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Database: PDB
Entry: 5TTG
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Original site: 5TTG 
HEADER    TRANSFERASE                             03-NOV-16   5TTG              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF GLP WITH MS012               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 879-1159;                                     
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1,EU-HMTASE1,
COMPND   6 G9A-LIKE PROTEIN 1,GLP1,HISTONE H3-K9 METHYLTRANSFERASE 5,H3-K9-     
COMPND   7 HMTASE 5,LYSINE N-METHYLTRANSFERASE 1D;                              
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 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: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-LIC                                 
KEYWDS    EHMT1, GLP, MS012, METHYLTRANSFERASE, STRUCTURAL GENOMICS, STRUCTURAL 
KEYWDS   2 GENOMICS CONSORTIUM, SGC, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,J.LIU,Y.XIONG,N.BABAULT,J.JIN,W.TEMPEL,C.BOUNTRA,       
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,H.WU,P.J.BROWN,STRUCTURAL GENOMICS        
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   2   23-MAY-18 5TTG    1       JRNL                                     
REVDAT   1   01-FEB-17 5TTG    0                                                
JRNL        AUTH   Y.XIONG,F.LI,N.BABAULT,A.DONG,H.ZENG,H.WU,X.CHEN,            
JRNL        AUTH 2 C.H.ARROWSMITH,P.J.BROWN,J.LIU,M.VEDADI,J.JIN                
JRNL        TITL   DISCOVERY OF POTENT AND SELECTIVE INHIBITORS FOR G9A-LIKE    
JRNL        TITL 2 PROTEIN (GLP) LYSINE METHYLTRANSFERASE.                      
JRNL        REF    J. MED. CHEM.                 V.  60  1876 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28135087                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01645                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 84739                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1745                            
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) : 1.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.71                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 137                                     
REMARK   3   SOLVENT ATOMS            : 633                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63000                                              
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : 0.11000                                              
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): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.079         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.660         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4621 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4190 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6295 ; 1.448 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9597 ; 1.042 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   580 ; 5.919 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   231 ;31.794 ;22.554       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   741 ;11.390 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;12.638 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   652 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5491 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1179 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2186 ; 1.172 ; 2.007       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2186 ; 1.171 ; 2.007       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2750 ; 1.951 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   2000       A    2000      1                      
REMARK   3           1     B   2000       B    2000      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):     48 ; 0.850 ; 0.500           
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 RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5TTG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224680.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88300                            
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: 3K5K                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 20% IPROP, 0.1 M           
REMARK 280  NACITRATE PH5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.21450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.05650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.05650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.21450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     GLY A   980                                                      
REMARK 465     SER A   981                                                      
REMARK 465     ASN A   982                                                      
REMARK 465     SER A   983                                                      
REMARK 465     GLN A   984                                                      
REMARK 465     VAL A   985                                                      
REMARK 465     TRP A   986                                                      
REMARK 465     SER A   987                                                      
REMARK 465     ALA A   988                                                      
REMARK 465     LEU A   989                                                      
REMARK 465     GLN A   990                                                      
REMARK 465     MET A   991                                                      
REMARK 465     SER A   992                                                      
REMARK 465     LYS A   993                                                      
REMARK 465     ALA A   994                                                      
REMARK 465     LEU A   995                                                      
REMARK 465     GLN A   996                                                      
REMARK 465     ASP A   997                                                      
REMARK 465     SER A   998                                                      
REMARK 465     ALA A   999                                                      
REMARK 465     PRO A  1000                                                      
REMARK 465     ASP A  1001                                                      
REMARK 465     ARG A  1002                                                      
REMARK 465     PRO A  1003                                                      
REMARK 465     SER A  1004                                                      
REMARK 465     PRO A  1005                                                      
REMARK 465     LYS A  1180                                                      
REMARK 465     GLY B   980                                                      
REMARK 465     SER B   981                                                      
REMARK 465     ASN B   982                                                      
REMARK 465     SER B   983                                                      
REMARK 465     GLN B   984                                                      
REMARK 465     VAL B   985                                                      
REMARK 465     TRP B   986                                                      
REMARK 465     SER B   987                                                      
REMARK 465     ALA B   988                                                      
REMARK 465     LEU B   989                                                      
REMARK 465     GLN B   990                                                      
REMARK 465     MET B   991                                                      
REMARK 465     SER B   992                                                      
REMARK 465     LYS B   993                                                      
REMARK 465     ALA B   994                                                      
REMARK 465     LEU B   995                                                      
REMARK 465     GLN B   996                                                      
REMARK 465     ASP B   997                                                      
REMARK 465     SER B   998                                                      
REMARK 465     ALA B   999                                                      
REMARK 465     PRO B  1000                                                      
REMARK 465     ASP B  1001                                                      
REMARK 465     ARG B  1002                                                      
REMARK 465     PRO B  1003                                                      
REMARK 465     SER B  1004                                                      
REMARK 465     PRO B  1005                                                      
REMARK 465     ASN B  1179                                                      
REMARK 465     LYS B  1180                                                      
REMARK 465     ASP B  1181                                                      
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 A1006    CG1  CG2                                            
REMARK 470     ARG A1008    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A1086    CG   CD   CE   NZ                                   
REMARK 470     GLU A1098    CD   OE1  OE2                                       
REMARK 470     ARG A1134    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A1169    CD   OE1  OE2                                       
REMARK 470     ASN A1179    CG   OD1  ND2                                       
REMARK 470     ASP A1181    CG   OD1  OD2                                       
REMARK 470     GLU A1183    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1262    CE   NZ                                             
REMARK 470     VAL B1006    CG1  CG2                                            
REMARK 470     ARG B1020    CZ   NH1  NH2                                       
REMARK 470     GLN B1077    CD   OE1  NE2                                       
REMARK 470     MET B1080    CG   SD   CE                                        
REMARK 470     LYS B1086    CD   CE   NZ                                        
REMARK 470     ARG B1134    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B1166    CG   OD1  OD2                                       
REMARK 470     GLU B1169    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1183    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1252    NZ                                                  
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 A1013      106.32   -165.14                                   
REMARK 500    THR A1047      -85.72   -101.03                                   
REMARK 500    ASN A1051       64.13     34.25                                   
REMARK 500    ASP A1066     -153.35   -112.61                                   
REMARK 500    MET A1080      -53.51     78.14                                   
REMARK 500    MET A1080      -56.39     80.80                                   
REMARK 500    ASN A1117       49.72    -94.23                                   
REMARK 500    VAL A1119      -64.20   -138.59                                   
REMARK 500    ASP A1135       17.27   -143.72                                   
REMARK 500    ASN A1194     -162.83   -107.25                                   
REMARK 500    MET A1214      -91.62   -132.34                                   
REMARK 500    ASP B1013      103.60   -163.77                                   
REMARK 500    SER B1036       15.35   -140.15                                   
REMARK 500    THR B1047      -86.79   -102.78                                   
REMARK 500    ASP B1066     -148.57   -120.91                                   
REMARK 500    MET B1080      -60.32     78.33                                   
REMARK 500    GLU B1098       70.95   -153.12                                   
REMARK 500    GLU B1098       61.50   -155.18                                   
REMARK 500    ASN B1117       48.72    -94.48                                   
REMARK 500    VAL B1119      -60.63   -135.94                                   
REMARK 500    ASP B1135       14.89   -141.15                                   
REMARK 500    ASN B1194     -163.05   -108.93                                   
REMARK 500    MET B1214      -90.54   -132.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     7KZ A 1302                                                       
REMARK 610     7KZ B 1302                                                       
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 A1305  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1064   SG  107.6                                              
REMARK 620 3 CYS A1068   SG  106.0 106.6                                        
REMARK 620 4 CYS A1073   SG  110.5 108.2 117.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1075   SG  115.4                                              
REMARK 620 3 CYS A1105   SG  107.8 111.0                                        
REMARK 620 4 CYS A1109   SG  106.3  97.8 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1068   SG                                                     
REMARK 620 2 CYS A1105   SG  112.9                                              
REMARK 620 3 CYS A1111   SG  104.3 107.1                                        
REMARK 620 4 CYS A1115   SG  112.6 105.3 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1306  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1203   SG                                                     
REMARK 620 2 CYS A1256   SG  113.0                                              
REMARK 620 3 CYS A1258   SG  107.4 108.1                                        
REMARK 620 4 CYS A1263   SG  106.1 106.2 116.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1305  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1064   SG  108.9                                              
REMARK 620 3 CYS B1068   SG  104.7 106.8                                        
REMARK 620 4 CYS B1073   SG  111.3 107.5 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1075   SG  113.1                                              
REMARK 620 3 CYS B1105   SG  107.3 111.9                                        
REMARK 620 4 CYS B1109   SG  107.6  99.1 117.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1068   SG                                                     
REMARK 620 2 CYS B1105   SG  110.9                                              
REMARK 620 3 CYS B1111   SG  105.1 108.6                                        
REMARK 620 4 CYS B1115   SG  111.2 106.7 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1306  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1203   SG                                                     
REMARK 620 2 CYS B1256   SG  116.1                                              
REMARK 620 3 CYS B1258   SG  107.9 104.3                                        
REMARK 620 4 CYS B1263   SG  104.6 106.8 117.7                                  
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 SAM A 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7KZ A 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1308                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7KZ B 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 1307                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TTF   RELATED DB: PDB                                   
DBREF  5TTG A  982  1266  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
DBREF  5TTG B  982  1266  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
SEQADV 5TTG GLY A  980  UNP  Q9H9B1              EXPRESSION TAG                 
SEQADV 5TTG SER A  981  UNP  Q9H9B1              EXPRESSION TAG                 
SEQADV 5TTG GLY B  980  UNP  Q9H9B1              EXPRESSION TAG                 
SEQADV 5TTG SER B  981  UNP  Q9H9B1              EXPRESSION TAG                 
SEQRES   1 A  287  GLY SER ASN SER GLN VAL TRP SER ALA LEU GLN MET SER          
SEQRES   2 A  287  LYS ALA LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO          
SEQRES   3 A  287  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   4 A  287  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   5 A  287  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   6 A  287  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   7 A  287  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   8 A  287  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   9 A  287  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES  10 A  287  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES  11 A  287  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  12 A  287  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  13 A  287  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  14 A  287  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  15 A  287  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  16 A  287  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  17 A  287  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  18 A  287  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  19 A  287  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  20 A  287  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  21 A  287  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  22 A  287  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  23 A  287  SER                                                          
SEQRES   1 B  287  GLY SER ASN SER GLN VAL TRP SER ALA LEU GLN MET SER          
SEQRES   2 B  287  LYS ALA LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO          
SEQRES   3 B  287  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   4 B  287  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   5 B  287  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   6 B  287  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   7 B  287  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   8 B  287  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   9 B  287  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES  10 B  287  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES  11 B  287  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  12 B  287  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  13 B  287  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  14 B  287  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  15 B  287  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  16 B  287  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  17 B  287  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  18 B  287  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  19 B  287  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  20 B  287  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  21 B  287  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  22 B  287  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  23 B  287  SER                                                          
HET    SAM  A1301      27                                                       
HET    7KZ  A1302      25                                                       
HET     ZN  A1303       1                                                       
HET     ZN  A1304       1                                                       
HET     ZN  A1305       1                                                       
HET     ZN  A1306       1                                                       
HET     CL  A1307       1                                                       
HET    GOL  A1308       6                                                       
HET    UNX  A1309       1                                                       
HET    UNX  A1310       1                                                       
HET    UNX  A1311       1                                                       
HET    UNX  A1312       1                                                       
HET    UNX  A1313       1                                                       
HET    UNX  A1314       1                                                       
HET    SAM  B1301      27                                                       
HET    7KZ  B1302      24                                                       
HET     ZN  B1303       1                                                       
HET     ZN  B1304       1                                                       
HET     ZN  B1305       1                                                       
HET     ZN  B1306       1                                                       
HET    DMS  B1307       4                                                       
HET    UNX  B1308       1                                                       
HET    UNX  B1309       1                                                       
HET    UNX  B1310       1                                                       
HET    UNX  B1311       1                                                       
HET    UNX  B1312       1                                                       
HET    UNX  B1313       1                                                       
HET    UNX  B1314       1                                                       
HET    UNX  B1315       1                                                       
HET    UNX  B1316       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     7KZ N4-(1-METHYLPIPERIDIN-4-YL)-N2-HEXYL-6,7-                        
HETNAM   2 7KZ  DIMETHOXYQUINAZOLINE-2,4-DIAMINE                                
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     7KZ N~2~-HEXYL-6,7-DIMETHOXY-N~4~-(1-METHYLPIPERIDIN-4-YL)           
HETSYN   2 7KZ  QUINAZOLINE-2,4-DIAMINE                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   4  7KZ    2(C22 H35 N5 O2)                                             
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   9   CL    CL 1-                                                        
FORMUL  10  GOL    C3 H8 O3                                                     
FORMUL  11  UNX    15(X)                                                        
FORMUL  23  DMS    C2 H6 O S                                                    
FORMUL  33  HOH   *633(H2 O)                                                    
HELIX    1 AA1 ASN A 1055  LEU A 1059  5                                   5    
HELIX    2 AA2 CYS A 1073  SER A 1079  1                                   7    
HELIX    3 AA3 VAL A 1119  GLY A 1123  5                                   5    
HELIX    4 AA4 ASP A 1162  ASP A 1166  1                                   5    
HELIX    5 AA5 VAL A 1195  ILE A 1199  5                                   5    
HELIX    6 AA6 GLY A 1243  GLY A 1251  1                                   9    
HELIX    7 AA7 ASN B 1055  LEU B 1059  5                                   5    
HELIX    8 AA8 CYS B 1073  SER B 1079  1                                   7    
HELIX    9 AA9 VAL B 1119  GLY B 1123  5                                   5    
HELIX   10 AB1 ASP B 1162  ASP B 1166  1                                   5    
HELIX   11 AB2 VAL B 1195  ILE B 1199  5                                   5    
HELIX   12 AB3 GLY B 1243  GLY B 1251  1                                   9    
SHEET    1 AA1 4 ARG A1008  SER A1011  0                                        
SHEET    2 AA1 4 CYS A1025  ASN A1027 -1  O  CYS A1025   N  SER A1011           
SHEET    3 AA1 4 LEU A1128  ARG A1132  1  O  LEU A1130   N  VAL A1026           
SHEET    4 AA1 4 TRP A1138  SER A1142 -1  O  GLY A1139   N  TYR A1131           
SHEET    1 AA2 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA2 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA2 3 GLY A1157  SER A1161 -1  N  GLU A1158   O  ASP A1188           
SHEET    1 AA3 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA3 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA3 3 LEU A1174  ASP A1176 -1  N  PHE A1175   O  ILE A1187           
SHEET    1 AA4 4 ILE A1102  PHE A1103  0                                        
SHEET    2 AA4 4 LEU A1207  PHE A1213  1  O  PHE A1213   N  ILE A1102           
SHEET    3 AA4 4 ARG A1223  SER A1228 -1  O  ALA A1225   N  VAL A1210           
SHEET    4 AA4 4 PHE A1151  TYR A1155 -1  N  CYS A1153   O  PHE A1226           
SHEET    1 AA5 2 ASN A1200  HIS A1201  0                                        
SHEET    2 AA5 2 GLY A1239  PHE A1240  1  O  PHE A1240   N  ASN A1200           
SHEET    1 AA6 4 ARG B1008  SER B1011  0                                        
SHEET    2 AA6 4 CYS B1025  ASN B1027 -1  O  CYS B1025   N  SER B1011           
SHEET    3 AA6 4 LEU B1128  ARG B1132  1  O  LEU B1130   N  VAL B1026           
SHEET    4 AA6 4 TRP B1138  SER B1142 -1  O  GLY B1139   N  TYR B1131           
SHEET    1 AA7 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA7 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA7 3 GLY B1157  SER B1161 -1  N  GLU B1158   O  ASP B1188           
SHEET    1 AA8 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA8 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA8 3 LEU B1174  ASP B1176 -1  N  PHE B1175   O  ILE B1187           
SHEET    1 AA9 4 ILE B1102  PHE B1103  0                                        
SHEET    2 AA9 4 LEU B1207  PHE B1213  1  O  PHE B1213   N  ILE B1102           
SHEET    3 AA9 4 ARG B1223  SER B1228 -1  O  ALA B1225   N  VAL B1210           
SHEET    4 AA9 4 PHE B1151  TYR B1155 -1  N  VAL B1152   O  PHE B1226           
SHEET    1 AB1 2 ASN B1200  HIS B1201  0                                        
SHEET    2 AB1 2 GLY B1239  PHE B1240  1  O  PHE B1240   N  ASN B1200           
LINK         SG  CYS A1062                ZN    ZN A1305     1555   1555  2.35  
LINK         SG  CYS A1062                ZN    ZN A1303     1555   1555  2.40  
LINK         SG  CYS A1064                ZN    ZN A1305     1555   1555  2.33  
LINK         SG  CYS A1068                ZN    ZN A1304     1555   1555  2.33  
LINK         SG  CYS A1068                ZN    ZN A1305     1555   1555  2.34  
LINK         SG  CYS A1073                ZN    ZN A1305     1555   1555  2.30  
LINK         SG  CYS A1075                ZN    ZN A1303     1555   1555  2.35  
LINK         SG  CYS A1105                ZN    ZN A1304     1555   1555  2.33  
LINK         SG  CYS A1105                ZN    ZN A1303     1555   1555  2.36  
LINK         SG  CYS A1109                ZN    ZN A1303     1555   1555  2.34  
LINK         SG  CYS A1111                ZN    ZN A1304     1555   1555  2.29  
LINK         SG  CYS A1115                ZN    ZN A1304     1555   1555  2.33  
LINK         SG  CYS A1203                ZN    ZN A1306     1555   1555  2.37  
LINK         SG  CYS A1256                ZN    ZN A1306     1555   1555  2.31  
LINK         SG  CYS A1258                ZN    ZN A1306     1555   1555  2.32  
LINK         SG  CYS A1263                ZN    ZN A1306     1555   1555  2.32  
LINK         SG  CYS B1062                ZN    ZN B1305     1555   1555  2.38  
LINK         SG  CYS B1062                ZN    ZN B1303     1555   1555  2.36  
LINK         SG  CYS B1064                ZN    ZN B1305     1555   1555  2.29  
LINK         SG  CYS B1068                ZN    ZN B1305     1555   1555  2.34  
LINK         SG  CYS B1068                ZN    ZN B1304     1555   1555  2.32  
LINK         SG  CYS B1073                ZN    ZN B1305     1555   1555  2.30  
LINK         SG  CYS B1075                ZN    ZN B1303     1555   1555  2.33  
LINK         SG  CYS B1105                ZN    ZN B1303     1555   1555  2.32  
LINK         SG  CYS B1105                ZN    ZN B1304     1555   1555  2.37  
LINK         SG  CYS B1109                ZN    ZN B1303     1555   1555  2.35  
LINK         SG  CYS B1111                ZN    ZN B1304     1555   1555  2.29  
LINK         SG  CYS B1115                ZN    ZN B1304     1555   1555  2.30  
LINK         SG  CYS B1203                ZN    ZN B1306     1555   1555  2.39  
LINK         SG  CYS B1256                ZN    ZN B1306     1555   1555  2.30  
LINK         SG  CYS B1258                ZN    ZN B1306     1555   1555  2.32  
LINK         SG  CYS B1263                ZN    ZN B1306     1555   1555  2.30  
SITE     1 AC1 20 MET A1136  GLY A1137  TRP A1138  SER A1172                    
SITE     2 AC1 20 TYR A1173  ARG A1197  PHE A1198  ASN A1200                    
SITE     3 AC1 20 HIS A1201  TYR A1242  PHE A1246  CYS A1256                    
SITE     4 AC1 20 ARG A1257  HOH A1443  HOH A1492  HOH A1522                    
SITE     5 AC1 20 HOH A1532  HOH A1535  HOH A1608  HOH A1621                    
SITE     1 AC2 11 ALA A1165  ASP A1166  ARG A1168  ASP A1171                    
SITE     2 AC2 11 LEU A1174  ASP A1176  CYS A1186  ARG A1245                    
SITE     3 AC2 11 PHE A1246  ILE A1249  LYS A1250                               
SITE     1 AC3  4 CYS A1062  CYS A1075  CYS A1105  CYS A1109                    
SITE     1 AC4  4 CYS A1068  CYS A1105  CYS A1111  CYS A1115                    
SITE     1 AC5  4 CYS A1062  CYS A1064  CYS A1068  CYS A1073                    
SITE     1 AC6  4 CYS A1203  CYS A1256  CYS A1258  CYS A1263                    
SITE     1 AC7  5 VAL A1119  ASN A1122  ARG A1125  LYS B1262                    
SITE     2 AC7  5 HOH B1435                                                     
SITE     1 AC8  7 ASN A1044  LEU A1159  LEU A1177  HIS A1216                    
SITE     2 AC8  7 PHE A1221  PRO A1222  ARG A1223                               
SITE     1 AC9 18 MET B1136  GLY B1137  TRP B1138  SER B1172                    
SITE     2 AC9 18 TYR B1173  ARG B1197  PHE B1198  ASN B1200                    
SITE     3 AC9 18 HIS B1201  TYR B1242  PHE B1246  CYS B1256                    
SITE     4 AC9 18 ARG B1257  HOH B1420  HOH B1442  HOH B1492                    
SITE     5 AC9 18 HOH B1536  HOH B1591                                          
SITE     1 AD1 11 ALA B1165  ASP B1166  ARG B1168  ASP B1171                    
SITE     2 AD1 11 LEU B1174  ASP B1176  CYS B1186  ARG B1245                    
SITE     3 AD1 11 PHE B1246  ILE B1249  LYS B1250                               
SITE     1 AD2  4 CYS B1062  CYS B1075  CYS B1105  CYS B1109                    
SITE     1 AD3  4 CYS B1068  CYS B1105  CYS B1111  CYS B1115                    
SITE     1 AD4  4 CYS B1062  CYS B1064  CYS B1068  CYS B1073                    
SITE     1 AD5  4 CYS B1203  CYS B1256  CYS B1258  CYS B1263                    
SITE     1 AD6  5 LEU A1078  CYS B1064  ILE B1065  ASP B1066                    
SITE     2 AD6  5 SER B1070                                                     
CRYST1   74.429   95.900  102.113  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      0.013436  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010428  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009793        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.312620 -0.626279 -0.714174      -36.37682    1                    
MTRIX2   2 -0.638671 -0.695124  0.330004      -26.65601    1                    
MTRIX3   2 -0.703113  0.352956 -0.617295      -43.60168    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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