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Database: PDB
Entry: 5V21
LinkDB: 5V21
Original site: 5V21 
HEADER    TRANSFERASE                             02-MAR-17   5V21              
TITLE     CRYSTAL STRUCTURE OF HUMAN SETD2 SET-DOMAIN IN COMPLEX WITH H3K36M    
TITLE    2 PEPTIDE AND SAM                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 1435-1711);                       
COMPND   5 SYNONYM: HIF-1,HUNTINGTIN YEAST PARTNER B,HUNTINGTIN-INTERACTING     
COMPND   6 PROTEIN 1,HIP-1,HUNTINGTIN-INTERACTING PROTEIN B,LYSINE N-           
COMPND   7 METHYLTRANSFERASE 3A,SET DOMAIN-CONTAINING PROTEIN 2,HSET2,P231HBP;  
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: HISTONE H3K36M PEPTIDE;                                    
COMPND  12 CHAIN: B;                                                            
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: SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069;             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    METHYLTRANSFERASE, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,L.TONG                                                        
REVDAT   4   07-MAR-18 5V21    1       REMARK                                   
REVDAT   3   27-SEP-17 5V21    1       REMARK                                   
REVDAT   2   29-MAR-17 5V21    1       JRNL                                     
REVDAT   1   22-MAR-17 5V21    0                                                
JRNL        AUTH   Y.ZHANG,C.M.SHAN,J.WANG,K.BAO,L.TONG,S.JIA                   
JRNL        TITL   MOLECULAR BASIS FOR THE ROLE OF ONCOGENIC HISTONE MUTATIONS  
JRNL        TITL 2 IN MODULATING H3K36 METHYLATION.                             
JRNL        REF    SCI REP                       V.   7 43906 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28256625                                                     
JRNL        DOI    10.1038/SREP43906                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7_650                                       
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) : 2.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 13077                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 671                             
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 29.5297 -  4.1272    0.99     2710   146  0.1643 0.2072        
REMARK   3     2  4.1272 -  3.2773    0.98     2569   137  0.1921 0.2857        
REMARK   3     3  3.2773 -  2.8634    0.96     2460   137  0.2289 0.2806        
REMARK   3     4  2.8634 -  2.6018    0.93     2396   126  0.2598 0.3319        
REMARK   3     5  2.6018 -  2.4154    0.90     2271   125  0.2834 0.3536        
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   : 1.01                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 27.36                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.430           
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) : 16.39950                                             
REMARK   3    B22 (A**2) : -4.38660                                             
REMARK   3    B33 (A**2) : -12.01290                                            
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      :  0.016           2169                                  
REMARK   3   ANGLE     :  1.415           2911                                  
REMARK   3   CHIRALITY :  0.105            293                                  
REMARK   3   PLANARITY :  0.007            380                                  
REMARK   3   DIHEDRAL  : 17.282            819                                  
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 5V21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226762.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-003                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13529                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: PHENIX                                                
REMARK 200 STARTING MODEL: 4H12                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M KSCN, 24% (V/V) PEG 2000 MME, PH   
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.24650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.58950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.15800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.58950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.24650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.15800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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  1415                                                      
REMARK 465     HIS A  1416                                                      
REMARK 465     HIS A  1417                                                      
REMARK 465     HIS A  1418                                                      
REMARK 465     HIS A  1419                                                      
REMARK 465     HIS A  1420                                                      
REMARK 465     HIS A  1421                                                      
REMARK 465     SER A  1422                                                      
REMARK 465     SER A  1423                                                      
REMARK 465     GLY A  1424                                                      
REMARK 465     ARG A  1425                                                      
REMARK 465     GLU A  1426                                                      
REMARK 465     ASN A  1427                                                      
REMARK 465     LEU A  1428                                                      
REMARK 465     TYR A  1429                                                      
REMARK 465     PHE A  1430                                                      
REMARK 465     GLN A  1431                                                      
REMARK 465     GLY A  1432                                                      
REMARK 465     HIS A  1433                                                      
REMARK 465     MET A  1434                                                      
REMARK 465     GLU A  1435                                                      
REMARK 465     THR A  1436                                                      
REMARK 465     SER A  1437                                                      
REMARK 465     VAL A  1438                                                      
REMARK 465     PRO A  1439                                                      
REMARK 465     PRO A  1440                                                      
REMARK 465     GLY A  1441                                                      
REMARK 465     SER A  1442                                                      
REMARK 465     ALA A  1443                                                      
REMARK 465     LEU A  1444                                                      
REMARK 465     VAL A  1445                                                      
REMARK 465     GLY A  1446                                                      
REMARK 465     LYS A  1486                                                      
REMARK 465     LYS A  1487                                                      
REMARK 465     ASN A  1488                                                      
REMARK 465     LYS A  1489                                                      
REMARK 465     SER A  1490                                                      
REMARK 465     HIS A  1491                                                      
REMARK 465     ARG A  1492                                                      
REMARK 465     ASP A  1493                                                      
REMARK 465     ILE A  1494                                                      
REMARK 465     LYS A  1495                                                      
REMARK 465     ARG A  1496                                                      
REMARK 465     MET A  1497                                                      
REMARK 465     MET A  1704                                                      
REMARK 465     LYS A  1705                                                      
REMARK 465     LYS A  1706                                                      
REMARK 465     GLU A  1707                                                      
REMARK 465     ARG A  1708                                                      
REMARK 465     SER A  1709                                                      
REMARK 465     ARG A  1710                                                      
REMARK 465     LYS A  1711                                                      
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    VAL A1576      -68.85    -97.84                                   
REMARK 500    LYS A1600       38.67     70.38                                   
REMARK 500    LEU A1609      -60.94   -107.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  106.2                                              
REMARK 620 3 CYS A1516   SG  117.0 107.1                                        
REMARK 620 4 CYS A1520   SG  110.7 103.4 111.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1516   SG                                                     
REMARK 620 2 CYS A1529   SG  122.4                                              
REMARK 620 3 CYS A1533   SG  101.7 108.4                                        
REMARK 620 4 CYS A1539   SG  108.9 104.6 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1631   SG                                                     
REMARK 620 2 CYS A1678   SG  116.6                                              
REMARK 620 3 CYS A1680   SG  106.7 111.3                                        
REMARK 620 4 CYS A1685   SG  108.8 105.3 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1804                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V22   RELATED DB: PDB                                   
DBREF  5V21 A 1435  1711  UNP    Q9BYW2   SETD2_HUMAN   1435   1711             
DBREF  5V21 B   29    43  PDB    5V21     5V21            29     43             
SEQADV 5V21 MET A 1415  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5V21 HIS A 1416  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1417  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 SER A 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 SER A 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 GLY A 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 ARG A 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 GLU A 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 ASN A 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 LEU A 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 TYR A 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 PHE A 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 GLN A 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 GLY A 1432  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 HIS A 1433  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V21 MET A 1434  UNP  Q9BYW2              EXPRESSION TAG                 
SEQRES   1 A  297  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  297  LEU TYR PHE GLN GLY HIS MET GLU THR SER VAL PRO PRO          
SEQRES   3 A  297  GLY SER ALA LEU VAL GLY PRO SER CYS VAL MET ASP ASP          
SEQRES   4 A  297  PHE ARG ASP PRO GLN ARG TRP LYS GLU CYS ALA LYS GLN          
SEQRES   5 A  297  GLY LYS MET PRO CYS TYR PHE ASP LEU ILE GLU GLU ASN          
SEQRES   6 A  297  VAL TYR LEU THR GLU ARG LYS LYS ASN LYS SER HIS ARG          
SEQRES   7 A  297  ASP ILE LYS ARG MET GLN CYS GLU CYS THR PRO LEU SER          
SEQRES   8 A  297  LYS ASP GLU ARG ALA GLN GLY GLU ILE ALA CYS GLY GLU          
SEQRES   9 A  297  ASP CYS LEU ASN ARG LEU LEU MET ILE GLU CYS SER SER          
SEQRES  10 A  297  ARG CYS PRO ASN GLY ASP TYR CYS SER ASN ARG ARG PHE          
SEQRES  11 A  297  GLN ARG LYS GLN HIS ALA ASP VAL GLU VAL ILE LEU THR          
SEQRES  12 A  297  GLU LYS LYS GLY TRP GLY LEU ARG ALA ALA LYS ASP LEU          
SEQRES  13 A  297  PRO SER ASN THR PHE VAL LEU GLU TYR CYS GLY GLU VAL          
SEQRES  14 A  297  LEU ASP HIS LYS GLU PHE LYS ALA ARG VAL LYS GLU TYR          
SEQRES  15 A  297  ALA ARG ASN LYS ASN ILE HIS TYR TYR PHE MET ALA LEU          
SEQRES  16 A  297  LYS ASN ASP GLU ILE ILE ASP ALA THR GLN LYS GLY ASN          
SEQRES  17 A  297  CYS SER ARG PHE MET ASN HIS SER CYS GLU PRO ASN CYS          
SEQRES  18 A  297  GLU THR GLN LYS TRP THR VAL ASN GLY GLN LEU ARG VAL          
SEQRES  19 A  297  GLY PHE PHE THR THR LYS LEU VAL PRO SER GLY SER GLU          
SEQRES  20 A  297  LEU THR PHE ASP TYR GLN PHE GLN ARG TYR GLY LYS GLU          
SEQRES  21 A  297  ALA GLN LYS CYS PHE CYS GLY SER ALA ASN CYS ARG GLY          
SEQRES  22 A  297  TYR LEU GLY GLY GLU ASN ARG VAL SER ILE ARG ALA ALA          
SEQRES  23 A  297  GLY GLY LYS MET LYS LYS GLU ARG SER ARG LYS                  
SEQRES   1 B   15  ALA PRO ALA THR GLY GLY VAL MET LYS PRO HIS ARG TYR          
SEQRES   2 B   15  ARG PRO                                                      
HET     ZN  A1801       1                                                       
HET     ZN  A1802       1                                                       
HET     ZN  A1803       1                                                       
HET    SAM  A1804      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  SAM    C15 H22 N6 O5 S                                              
FORMUL   7  HOH   *36(H2 O)                                                     
HELIX    1 AA1 ASP A 1452  ARG A 1455  5                                   4    
HELIX    2 AA2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3 AA3 SER A 1505  GLN A 1511  1                                   7    
HELIX    4 AA4 CYS A 1520  LEU A 1525  1                                   6    
HELIX    5 AA5 ASN A 1535  CYS A 1539  5                                   5    
HELIX    6 AA6 ARG A 1542  LYS A 1547  1                                   6    
HELIX    7 AA7 ASP A 1585  LYS A 1600  1                                  16    
HELIX    8 AA8 CYS A 1623  MET A 1627  5                                   5    
HELIX    9 AA9 SER A 1696  GLY A 1701  1                                   6    
SHEET    1 AA1 5 SER A1448  VAL A1450  0                                        
SHEET    2 AA1 5 VAL A1552  LEU A1556 -1  O  VAL A1554   N  CYS A1449           
SHEET    3 AA1 5 TRP A1562  ALA A1566 -1  O  ARG A1565   N  GLU A1553           
SHEET    4 AA1 5 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    5 AA1 5 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
SHEET    1 AA2 4 ASP A1474  LEU A1475  0                                        
SHEET    2 AA2 4 GLU A1613  GLY A1621  1  O  GLN A1619   N  ASP A1474           
SHEET    3 AA2 4 GLY A1581  LEU A1584 -1  N  LEU A1584   O  ILE A1614           
SHEET    4 AA2 4 VAL A1480  TYR A1481  1  N  VAL A1480   O  GLY A1581           
SHEET    1 AA3 5 ASP A1474  LEU A1475  0                                        
SHEET    2 AA3 5 GLU A1613  GLY A1621  1  O  GLN A1619   N  ASP A1474           
SHEET    3 AA3 5 PHE A1606  LYS A1610 -1  N  LYS A1610   O  GLU A1613           
SHEET    4 AA3 5 GLY B  34  MET B  36  1  O  MET B  36   N  PHE A1606           
SHEET    5 AA3 5 GLN A1669  ARG A1670 -1  N  GLN A1669   O  VAL B  35           
SHEET    1 AA4 3 PHE A1575  GLU A1578  0                                        
SHEET    2 AA4 3 GLN A1645  THR A1652 -1  O  PHE A1650   N  VAL A1576           
SHEET    3 AA4 3 CYS A1635  VAL A1642 -1  N  VAL A1642   O  GLN A1645           
LINK         SG  CYS A1499                ZN    ZN A1802     1555   1555  2.18  
LINK         SG  CYS A1501                ZN    ZN A1802     1555   1555  2.28  
LINK         SG  CYS A1516                ZN    ZN A1801     1555   1555  2.31  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.39  
LINK         SG  CYS A1520                ZN    ZN A1802     1555   1555  2.42  
LINK         SG  CYS A1529                ZN    ZN A1801     1555   1555  2.35  
LINK         SG  CYS A1533                ZN    ZN A1801     1555   1555  2.52  
LINK         SG  CYS A1539                ZN    ZN A1801     1555   1555  2.26  
LINK         SG  CYS A1631                ZN    ZN A1803     1555   1555  2.36  
LINK         SG  CYS A1678                ZN    ZN A1803     1555   1555  2.26  
LINK         SG  CYS A1680                ZN    ZN A1803     1555   1555  2.34  
LINK         SG  CYS A1685                ZN    ZN A1803     1555   1555  2.39  
SITE     1 AC1  5 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     2 AC1  5  ZN A1802                                                     
SITE     1 AC2  5 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     2 AC2  5  ZN A1801                                                     
SITE     1 AC3  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC4 15 LYS A1560  GLY A1561  TRP A1562  HIS A1603                    
SITE     2 AC4 15 TYR A1604  TYR A1605  ARG A1625  PHE A1626                    
SITE     3 AC4 15 ASN A1628  HIS A1629  TYR A1666  GLN A1676                    
SITE     4 AC4 15 LYS A1677  CYS A1678  PHE A1679                               
CRYST1   58.493   76.316   77.179  90.00  90.00  90.00 P 21 21 21    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      0.017096  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013103  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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