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Database: PDB
Entry: 1N6C
LinkDB: 1N6C
Original site: 1N6C 
HEADER    TRANSFERASE                             09-NOV-02   1N6C              
TITLE     STRUCTURE OF SET7/9                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET DOMAIN-CONTAINING PROTEIN 7;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 70-366;                                           
COMPND   5 SYNONYM: SET7/9 METHYLTRANSFERASE;                                   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21[DE3];                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    PROTEIN-LIGAND COMPLEX, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.W.KWON,J.H.CHANG,Y.CHO                                              
REVDAT   3   23-APR-14 1N6C    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 1N6C    1       VERSN                                    
REVDAT   1   04-FEB-03 1N6C    0                                                
JRNL        AUTH   T.KWON,J.H.CHANG,E.KWAK,C.W.LEE,A.JOACHIMIAK,Y.C.KIM,J.LEE,  
JRNL        AUTH 2 Y.CHO                                                        
JRNL        TITL   MECHANISM OF HISTONE LYSINE METHYL TRANSFER REVEALED BY THE  
JRNL        TITL 2 STRUCTURE OF SET7/9-ADOMET                                   
JRNL        REF    EMBO J.                       V.  22   292 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12514135                                                     
JRNL        DOI    10.1093/EMBOJ/CDG025                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 165555.550                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20165                          
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 SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1179                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2217                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 133                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2207                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52000                                             
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 1.04000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.700                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.970                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.370 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.330 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.130 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.240 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 39.14                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : FSAM.PARAM                                     
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : FSAM.TOP                                       
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017573.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6B                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, LITHIUM SULFATE,       
REMARK 280  SODIUM CITRATE, DTT, PH 5.8, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.23450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.72700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.72700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.61725            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.72700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.72700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       82.85175            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.72700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.72700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       27.61725            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.72700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.72700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       82.85175            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       55.23450            
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 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    70                                                      
REMARK 465     GLN A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     TYR A    74                                                      
REMARK 465     THR A    75                                                      
REMARK 465     TYR A    76                                                      
REMARK 465     GLU A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     ASP A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     GLN A   364                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A   279     ND2  ASN A   282              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 152      -48.66   -134.25                                   
REMARK 500    ASP A 194       57.87   -143.88                                   
REMARK 500    THR A 197     -167.26   -122.74                                   
REMARK 500    GLU A 279      -81.24    -12.44                                   
REMARK 500    ALA A 362       62.35     60.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N6A   RELATED DB: PDB                                   
REMARK 900 RESIDUES 108-366 OF THE SAME PROTEIN                                 
DBREF  1N6C A   70   366  UNP    Q8WTS6   SET7_HUMAN      70    366             
SEQRES   1 A  297  GLY GLN GLY VAL TYR THR TYR GLU ASP GLY GLY VAL LEU          
SEQRES   2 A  297  GLN GLY THR TYR VAL ASP GLY GLU LEU ASN GLY PRO ALA          
SEQRES   3 A  297  GLN GLU TYR ASP THR ASP GLY ARG LEU ILE PHE LYS GLY          
SEQRES   4 A  297  GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE          
SEQRES   5 A  297  TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN          
SEQRES   6 A  297  GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL          
SEQRES   7 A  297  TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE          
SEQRES   8 A  297  ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET          
SEQRES   9 A  297  SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO          
SEQRES  10 A  297  GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER          
SEQRES  11 A  297  CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU          
SEQRES  12 A  297  SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER          
SEQRES  13 A  297  ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO          
SEQRES  14 A  297  ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR          
SEQRES  15 A  297  HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY          
SEQRES  16 A  297  ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL          
SEQRES  17 A  297  PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER          
SEQRES  18 A  297  LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS          
SEQRES  19 A  297  ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE          
SEQRES  20 A  297  LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU          
SEQRES  21 A  297  GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO          
SEQRES  22 A  297  GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL          
SEQRES  23 A  297  GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS                  
HET    SAM  A 402      27                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  HOH   *130(H2 O)                                                    
HELIX    1   1 ASP A  209  ARG A  215  1                                   7    
HELIX    2   2 THR A  251  ARG A  258  1                                   8    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 PRO A  278  HIS A  283  5                                   6    
HELIX    5   5 LEU A  291  ALA A  295  5                                   5    
HELIX    6   6 PRO A  350  GLN A  361  1                                  12    
SHEET    1   A13 LEU A  82  GLN A  83  0                                        
SHEET    2   A13 GLU A  90  TYR A  98 -1  O  GLN A  96   N  GLN A  83           
SHEET    3   A13 TYR A  86  VAL A  87 -1  N  VAL A  87   O  GLU A  90           
SHEET    4   A13 GLU A  90  TYR A  98 -1  O  GLU A  90   N  VAL A  87           
SHEET    5   A13 LEU A 104  LYS A 111 -1  N  ILE A 105   O  GLU A  97           
SHEET    6   A13 ILE A 114  TYR A 122 -1  O  ILE A 114   N  LYS A 111           
SHEET    7   A13 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    8   A13 GLY A 141  VAL A 147 -1  O  ALA A 145   N  VAL A 130           
SHEET    9   A13 THR A 153  ILE A 160 -1  N  LEU A 155   O  TYR A 146           
SHEET   10   A13 GLU A 163  GLU A 176 -1  O  GLU A 163   N  ILE A 160           
SHEET   11   A13 VAL A 190  TYR A 191 -1  N  TYR A 191   O  GLY A 167           
SHEET   12   A13 GLU A 163  GLU A 176 -1  O  GLY A 167   N  TYR A 191           
SHEET   13   A13 ARG A 179  LEU A 184 -1  O  ARG A 179   N  GLU A 176           
SHEET    1   B 4 VAL A 216  GLU A 220  0                                        
SHEET    2   B 4 GLU A 228  SER A 232 -1  N  GLY A 229   O  ALA A 219           
SHEET    3   B 4 GLU A 330  VAL A 333 -1  N  LEU A 331   O  LEU A 230           
SHEET    4   B 4 ASN A 296  HIS A 297  1  O  ASN A 296   N  VAL A 333           
SHEET    1   C 3 VAL A 241  TYR A 245  0                                        
SHEET    2   C 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3   C 3 CYS A 303  HIS A 310 -1  N  ILE A 304   O  ARG A 320           
SHEET    1   D 3 VAL A 248  ILE A 250  0                                        
SHEET    2   D 3 VAL A 274  ASP A 276 -1  N  VAL A 274   O  ILE A 250           
SHEET    3   D 3 LEU A 267  SER A 268 -1  O  LEU A 267   N  ILE A 275           
SITE     1 AC1 14 ALA A 226  GLU A 228  GLY A 264  ASN A 265                    
SITE     2 AC1 14 HIS A 293  LYS A 294  ALA A 295  ASN A 296                    
SITE     3 AC1 14 HIS A 297  TYR A 335  TRP A 352  GLU A 356                    
SITE     4 AC1 14 HOH A1021  HOH A1049                                          
CRYST1   93.454   93.454  110.469  90.00  90.00  90.00 P 41 21 2     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      0.010700  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010700  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009052        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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