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Database: PDB
Entry: 5AYF
LinkDB: 5AYF
Original site: 5AYF 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       20-AUG-15   5AYF              
TITLE     CRYSTAL STRUCTURE OF SET7/9 IN COMPLEX WITH CYPROHEPTADINE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 111-366;                                      
COMPND   5 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE SETD7,H3-K4-HMTASE SETD7,   
COMPND   6 LYSINE N-METHYLTRANSFERASE 7,SET DOMAIN-CONTAINING PROTEIN 7,SET7/9; 
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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: SETD7, KIAA1717, KMT7, SET7, SET9;                             
SOURCE   6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS;                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PX100709-08                               
KEYWDS    SET DOMAIN, METHYLTRANSFERASE, INHIBITOR, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.NIWA,N.HANDA,Y.TAKEMOTO,A.ITO,Y.TOMABECHI,T.UMEHARA,M.SHIROUZU,     
AUTHOR   2 M.YOSHIDA,S.YOKOYAMA                                                 
REVDAT   2   18-MAY-16 5AYF    1       JRNL                                     
REVDAT   1   27-APR-16 5AYF    0                                                
JRNL        AUTH   Y.TAKEMOTO,A.ITO,H.NIWA,M.OKAMURA,T.FUJIWARA,T.HIRANO,       
JRNL        AUTH 2 N.HANDA,T.UMEHARA,T.SONODA,K.OGAWA,M.TARIQ,N.NISHINO,S.DAN,  
JRNL        AUTH 3 H.KAGECHIKA,T.YAMORI,S.YOKOYAMA,M.YOSHIDA                    
JRNL        TITL   IDENTIFICATION OF CYPROHEPTADINE AS AN INHIBITOR OF SET      
JRNL        TITL 2 DOMAIN CONTAINING LYSINE METHYLTRANSFERASE 7/9 (SET7/9) THAT 
JRNL        TITL 3 REGULATES ESTROGEN-DEPENDENT TRANSCRIPTION                   
JRNL        REF    J.MED.CHEM.                   V.  59  3650 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27088648                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01732                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.62                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18856                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1119                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 25.6178 -  4.0063    1.00     2382   137  0.1874 0.2175        
REMARK   3     2  4.0063 -  3.1818    1.00     2273   137  0.1755 0.2466        
REMARK   3     3  3.1818 -  2.7802    1.00     2223   130  0.2033 0.2939        
REMARK   3     4  2.7802 -  2.5262    1.00     2193   150  0.2157 0.2815        
REMARK   3     5  2.5262 -  2.3453    1.00     2192   134  0.2030 0.3213        
REMARK   3     6  2.3453 -  2.2071    1.00     2204   135  0.2056 0.2706        
REMARK   3     7  2.2071 -  2.0966    1.00     2169   151  0.2027 0.2745        
REMARK   3     8  2.0966 -  2.0054    0.97     2101   145  0.2037 0.2551        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 39.29                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.45940                                             
REMARK   3    B22 (A**2) : 2.47720                                              
REMARK   3    B33 (A**2) : -2.01780                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           2007                                  
REMARK   3   ANGLE     :  1.085           2728                                  
REMARK   3   CHIRALITY :  0.075            289                                  
REMARK   3   PLANARITY :  0.005            352                                  
REMARK   3   DIHEDRAL  : 15.555            727                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5AYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1300000193.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18892                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
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: 1N6A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 31% PEG 6000,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.23150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.68300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.23150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       19.68300            
REMARK 290   SMTRY3   4  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 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   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     SER A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     SER A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     UNK A   337                                                      
REMARK 465     UNK A   338                                                      
REMARK 465     UNK A   345                                                      
REMARK 465     UNK A   346                                                      
REMARK 465     UNK A   347                                                      
REMARK 465     UNK A   348                                                      
REMARK 465     UNK A   349                                                      
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      -51.31   -147.06                                   
REMARK 500    ASP A 194       53.92   -146.83                                   
REMARK 500    THR A 197     -166.60   -124.33                                   
REMARK 500    SER A 202      149.85   -174.48                                   
REMARK 500    TYR A 245       77.73   -106.35                                   
REMARK 500    CYS A 288       17.58   -142.42                                   
REMARK 500    UNK A 343     -150.60    123.45                                   
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C7H A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 403                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE ELECTRON DENSITY OF RESIDUES A337-A349 IS WEAK. SIX RESIDUES     
REMARK 999 WERE PLACED BUT THEIR RESIDUE NUMBERS A339-A344 ARE NOT CONCLUSIVE   
REMARK 999 AND LABELED UNK. REAL SEQUENCE FOR RESIDUES A337-A349 SHOULD BE      
REMARK 999 YDHSPPGKSGPEA.                                                       
DBREF  5AYF A  111   366  UNP    Q8WTS6   SETD7_HUMAN    111    366             
SEQADV 5AYF GLY A  104  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF SER A  105  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF SER A  106  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF GLY A  107  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF SER A  108  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF SER A  109  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF GLY A  110  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5AYF UNK A  337  UNP  Q8WTS6    TYR   337 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  338  UNP  Q8WTS6    ASP   338 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  339  UNP  Q8WTS6    HIS   339 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  340  UNP  Q8WTS6    SER   340 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  341  UNP  Q8WTS6    PRO   341 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  342  UNP  Q8WTS6    PRO   342 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  343  UNP  Q8WTS6    GLY   343 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  344  UNP  Q8WTS6    LYS   344 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  345  UNP  Q8WTS6    SER   345 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  346  UNP  Q8WTS6    GLY   346 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  347  UNP  Q8WTS6    PRO   347 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  348  UNP  Q8WTS6    GLU   348 SEE SEQUENCE DETAILS           
SEQADV 5AYF UNK A  349  UNP  Q8WTS6    ALA   349 SEE SEQUENCE DETAILS           
SEQRES   1 A  263  GLY SER SER GLY SER SER GLY LYS ASP ASN ILE ARG HIS          
SEQRES   2 A  263  GLY VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU          
SEQRES   3 A  263  VAL GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU          
SEQRES   4 A  263  LYS ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU          
SEQRES   5 A  263  TYR GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS          
SEQRES   6 A  263  LEU ALA THR LEU MET SER THR GLU GLU GLY ARG PRO HIS          
SEQRES   7 A  263  PHE GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP          
SEQRES   8 A  263  LYS SER THR SER SER CYS ILE SER THR ASN ALA LEU LEU          
SEQRES   9 A  263  PRO ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU          
SEQRES  10 A  263  SER LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS          
SEQRES  11 A  263  VAL ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN          
SEQRES  12 A  263  GLY VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP          
SEQRES  13 A  263  TRP ALA LEU ASN GLY ASN THR LEU SER LEU ASP GLU GLU          
SEQRES  14 A  263  THR VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER          
SEQRES  15 A  263  LYS TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER          
SEQRES  16 A  263  PHE THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS PRO          
SEQRES  17 A  263  ARG PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA          
SEQRES  18 A  263  VAL GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY UNK          
SEQRES  19 A  263  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK PRO          
SEQRES  20 A  263  GLU TRP TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA THR          
SEQRES  21 A  263  GLN GLN LYS                                                  
HET    SAM  A 401      27                                                       
HET    C7H  A 402      22                                                       
HET    TRS  A 403       8                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     C7H 4-(DIBENZO[1,2-A:2',1'-D][7]ANNULEN-11-YLIDENE)-1-               
HETNAM   2 C7H  METHYL-PIPERIDINE                                               
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     C7H CYPROHEPTADINE                                                   
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  C7H    C21 H21 N                                                    
FORMUL   4  TRS    C4 H12 N O3 1+                                               
FORMUL   5  HOH   *179(H2 O)                                                    
HELIX    1 AA1 ASP A  209  GLU A  214  1                                   6    
HELIX    2 AA2 THR A  251  SER A  257  1                                   7    
HELIX    3 AA3 ASP A  259  ASN A  263  5                                   5    
HELIX    4 AA4 LEU A  291  ALA A  295  5                                   5    
HELIX    5 AA5 GLU A  351  THR A  363  1                                  13    
SHEET    1 AA1 6 VAL A 118  TYR A 122  0                                        
SHEET    2 AA1 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3 AA1 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4 AA1 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5 AA1 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6 AA1 6 ARG A 179  LEU A 184 -1  O  HIS A 181   N  SER A 174           
SHEET    1 AA2 6 VAL A 118  TYR A 122  0                                        
SHEET    2 AA2 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3 AA2 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4 AA2 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5 AA2 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6 AA2 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1 AA3 4 VAL A 216  GLU A 220  0                                        
SHEET    2 AA3 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3 AA3 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4 AA3 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1 AA4 3 VAL A 241  TYR A 245  0                                        
SHEET    2 AA4 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3 AA4 3 CYS A 303  HIS A 310 -1  N  ILE A 304   O  ARG A 320           
SHEET    1 AA5 3 VAL A 248  ILE A 250  0                                        
SHEET    2 AA5 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3 AA5 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
LINK         C   UNK A 339                 N   UNK A 340     1555   1555  1.33  
LINK         C   UNK A 340                 N   UNK A 341     1555   1555  1.34  
LINK         C   UNK A 341                 N   UNK A 342     1555   1555  1.33  
LINK         C   UNK A 342                 N   UNK A 343     1555   1555  1.33  
LINK         C   UNK A 343                 N   UNK A 344     1555   1555  1.33  
CISPEP   1 GLU A  279    PRO A  280          0         2.87                     
SITE     1 AC1 17 ILE A 223  ALA A 226  GLU A 228  GLY A 264                    
SITE     2 AC1 17 ASN A 265  HIS A 293  LYS A 294  ALA A 295                    
SITE     3 AC1 17 ASN A 296  HIS A 297  TYR A 335  TRP A 352                    
SITE     4 AC1 17 HOH A 534  HOH A 579  HOH A 581  HOH A 588                    
SITE     5 AC1 17 HOH A 626                                                     
SITE     1 AC2  6 TYR A 245  ASN A 263  GLY A 264  THR A 266                    
SITE     2 AC2  6 TYR A 305  TYR A 335                                          
SITE     1 AC3 10 GLY A 237  PRO A 238  THR A 240  ALA A 362                    
SITE     2 AC3 10 THR A 363  GLN A 365  HOH A 523  HOH A 533                    
SITE     3 AC3 10 HOH A 604  HOH A 609                                          
CRYST1  102.463   39.366   67.275  90.00  90.00  90.00 P 21 21 2     4          
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      0.009760  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014864        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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