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Database: PDB
Entry: 5UPD
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Original site: 5UPD 
HEADER    TRANSFERASE                             02-FEB-17   5UPD              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN WOLF-HIRSCHHORN SYNDROME CANDIDATE  
TITLE    2 1-LIKE PROTEIN 1 (WHSC1L1)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE NSD3;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NUCLEAR SET DOMAIN-CONTAINING PROTEIN 3,PROTEIN WHISTLE,    
COMPND   5 WHSC1-LIKE 1 ISOFORM 9 WITH METHYLTRANSFERASE ACTIVITY TO LYSINE,    
COMPND   6 WOLF-HIRSCHHORN SYNDROME CANDIDATE 1-LIKE PROTEIN 1,WHSC1-LIKE       
COMPND   7 PROTEIN 1;                                                           
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: WHSC1L1, NSD3, DC28;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PRARE-V2R;                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, METHYL TRANSFERASE, SGC, TRANSFERASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.TEMPEL,W.YU,A.DONG,T.CEROVINA,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS, 
AUTHOR   2 P.J.BROWN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)                  
REVDAT   2   08-MAR-17 5UPD    1       SPRSDE                                   
REVDAT   1   15-FEB-17 5UPD    0                                                
SPRSDE     08-MAR-17 5UPD      4YZ8                                             
JRNL        AUTH   W.TEMPEL,W.YU,A.DONG,T.CEROVINA,C.BOUNTRA,C.H.ARROWSMITH,    
JRNL        AUTH 2 A.M.EDWARDS,P.J.BROWN,H.WU                                   
JRNL        TITL   METHYLTRANSFERASE DOMAIN OF HUMAN WOLF-HIRSCHHORN SYNDROME   
JRNL        TITL 2 CANDIDATE 1-LIKE PROTEIN 1 (WHSC1L1)                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21949                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1118                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1596                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1644                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.35000                                              
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : -0.93000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.47000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.091         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.051         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1781 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1600 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2407 ; 1.801 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3725 ; 1.033 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   224 ; 6.008 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    86 ;30.055 ;23.837       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   312 ;13.356 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.717 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   253 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1986 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   361 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   864 ; 2.221 ; 2.332       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   864 ; 2.221 ; 2.332       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1079 ; 3.416 ; 3.487       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ARP/WARP WAS USED FOR AUTOMATED MODEL     
REMARK   3  BUILDING. COOT WAS USED FOR INTERACTIVE MODEL BUILDING.             
REMARK   3  PHENIX.MOLPROBITY WAS USED FOR VALIDATION OF MODEL GEOMETRY         
REMARK   4                                                                      
REMARK   4 5UPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226237.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-15                          
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               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97957                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2, XDS                          
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.31                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23067                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3OOI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-5000-MME, 0.1 M BIS-TRIS, 0.02   
REMARK 280  M SARCOSINE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.40500            
REMARK 290   SMTRY3   2  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 300 REMARK: AUTHOR-DETERMINED QUATERNARY STRUCTURE: NOT AVAILABLE        
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  1053                                                      
REMARK 465     GLN A  1054                                                      
REMARK 465     ARG A  1055                                                      
REMARK 465     GLU A  1056                                                      
REMARK 465     SER A  1057                                                      
REMARK 465     LYS A  1058                                                      
REMARK 465     GLU A  1059                                                      
REMARK 465     ALA A  1060                                                      
REMARK 465     LEU A  1061                                                      
REMARK 465     GLU A  1062                                                      
REMARK 465     ILE A  1063                                                      
REMARK 465     GLU A  1064                                                      
REMARK 465     LYS A  1065                                                      
REMARK 465     ASN A  1066                                                      
REMARK 465     SER A  1067                                                      
REMARK 465     ARG A  1068                                                      
REMARK 465     ASP A  1264                                                      
REMARK 465     CYS A  1265                                                      
REMARK 465     LEU A  1266                                                      
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     LYS A1069    N    CB   CG   CD   CE   NZ                         
REMARK 470     LYS A1077    NZ                                                  
REMARK 470     LYS A1084    CE   NZ                                             
REMARK 470     GLN A1086    CG   CD   OE1  NE2                                  
REMARK 470     ILE A1087    CG1  CG2  CD1                                       
REMARK 470     GLN A1088    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1105    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1111    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1113    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1154    NH1  NH2                                            
REMARK 470     LYS A1166    CD   CE   NZ                                        
REMARK 470     LYS A1206    CD   CE   NZ                                        
REMARK 470     LEU A1263    C    O    CB   CG   CD1  CD2                        
REMARK 470     GLY A1285    C    O                                              
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 A1217     -163.30   -124.02                                   
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 A1319  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1098   SG                                                     
REMARK 620 2 CYS A1100   SG  105.1                                              
REMARK 620 3 CYS A1108   SG  105.8 105.2                                        
REMARK 620 4 CYS A1114   SG  116.2 107.2 116.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1320  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1108   SG                                                     
REMARK 620 2 CYS A1123   SG  112.9                                              
REMARK 620 3 CYS A1128   SG  103.2 116.3                                        
REMARK 620 4 CYS A1134   SG  112.2 102.7 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1321  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1226   SG                                                     
REMARK 620 2 CYS A1273   SG  118.0                                              
REMARK 620 3 CYS A1275   SG  105.4 105.5                                        
REMARK 620 4 CYS A1280   SG  109.6 108.7 109.2                                  
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 SAM A 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1319                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1321                 
DBREF  5UPD A 1054  1285  UNP    Q9BZ95   NSD3_HUMAN    1054   1285             
SEQADV 5UPD GLY A 1053  UNP  Q9BZ95              EXPRESSION TAG                 
SEQRES   1 A  233  GLY GLN ARG GLU SER LYS GLU ALA LEU GLU ILE GLU LYS          
SEQRES   2 A  233  ASN SER ARG LYS PRO PRO PRO TYR LYS HIS ILE LYS ALA          
SEQRES   3 A  233  ASN LYS VAL ILE GLY LYS VAL GLN ILE GLN VAL ALA ASP          
SEQRES   4 A  233  LEU SER GLU ILE PRO ARG CYS ASN CYS LYS PRO ALA ASP          
SEQRES   5 A  233  GLU ASN PRO CYS GLY LEU GLU SER GLU CYS LEU ASN ARG          
SEQRES   6 A  233  MET LEU GLN TYR GLU CYS HIS PRO GLN VAL CYS PRO ALA          
SEQRES   7 A  233  GLY ASP ARG CYS GLN ASN GLN CYS PHE THR LYS ARG LEU          
SEQRES   8 A  233  TYR PRO ASP ALA GLU ILE ILE LYS THR GLU ARG ARG GLY          
SEQRES   9 A  233  TRP GLY LEU ARG THR LYS ARG SER ILE LYS LYS GLY GLU          
SEQRES  10 A  233  PHE VAL ASN GLU TYR VAL GLY GLU LEU ILE ASP GLU GLU          
SEQRES  11 A  233  GLU CYS ARG LEU ARG ILE LYS ARG ALA HIS GLU ASN SER          
SEQRES  12 A  233  VAL THR ASN PHE TYR MET LEU THR VAL THR LYS ASP ARG          
SEQRES  13 A  233  ILE ILE ASP ALA GLY PRO LYS GLY ASN TYR SER ARG PHE          
SEQRES  14 A  233  MET ASN HIS SER CYS ASN PRO ASN CYS GLU THR GLN LYS          
SEQRES  15 A  233  TRP THR VAL ASN GLY ASP VAL ARG VAL GLY LEU PHE ALA          
SEQRES  16 A  233  LEU CYS ASP ILE PRO ALA GLY MET GLU LEU THR PHE ASN          
SEQRES  17 A  233  TYR ASN LEU ASP CYS LEU GLY ASN GLY ARG THR GLU CYS          
SEQRES  18 A  233  HIS CYS GLY ALA ASP ASN CYS SER GLY PHE LEU GLY              
HET    SAM  A1301      27                                                       
HET    UNX  A1302       1                                                       
HET    UNX  A1303       1                                                       
HET    UNX  A1304       1                                                       
HET    UNX  A1305       1                                                       
HET    UNX  A1306       1                                                       
HET    UNX  A1307       1                                                       
HET    UNX  A1308       1                                                       
HET    UNX  A1309       1                                                       
HET    UNX  A1310       1                                                       
HET    UNX  A1311       1                                                       
HET    UNX  A1312       1                                                       
HET    UNX  A1313       1                                                       
HET    UNX  A1314       1                                                       
HET    UNX  A1315       1                                                       
HET    UNX  A1316       1                                                       
HET    UNX  A1317       1                                                       
HET    UNX  A1318       1                                                       
HET     ZN  A1319       1                                                       
HET     ZN  A1320       1                                                       
HET     ZN  A1321       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  UNX    17(X)                                                        
FORMUL  20   ZN    3(ZN 2+)                                                     
FORMUL  23  HOH   *144(H2 O)                                                    
HELIX    1 AA1 ASP A 1091  ILE A 1095  5                                   5    
HELIX    2 AA2 CYS A 1114  LEU A 1119  1                                   6    
HELIX    3 AA3 GLN A 1137  ARG A 1142  1                                   6    
HELIX    4 AA4 ASP A 1180  ASN A 1194  1                                  15    
HELIX    5 AA5 ASN A 1217  MET A 1222  5                                   6    
SHEET    1 AA1 2 LYS A1074  HIS A1075  0                                        
SHEET    2 AA1 2 LYS A1215  GLY A1216  1  O  GLY A1216   N  LYS A1074           
SHEET    1 AA2 4 LYS A1080  VAL A1081  0                                        
SHEET    2 AA2 4 GLU A1177  ILE A1179  1  O  LEU A1178   N  LYS A1080           
SHEET    3 AA2 4 ARG A1208  ASP A1211 -1  O  ASP A1211   N  GLU A1177           
SHEET    4 AA2 4 MET A1201  THR A1205 -1  N  LEU A1202   O  ILE A1210           
SHEET    1 AA3 2 ALA A1147  LYS A1151  0                                        
SHEET    2 AA3 2 TRP A1157  THR A1161 -1  O  ARG A1160   N  GLU A1148           
SHEET    1 AA4 3 PHE A1170  TYR A1174  0                                        
SHEET    2 AA4 3 ASP A1240  ALA A1247 -1  O  LEU A1245   N  VAL A1171           
SHEET    3 AA4 3 CYS A1230  VAL A1237 -1  N  TRP A1235   O  ARG A1242           
SHEET    1 AA5 2 ASN A1223  HIS A1224  0                                        
SHEET    2 AA5 2 THR A1258  PHE A1259  1  O  PHE A1259   N  ASN A1223           
LINK         SG  CYS A1098                ZN    ZN A1319     1555   1555  2.32  
LINK         SG  CYS A1100                ZN    ZN A1319     1555   1555  2.36  
LINK         SG  CYS A1108                ZN    ZN A1319     1555   1555  2.22  
LINK         SG  CYS A1108                ZN    ZN A1320     1555   1555  2.36  
LINK         SG  CYS A1114                ZN    ZN A1319     1555   1555  2.37  
LINK         SG  CYS A1123                ZN    ZN A1320     1555   1555  2.36  
LINK         SG  CYS A1128                ZN    ZN A1320     1555   1555  2.37  
LINK         SG  CYS A1134                ZN    ZN A1320     1555   1555  2.25  
LINK         SG  CYS A1226                ZN    ZN A1321     1555   1555  2.38  
LINK         SG  CYS A1273                ZN    ZN A1321     1555   1555  2.30  
LINK         SG  CYS A1275                ZN    ZN A1321     1555   1555  2.32  
LINK         SG  CYS A1280                ZN    ZN A1321     1555   1555  2.33  
SITE     1 AC1 19 ARG A1155  TRP A1157  THR A1197  ASN A1198                    
SITE     2 AC1 19 PHE A1199  TYR A1200  ARG A1220  ASN A1223                    
SITE     3 AC1 19 HIS A1224  TYR A1261  GLU A1272  CYS A1273                    
SITE     4 AC1 19 HIS A1274  LEU A1284  HOH A1433  HOH A1438                    
SITE     5 AC1 19 HOH A1444  HOH A1456  HOH A1483                               
SITE     1 AC2  4 CYS A1098  CYS A1100  CYS A1108  CYS A1114                    
SITE     1 AC3  4 CYS A1108  CYS A1123  CYS A1128  CYS A1134                    
SITE     1 AC4  4 CYS A1226  CYS A1273  CYS A1275  CYS A1280                    
CRYST1   44.160   62.810   48.840  90.00 109.78  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022645  0.000000  0.008144        0.00000                         
SCALE2      0.000000  0.015921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021759        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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