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Database: PDB
Entry: 5V22
LinkDB: 5V22
Original site: 5V22 
HEADER    TRANSFERASE                             02-MAR-17   5V22              
TITLE     CRYSTAL STRUCTURE OF HUMAN SETD2 SET-DOMAIN IN COMPLEX WITH H3K36M    
TITLE    2 PEPTIDE AND SAH                                                      
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   3   27-SEP-17 5V22    1       REMARK                                   
REVDAT   2   29-MAR-17 5V22    1       JRNL                                     
REVDAT   1   22-MAR-17 5V22    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.    2.40 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 14082                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 714                             
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 40.0000 -  4.1003    0.99     2864   154  0.1702 0.2306        
REMARK   3     2  4.1003 -  3.2550    0.99     2740   144  0.1865 0.2463        
REMARK   3     3  3.2550 -  2.8437    0.98     2695   141  0.2173 0.2593        
REMARK   3     4  2.8437 -  2.5837    0.96     2617   139  0.2292 0.2973        
REMARK   3     5  2.5837 -  2.4000    0.92     2452   136  0.2461 0.3521        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 23.63                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.060           
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) : 12.23870                                             
REMARK   3    B22 (A**2) : -10.23250                                            
REMARK   3    B33 (A**2) : -2.00610                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           2167                                  
REMARK   3   ANGLE     :  0.797           2909                                  
REMARK   3   CHIRALITY :  0.055            292                                  
REMARK   3   PLANARITY :  0.002            380                                  
REMARK   3   DIHEDRAL  : 17.539            832                                  
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 5V22 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_1000226764.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-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) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14491                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
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   (%): 50.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
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       30.14350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.26350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.59800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.26350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.14350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.59800            
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: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A  1671     O    HOH A  1901              2.02            
REMARK 500   O    HOH A  1977     O    HOH A  1980              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A1571      151.25    -49.77                                   
REMARK 500    VAL A1576      -63.34   -105.16                                   
REMARK 500    LEU A1609      -62.75   -104.42                                   
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  110.5                                              
REMARK 620 3 CYS A1516   SG  109.3 109.9                                        
REMARK 620 4 CYS A1520   SG  110.7 104.1 112.3                                  
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  119.8                                              
REMARK 620 3 CYS A1533   SG   98.5 116.1                                        
REMARK 620 4 CYS A1539   SG  110.0 103.6 108.6                                  
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  111.9                                              
REMARK 620 3 CYS A1680   SG  110.5 107.0                                        
REMARK 620 4 CYS A1685   SG  112.1 105.8 109.3                                  
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 SAH A 1804                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V21   RELATED DB: PDB                                   
REMARK 900 5V21 CONTAINS THE SAME PROTEIN COMPLEXED WITH ZN AND SAM             
DBREF  5V22 A 1435  1711  UNP    Q9BYW2   SETD2_HUMAN   1435   1711             
DBREF  5V22 B   29    43  PDB    5V22     5V22            29     43             
SEQADV 5V22 MET A 1415  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5V22 HIS A 1416  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1417  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 SER A 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 SER A 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 GLY A 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 ARG A 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 GLU A 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 ASN A 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 LEU A 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 TYR A 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 PHE A 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 GLN A 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 GLY A 1432  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 HIS A 1433  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5V22 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    SAH  A1804      45                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  SAH    C14 H20 N6 O5 S                                              
FORMUL   7  HOH   *85(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  GLY A 1512  1                                   8    
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  ASN A 1599  1                                  15    
HELIX    8 AA8 ASN A 1622  MET A 1627  5                                   6    
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  GLY A1563   N  ILE A1555           
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 2 ASP A1474  LEU A1475  0                                        
SHEET    2 AA2 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1 AA3 6 VAL A1480  TYR A1481  0                                        
SHEET    2 AA3 6 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3 AA3 6 GLU A1613  ASP A1616 -1  O  ILE A1614   N  LEU A1584           
SHEET    4 AA3 6 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    5 AA3 6 GLY B  34  MET B  36  1  O  MET B  36   N  PHE A1606           
SHEET    6 AA3 6 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  TRP A1640   O  ARG A1647           
LINK         SG  CYS A1499                ZN    ZN A1802     1555   1555  2.28  
LINK         SG  CYS A1501                ZN    ZN A1802     1555   1555  2.31  
LINK         SG  CYS A1516                ZN    ZN A1801     1555   1555  2.33  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.46  
LINK         SG  CYS A1520                ZN    ZN A1802     1555   1555  2.37  
LINK         SG  CYS A1529                ZN    ZN A1801     1555   1555  2.38  
LINK         SG  CYS A1533                ZN    ZN A1801     1555   1555  2.39  
LINK         SG  CYS A1539                ZN    ZN A1801     1555   1555  2.28  
LINK         SG  CYS A1631                ZN    ZN A1803     1555   1555  2.42  
LINK         SG  CYS A1678                ZN    ZN A1803     1555   1555  2.31  
LINK         SG  CYS A1680                ZN    ZN A1803     1555   1555  2.31  
LINK         SG  CYS A1685                ZN    ZN A1803     1555   1555  2.47  
SITE     1 AC1  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC2  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC3  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC4 17 LYS A1560  GLY A1561  TRP A1562  ILE A1602                    
SITE     2 AC4 17 HIS A1603  TYR A1604  TYR A1605  ARG A1625                    
SITE     3 AC4 17 PHE A1626  ASN A1628  HIS A1629  TYR A1666                    
SITE     4 AC4 17 GLN A1676  LYS A1677  CYS A1678  PHE A1679                    
SITE     5 AC4 17 HOH A1936                                                     
CRYST1   60.287   77.196   76.527  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      0.016587  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013067        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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