  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    879   1159             
DBREF  5T0K B  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    879   1159             
DBREF  5T0K P    1    15  PDB    5T0K     5T0K             1     15             
DBREF  5T0K Q    1    15  PDB    5T0K     5T0K             1     15             
SEQRES   1 A  281  ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS ARG ASP          
SEQRES   2 A  281  VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL          
SEQRES   3 A  281  ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS          
SEQRES   4 A  281  TYR ILE SER GLU ASN CYS GLU THR SER THR MET ASN ILE          
SEQRES   5 A  281  ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR CYS VAL          
SEQRES   6 A  281  ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY GLN LEU          
SEQRES   7 A  281  SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU          
SEQRES   8 A  281  GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU          
SEQRES   9 A  281  CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS LYS ASN          
SEQRES  10 A  281  ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU GLN LEU          
SEQRES  11 A  281  TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG ALA LEU          
SEQRES  12 A  281  GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU TYR VAL          
SEQRES  13 A  281  GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL ARG GLU          
SEQRES  14 A  281  ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY          
SEQRES  15 A  281  GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE          
SEQRES  16 A  281  SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE          
SEQRES  17 A  281  PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU ARG PHE          
SEQRES  18 A  281  PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE ARG THR          
SEQRES  19 A  281  GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP          
SEQRES  20 A  281  ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS GLY SER          
SEQRES  21 A  281  GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA LEU GLU          
SEQRES  22 A  281  GLN SER ARG LEU ALA ARG LEU ASP                              
SEQRES   1 B  281  ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS ARG ASP          
SEQRES   2 B  281  VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL          
SEQRES   3 B  281  ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS          
SEQRES   4 B  281  TYR ILE SER GLU ASN CYS GLU THR SER THR MET ASN ILE          
SEQRES   5 B  281  ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR CYS VAL          
SEQRES   6 B  281  ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY GLN LEU          
SEQRES   7 B  281  SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU          
SEQRES   8 B  281  GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU          
SEQRES   9 B  281  CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS LYS ASN          
SEQRES  10 B  281  ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU GLN LEU          
SEQRES  11 B  281  TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG ALA LEU          
SEQRES  12 B  281  GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU TYR VAL          
SEQRES  13 B  281  GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL ARG GLU          
SEQRES  14 B  281  ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY          
SEQRES  15 B  281  GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE          
SEQRES  16 B  281  SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE          
SEQRES  17 B  281  PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU ARG PHE          
SEQRES  18 B  281  PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE ARG THR          
SEQRES  19 B  281  GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP          
SEQRES  20 B  281  ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS GLY SER          
SEQRES  21 B  281  GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA LEU GLU          
SEQRES  22 B  281  GLN SER ARG LEU ALA ARG LEU ASP                              
SEQRES   1 P   15  ALA ARG THR LYS GLN THR ALA ARG MET SER THR GLY GLY          
SEQRES   2 P   15  LYS ALA                                                      
SEQRES   1 Q   15  ALA ARG THR LYS GLN THR ALA ARG MET SER THR GLY GLY          
SEQRES   2 Q   15  LYS ALA                                                      
HET     ZN  A1300       1                                                       
HET     ZN  A1301       1                                                       
HET     ZN  A1302       1                                                       
HET     ZN  A1303       1                                                       
HET    SAM  A1304      27                                                       
HET     ZN  B1300       1                                                       
HET     ZN  B1301       1                                                       
HET     ZN  B1302       1                                                       
HET     ZN  B1303       1                                                       
HET    SAM  B1304      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   9  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  15  HOH   *688(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  SER A  991  1                                   7    
HELIX    3 AA3 VAL A 1031  GLY A 1035  5                                   5    
HELIX    4 AA4 ASP A 1074  ASP A 1078  1                                   5    
HELIX    5 AA5 ILE A 1107  ILE A 1111  5                                   5    
HELIX    6 AA6 GLY A 1155  SER A 1163  1                                   9    
HELIX    7 AA7 SER A 1178  SER A 1187  1                                  10    
HELIX    8 AA8 ILE B  921  ASP B  925  5                                   5    
HELIX    9 AA9 ASN B  967  LEU B  971  5                                   5    
HELIX   10 AB1 CYS B  985  SER B  991  1                                   7    
HELIX   11 AB2 VAL B 1031  GLY B 1035  5                                   5    
HELIX   12 AB3 ASP B 1074  ASP B 1078  1                                   5    
HELIX   13 AB4 ILE B 1107  ILE B 1111  5                                   5    
HELIX   14 AB5 GLY B 1155  SER B 1163  1                                   9    
HELIX   15 AB6 SER B 1178  ARG B 1191  1                                  14    
SHEET    1 AA1 3 CYS A 937  VAL A 938  0                                        
SHEET    2 AA1 3 LEU A1040  ARG A1044  1  O  LEU A1042   N  VAL A 938           
SHEET    3 AA1 3 TRP A1050  ALA A1054 -1  O  GLY A1051   N  TYR A1043           
SHEET    1 AA2 4 LYS A 951  TYR A 952  0                                        
SHEET    2 AA2 4 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA2 4 GLY A1069  SER A1073 -1  N  ILE A1072   O  CYS A1098           
SHEET    4 AA2 4 CYS A 957  GLU A 958  1  N  CYS A 957   O  LEU A1071           
SHEET    1 AA3 3 LYS A 951  TYR A 952  0                                        
SHEET    2 AA3 3 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA3 3 LEU A1086  ASP A1088 -1  N  PHE A1087   O  ILE A1099           
SHEET    1 AA4 4 ILE A1014  PHE A1015  0                                        
SHEET    2 AA4 4 ILE A1119  PHE A1125  1  O  PHE A1125   N  ILE A1014           
SHEET    3 AA4 4 ARG A1135  SER A1140 -1  O  ALA A1137   N  VAL A1122           
SHEET    4 AA4 4 PHE A1063  TYR A1067 -1  N  ILE A1064   O  PHE A1138           
SHEET    1 AA5 2 ASN A1112  HIS A1113  0                                        
SHEET    2 AA5 2 GLY A1151  PHE A1152  1  O  PHE A1152   N  ASN A1112           
SHEET    1 AA6 3 CYS B 937  VAL B 938  0                                        
SHEET    2 AA6 3 LEU B1040  ARG B1044  1  O  LEU B1042   N  VAL B 938           
SHEET    3 AA6 3 TRP B1050  ALA B1054 -1  O  GLY B1051   N  TYR B1043           
SHEET    1 AA7 4 LYS B 951  TYR B 952  0                                        
SHEET    2 AA7 4 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA7 4 GLY B1069  SER B1073 -1  N  GLU B1070   O  ASP B1100           
SHEET    4 AA7 4 CYS B 957  GLU B 958  1  N  CYS B 957   O  LEU B1071           
SHEET    1 AA8 3 LYS B 951  TYR B 952  0                                        
SHEET    2 AA8 3 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA8 3 LEU B1086  ASP B1088 -1  N  PHE B1087   O  ILE B1099           
SHEET    1 AA9 4 ILE B1014  PHE B1015  0                                        
SHEET    2 AA9 4 ILE B1119  PHE B1125  1  O  PHE B1125   N  ILE B1014           
SHEET    3 AA9 4 ARG B1135  SER B1140 -1  O  ALA B1137   N  VAL B1122           
SHEET    4 AA9 4 PHE B1063  TYR B1067 -1  N  ILE B1064   O  PHE B1138           
SHEET    1 AB1 2 ASN B1112  HIS B1113  0                                        
SHEET    2 AB1 2 GLY B1151  PHE B1152  1  O  PHE B1152   N  ASN B1112           
SSBOND   1 CYS A  937    CYS A  946                          1555   1555  2.04  
SSBOND   2 CYS B  937    CYS B  946                          1555   1555  2.04  
LINK         SG  CYS A 974                ZN    ZN A1300     1555   1555  2.39  
LINK         SG  CYS A 974                ZN    ZN A1302     1555   1555  2.33  
LINK         SG  CYS A 976                ZN    ZN A1302     1555   1555  2.35  
LINK         SG  CYS A 980                ZN    ZN A1301     1555   1555  2.32  
LINK         SG  CYS A 980                ZN    ZN A1302     1555   1555  2.37  
LINK         SG  CYS A 985                ZN    ZN A1302     1555   1555  2.27  
LINK         SG  CYS A 987                ZN    ZN A1300     1555   1555  2.30  
LINK         SG  CYS A1017                ZN    ZN A1300     1555   1555  2.38  
LINK         SG  CYS A1017                ZN    ZN A1301     1555   1555  2.35  
LINK         SG  CYS A1021                ZN    ZN A1300     1555   1555  2.32  
LINK         SG  CYS A1023                ZN    ZN A1301     1555   1555  2.29  
LINK         SG  CYS A1027                ZN    ZN A1301     1555   1555  2.28  
LINK         SG  CYS A1115                ZN    ZN A1303     1555   1555  2.42  
LINK         SG  CYS A1168                ZN    ZN A1303     1555   1555  2.28  
LINK         SG  CYS A1170                ZN    ZN A1303     1555   1555  2.35  
LINK         SG  CYS A1175                ZN    ZN A1303     1555   1555  2.29  
LINK         SG  CYS B 974                ZN    ZN B1300     1555   1555  2.36  
LINK         SG  CYS B 974                ZN    ZN B1301     1555   1555  2.42  
LINK         SG  CYS B 976                ZN    ZN B1300     1555   1555  2.36  
LINK         SG  CYS B 980                ZN    ZN B1300     1555   1555  2.36  
LINK         SG  CYS B 980                ZN    ZN B1302     1555   1555  2.34  
LINK         SG  CYS B 985                ZN    ZN B1300     1555   1555  2.31  
LINK         SG  CYS B 987                ZN    ZN B1301     1555   1555  2.28  
LINK         SG  CYS B1017                ZN    ZN B1302     1555   1555  2.38  
LINK         SG  CYS B1017                ZN    ZN B1301     1555   1555  2.35  
LINK         SG  CYS B1021                ZN    ZN B1301     1555   1555  2.35  
LINK         SG  CYS B1023                ZN    ZN B1302     1555   1555  2.33  
LINK         SG  CYS B1027                ZN    ZN B1302     1555   1555  2.32  
LINK         SG  CYS B1115                ZN    ZN B1303     1555   1555  2.43  
LINK         SG  CYS B1168                ZN    ZN B1303     1555   1555  2.29  
LINK         SG  CYS B1170                ZN    ZN B1303     1555   1555  2.34  
LINK         SG  CYS B1175                ZN    ZN B1303     1555   1555  2.31  
SITE     1 AC1  4 CYS A 974  CYS A 987  CYS A1017  CYS A1021                    
SITE     1 AC2  4 CYS A 980  CYS A1017  CYS A1023  CYS A1027                    
SITE     1 AC3  4 CYS A 974  CYS A 976  CYS A 980  CYS A 985                    
SITE     1 AC4  4 CYS A1115  CYS A1168  CYS A1170  CYS A1175                    
SITE     1 AC5 20 MET A1048  TRP A1050  SER A1084  TYR A1085                    
SITE     2 AC5 20 ARG A1109  PHE A1110  ILE A1111  ASN A1112                    
SITE     3 AC5 20 HIS A1113  TYR A1154  PHE A1158  PHE A1166                    
SITE     4 AC5 20 THR A1167  CYS A1168  GLN A1169  HOH A1454                    
SITE     5 AC5 20 HOH A1483  HOH A1486  HOH A1593  HOH A1595                    
SITE     1 AC6  4 CYS B 974  CYS B 976  CYS B 980  CYS B 985                    
SITE     1 AC7  4 CYS B 974  CYS B 987  CYS B1017  CYS B1021                    
SITE     1 AC8  4 CYS B 980  CYS B1017  CYS B1023  CYS B1027                    
SITE     1 AC9  4 CYS B1115  CYS B1168  CYS B1170  CYS B1175                    
SITE     1 AD1 21 MET B1048  TRP B1050  SER B1084  TYR B1085                    
SITE     2 AD1 21 ARG B1109  PHE B1110  ILE B1111  ASN B1112                    
SITE     3 AD1 21 HIS B1113  TYR B1154  PHE B1158  PHE B1166                    
SITE     4 AD1 21 THR B1167  CYS B1168  GLN B1169  HOH B1419                    
SITE     5 AD1 21 HOH B1472  HOH B1534  HOH B1556  HOH B1583                    
SITE     6 AD1 21 HOH B1609                                                     
CRYST1   75.101   92.307   93.143  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013315  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010833  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010736        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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