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Database: PDB
Entry: 2RFI
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HEADER    TRANSFERASE                             30-SEP-07   2RFI              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN EUCHROMATIC            
TITLE    2 HISTONE METHYLTRANSFERASE 1 IN COMPLEX WITH SAH AND                  
TITLE    3 DIMETHYLATED H3K9 PEPTIDE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9            
COMPND   3 SPECIFIC 5;                                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: CATALYTIC DOMAIN: RESIDUES 951-1235;                       
COMPND   6 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 5, H3-K9-HMTASE 5,          
COMPND   7 EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-                
COMPND   8 HMTASE1, G9A-LIKE PROTEIN 1, GLP1;                                   
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: HISTONE H3;                                                
COMPND  13 CHAIN: P, Q;                                                         
COMPND  14 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, KIAA1876;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-THROMBIN-LIC;                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC DIMETHYLATED H3K9 PEPTIDE                   
KEYWDS    EUCHROMATIC HISTONE METHYLTRANSFERASE 1, STRUCTURAL                   
KEYWDS   2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, ALTERNATIVE           
KEYWDS   3 SPLICING, ANK REPEAT, CHROMATIN REGULATOR, NUCLEUS,                  
KEYWDS   4 PHOSPHORYLATION, POLYMORPHISM, S-ADENOSYL-L-METHIONINE,              
KEYWDS   5 ACETYLATION, CHROMOSOMAL PROTEIN, DNA DAMAGE, DNA REPAIR,            
KEYWDS   6 DNA-BINDING, METHYLATION, NUCLEOSOME CORE, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MIN,H.WU,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,            
AUTHOR   2 A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,STRUCTURAL GENOMICS            
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   3   02-MAR-10 2RFI    1       JRNL                                     
REVDAT   2   24-FEB-09 2RFI    1       VERSN                                    
REVDAT   1   23-OCT-07 2RFI    0                                                
JRNL        AUTH   H.WU,J.MIN,V.V.LUNIN,T.ANTOSHENKO,L.DOMBROVSKI,              
JRNL        AUTH 2 H.ZENG,A.ALLALI-HASSANI,V.CAMPAGNA-SLATER,M.VEDADI,          
JRNL        AUTH 3 C.H.ARROWSMITH,A.N.PLOTNIKOV,M.SCHAPIRA                      
JRNL        TITL   STRUCTURAL BIOLOGY OF HUMAN H3K9 METHYLTRANSFERASES          
JRNL        REF    PLOS ONE                      V.   5 E8570 2010              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   20084102                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0008570                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 85102                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4475                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4267                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 228                          
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4322                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 686                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.708         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4481 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6065 ; 1.171 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   534 ; 5.662 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   235 ;30.280 ;22.511       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   733 ;12.132 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;15.861 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   629 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3514 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2064 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3105 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   582 ; 0.111 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    26 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.098 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2772 ; 0.763 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4345 ; 1.272 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1974 ; 1.773 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1720 ; 2.740 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2RFI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044795.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89676                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2IGQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 10% ISOPROPANOL, 0.1M      
REMARK 280  BICINE PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K      
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       42.29650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.83500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.81350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.83500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.29650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.81350            
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: 1560 ANGSTROM**2                          
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: 1360 ANGSTROM**2                          
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: 5780 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, 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     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     VAL B   975                                                      
REMARK 465     GLU B   976                                                      
REMARK 465     ARG B   977                                                      
REMARK 465     ASP B  1147                                                      
REMARK 465     ASN B  1148                                                      
REMARK 465     LYS B  1149                                                      
REMARK 465     ASP B  1150                                                      
REMARK 465     GLY B  1151                                                      
REMARK 465     GLU B  1152                                                      
REMARK 465     THR P     1                                                      
REMARK 465     GLY P    10                                                      
REMARK 465     GLY P    11                                                      
REMARK 465     THR Q     1                                                      
REMARK 465     LYS Q     2                                                      
REMARK 465     GLN Q     3                                                      
REMARK 465     GLY Q    10                                                      
REMARK 465     GLY Q    11                                                      
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     SER B1235    OG                                                  
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      107.83   -169.42                                   
REMARK 500    THR A1016      -88.02   -101.63                                   
REMARK 500    ASP A1035     -148.01   -117.56                                   
REMARK 500    MET A1049      -60.09     80.50                                   
REMARK 500    ASN A1086       47.77    -92.31                                   
REMARK 500    VAL A1088      -60.52   -141.04                                   
REMARK 500    ASP A1104       14.87   -140.83                                   
REMARK 500    ASN A1163     -163.46   -113.91                                   
REMARK 500    MET A1183      -91.18   -130.44                                   
REMARK 500    ASP B 982      107.01   -166.44                                   
REMARK 500    ASP B 999     -157.21   -142.99                                   
REMARK 500    SER B1005       12.20   -142.96                                   
REMARK 500    THR B1016      -84.89   -102.14                                   
REMARK 500    ASP B1035     -155.30   -118.01                                   
REMARK 500    MET B1049      -56.08     81.63                                   
REMARK 500    ASN B1086       46.31    -94.29                                   
REMARK 500    VAL B1088      -62.07   -136.90                                   
REMARK 500    ASN B1163     -164.15   -116.62                                   
REMARK 500    MET B1183      -89.19   -131.74                                   
REMARK 500    HIS B1234       36.73   -141.79                                   
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 A1609        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1610        DISTANCE =  6.83 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 A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1044   SG  114.0                                              
REMARK 620 3 CYS A1074   SG  109.3 112.3                                        
REMARK 620 4 CYS A1078   SG  104.2  99.1 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1033   SG  108.6                                              
REMARK 620 3 CYS A1037   SG  104.0 107.8                                        
REMARK 620 4 CYS A1042   SG  112.1 108.1 115.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1037   SG                                                     
REMARK 620 2 CYS A1074   SG  112.6                                              
REMARK 620 3 CYS A1080   SG  104.6 109.0                                        
REMARK 620 4 CYS A1084   SG  112.0 103.8 115.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1172   SG                                                     
REMARK 620 2 CYS A1225   SG  114.3                                              
REMARK 620 3 CYS A1227   SG  108.1 105.2                                        
REMARK 620 4 CYS A1232   SG  106.7 107.3 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1031   SG                                                     
REMARK 620 2 CYS B1044   SG  115.4                                              
REMARK 620 3 CYS B1074   SG  109.2 109.2                                        
REMARK 620 4 CYS B1078   SG  105.4  99.1 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1031   SG                                                     
REMARK 620 2 CYS B1033   SG  108.3                                              
REMARK 620 3 CYS B1037   SG  106.8 108.0                                        
REMARK 620 4 CYS B1042   SG  110.3 106.4 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1037   SG                                                     
REMARK 620 2 CYS B1074   SG  111.2                                              
REMARK 620 3 CYS B1080   SG  105.7 107.8                                        
REMARK 620 4 CYS B1084   SG  111.9 105.8 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1172   SG                                                     
REMARK 620 2 CYS B1225   SG  112.5                                              
REMARK 620 3 CYS B1227   SG  117.3 105.8                                        
REMARK 620 4 CYS B1232   SG   91.3 105.4 123.9                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IGQ   RELATED DB: PDB                                   
REMARK 900 HUMAN EUCHROMATIC HISTONE METHYLTRANSFERASE 1                        
DBREF  2RFI A  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  2RFI B  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  2RFI P    1    11  PDB    2RFI     2RFI             1     11             
DBREF  2RFI Q    1    11  PDB    2RFI     2RFI             1     11             
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 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 P   11  THR LYS GLN THR ALA ARG MLY SER THR GLY GLY                  
SEQRES   1 Q   11  THR LYS GLN THR ALA ARG MLY SER THR GLY GLY                  
MODRES 2RFI MLY P    7  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2RFI MLY Q    7  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  P   7      11                                                       
HET    MLY  Q   7      11                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET     ZN  B 504       1                                                       
HET    SAH  A 101      26                                                       
HET    SAH  A 102      26                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3  MLY    2(C8 H18 N2 O2)                                              
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL  13  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  14  HOH   *686(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  ASP A 1135  1                                   5    
HELIX    5   5 VAL A 1164  ILE A 1168  5                                   5    
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  ARG B 1137  1                                   7    
HELIX   11  11 VAL B 1164  ILE B 1168  5                                   5    
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  O  ASN A 996   N  ARG A 977           
SHEET    3   A 4 LEU A1097  ARG A1101  1  O  LEU A1099   N  VAL A 995           
SHEET    4   A 4 TRP A1107  SER A1111 -1  O  GLY A1108   N  TYR A1100           
SHEET    1   B 3 LYS A1008  TYR A1009  0                                        
SHEET    2   B 3 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   B 3 GLY A1126  SER A1130 -1  N  ILE A1129   O  CYS A1155           
SHEET    1   C 3 LYS A1008  TYR A1009  0                                        
SHEET    2   C 3 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   C 3 LEU A1143  ASP A1145 -1  N  PHE A1144   O  ILE A1156           
SHEET    1   D 4 ILE A1071  PHE A1072  0                                        
SHEET    2   D 4 LEU A1176  PHE A1182  1  O  ARG A1180   N  ILE A1071           
SHEET    3   D 4 ARG A1192  SER A1197 -1  O  ALA A1194   N  VAL A1179           
SHEET    4   D 4 PHE A1120  TYR A1124 -1  N  CYS A1122   O  PHE A1195           
SHEET    1   E 2 ASN A1169  HIS A1170  0                                        
SHEET    2   E 2 GLY A1208  PHE A1209  1  O  PHE A1209   N  ASN A1169           
SHEET    1   F 3 CYS B 994  VAL B 995  0                                        
SHEET    2   F 3 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    3   F 3 TRP B1107  SER B1111 -1  O  GLY B1108   N  TYR B1100           
SHEET    1   G 3 LYS B1008  TYR B1009  0                                        
SHEET    2   G 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   G 3 GLY B1126  SER B1130 -1  N  GLU B1127   O  ASP B1157           
SHEET    1   H 3 LYS B1008  TYR B1009  0                                        
SHEET    2   H 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   H 3 LEU B1143  ASP B1145 -1  N  PHE B1144   O  ILE B1156           
SHEET    1   I 4 ILE B1071  PHE B1072  0                                        
SHEET    2   I 4 LEU B1176  PHE B1182  1  O  PHE B1182   N  ILE B1071           
SHEET    3   I 4 ARG B1192  SER B1197 -1  O  ALA B1194   N  VAL B1179           
SHEET    4   I 4 PHE B1120  TYR B1124 -1  N  CYS B1122   O  PHE B1195           
SHEET    1   J 2 ASN B1169  HIS B1170  0                                        
SHEET    2   J 2 GLY B1208  PHE B1209  1  O  PHE B1209   N  ASN B1169           
LINK         SG  CYS A1031                ZN    ZN A 501     1555   1555  2.38  
LINK         SG  CYS A1031                ZN    ZN A 503     1555   1555  2.44  
LINK         SG  CYS A1033                ZN    ZN A 503     1555   1555  2.29  
LINK         SG  CYS A1037                ZN    ZN A 502     1555   1555  2.28  
LINK         SG  CYS A1037                ZN    ZN A 503     1555   1555  2.39  
LINK         SG  CYS A1042                ZN    ZN A 503     1555   1555  2.36  
LINK         SG  CYS A1044                ZN    ZN A 501     1555   1555  2.33  
LINK         SG  CYS A1074                ZN    ZN A 501     1555   1555  2.42  
LINK         SG  CYS A1074                ZN    ZN A 502     1555   1555  2.40  
LINK         SG  CYS A1078                ZN    ZN A 501     1555   1555  2.39  
LINK         SG  CYS A1080                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A1084                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A1172                ZN    ZN A 504     1555   1555  2.46  
LINK         SG  CYS A1225                ZN    ZN A 504     1555   1555  2.37  
LINK         SG  CYS A1227                ZN    ZN A 504     1555   1555  2.34  
LINK         SG  CYS A1232                ZN    ZN A 504     1555   1555  2.38  
LINK         SG  CYS B1031                ZN    ZN B 501     1555   1555  2.42  
LINK         SG  CYS B1031                ZN    ZN B 503     1555   1555  2.37  
LINK         SG  CYS B1033                ZN    ZN B 503     1555   1555  2.33  
LINK         SG  CYS B1037                ZN    ZN B 503     1555   1555  2.36  
LINK         SG  CYS B1037                ZN    ZN B 502     1555   1555  2.34  
LINK         SG  CYS B1042                ZN    ZN B 503     1555   1555  2.33  
LINK         SG  CYS B1044                ZN    ZN B 501     1555   1555  2.34  
LINK         SG  CYS B1074                ZN    ZN B 501     1555   1555  2.39  
LINK         SG  CYS B1074                ZN    ZN B 502     1555   1555  2.42  
LINK         SG  CYS B1078                ZN    ZN B 501     1555   1555  2.34  
LINK         SG  CYS B1080                ZN    ZN B 502     1555   1555  2.32  
LINK         SG  CYS B1084                ZN    ZN B 502     1555   1555  2.31  
LINK         SG  CYS B1172                ZN    ZN B 504     1555   1555  2.48  
LINK         SG  CYS B1225                ZN    ZN B 504     1555   1555  2.41  
LINK         SG  CYS B1227                ZN    ZN B 504     1555   1555  2.00  
LINK         SG  CYS B1232                ZN    ZN B 504     1555   1555  2.76  
LINK         C   ARG P   6                 N   MLY P   7     1555   1555  1.52  
LINK         C   MLY P   7                 N   SER P   8     1555   1555  1.55  
LINK         C   ARG Q   6                 N   MLY Q   7     1555   1555  1.33  
LINK         C   MLY Q   7                 N   SER Q   8     1555   1555  1.33  
SITE     1 AC1  4 CYS A1031  CYS A1044  CYS A1074  CYS A1078                    
SITE     1 AC2  4 CYS A1037  CYS A1074  CYS A1080  CYS A1084                    
SITE     1 AC3  4 CYS A1031  CYS A1033  CYS A1037  CYS A1042                    
SITE     1 AC4  4 CYS A1172  CYS A1225  CYS A1227  CYS A1232                    
SITE     1 AC5  4 CYS B1031  CYS B1044  CYS B1074  CYS B1078                    
SITE     1 AC6  4 CYS B1037  CYS B1074  CYS B1080  CYS B1084                    
SITE     1 AC7  4 CYS B1031  CYS B1033  CYS B1037  CYS B1042                    
SITE     1 AC8  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
SITE     1 AC9 21 MET A1105  TRP A1107  SER A1141  TYR A1142                    
SITE     2 AC9 21 ARG A1166  PHE A1167  ASN A1169  HIS A1170                    
SITE     3 AC9 21 TYR A1211  PHE A1215  PHE A1223  CYS A1225                    
SITE     4 AC9 21 ARG A1226  HOH A1322  HOH A1357  HOH A1390                    
SITE     5 AC9 21 HOH A1446  HOH A1460  HOH A1462  HOH A1472                    
SITE     6 AC9 21 MLY P   7                                                     
SITE     1 BC1 11 HOH A1517  MET B1105  TRP B1107  ARG B1166                    
SITE     2 BC1 11 ASN B1169  HIS B1170  TYR B1211  PHE B1223                    
SITE     3 BC1 11 SER B1224  CYS B1225  ARG B1226                               
CRYST1   84.593   85.627   95.670  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      0.011821  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011679  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010453        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system