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Database: PDB
Entry: 2R3A
LinkDB: 2R3A
Original site: 2R3A 
HEADER    TRANSFERASE                             29-AUG-07   2R3A              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN SUPPRESSOR OF VARIEGATION           
TITLE    2 3-9 HOMOLOG 2                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H2;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: METHYLTRANSFERASE DOMAIN: RESIDUES 112-410;                
COMPND   5 SYNONYM: SUPPRESSOR OF VARIEGATION 3-9 HOMOLOG 2, SU(VAR)3-          
COMPND   6 9 HOMOLOG 2, HISTONE H3-K9 METHYLTRANSFERASE 2, H3-K9-               
COMPND   7 HMTASE 2;                                                            
COMPND   8 EC: 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: SUV39H2;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P15MHL                                    
KEYWDS    HISTONE H3-K9 METHYLTRANSFERASE 2, HISTONE-LYSINE N-                  
KEYWDS   2 METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 2, ALTERNATIVE               
KEYWDS   3 SPLICING, CELL CYCLE, CHROMATIN REGULATOR, CHROMOSOMAL               
KEYWDS   4 PROTEIN, DIFFERENTIATION, NUCLEUS, REPRESSOR, S-ADENOSYL-L-          
KEYWDS   5 METHIONINE, TELOMERE, TRANSCRIPTION, TRANSCRIPTION                   
KEYWDS   6 REGULATION, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS                 
KEYWDS   7 CONSORTIUM, SGC, TRANSFERASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.V.LUNIN,H.WU,H.ZENG,H.REN,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,          
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,J.MIN,          
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   02-MAR-10 2R3A    1       JRNL                                     
REVDAT   2   24-FEB-09 2R3A    1       VERSN                                    
REVDAT   1   11-SEP-07 2R3A    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21763                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1182                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1478                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2153                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 254                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39000                                              
REMARK   3    B22 (A**2) : -1.75000                                             
REMARK   3    B33 (A**2) : 1.63000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.41000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.147         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.647         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2235 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3024 ; 1.551 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   271 ; 6.371 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;38.523 ;23.945       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   372 ;14.017 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.600 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   325 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1718 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1009 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1537 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   202 ; 0.146 ; 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):    42 ; 0.167 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.119 ; 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):  1400 ; 0.966 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2193 ; 1.585 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   965 ; 2.591 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   830 ; 3.833 ; 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   : 1.40                                          
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 2R3A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044370.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22956                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1MHV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 10000, 0.1 M HEPES PH 7.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.96250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     GLU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     ASP A   268                                                      
REMARK 465     ILE A   269                                                      
REMARK 465     SER A   270                                                      
REMARK 465     SER A   271                                                      
REMARK 465     ASP A   272                                                      
REMARK 465     SER A   273                                                      
REMARK 465     ILE A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     HIS A   276                                                      
REMARK 465     SER A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     ALA A   279                                                      
REMARK 465     LYS A   280                                                      
REMARK 465     LYS A   281                                                      
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     ARG A  36    NE   CZ   NH1  NH2                                  
REMARK 470     THR A  77    OG1  CG2                                            
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     ARG A 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 227    NE2                                                 
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    CYS A  90     -169.70   -127.72                                   
REMARK 500    ASN A 213     -155.87   -111.31                                   
REMARK 500    ILE A 233      -91.52   -115.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  49        23.2      L          L   OUTSIDE RANGE           
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 A 470        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 476        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH A 518        DISTANCE =  5.51 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 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 222   SG                                                     
REMARK 620 2 CYS A 289   SG  106.7                                              
REMARK 620 3 CYS A 294   SG  113.2 111.4                                        
REMARK 620 4 CYS A 287   SG  110.0 110.0 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  82   SG                                                     
REMARK 620 2 CYS A  80   SG  107.6                                              
REMARK 620 3 CYS A  85   SG  110.0 103.9                                        
REMARK 620 4 CYS A  90   SG  115.7 111.4 107.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  91   SG                                                     
REMARK 620 2 CYS A 122   SG   92.2                                              
REMARK 620 3 CYS A 118   SG  121.1 114.6                                        
REMARK 620 4 CYS A  80   SG  119.8 102.2 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  85   SG                                                     
REMARK 620 2 CYS A 128   SG  105.6                                              
REMARK 620 3 CYS A 118   SG  110.8 106.0                                        
REMARK 620 4 CYS A 124   SG  115.1 111.0 107.9                                  
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 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 305                 
DBREF  2R3A A    1   299  UNP    Q9H5I1   SUV92_HUMAN    112    410             
SEQADV 2R3A GLY A    0  UNP  Q9H5I1              EXPRESSION TAG                 
SEQRES   1 A  300  GLY PRO LYS ASP ASN ASN LYS THR LEU LYS PRO ALA ILE          
SEQRES   2 A  300  ALA GLU TYR ILE VAL LYS LYS ALA LYS GLN ARG ILE ALA          
SEQRES   3 A  300  LEU GLN ARG TRP GLN ASP GLU LEU ASN ARG ARG LYS ASN          
SEQRES   4 A  300  HIS LYS GLY MET ILE PHE VAL GLU ASN THR VAL ASP LEU          
SEQRES   5 A  300  GLU GLY PRO PRO SER ASP PHE TYR TYR ILE ASN GLU TYR          
SEQRES   6 A  300  LYS PRO ALA PRO GLY ILE SER LEU VAL ASN GLU ALA THR          
SEQRES   7 A  300  PHE GLY CYS SER CYS THR ASP CYS PHE PHE GLN LYS CYS          
SEQRES   8 A  300  CYS PRO ALA GLU ALA GLY VAL LEU LEU ALA TYR ASN LYS          
SEQRES   9 A  300  ASN GLN GLN ILE LYS ILE PRO PRO GLY THR PRO ILE TYR          
SEQRES  10 A  300  GLU CYS ASN SER ARG CYS GLN CYS GLY PRO ASP CYS PRO          
SEQRES  11 A  300  ASN ARG ILE VAL GLN LYS GLY THR GLN TYR SER LEU CYS          
SEQRES  12 A  300  ILE PHE ARG THR SER ASN GLY ARG GLY TRP GLY VAL LYS          
SEQRES  13 A  300  THR LEU VAL LYS ILE LYS ARG MET SER PHE VAL MET GLU          
SEQRES  14 A  300  TYR VAL GLY GLU VAL ILE THR SER GLU GLU ALA GLU ARG          
SEQRES  15 A  300  ARG GLY GLN PHE TYR ASP ASN LYS GLY ILE THR TYR LEU          
SEQRES  16 A  300  PHE ASP LEU ASP TYR GLU SER ASP GLU PHE THR VAL ASP          
SEQRES  17 A  300  ALA ALA ARG TYR GLY ASN VAL SER HIS PHE VAL ASN HIS          
SEQRES  18 A  300  SER CYS ASP PRO ASN LEU GLN VAL PHE ASN VAL PHE ILE          
SEQRES  19 A  300  ASP ASN LEU ASP THR ARG LEU PRO ARG ILE ALA LEU PHE          
SEQRES  20 A  300  SER THR ARG THR ILE ASN ALA GLY GLU GLU LEU THR PHE          
SEQRES  21 A  300  ASP TYR GLN MET LYS GLY SER GLY ASP ILE SER SER ASP          
SEQRES  22 A  300  SER ILE ASP HIS SER PRO ALA LYS LYS ARG VAL ARG THR          
SEQRES  23 A  300  VAL CYS LYS CYS GLY ALA VAL THR CYS ARG GLY TYR LEU          
SEQRES  24 A  300  ASN                                                          
HET     ZN  A 300       1                                                       
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET    SAM  A 304      27                                                       
HET    SER  A 305       7                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     SER SERINE                                                           
FORMUL   2   ZN    4(ZN 2+)                                                     
FORMUL   6  SAM    C15 H22 N6 O5 S                                              
FORMUL   7  SER    C3 H7 N O3                                                   
FORMUL   8  HOH   *254(H2 O)                                                    
HELIX    1   1 ALA A   13  LYS A   37  1                                  25    
HELIX    2   2 CYS A   90  ALA A   95  1                                   6    
HELIX    3   3 ILE A  132  GLY A  136  5                                   5    
HELIX    4   4 SER A  176  PHE A  185  1                                  10    
HELIX    5   5 ASP A  187  TYR A  193  1                                   7    
HELIX    6   6 ASN A  213  VAL A  218  5                                   6    
HELIX    7   7 ASP A  260  LYS A  264  5                                   5    
SHEET    1   A 5 ILE A  43  GLU A  46  0                                        
SHEET    2   A 5 LEU A 141  ARG A 145  1  O  ILE A 143   N  PHE A  44           
SHEET    3   A 5 TRP A 152  THR A 156 -1  O  LYS A 155   N  CYS A 142           
SHEET    4   A 5 GLU A 256  PHE A 259 -1  O  LEU A 257   N  VAL A 154           
SHEET    5   A 5 ASN A 219  HIS A 220  1  N  ASN A 219   O  PHE A 259           
SHEET    1   B 2 TYR A  59  TYR A  60  0                                        
SHEET    2   B 2 TYR A 211  GLY A 212  1  O  GLY A 212   N  TYR A  59           
SHEET    1   C 4 LYS A  65  PRO A  66  0                                        
SHEET    2   C 4 GLU A 172  THR A 175  1  O  VAL A 173   N  LYS A  65           
SHEET    3   C 4 PHE A 204  ASP A 207 -1  O  THR A 205   N  ILE A 174           
SHEET    4   C 4 LEU A 194  ASP A 196 -1  N  PHE A 195   O  VAL A 206           
SHEET    1   D 4 ILE A 115  TYR A 116  0                                        
SHEET    2   D 4 LEU A 226  PHE A 232  1  O  ASN A 230   N  ILE A 115           
SHEET    3   D 4 ARG A 242  SER A 247 -1  O  ARG A 242   N  VAL A 231           
SHEET    4   D 4 PHE A 165  TYR A 169 -1  N  MET A 167   O  LEU A 245           
LINK        ZN    ZN A 300                 SG  CYS A 222     1555   1555  2.40  
LINK        ZN    ZN A 300                 SG  CYS A 289     1555   1555  2.31  
LINK        ZN    ZN A 300                 SG  CYS A 294     1555   1555  2.40  
LINK        ZN    ZN A 300                 SG  CYS A 287     1555   1555  2.34  
LINK        ZN    ZN A 301                 SG  CYS A  82     1555   1555  2.40  
LINK        ZN    ZN A 301                 SG  CYS A  80     1555   1555  2.39  
LINK        ZN    ZN A 301                 SG  CYS A  85     1555   1555  2.25  
LINK        ZN    ZN A 301                 SG  CYS A  90     1555   1555  2.42  
LINK        ZN    ZN A 302                 SG  CYS A  91     1555   1555  2.28  
LINK        ZN    ZN A 302                 SG  CYS A 122     1555   1555  2.35  
LINK        ZN    ZN A 302                 SG  CYS A 118     1555   1555  2.44  
LINK        ZN    ZN A 302                 SG  CYS A  80     1555   1555  2.41  
LINK        ZN    ZN A 303                 SG  CYS A  85     1555   1555  2.36  
LINK        ZN    ZN A 303                 SG  CYS A 128     1555   1555  2.39  
LINK        ZN    ZN A 303                 SG  CYS A 118     1555   1555  2.36  
LINK        ZN    ZN A 303                 SG  CYS A 124     1555   1555  2.28  
SITE     1 AC1  4 CYS A 222  CYS A 287  CYS A 289  CYS A 294                    
SITE     1 AC2  4 CYS A  80  CYS A  82  CYS A  85  CYS A  90                    
SITE     1 AC3  4 CYS A  80  CYS A  91  CYS A 118  CYS A 122                    
SITE     1 AC4  4 CYS A  85  CYS A 118  CYS A 124  CYS A 128                    
SITE     1 AC5 22 ARG A 150  GLY A 151  TRP A 152  LYS A 189                    
SITE     2 AC5 22 THR A 192  TYR A 193  HIS A 216  PHE A 217                    
SITE     3 AC5 22 VAL A 218  ASN A 219  HIS A 220  TYR A 261                    
SITE     4 AC5 22 VAL A 286  CYS A 287  LYS A 288  CYS A 289                    
SITE     5 AC5 22 LEU A 298  HOH A 324  HOH A 415  HOH A 486                    
SITE     6 AC5 22 HOH A 488  HOH A 490                                          
SITE     1 AC6  7 THR A  83  ASP A  84  CYS A  85  GLY A 125                    
SITE     2 AC6  7 CYS A 128  HOH A 554  HOH A 557                               
CRYST1   45.748   63.925   64.529  90.00 109.33  90.00 P 1 21 1      2          
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      0.021859  0.000000  0.007669        0.00000                         
SCALE2      0.000000  0.015643  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016423        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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