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Database: PDB
Entry: 3SW9
LinkDB: 3SW9
Original site: 3SW9 
HEADER    TRANSFERASE                             13-JUL-11   3SW9              
TITLE     GLP (G9A-LIKE PROTEIN) SET DOMAIN IN COMPLEX WITH DNMT3AK44ME0 PEPTIDE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 982-1266;                                     
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-       
COMPND   6 HMTASE1, G9A-LIKE PROTEIN 1, GLP, GLP1, HISTONE H3-K9                
COMPND   7 METHYLTRANSFERASE 5, H3-K9-HMTASE 5, LYSINE N-METHYLTRANSFERASE 1D;  
COMPND   8 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND  12 CHAIN: P, Q;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 39-50;                                        
COMPND  14 SYNONYM: DNMT3A, DNA METHYLTRANSFERASE MMUIIIA, DNA MTASE MMUIIIA,   
COMPND  15 M.MMUIIIA;                                                           
COMPND  16 EC: 2.1.1.37;                                                        
COMPND  17 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: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PXC681;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090                                                
KEYWDS    EPIGENETICS, NON-HISTONE LYSINE METHYLATION, SET DOMAIN, PROTEIN      
KEYWDS   2 LYSINE METHYLTRANSFERASE, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHANG,J.R.HORTON,X.ZHANG,X.CHENG                                    
REVDAT   2   18-APR-18 3SW9    1       REMARK                                   
REVDAT   1   07-DEC-11 3SW9    0                                                
JRNL        AUTH   Y.CHANG,L.SUN,K.KOKURA,J.R.HORTON,M.FUKUDA,A.ESPEJO,V.IZUMI, 
JRNL        AUTH 2 J.M.KOOMEN,M.T.BEDFORD,X.ZHANG,Y.SHINKAI,J.FANG,X.CHENG      
JRNL        TITL   MPP8 MEDIATES THE INTERACTIONS BETWEEN DNA METHYLTRANSFERASE 
JRNL        TITL 2 DNMT3A AND H3K9 METHYLTRANSFERASE GLP/G9A.                   
JRNL        REF    NAT COMMUN                    V.   2   533 2011              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   22086334                                                     
JRNL        DOI    10.1038/NCOMMS1549                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13472                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 674                             
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 28.6900 -  5.2014    1.00     2743   145  0.1736 0.2352        
REMARK   3     2  5.2014 -  4.1324    0.99     2599   139  0.1461 0.2113        
REMARK   3     3  4.1324 -  3.6112    0.99     2586   132  0.1550 0.2455        
REMARK   3     4  3.6112 -  3.2816    0.98     2516   139  0.1870 0.2943        
REMARK   3     5  3.2816 -  3.0466    0.91     2354   119  0.2183 0.3153        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 12.90                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.130           
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) : -0.36290                                             
REMARK   3    B22 (A**2) : 2.77370                                              
REMARK   3    B33 (A**2) : -2.41080                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.008           4416                                  
REMARK   3   ANGLE     :  1.222           5981                                  
REMARK   3   CHIRALITY :  0.085            626                                  
REMARK   3   PLANARITY :  0.006            791                                  
REMARK   3   DIHEDRAL  : 17.683           1669                                  
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 3SW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066730.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-10                          
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                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07169                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13788                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3MO5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 16% POLYETHYLENE GLYCOL     
REMARK 280  4000 AND 8% ISOPROPANOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 289K                                                    
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       40.07000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.53500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.57000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.53500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.07000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.57000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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: 1280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, 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   951                                                      
REMARK 465     SER A   952                                                      
REMARK 465     GLN A   953                                                      
REMARK 465     VAL A   954                                                      
REMARK 465     TRP A   955                                                      
REMARK 465     SER A   956                                                      
REMARK 465     ALA A   957                                                      
REMARK 465     LEU A   958                                                      
REMARK 465     GLN A   959                                                      
REMARK 465     MET A   960                                                      
REMARK 465     SER A   961                                                      
REMARK 465     LYS A   962                                                      
REMARK 465     ALA A   963                                                      
REMARK 465     LEU A   964                                                      
REMARK 465     GLN A   965                                                      
REMARK 465     ASP A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     ALA A   968                                                      
REMARK 465     PRO A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     ARG A   971                                                      
REMARK 465     PRO A   972                                                      
REMARK 465     SER A   973                                                      
REMARK 465     PRO A   974                                                      
REMARK 465     SER P    39                                                      
REMARK 465     ALA P    40                                                      
REMARK 465     GLY P    46                                                      
REMARK 465     ARG P    47                                                      
REMARK 465     PRO P    48                                                      
REMARK 465     GLY P    49                                                      
REMARK 465     ARG P    50                                                      
REMARK 465     ASN B   951                                                      
REMARK 465     SER B   952                                                      
REMARK 465     GLN B   953                                                      
REMARK 465     VAL B   954                                                      
REMARK 465     TRP B   955                                                      
REMARK 465     SER B   956                                                      
REMARK 465     ALA B   957                                                      
REMARK 465     LEU B   958                                                      
REMARK 465     GLN B   959                                                      
REMARK 465     MET B   960                                                      
REMARK 465     SER B   961                                                      
REMARK 465     LYS B   962                                                      
REMARK 465     ALA B   963                                                      
REMARK 465     LEU B   964                                                      
REMARK 465     GLN B   965                                                      
REMARK 465     ASP B   966                                                      
REMARK 465     SER B   967                                                      
REMARK 465     ALA B   968                                                      
REMARK 465     PRO B   969                                                      
REMARK 465     ASP B   970                                                      
REMARK 465     ARG B   971                                                      
REMARK 465     PRO B   972                                                      
REMARK 465     SER B   973                                                      
REMARK 465     PRO B   974                                                      
REMARK 465     SER Q    39                                                      
REMARK 465     ALA Q    40                                                      
REMARK 465     ARG Q    47                                                      
REMARK 465     PRO Q    48                                                      
REMARK 465     GLY Q    49                                                      
REMARK 465     ARG Q    50                                                      
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     VAL A 975    CG1  CG2                                            
REMARK 470     ARG A 981    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A1104    CG   OD1  OD2                                       
REMARK 470     GLU A1138    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1149    CG   CD   CE   NZ                                   
REMARK 470     ASP A1150    CG   OD1  OD2                                       
REMARK 470     VAL B 975    CG1  CG2                                            
REMARK 470     ARG B 981    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1104    CG   OD1  OD2                                       
REMARK 470     GLU B1138    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1149    CG   CD   CE   NZ                                   
REMARK 470     ASP B1150    CG   OD1  OD2                                       
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 982       94.44   -165.71                                   
REMARK 500    ASP A 999     -162.62   -161.99                                   
REMARK 500    CYS A1003      133.63    -39.20                                   
REMARK 500    SER A1005       19.75   -146.03                                   
REMARK 500    ASN A1006       30.69    -87.99                                   
REMARK 500    ASP A1035     -157.65   -109.66                                   
REMARK 500    MET A1049      -55.54     75.10                                   
REMARK 500    CYS A1078      153.90    -49.59                                   
REMARK 500    ASN A1086       44.00    -95.13                                   
REMARK 500    VAL A1088      -67.43   -147.47                                   
REMARK 500    ASP A1131      -59.66    -29.50                                   
REMARK 500    ASP A1147       84.39    -65.66                                   
REMARK 500    ASP A1150       24.24    -79.45                                   
REMARK 500    ASN A1163     -158.21    -93.54                                   
REMARK 500    GLU A1173       57.72   -114.88                                   
REMARK 500    MET A1183      -93.45   -124.36                                   
REMARK 500    ILE A1218      -65.51   -101.13                                   
REMARK 500    ARG A1226       32.66    -83.87                                   
REMARK 500    GLU B 976       93.83    -48.70                                   
REMARK 500    SER B 980      131.18   -170.61                                   
REMARK 500    ASP B 982      106.87   -168.89                                   
REMARK 500    ALA B 997       45.56   -105.27                                   
REMARK 500    VAL B 998      -28.23   -140.55                                   
REMARK 500    ASP B 999     -148.09   -158.81                                   
REMARK 500    GLU B1001      138.92    -18.75                                   
REMARK 500    SER B1005       -1.53   -145.98                                   
REMARK 500    ASN B1006       42.25    -77.28                                   
REMARK 500    ASN B1020       37.54    -91.90                                   
REMARK 500    ASP B1035     -151.15   -111.68                                   
REMARK 500    MET B1049      -75.37     71.86                                   
REMARK 500    PRO B1069     -171.17    -68.12                                   
REMARK 500    ASN B1086       34.75    -78.19                                   
REMARK 500    VAL B1088      -58.37   -154.46                                   
REMARK 500    ASP B1147       80.98      7.67                                   
REMARK 500    LYS B1149      -50.90     72.19                                   
REMARK 500    GLU B1173       59.96   -116.16                                   
REMARK 500    MET B1183      -90.40   -134.20                                   
REMARK 500    ALA B1203      119.85    -34.27                                   
REMARK 500    LYS B1221        6.46    -68.96                                   
REMARK 500    ARG B1226       30.50    -98.68                                   
REMARK 500    HIS B1234       40.60   -145.19                                   
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 B   6  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1037   SG                                                     
REMARK 620 2 CYS B1074   SG  111.7                                              
REMARK 620 3 CYS B1080   SG  109.1  99.9                                        
REMARK 620 4 CYS B1084   SG  108.7  93.8 131.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1225   SG                                                     
REMARK 620 2 CYS A1172   SG  118.8                                              
REMARK 620 3 CYS A1232   SG  100.6 112.5                                        
REMARK 620 4 CYS A1227   SG  108.5 107.3 108.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1037   SG                                                     
REMARK 620 2 CYS A1033   SG   99.1                                              
REMARK 620 3 CYS A1042   SG  104.8 106.3                                        
REMARK 620 4 CYS A1031   SG  110.5 112.0 121.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   5  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1044   SG                                                     
REMARK 620 2 CYS B1074   SG  113.6                                              
REMARK 620 3 CYS B1031   SG  104.5 116.9                                        
REMARK 620 4 CYS B1078   SG   93.9 124.4  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1080   SG                                                     
REMARK 620 2 CYS A1084   SG  139.9                                              
REMARK 620 3 CYS A1074   SG  103.3  97.8                                        
REMARK 620 4 CYS A1037   SG   99.5 110.1 100.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   7  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1031   SG                                                     
REMARK 620 2 CYS B1037   SG  112.1                                              
REMARK 620 3 CYS B1042   SG  107.7 113.4                                        
REMARK 620 4 CYS B1033   SG  105.9 102.7 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   8  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1225   SG                                                     
REMARK 620 2 CYS B1227   SG   90.9                                              
REMARK 620 3 CYS B1232   SG   97.2 108.9                                        
REMARK 620 4 CYS B1172   SG  127.0 117.4 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1074   SG  114.2                                              
REMARK 620 3 CYS A1078   SG   95.1 131.6                                        
REMARK 620 4 CYS A1044   SG  112.8 108.5  92.6                                  
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 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG B 102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MO5   RELATED DB: PDB                                   
REMARK 900 HUMAN G9A-LIKE (GLP, ALSO KNOWN AS EHMT1)                            
REMARK 900 RELATED ID: 3SWC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SVM   RELATED DB: PDB                                   
DBREF  3SW9 A  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
DBREF  3SW9 P   39    50  UNP    O88508   DNM3A_MOUSE     39     50             
DBREF  3SW9 B  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
DBREF  3SW9 Q   39    50  UNP    O88508   DNM3A_MOUSE     39     50             
SEQRES   1 A  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 A  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 A  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 A  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 A  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 A  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 A  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 A  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 A  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 A  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 A  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 A  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 A  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 A  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 A  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 A  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 A  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 A  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 A  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 A  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 A  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 A  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
SEQRES   1 P   12  SER ALA THR ALA ARG LYS VAL GLY ARG PRO GLY ARG              
SEQRES   1 B  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 B  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 B  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 B  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 B  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 B  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 B  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 B  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 B  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 B  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 B  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 B  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 B  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 B  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 B  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 B  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 B  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 B  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 B  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 B  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 B  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 B  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
SEQRES   1 Q   12  SER ALA THR ALA ARG LYS VAL GLY ARG PRO GLY ARG              
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   4       1                                                       
HET    SFG  A 101      27                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET     ZN  B   7       1                                                       
HET     ZN  B   8       1                                                       
HET    SFG  B 102      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SFG SINEFUNGIN                                                       
HETSYN     SFG ADENOSYL-ORNITHINE                                               
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   9  SFG    2(C15 H23 N7 O5)                                             
FORMUL  15  HOH   *23(H2 O)                                                     
HELIX    1   1 ASN A 1024  LEU A 1028  5                                   5    
HELIX    2   2 CYS A 1042  SER A 1048  1                                   7    
HELIX    3   3 VAL A 1088  GLY A 1092  5                                   5    
HELIX    4   4 ASP A 1131  VAL A 1136  1                                   6    
HELIX    5   5 ASN A 1163  ILE A 1168  5                                   6    
HELIX    6   6 GLY A 1212  GLY A 1220  1                                   9    
HELIX    7   7 ASN B 1024  LEU B 1028  5                                   5    
HELIX    8   8 CYS B 1042  SER B 1048  1                                   7    
HELIX    9   9 VAL B 1088  GLY B 1092  5                                   5    
HELIX   10  10 ASP B 1131  VAL B 1136  1                                   6    
HELIX   11  11 ASN B 1163  ILE B 1168  5                                   6    
HELIX   12  12 GLY B 1212  GLY B 1220  1                                   9    
SHEET    1   A 4 ARG A 977  SER A 980  0                                        
SHEET    2   A 4 CYS A 994  ASN A 996 -1  N  ASN A 996   O  ARG A 977           
SHEET    3   A 4 LEU A1097  THR A1102  1  O  LEU A1099   N  VAL A 995           
SHEET    4   A 4 GLY A1106  SER A1111 -1  O  GLY A1106   N  THR A1102           
SHEET    1   B 2 LYS A1008  TYR A1009  0                                        
SHEET    2   B 2 TYR A1161  GLY A1162  1  O  GLY A1162   N  LYS A1008           
SHEET    1   C 4 CYS A1014  VAL A1015  0                                        
SHEET    2   C 4 GLU A1127  SER A1130  1  O  LEU A1128   N  CYS A1014           
SHEET    3   C 4 TYR A1154  ASP A1157 -1  O  CYS A1155   N  ILE A1129           
SHEET    4   C 4 LEU A1143  LEU A1146 -1  N  LEU A1146   O  TYR A1154           
SHEET    1   D 4 ILE A1071  PHE A1072  0                                        
SHEET    2   D 4 LEU A1176  PHE A1182  1  O  PHE A1182   N  ILE A1071           
SHEET    3   D 4 ARG A1192  SER A1197 -1  O  ARG A1192   N  VAL A1181           
SHEET    4   D 4 PHE A1120  TYR A1124 -1  N  CYS A1122   O  PHE A1195           
SHEET    1   E 4 ILE B 978  SER B 980  0                                        
SHEET    2   E 4 CYS B 994  VAL B 995 -1  O  CYS B 994   N  SER B 980           
SHEET    3   E 4 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    4   E 4 TRP B1107  SER B1111 -1  O  GLY B1108   N  TYR B1100           
SHEET    1   F 4 CYS B1014  VAL B1015  0                                        
SHEET    2   F 4 GLU B1127  SER B1130  1  O  LEU B1128   N  CYS B1014           
SHEET    3   F 4 TYR B1154  ASP B1157 -1  O  CYS B1155   N  ILE B1129           
SHEET    4   F 4 LEU B1143  ASP B1145 -1  N  PHE B1144   O  ILE B1156           
SHEET    1   G 4 LEU B1070  PHE B1072  0                                        
SHEET    2   G 4 LEU B1176  PHE B1182  1  O  PHE B1182   N  ILE B1071           
SHEET    3   G 4 ARG B1192  SER B1197 -1  O  ALA B1194   N  VAL B1179           
SHEET    4   G 4 PHE B1120  GLU B1123 -1  N  CYS B1122   O  PHE B1195           
SHEET    1   H 2 ASN B1169  HIS B1170  0                                        
SHEET    2   H 2 GLY B1208  PHE B1209  1  O  PHE B1209   N  ASN B1169           
LINK         SG  CYS B1037                ZN    ZN B   6     1555   1555  2.23  
LINK         SG  CYS A1225                ZN    ZN A   4     1555   1555  2.26  
LINK         SG  CYS A1037                ZN    ZN A   3     1555   1555  2.26  
LINK         SG  CYS B1044                ZN    ZN B   5     1555   1555  2.33  
LINK         SG  CYS A1080                ZN    ZN A   2     1555   1555  2.33  
LINK         SG  CYS A1084                ZN    ZN A   2     1555   1555  2.33  
LINK         SG  CYS B1031                ZN    ZN B   7     1555   1555  2.34  
LINK         SG  CYS B1074                ZN    ZN B   5     1555   1555  2.35  
LINK         SG  CYS B1225                ZN    ZN B   8     1555   1555  2.36  
LINK         SG  CYS A1031                ZN    ZN A   1     1555   1555  2.37  
LINK         SG  CYS B1037                ZN    ZN B   7     1555   1555  2.37  
LINK         SG  CYS A1074                ZN    ZN A   1     1555   1555  2.38  
LINK         SG  CYS A1033                ZN    ZN A   3     1555   1555  2.38  
LINK         SG  CYS B1074                ZN    ZN B   6     1555   1555  2.39  
LINK         SG  CYS B1227                ZN    ZN B   8     1555   1555  2.39  
LINK         SG  CYS B1080                ZN    ZN B   6     1555   1555  2.39  
LINK         SG  CYS A1074                ZN    ZN A   2     1555   1555  2.40  
LINK         SG  CYS A1078                ZN    ZN A   1     1555   1555  2.43  
LINK         SG  CYS A1172                ZN    ZN A   4     1555   1555  2.48  
LINK         SG  CYS A1044                ZN    ZN A   1     1555   1555  2.49  
LINK         SG  CYS B1084                ZN    ZN B   6     1555   1555  2.49  
LINK         SG  CYS B1042                ZN    ZN B   7     1555   1555  2.49  
LINK         SG  CYS A1042                ZN    ZN A   3     1555   1555  2.49  
LINK         SG  CYS B1031                ZN    ZN B   5     1555   1555  2.53  
LINK         SG  CYS A1031                ZN    ZN A   3     1555   1555  2.56  
LINK         SG  CYS B1033                ZN    ZN B   7     1555   1555  2.56  
LINK         SG  CYS B1078                ZN    ZN B   5     1555   1555  2.57  
LINK         SG  CYS B1232                ZN    ZN B   8     1555   1555  2.60  
LINK         SG  CYS A1232                ZN    ZN A   4     1555   1555  2.61  
LINK         SG  CYS A1227                ZN    ZN A   4     1555   1555  2.63  
LINK         SG  CYS A1037                ZN    ZN A   2     1555   1555  2.65  
LINK         SG  CYS B1172                ZN    ZN B   8     1555   1555  2.79  
SITE     1 AC1  7  ZN A   2   ZN A   3  CYS A1031  CYS A1044                    
SITE     2 AC1  7 CYS A1074  CYS A1078  CYS A1080                               
SITE     1 AC2  5  ZN A   1  CYS A1037  CYS A1074  CYS A1080                    
SITE     2 AC2  5 CYS A1084                                                     
SITE     1 AC3  5  ZN A   1  CYS A1031  CYS A1033  CYS A1037                    
SITE     2 AC3  5 CYS A1042                                                     
SITE     1 AC4  4 CYS A1172  CYS A1225  CYS A1227  CYS A1232                    
SITE     1 AC5  6  ZN B   6  CYS B1031  CYS B1044  CYS B1074                    
SITE     2 AC5  6 CYS B1078  CYS B1080                                          
SITE     1 AC6  6  ZN B   5   ZN B   7  CYS B1037  CYS B1074                    
SITE     2 AC6  6 CYS B1080  CYS B1084                                          
SITE     1 AC7  5  ZN B   6  CYS B1031  CYS B1033  CYS B1037                    
SITE     2 AC7  5 CYS B1042                                                     
SITE     1 AC8  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
SITE     1 AC9 15 MET A1105  TRP A1107  SER A1141  TYR A1142                    
SITE     2 AC9 15 ARG A1166  PHE A1167  ASN A1169  HIS A1170                    
SITE     3 AC9 15 TYR A1211  PHE A1223  SER A1224  CYS A1225                    
SITE     4 AC9 15 ARG A1226  CYS A1227  LYS P  44                               
SITE     1 BC1 15 MET B1105  TRP B1107  SER B1141  TYR B1142                    
SITE     2 BC1 15 ARG B1166  PHE B1167  ASN B1169  HIS B1170                    
SITE     3 BC1 15 TYR B1211  PHE B1215  SER B1224  CYS B1225                    
SITE     4 BC1 15 ARG B1226  CYS B1227  LYS Q  44                               
CRYST1   80.140   91.140   95.070  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      0.012478  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010972  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010519        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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