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Database: PDB
Entry: 3QXY
LinkDB: 3QXY
Original site: 3QXY 
HEADER    TRANSFERASE                             02-MAR-11   3QXY              
TITLE     HUMAN SETD6 IN COMPLEX WITH RELA LYS310                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SETD6;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SET DOMAIN-CONTAINING PROTEIN 6;                            
COMPND   5 EC: 2.1.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION FACTOR P65;                                  
COMPND   9 CHAIN: P, Q;                                                         
COMPND  10 FRAGMENT: UNP Q04206 RESIDUES 302-316;                               
COMPND  11 SYNONYM: NUCLEAR FACTOR NF-KAPPA-B P65 SUBUNIT, NUCLEAR FACTOR OF    
COMPND  12 KAPPA LIGHT POLYPEPTIDE GENE ENHANCER IN B-CELLS 3;                  
COMPND  13 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: SETD6;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PXC862;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  15 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).           
KEYWDS    EPIGENETICS, PROTEIN LYSINE METHYLTRANSFERASE, TRANSFERASE, NF-KB     
KEYWDS   2 NETWORK VIA METHYLLYSINE SIGNALING                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHANG,D.LEVY,J.R.HORTON,J.PENG,X.ZHANG,O.GOZANI,X.CHENG             
REVDAT   3   07-SEP-11 3QXY    1       JRNL                                     
REVDAT   2   10-AUG-11 3QXY    1       JRNL   VERSN                             
REVDAT   1   25-MAY-11 3QXY    0                                                
JRNL        AUTH   Y.CHANG,D.LEVY,J.R.HORTON,J.PENG,X.ZHANG,O.GOZANI,X.CHENG    
JRNL        TITL   STRUCTURAL BASIS OF SETD6-MEDIATED REGULATION OF THE NF-KB   
JRNL        TITL 2 NETWORK VIA METHYL-LYSINE SIGNALING.                         
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  6380 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21515635                                                     
JRNL        DOI    10.1093/NAR/GKR256                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 107141                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.620                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3881                            
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 34.6679 -  4.5086    0.99    10853   420  0.1719 0.2178        
REMARK   3     2  4.5086 -  3.5798    0.99    10759   421  0.1480 0.2199        
REMARK   3     3  3.5798 -  3.1276    0.98    10745   418  0.1689 0.2093        
REMARK   3     4  3.1276 -  2.8418    0.97    10597   407  0.1909 0.2552        
REMARK   3     5  2.8418 -  2.6382    0.96    10518   388  0.1862 0.2542        
REMARK   3     6  2.6382 -  2.4827    0.95    10373   350  0.1779 0.2566        
REMARK   3     7  2.4827 -  2.3584    0.93    10244   353  0.1719 0.2225        
REMARK   3     8  2.3584 -  2.2557    0.92    10011   400  0.1525 0.2110        
REMARK   3     9  2.2557 -  2.1689    0.90     9798   364  0.1592 0.2116        
REMARK   3    10  2.1689 -  2.0941    0.86     9362   360  0.1672 0.2221        
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              : 0.33                                          
REMARK   3   B_SOL              : 34.92                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.80130                                             
REMARK   3    B22 (A**2) : 1.05960                                              
REMARK   3    B33 (A**2) : 5.74170                                              
REMARK   3    B12 (A**2) : 1.69780                                              
REMARK   3    B13 (A**2) : -2.57150                                             
REMARK   3    B23 (A**2) : -2.75500                                             
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      :  0.006           6843                                  
REMARK   3   ANGLE     :  1.053           9284                                  
REMARK   3   CHIRALITY :  0.069           1062                                  
REMARK   3   PLANARITY :  0.005           1175                                  
REMARK   3   DIHEDRAL  : 14.072           2507                                  
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 3QXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064243.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110964                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.12700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SGXPRO                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (W/V) POLYETHYLENE GLYCOL (PEG)      
REMARK 280  3350, 0.1 M DI-AMMONIUM HYDROGEN CITRATE, PH 4.6, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 18.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q                                  
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     ASP A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     GLY A   391                                                      
REMARK 465     ASP A   392                                                      
REMARK 465     ASP A   393                                                      
REMARK 465     ARG P   302                                                      
REMARK 465     LYS P   303                                                      
REMARK 465     ARG P   304                                                      
REMARK 465     THR P   305                                                      
REMARK 465     TYR P   306                                                      
REMARK 465     GLU P   307                                                      
REMARK 465     THR P   308                                                      
REMARK 465     PHE P   309                                                      
REMARK 465     SER P   311                                                      
REMARK 465     ILE P   312                                                      
REMARK 465     MET P   313                                                      
REMARK 465     LYS P   314                                                      
REMARK 465     LYS P   315                                                      
REMARK 465     SER P   316                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     ASP B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     ASP B   234                                                      
REMARK 465     GLU B   235                                                      
REMARK 465     LYS B   236                                                      
REMARK 465     GLU B   237                                                      
REMARK 465     ASP B   388                                                      
REMARK 465     GLY B   389                                                      
REMARK 465     GLY B   390                                                      
REMARK 465     GLY B   391                                                      
REMARK 465     ASP B   392                                                      
REMARK 465     ASP B   393                                                      
REMARK 465     LYS B   394                                                      
REMARK 465     ARG B   395                                                      
REMARK 465     GLU B   396                                                      
REMARK 465     GLU B   397                                                      
REMARK 465     GLY B   398                                                      
REMARK 465     ARG Q   302                                                      
REMARK 465     LYS Q   303                                                      
REMARK 465     ARG Q   304                                                      
REMARK 465     THR Q   305                                                      
REMARK 465     TYR Q   306                                                      
REMARK 465     GLU Q   307                                                      
REMARK 465     THR Q   308                                                      
REMARK 465     PHE Q   309                                                      
REMARK 465     SER Q   311                                                      
REMARK 465     ILE Q   312                                                      
REMARK 465     MET Q   313                                                      
REMARK 465     LYS Q   314                                                      
REMARK 465     LYS Q   315                                                      
REMARK 465     SER Q   316                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  19    CG   CD1  CD2                                       
REMARK 470     ASP A  20    CG   OD1  OD2                                       
REMARK 470     GLN A  69    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 162    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 236    CG   CD   CE   NZ                                   
REMARK 470     GLU A 237    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 327    CG   CD   CE   NZ                                   
REMARK 470     GLU A 329    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 337    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 379    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 380    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 382    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 383    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 384    CG   CD1  CD2                                       
REMARK 470     LYS A 385    CG   CD   CE   NZ                                   
REMARK 470     ASP A 386    CG   OD1  OD2                                       
REMARK 470     GLN A 387    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 394    CG   CD   CE   NZ                                   
REMARK 470     ARG A 395    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  19    CG   CD1  CD2                                       
REMARK 470     ASP B  20    CG   OD1  OD2                                       
REMARK 470     GLN B  69    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 185    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 327    CG   CD   CE   NZ                                   
REMARK 470     GLU B 329    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 344    CG   CD   CE   NZ                                   
REMARK 470     GLU B 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 360    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 379    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 382    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 383    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 385    CG   CD   CE   NZ                                   
REMARK 470     ASP B 386    CG   OD1  OD2                                       
REMARK 470     GLN B 387    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  73      131.11   -170.11                                   
REMARK 500    ILE A 191      -58.99   -127.12                                   
REMARK 500    ALA A 246      -54.96     77.50                                   
REMARK 500    ASP A 386      -72.44   -106.60                                   
REMARK 500    ALA B  73      130.15   -170.58                                   
REMARK 500    ILE B 191      -57.85   -130.93                                   
REMARK 500    GLU B 230      -71.55   -104.58                                   
REMARK 500    ALA B 246      -53.90     77.59                                   
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 6734                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 6735                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 479                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS SEQUENCE CORRESPONDS TO ISOFORM 2 OF HUMAN SETD6 (NP_079136)    
DBREF  3QXY A    1   473  UNP    Q8TBK2   SETD6_HUMAN      1    449             
DBREF  3QXY P  302   316  UNP    Q04206   TF65_HUMAN     302    316             
DBREF  3QXY B    1   473  UNP    Q8TBK2   SETD6_HUMAN      1    449             
DBREF  3QXY Q  302   316  UNP    Q04206   TF65_HUMAN     302    316             
SEQRES   1 A  449  MET ALA THR GLN ALA LYS ARG PRO ARG VAL ALA GLY PRO          
SEQRES   2 A  449  VAL ASP GLY GLY ASP LEU ASP PRO VAL ALA CYS PHE LEU          
SEQRES   3 A  449  SER TRP CYS ARG ARG VAL GLY LEU GLU LEU SER PRO LYS          
SEQRES   4 A  449  VAL ALA VAL SER ARG GLN GLY THR VAL ALA GLY TYR GLY          
SEQRES   5 A  449  MET VAL ALA ARG GLU SER VAL GLN ALA GLY GLU LEU LEU          
SEQRES   6 A  449  PHE VAL VAL PRO ARG ALA ALA LEU LEU SER GLN HIS THR          
SEQRES   7 A  449  CYS SER ILE GLY GLY LEU LEU GLU ARG GLU ARG VAL ALA          
SEQRES   8 A  449  LEU GLN SER GLN SER GLY TRP VAL PRO LEU LEU LEU ALA          
SEQRES   9 A  449  LEU LEU HIS GLU LEU GLN ALA PRO ALA SER ARG TRP ARG          
SEQRES  10 A  449  PRO TYR PHE ALA LEU TRP PRO GLU LEU GLY ARG LEU GLU          
SEQRES  11 A  449  HIS PRO MET PHE TRP PRO GLU GLU GLU ARG ARG CYS LEU          
SEQRES  12 A  449  LEU GLN GLY THR GLY VAL PRO GLU ALA VAL GLU LYS ASP          
SEQRES  13 A  449  LEU ALA ASN ILE ARG SER GLU TYR GLN SER ILE VAL LEU          
SEQRES  14 A  449  PRO PHE MET GLU ALA HIS PRO ASP LEU PHE SER LEU ARG          
SEQRES  15 A  449  VAL ARG SER LEU GLU LEU TYR HIS GLN LEU VAL ALA LEU          
SEQRES  16 A  449  VAL MET ALA TYR SER PHE GLN GLU PRO LEU GLU GLU GLU          
SEQRES  17 A  449  GLU ASP GLU LYS GLU PRO ASN SER PRO VAL MET VAL PRO          
SEQRES  18 A  449  ALA ALA ASP ILE LEU ASN HIS LEU ALA ASN HIS ASN ALA          
SEQRES  19 A  449  ASN LEU GLU TYR SER ALA ASN CYS LEU ARG MET VAL ALA          
SEQRES  20 A  449  THR GLN PRO ILE PRO LYS GLY HIS GLU ILE PHE ASN THR          
SEQRES  21 A  449  TYR GLY GLN MET ALA ASN TRP GLN LEU ILE HIS MET TYR          
SEQRES  22 A  449  GLY PHE VAL GLU PRO TYR PRO ASP ASN THR ASP ASP THR          
SEQRES  23 A  449  ALA ASP ILE GLN MET VAL THR VAL ARG GLU ALA ALA LEU          
SEQRES  24 A  449  GLN GLY THR LYS THR GLU ALA GLU ARG HIS LEU VAL TYR          
SEQRES  25 A  449  GLU ARG TRP ASP PHE LEU CYS LYS LEU GLU MET VAL GLY          
SEQRES  26 A  449  GLU GLU GLY ALA PHE VAL ILE GLY ARG GLU GLU VAL LEU          
SEQRES  27 A  449  THR GLU GLU GLU LEU THR THR THR LEU LYS VAL LEU CYS          
SEQRES  28 A  449  MET PRO ALA GLU GLU PHE ARG GLU LEU LYS ASP GLN ASP          
SEQRES  29 A  449  GLY GLY GLY ASP ASP LYS ARG GLU GLU GLY SER LEU THR          
SEQRES  30 A  449  ILE THR ASN ILE PRO LYS LEU LYS ALA SER TRP ARG GLN          
SEQRES  31 A  449  LEU LEU GLN ASN SER VAL LEU LEU THR LEU GLN THR TYR          
SEQRES  32 A  449  ALA THR ASP LEU LYS THR ASP GLN GLY LEU LEU SER ASN          
SEQRES  33 A  449  LYS GLU VAL TYR ALA LYS LEU SER TRP ARG GLU GLN GLN          
SEQRES  34 A  449  ALA LEU GLN VAL ARG TYR GLY GLN LYS MET ILE LEU HIS          
SEQRES  35 A  449  GLN LEU LEU GLU LEU THR SER                                  
SEQRES   1 P   15  ARG LYS ARG THR TYR GLU THR PHE LYS SER ILE MET LYS          
SEQRES   2 P   15  LYS SER                                                      
SEQRES   1 B  449  MET ALA THR GLN ALA LYS ARG PRO ARG VAL ALA GLY PRO          
SEQRES   2 B  449  VAL ASP GLY GLY ASP LEU ASP PRO VAL ALA CYS PHE LEU          
SEQRES   3 B  449  SER TRP CYS ARG ARG VAL GLY LEU GLU LEU SER PRO LYS          
SEQRES   4 B  449  VAL ALA VAL SER ARG GLN GLY THR VAL ALA GLY TYR GLY          
SEQRES   5 B  449  MET VAL ALA ARG GLU SER VAL GLN ALA GLY GLU LEU LEU          
SEQRES   6 B  449  PHE VAL VAL PRO ARG ALA ALA LEU LEU SER GLN HIS THR          
SEQRES   7 B  449  CYS SER ILE GLY GLY LEU LEU GLU ARG GLU ARG VAL ALA          
SEQRES   8 B  449  LEU GLN SER GLN SER GLY TRP VAL PRO LEU LEU LEU ALA          
SEQRES   9 B  449  LEU LEU HIS GLU LEU GLN ALA PRO ALA SER ARG TRP ARG          
SEQRES  10 B  449  PRO TYR PHE ALA LEU TRP PRO GLU LEU GLY ARG LEU GLU          
SEQRES  11 B  449  HIS PRO MET PHE TRP PRO GLU GLU GLU ARG ARG CYS LEU          
SEQRES  12 B  449  LEU GLN GLY THR GLY VAL PRO GLU ALA VAL GLU LYS ASP          
SEQRES  13 B  449  LEU ALA ASN ILE ARG SER GLU TYR GLN SER ILE VAL LEU          
SEQRES  14 B  449  PRO PHE MET GLU ALA HIS PRO ASP LEU PHE SER LEU ARG          
SEQRES  15 B  449  VAL ARG SER LEU GLU LEU TYR HIS GLN LEU VAL ALA LEU          
SEQRES  16 B  449  VAL MET ALA TYR SER PHE GLN GLU PRO LEU GLU GLU GLU          
SEQRES  17 B  449  GLU ASP GLU LYS GLU PRO ASN SER PRO VAL MET VAL PRO          
SEQRES  18 B  449  ALA ALA ASP ILE LEU ASN HIS LEU ALA ASN HIS ASN ALA          
SEQRES  19 B  449  ASN LEU GLU TYR SER ALA ASN CYS LEU ARG MET VAL ALA          
SEQRES  20 B  449  THR GLN PRO ILE PRO LYS GLY HIS GLU ILE PHE ASN THR          
SEQRES  21 B  449  TYR GLY GLN MET ALA ASN TRP GLN LEU ILE HIS MET TYR          
SEQRES  22 B  449  GLY PHE VAL GLU PRO TYR PRO ASP ASN THR ASP ASP THR          
SEQRES  23 B  449  ALA ASP ILE GLN MET VAL THR VAL ARG GLU ALA ALA LEU          
SEQRES  24 B  449  GLN GLY THR LYS THR GLU ALA GLU ARG HIS LEU VAL TYR          
SEQRES  25 B  449  GLU ARG TRP ASP PHE LEU CYS LYS LEU GLU MET VAL GLY          
SEQRES  26 B  449  GLU GLU GLY ALA PHE VAL ILE GLY ARG GLU GLU VAL LEU          
SEQRES  27 B  449  THR GLU GLU GLU LEU THR THR THR LEU LYS VAL LEU CYS          
SEQRES  28 B  449  MET PRO ALA GLU GLU PHE ARG GLU LEU LYS ASP GLN ASP          
SEQRES  29 B  449  GLY GLY GLY ASP ASP LYS ARG GLU GLU GLY SER LEU THR          
SEQRES  30 B  449  ILE THR ASN ILE PRO LYS LEU LYS ALA SER TRP ARG GLN          
SEQRES  31 B  449  LEU LEU GLN ASN SER VAL LEU LEU THR LEU GLN THR TYR          
SEQRES  32 B  449  ALA THR ASP LEU LYS THR ASP GLN GLY LEU LEU SER ASN          
SEQRES  33 B  449  LYS GLU VAL TYR ALA LYS LEU SER TRP ARG GLU GLN GLN          
SEQRES  34 B  449  ALA LEU GLN VAL ARG TYR GLY GLN LYS MET ILE LEU HIS          
SEQRES  35 B  449  GLN LEU LEU GLU LEU THR SER                                  
SEQRES   1 Q   15  ARG LYS ARG THR TYR GLU THR PHE LYS SER ILE MET LYS          
SEQRES   2 Q   15  LYS SER                                                      
HET    SAM  A6734      27                                                       
HET    EDO  A 474       4                                                       
HET    EDO  A 475       4                                                       
HET    EDO  A 476       4                                                       
HET    EDO  A 477       4                                                       
HET    EDO  A 478       4                                                       
HET    EDO  A 479       4                                                       
HET    EDO  A 480       4                                                       
HET    EDO  A 481       4                                                       
HET    EDO  A 482       4                                                       
HET    EDO  A 483       4                                                       
HET    EDO  A 484       4                                                       
HET    SAM  B6735      27                                                       
HET    EDO  B 474       4                                                       
HET    EDO  B 475       4                                                       
HET    EDO  B 476       4                                                       
HET    EDO  B 477       4                                                       
HET    EDO  B 478       4                                                       
HET    EDO  B 479       4                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   6  EDO    17(C2 H6 O2)                                                 
FORMUL  24  HOH   *667(H2 O)                                                    
HELIX    1   1 LEU A   19  GLY A   33  1                                  15    
HELIX    2   2 ALA A   95  LEU A   97  5                                   3    
HELIX    3   3 ILE A  105  GLU A  112  1                                   8    
HELIX    4   4 ARG A  113  GLN A  117  5                                   5    
HELIX    5   5 TRP A  122  ALA A  135  1                                  14    
HELIX    6   6 TRP A  140  ALA A  145  1                                   6    
HELIX    7   7 GLU A  149  LEU A  153  5                                   5    
HELIX    8   8 HIS A  155  TRP A  159  5                                   5    
HELIX    9   9 PRO A  160  GLN A  169  1                                  10    
HELIX   10  10 GLY A  172  ILE A  191  1                                  20    
HELIX   11  11 ILE A  191  HIS A  199  1                                   9    
HELIX   12  12 SER A  204  ARG A  208  5                                   5    
HELIX   13  13 SER A  209  SER A  224  1                                  16    
HELIX   14  14 ALA A  246  LEU A  250  5                                   5    
HELIX   15  15 ALA A  289  GLY A  298  1                                  10    
HELIX   16  16 MET A  315  GLY A  325  1                                  11    
HELIX   17  17 THR A  328  LEU A  345  1                                  18    
HELIX   18  18 THR A  363  MET A  376  1                                  14    
HELIX   19  19 PRO A  377  GLN A  387  1                                  11    
HELIX   20  20 ASN A  404  LEU A  408  5                                   5    
HELIX   21  21 LYS A  409  GLN A  425  1                                  17    
HELIX   22  22 ASP A  430  ASN A  440  1                                  11    
HELIX   23  23 ASN A  440  LEU A  447  1                                   8    
HELIX   24  24 SER A  448  THR A  472  1                                  25    
HELIX   25  25 LEU B   19  GLY B   33  1                                  15    
HELIX   26  26 ALA B   95  LEU B   97  5                                   3    
HELIX   27  27 ILE B  105  GLU B  112  1                                   8    
HELIX   28  28 TRP B  122  GLN B  134  1                                  13    
HELIX   29  29 TRP B  140  ALA B  145  1                                   6    
HELIX   30  30 GLU B  149  LEU B  153  5                                   5    
HELIX   31  31 HIS B  155  TRP B  159  5                                   5    
HELIX   32  32 PRO B  160  GLN B  169  1                                  10    
HELIX   33  33 GLY B  172  ILE B  191  1                                  20    
HELIX   34  34 ILE B  191  HIS B  199  1                                   9    
HELIX   35  35 SER B  204  ARG B  208  5                                   5    
HELIX   36  36 SER B  209  SER B  224  1                                  16    
HELIX   37  37 ALA B  246  LEU B  250  5                                   5    
HELIX   38  38 ALA B  289  GLY B  298  1                                  10    
HELIX   39  39 MET B  315  GLY B  325  1                                  11    
HELIX   40  40 THR B  328  LEU B  345  1                                  18    
HELIX   41  41 THR B  363  MET B  376  1                                  14    
HELIX   42  42 PRO B  377  GLN B  387  1                                  11    
HELIX   43  43 ASN B  404  LEU B  408  5                                   5    
HELIX   44  44 LYS B  409  GLN B  425  1                                  17    
HELIX   45  45 ASP B  430  ASN B  440  1                                  11    
HELIX   46  46 ASN B  440  LEU B  447  1                                   8    
HELIX   47  47 SER B  448  THR B  472  1                                  25    
SHEET    1   A 4 GLU A  35  LEU A  36  0                                        
SHEET    2   A 4 LEU A  88  PRO A  93 -1  O  VAL A  91   N  GLU A  35           
SHEET    3   A 4 CYS A 266  ALA A 271 -1  O  LEU A 267   N  VAL A  92           
SHEET    4   A 4 ALA A 258  TYR A 262 -1  N  GLU A 261   O  ARG A 268           
SHEET    1   B 4 VAL A  64  SER A  67  0                                        
SHEET    2   B 4 GLY A  76  ALA A  79 -1  O  GLY A  76   N  SER A  67           
SHEET    3   B 4 GLU A 280  ASN A 283 -1  O  ILE A 281   N  MET A  77           
SHEET    4   B 4 ASN A 251  HIS A 252  1  N  ASN A 251   O  ASN A 283           
SHEET    1   C 2 THR A 310  GLN A 314  0                                        
SHEET    2   C 2 ALA A 353  GLY A 357 -1  O  ILE A 356   N  ALA A 311           
SHEET    1   D 4 GLU B  35  LEU B  36  0                                        
SHEET    2   D 4 LEU B  88  PRO B  93 -1  O  VAL B  91   N  GLU B  35           
SHEET    3   D 4 CYS B 266  ALA B 271 -1  O  MET B 269   N  LEU B  89           
SHEET    4   D 4 ALA B 258  TYR B 262 -1  N  GLU B 261   O  ARG B 268           
SHEET    1   E 3 VAL B  64  SER B  67  0                                        
SHEET    2   E 3 GLY B  76  ALA B  79 -1  O  GLY B  76   N  SER B  67           
SHEET    3   E 3 GLU B 280  ILE B 281 -1  O  ILE B 281   N  MET B  77           
SHEET    1   F 2 THR B 310  GLN B 314  0                                        
SHEET    2   F 2 ALA B 353  GLY B 357 -1  O  ILE B 356   N  ALA B 311           
CISPEP   1 TYR A  303    PRO A  304          0         3.40                     
CISPEP   2 TYR B  303    PRO B  304          0         1.46                     
SITE     1 AC1 21 ALA A  73  GLY A  74  TYR A  75  ALA A 222                    
SITE     2 AC1 21 TYR A 223  ASP A 248  ILE A 249  LEU A 250                    
SITE     3 AC1 21 ASN A 251  HIS A 252  TYR A 285  TYR A 297                    
SITE     4 AC1 21 PHE A 299  EDO A 480  HOH A 533  HOH A 568                    
SITE     5 AC1 21 HOH A 580  HOH A 606  HOH A 652  HOH A 668                    
SITE     6 AC1 21 LYS P 310                                                     
SITE     1 AC2  6 LEU A 150  GLY A 151  ARG A 152  LEU A 153                    
SITE     2 AC2  6 PHE A 158  GLN A 215                                          
SITE     1 AC3  3 SER A 120  ASN A 183  GLU A 187                               
SITE     1 AC4  6 LEU A 424  TYR A 427  ALA A 428  THR A 429                    
SITE     2 AC4  6 HOH A 532  HOH A 765                                          
SITE     1 AC5  5 THR A 368  GLU A 396  GLU A 397  GLY A 398                    
SITE     2 AC5  5 SER A 399                                                     
SITE     1 AC6  6 VAL A 300  TYR A 444  TRP A 449  GLN A 452                    
SITE     2 AC6  6 HOH A 626  HOH A 722                                          
SITE     1 AC7  4 ARG A  30  LEU A  34  LEU A  36  HOH A 573                    
SITE     1 AC8  7 HOH A  46  LEU A 253  VAL A 300  HOH A 626                    
SITE     2 AC8  7 HOH A 641  SAM A6734  LYS B 441                               
SITE     1 AC9  5 ASN A 440  GLU A 442  ARG B  68  GLY B  74                    
SITE     2 AC9  5 EDO B 477                                                     
SITE     1 BC1  6 LEU A 362  THR A 363  GLU A 364  GLU A 365                    
SITE     2 BC1  6 GLU A 366  HOH A 676                                          
SITE     1 BC2  7 GLN A 324  ASN A 418  LEU A 421  LEU A 422                    
SITE     2 BC2  7 GLN A 425  HOH A 584  HOH A 605                               
SITE     1 BC3  4 GLU A 161  ARG A 165  GLU A 178  HOH A 780                    
SITE     1 BC4 24 VAL B  72  ALA B  73  GLY B  74  TYR B  75                    
SITE     2 BC4 24 ALA B 222  TYR B 223  ASP B 248  ILE B 249                    
SITE     3 BC4 24 LEU B 250  ASN B 251  HIS B 252  TYR B 285                    
SITE     4 BC4 24 TYR B 297  PHE B 299  EDO B 477  HOH B 544                    
SITE     5 BC4 24 HOH B 555  HOH B 604  HOH B 646  HOH B 659                    
SITE     6 BC4 24 HOH B 672  HOH B 716  HOH B 723  LYS Q 310                    
SITE     1 BC5  5 VAL B 300  TYR B 444  GLN B 452  HOH B 581                    
SITE     2 BC5  5 HOH B 649                                                     
SITE     1 BC6  5 GLY B 170  THR B 171  GLY B 172  GLU B 175                    
SITE     2 BC6  5 GLN B 314                                                     
SITE     1 BC7  5 LEU B 424  TYR B 427  ALA B 428  THR B 429                    
SITE     2 BC7  5 HOH B 622                                                     
SITE     1 BC8  9 ASN A 440  GLU A 442  EDO A 481  HOH B  63                    
SITE     2 BC8  9 VAL B  72  TRP B 449  HOH B 604  HOH B 623                    
SITE     3 BC8  9 SAM B6735                                                     
SITE     1 BC9  3 SER B 120  ASN B 183  GLU B 187                               
SITE     1 CC1  6 GLU B 154  TRP B 159  TRP B 449  ARG B 450                    
SITE     2 CC1  6 GLN B 453  HOH B 610                                          
CRYST1   61.464   64.985   73.891  78.33  70.05  63.75 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016270 -0.008023 -0.005427        0.00000                         
SCALE2      0.000000  0.017158 -0.001047        0.00000                         
SCALE3      0.000000  0.000000  0.014424        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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