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Database: PDB
Entry: 3VUZ
LinkDB: 3VUZ
Original site: 3VUZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-JUL-12   3VUZ              
TITLE     CRYSTAL STRUCTURE OF HISTONE METHYLTRANSFERASE SET7/9 IN COMPLEX WITH 
TITLE    2 AAM-1                                                                
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,       
COMPND   7 SET7/9;                                                              
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: 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, TRANSFERASE, ADENOSYLMETHIONINE BINDING, TRANSFERASE-     
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.NIWA,N.HANDA,Y.TOMABECHI,K.HONDA,M.TOYAMA,N.OHSAWA,M.SHIROUZU,      
AUTHOR   2 H.KAGECHIKA,T.HIRANO,T.UMEHARA,S.YOKOYAMA                            
REVDAT   3   28-SEP-16 3VUZ    1       TITLE                                    
REVDAT   2   30-APR-14 3VUZ    1       JRNL                                     
REVDAT   1   27-MAR-13 3VUZ    0                                                
JRNL        AUTH   H.NIWA,N.HANDA,Y.TOMABECHI,K.HONDA,M.TOYAMA,N.OHSAWA,        
JRNL        AUTH 2 M.SHIROUZU,H.KAGECHIKA,T.HIRANO,T.UMEHARA,S.YOKOYAMA         
JRNL        TITL   STRUCTURES OF HISTONE METHYLTRANSFERASE SET7/9 IN COMPLEXES  
JRNL        TITL 2 WITH ADENOSYLMETHIONINE DERIVATIVES                          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69   595 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   23519668                                                     
JRNL        DOI    10.1107/S0907444912052092                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 9781                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.730                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 560                             
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 28.1915 -  3.9658    1.00     2421   142  0.1590 0.2065        
REMARK   3     2  3.9658 -  3.1491    1.00     2310   136  0.1781 0.2496        
REMARK   3     3  3.1491 -  2.7514    1.00     2266   137  0.2155 0.2912        
REMARK   3     4  2.7514 -  2.5000    1.00     2224   145  0.2711 0.3658        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 44.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.04                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.25140                                              
REMARK   3    B22 (A**2) : -8.25790                                             
REMARK   3    B33 (A**2) : 6.00660                                              
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      :  0.007           2005                                  
REMARK   3   ANGLE     :  1.111           2725                                  
REMARK   3   CHIRALITY :  0.070            290                                  
REMARK   3   PLANARITY :  0.004            354                                  
REMARK   3   DIHEDRAL  : 16.554            724                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:162)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2225   7.3409 -13.0894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3177 T22:   0.3986                                     
REMARK   3      T33:   0.6642 T12:   0.0437                                     
REMARK   3      T13:   0.0258 T23:  -0.0751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6957 L22:   0.2364                                     
REMARK   3      L33:   0.3430 L12:   0.0795                                     
REMARK   3      L13:  -0.7398 L23:  -0.2376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0984 S12:  -0.4210 S13:   0.6795                       
REMARK   3      S21:   0.1633 S22:   0.0794 S23:  -0.5422                       
REMARK   3      S31:  -0.1249 S32:   0.1670 S33:  -0.1534                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 163:362)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6592   3.4259 -18.3267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2332 T22:   0.1610                                     
REMARK   3      T33:   0.1133 T12:  -0.0188                                     
REMARK   3      T13:  -0.0151 T23:   0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0946 L22:   3.7415                                     
REMARK   3      L33:   2.1704 L12:  -0.9721                                     
REMARK   3      L13:  -0.0130 L23:  -0.2406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2430 S12:  -0.0702 S13:   0.1260                       
REMARK   3      S21:  -0.5384 S22:  -0.1798 S23:   0.4180                       
REMARK   3      S31:   0.1828 S32:  -0.2746 S33:  -0.0343                       
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 3VUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095532.                                      
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                             : 8.3-8.5                            
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9883                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.62500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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   (%): 46.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH8.3-8.5, 28-30% PEG      
REMARK 280  6000, 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       50.90350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.61150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.90350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       19.61150            
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     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     SER A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     THR A   363                                                      
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: 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    SER A   6     -149.66   -124.76                                   
REMARK 500    ARG A 152      -40.30   -135.33                                   
REMARK 500    THR A 197     -162.50   -123.07                                   
REMARK 500    ASP A 270     -160.87   -163.10                                   
REMARK 500    PHE A 360      -34.16   -153.23                                   
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 K15 A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VV0   RELATED DB: PDB                                   
DBREF  3VUZ A  111   366  UNP    Q8WTS6   SETD7_HUMAN    111    366             
SEQADV 3VUZ GLY A    1  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ SER A    2  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ SER A    3  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ GLY A    4  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ SER A    5  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ SER A    6  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3VUZ GLY A    7  UNP  Q8WTS6              EXPRESSION TAG                 
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 TYR          
SEQRES  19 A  263  ASP HIS SER PRO PRO GLY LYS SER GLY PRO GLU ALA 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    K15  A 401      32                                                       
HETNAM     K15 5'-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5'-              
HETNAM   2 K15  DEOXYADENOSINE                                                  
FORMUL   2  K15    C20 H33 N7 O5                                                
FORMUL   3  HOH   *69(H2 O)                                                     
HELIX    1   1 ASP A  209  ARG A  215  1                                   7    
HELIX    2   2 THR A  251  SER A  257  1                                   7    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
HELIX    5   5 PRO A  350  ALA A  359  1                                  10    
SHEET    1   A 6 VAL A 118  TYR A 122  0                                        
SHEET    2   A 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   A 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   A 6 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    5   A 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   A 6 ARG A 179  LEU A 184 -1  O  GLU A 183   N  THR A 171           
SHEET    1   B 6 VAL A 118  TYR A 122  0                                        
SHEET    2   B 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   B 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   B 6 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    5   B 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   B 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1   C 4 VAL A 216  GLU A 220  0                                        
SHEET    2   C 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3   C 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4   C 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1   D 3 VAL A 241  TYR A 245  0                                        
SHEET    2   D 3 GLY A 314  THR A 321 -1  O  ILE A 319   N  MET A 242           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  HIS A 310   O  GLY A 314           
SHEET    1   E 3 VAL A 248  ILE A 250  0                                        
SHEET    2   E 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   E 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
CISPEP   1 GLU A  279    PRO A  280          0         0.15                     
SITE     1 AC1 19 GLY A   4  ILE A 223  SER A 225  ALA A 226                    
SITE     2 AC1 19 GLU A 228  TYR A 245  GLY A 264  ASN A 265                    
SITE     3 AC1 19 THR A 266  ASN A 282  HIS A 293  LYS A 294                    
SITE     4 AC1 19 ASN A 296  HIS A 297  TYR A 305  TYR A 335                    
SITE     5 AC1 19 TYR A 337  TRP A 352  HOH A 523                               
CRYST1  101.807   39.223   67.045  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      0.009823  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025495  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014915        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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