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Database: PDB
Entry: 4FMU
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HEADER    TRANSFERASE                             18-JUN-12   4FMU              
TITLE     CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN SET DOMAIN-    
TITLE    2 CONTAINING PROTEIN 2 COMPOUND: PR-SNF                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HIF-1, HUNTINGTIN YEAST PARTNER B, HUNTINGTIN-INTERACTING   
COMPND   5 PROTEIN 1, HIP-1, HUNTINGTIN-INTERACTING PROTEIN B, LYSINE N-        
COMPND   6 METHYLTRANSFERASE 3A, SET DOMAIN-CONTAINING PROTEIN 2, HSET2,        
COMPND   7 P231HBP;                                                             
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069;             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)V2RPRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, SGC, METHYLTRANSFERASE,SET DOMAIN-    
KEYWDS   2 CONTAINING PROTEIN 2, PR-SNF, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,G.IBANEZ,W.ZHENG,W.TEMPEL,C.BOUNTRA,C.H.ARROWSMITH,     
AUTHOR   2 A.M.EDWARDS,P.J.BROWN,J.MIN,M.LUO,H.WU,STRUCTURAL GENOMICS           
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   3   14-NOV-12 4FMU    1       JRNL                                     
REVDAT   2   24-OCT-12 4FMU    1       JRNL                                     
REVDAT   1   05-SEP-12 4FMU    0                                                
JRNL        AUTH   W.ZHENG,G.IBANEZ,H.WU,G.BLUM,H.ZENG,A.DONG,F.LI,T.HAJIAN,    
JRNL        AUTH 2 A.ALLALI-HASSANI,M.F.AMAYA,A.SIARHEYEVA,W.YU,P.J.BROWN,      
JRNL        AUTH 3 M.SCHAPIRA,M.VEDADI,J.MIN,M.LUO                              
JRNL        TITL   SINEFUNGIN DERIVATIVES AS INHIBITORS AND STRUCTURE PROBES OF 
JRNL        TITL 2 PROTEIN LYSINE METHYLTRANSFERASE SETD2.                      
JRNL        REF    J.AM.CHEM.SOC.                V. 134 18004 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23043551                                                     
JRNL        DOI    10.1021/JA307060P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0, COOT 0.6                              
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 18431                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.195                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.235                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 937                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.23                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.04                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2618                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2141                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2471                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2127                   
REMARK   3   BIN FREE R VALUE                        : 0.2405                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.61                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 147                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1793                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -23.98070                                            
REMARK   3    B22 (A**2) : 13.52010                                             
REMARK   3    B33 (A**2) : 10.46070                                             
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.26                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.17                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1888   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2555   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 646    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 47     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 282    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 1888   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 242    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2154   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.99                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.84                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FMU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073096.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03321                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR 300 CCD                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.080                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3H6L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 10% ISOPRPANOL, 0.1M        
REMARK 280  HEPES PH 7.5, VAPOR DIFFUSION, HANGING 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       25.77350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.43200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.63850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.43200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.77350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.63850            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  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     GLU A  1484                                                      
REMARK 465     ARG A  1485                                                      
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     GLU A  1692                                                      
REMARK 465     ASN A  1693                                                      
REMARK 465     ARG A  1694                                                      
REMARK 465     VAL A  1695                                                      
REMARK 465     SER A  1696                                                      
REMARK 465     ILE A  1697                                                      
REMARK 465     ARG A  1698                                                      
REMARK 465     ALA A  1699                                                      
REMARK 465     ALA A  1700                                                      
REMARK 465     GLY A  1701                                                      
REMARK 465     GLY A  1702                                                      
REMARK 465     LYS A  1703                                                      
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 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 A1444    CG   CD1  CD2                                       
REMARK 470     ARG A1455    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A1458    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1459    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A1462    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1465    CG   CD   CE   NZ                                   
REMARK 470     GLN A1466    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1468    CG   CD   CE   NZ                                   
REMARK 470     GLU A1478    CD   OE1  OE2                                       
REMARK 470     MET A1497    CG   SD   CE                                        
REMARK 470     LYS A1506    CG   CD   CE   NZ                                   
REMARK 470     ASP A1507    CG   OD1  OD2                                       
REMARK 470     ARG A1509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A1511    CG   CD   OE1  NE2                                  
REMARK 470     ILE A1514    CD1                                                 
REMARK 470     ASP A1519    CG   OD1  OD2                                       
REMARK 470     LEU A1521    CD1  CD2                                            
REMARK 470     LYS A1568    CG   CD   CE   NZ                                   
REMARK 470     ILE A1602    CD1                                                 
REMARK 470     LYS A1610    CE   NZ                                             
REMARK 470     ASN A1611    CG   OD1  ND2                                       
REMARK 470     GLN A1619    CD   OE1  NE2                                       
REMARK 470     LEU A1655    CD1                                                 
REMARK 470     GLN A1667    CD   OE1  NE2                                       
REMARK 470     ARG A1670    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A1673    CG   CD   CE   NZ                                   
REMARK 470     GLU A1674    CG   CD   OE1  OE2                                  
REMARK 470     ASN A1684    CG   OD1  ND2                                       
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    ASN A1541       43.78   -102.66                                   
REMARK 500    VAL A1576      -71.16    -91.01                                   
REMARK 500    ASN A1684       30.99    -99.23                                   
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 A1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  111.1                                              
REMARK 620 3 CYS A1516   SG  109.9 105.7                                        
REMARK 620 4 CYS A1520   SG  115.1 104.0 110.5                                  
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 A1680   SG                                                     
REMARK 620 2 CYS A1678   SG  110.5                                              
REMARK 620 3 CYS A1631   SG  110.0 114.5                                        
REMARK 620 4 CYS A1685   SG  106.9 107.2 107.4                                  
REMARK 620 N                    1     2     3                                   
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 A1516   SG                                                     
REMARK 620 2 CYS A1533   SG   97.0                                              
REMARK 620 3 CYS A1539   SG  112.4 110.5                                        
REMARK 620 4 CYS A1529   SG  116.7 118.1 102.5                                  
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 0UM A 1804                
DBREF  4FMU A 1434  1711  UNP    Q9BYW2   SETD2_HUMAN   1434   1711             
SEQRES   1 A  278  GLY GLU THR SER VAL PRO PRO GLY SER ALA LEU VAL GLY          
SEQRES   2 A  278  PRO SER CYS VAL MET ASP ASP PHE ARG ASP PRO GLN ARG          
SEQRES   3 A  278  TRP LYS GLU CYS ALA LYS GLN GLY LYS MET PRO CYS TYR          
SEQRES   4 A  278  PHE ASP LEU ILE GLU GLU ASN VAL TYR LEU THR GLU ARG          
SEQRES   5 A  278  LYS LYS ASN LYS SER HIS ARG ASP ILE LYS ARG MET GLN          
SEQRES   6 A  278  CYS GLU CYS THR PRO LEU SER LYS ASP GLU ARG ALA GLN          
SEQRES   7 A  278  GLY GLU ILE ALA CYS GLY GLU ASP CYS LEU ASN ARG LEU          
SEQRES   8 A  278  LEU MET ILE GLU CYS SER SER ARG CYS PRO ASN GLY ASP          
SEQRES   9 A  278  TYR CYS SER ASN ARG ARG PHE GLN ARG LYS GLN HIS ALA          
SEQRES  10 A  278  ASP VAL GLU VAL ILE LEU THR GLU LYS LYS GLY TRP GLY          
SEQRES  11 A  278  LEU ARG ALA ALA LYS ASP LEU PRO SER ASN THR PHE VAL          
SEQRES  12 A  278  LEU GLU TYR CYS GLY GLU VAL LEU ASP HIS LYS GLU PHE          
SEQRES  13 A  278  LYS ALA ARG VAL LYS GLU TYR ALA ARG ASN LYS ASN ILE          
SEQRES  14 A  278  HIS TYR TYR PHE MET ALA LEU LYS ASN ASP GLU ILE ILE          
SEQRES  15 A  278  ASP ALA THR GLN LYS GLY ASN CYS SER ARG PHE MET ASN          
SEQRES  16 A  278  HIS SER CYS GLU PRO ASN CYS GLU THR GLN LYS TRP THR          
SEQRES  17 A  278  VAL ASN GLY GLN LEU ARG VAL GLY PHE PHE THR THR LYS          
SEQRES  18 A  278  LEU VAL PRO SER GLY SER GLU LEU THR PHE ASP TYR GLN          
SEQRES  19 A  278  PHE GLN ARG TYR GLY LYS GLU ALA GLN LYS CYS PHE CYS          
SEQRES  20 A  278  GLY SER ALA ASN CYS ARG GLY TYR LEU GLY GLY GLU ASN          
SEQRES  21 A  278  ARG VAL SER ILE ARG ALA ALA GLY GLY LYS MET LYS LYS          
SEQRES  22 A  278  GLU ARG SER ARG LYS                                          
HET     ZN  A1801       1                                                       
HET     ZN  A1802       1                                                       
HET     ZN  A1803       1                                                       
HET    0UM  A1804      30                                                       
HET    UNX  A1805       1                                                       
HET    UNX  A1806       1                                                       
HET    UNX  A1807       1                                                       
HET    UNX  A1808       1                                                       
HET    UNX  A1809       1                                                       
HET    UNX  A1810       1                                                       
HET    UNX  A1811       1                                                       
HET    UNX  A1812       1                                                       
HET    UNX  A1813       1                                                       
HET    UNX  A1814       1                                                       
HET    UNX  A1815       1                                                       
HET    UNX  A1816       1                                                       
HET    UNX  A1817       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     0UM (2S,5S)-2-AMINO-6-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-          
HETNAM   2 0UM  YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]-5-                       
HETNAM   3 0UM  (PROPYLAMINO)HEXANOIC ACID                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  0UM    C18 H29 N7 O5                                                
FORMUL   6  UNX    13(X)                                                        
FORMUL  19  HOH   *93(H2 O)                                                     
HELIX    1   1 ASP A 1452  ARG A 1455  5                                   4    
HELIX    2   2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3   3 SER A 1505  GLY A 1512  1                                   8    
HELIX    4   4 ASN A 1522  MET A 1526  5                                   5    
HELIX    5   5 ASN A 1535  CYS A 1539  5                                   5    
HELIX    6   6 ARG A 1542  LYS A 1547  1                                   6    
HELIX    7   7 ASP A 1585  ASN A 1599  1                                  15    
HELIX    8   8 ASN A 1622  MET A 1627  5                                   6    
SHEET    1   A 5 SER A1448  VAL A1450  0                                        
SHEET    2   A 5 VAL A1552  LEU A1556 -1  O  VAL A1554   N  CYS A1449           
SHEET    3   A 5 TRP A1562  ALA A1566 -1  O  ARG A1565   N  GLU A1553           
SHEET    4   A 5 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    5   A 5 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
SHEET    1   B 2 ASP A1474  LEU A1475  0                                        
SHEET    2   B 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1   C 4 VAL A1480  TYR A1481  0                                        
SHEET    2   C 4 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3   C 4 GLU A1613  ASP A1616 -1  O  ILE A1614   N  LEU A1584           
SHEET    4   C 4 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    1   D 3 PHE A1575  GLU A1578  0                                        
SHEET    2   D 3 GLN A1645  THR A1652 -1  O  PHE A1650   N  VAL A1576           
SHEET    3   D 3 CYS A1635  VAL A1642 -1  N  VAL A1642   O  GLN A1645           
LINK         SG  CYS A1499                ZN    ZN A1801     1555   1555  2.20  
LINK         SG  CYS A1680                ZN    ZN A1803     1555   1555  2.22  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.29  
LINK         SG  CYS A1678                ZN    ZN A1803     1555   1555  2.29  
LINK         SG  CYS A1533                ZN    ZN A1802     1555   1555  2.32  
LINK         SG  CYS A1539                ZN    ZN A1802     1555   1555  2.32  
LINK         SG  CYS A1501                ZN    ZN A1801     1555   1555  2.33  
LINK         SG  CYS A1631                ZN    ZN A1803     1555   1555  2.38  
LINK         SG  CYS A1516                ZN    ZN A1801     1555   1555  2.40  
LINK         SG  CYS A1529                ZN    ZN A1802     1555   1555  2.41  
LINK         SG  CYS A1520                ZN    ZN A1801     1555   1555  2.48  
LINK         SG  CYS A1685                ZN    ZN A1803     1555   1555  2.54  
SITE     1 AC1  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC2  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC3  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC4 22 LYS A1560  GLY A1561  TRP A1562  TYR A1579                    
SITE     2 AC4 22 ILE A1602  HIS A1603  TYR A1604  TYR A1605                    
SITE     3 AC4 22 ARG A1625  PHE A1626  MET A1627  ASN A1628                    
SITE     4 AC4 22 HIS A1629  PHE A1664  GLN A1676  LYS A1677                    
SITE     5 AC4 22 CYS A1678  PHE A1679  LEU A1689  HOH A1924                    
SITE     6 AC4 22 HOH A1940  HOH A1958                                          
CRYST1   51.547   77.277   78.864  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      0.019400  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012680        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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