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Database: PDB
Entry: 3OOI
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Original site: 3OOI 
HEADER    TRANSFERASE                             31-AUG-10   3OOI              
TITLE     CRYSTAL STRUCTURE OF HUMAN HISTONE-LYSINE N-METHYLTRANSFERASE NSD1 SET
TITLE    2 DOMAIN IN COMPLEX WITH S-ADENOSYL-L-METHIONINE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-36 AND H4    
COMPND   3 LYSINE-20 SPECIFIC;                                                  
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SET DOMAIN;                                                
COMPND   6 SYNONYM: NUCLEAR RECEPTOR-BINDING SET DOMAIN-CONTAINING PROTEIN 1,   
COMPND   7 H3-K36-HMTASE, H4-K20-HMTASE;                                        
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: NSD1, ARA267, KMT3B;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIPL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1                                  
KEYWDS    SET DOMAIN, HISTONE-LYSINE N-METHYLTRANSFERASE, S-ADENOSYL-L-         
KEYWDS   2 METHIONINE, TRANSFERASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.QIAO,M.WANG,R.M.XU                                                  
REVDAT   2   16-MAR-11 3OOI    1       JRNL                                     
REVDAT   1   22-DEC-10 3OOI    0                                                
JRNL        AUTH   Q.QIAO,Y.LI,Z.CHEN,M.WANG,D.REINBERG,R.M.XU                  
JRNL        TITL   THE STRUCTURE OF NSD1 REVEALS AN AUTOREGULATORY MECHANISM    
JRNL        TITL 2 UNDERLYING HISTONE H3K36 METHYLATION                         
JRNL        REF    J.BIOL.CHEM.                  V. 286  8361 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21196496                                                     
JRNL        DOI    10.1074/JBC.M110.204115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 30017                          
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) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1591                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2158                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.2280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1850                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 288                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.097         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.101         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2033 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2762 ; 1.196 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 5.093 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;31.658 ;24.158       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   364 ;11.954 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.908 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   288 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1588 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1233 ; 0.594 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2008 ; 1.161 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   800 ; 2.061 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   753 ; 3.498 ; 4.500       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   231                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5422   4.3511  -1.5978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0306 T22:   0.0129                                     
REMARK   3      T33:   0.0247 T12:   0.0009                                     
REMARK   3      T13:  -0.0171 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0075 L22:   0.6602                                     
REMARK   3      L33:   0.7123 L12:  -0.2563                                     
REMARK   3      L13:  -0.4410 L23:   0.2652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:  -0.0383 S13:  -0.0756                       
REMARK   3      S21:   0.0182 S22:   0.0107 S23:  -0.0190                       
REMARK   3      S31:   0.0342 S32:   0.0552 S33:   0.0217                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3OOI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061374.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-09; 09-NOV-09               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRF; BSRF                         
REMARK 200  BEAMLINE                       : BL17U; 1W2B                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8103; 1.2828, 1.2822, 1.0000     
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL; SI 111 CHANNEL     
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD; MARMOSAIC    
REMARK 200                                   225 MM CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31587                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 0.1M HEPES, 25%    
REMARK 280  PEG3350, 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       32.93750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.54300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.87550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.54300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.93750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.87550            
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: MONOMERIC                         
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 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 A 163     -161.34   -125.21                                   
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 A 233  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  44   SG                                                     
REMARK 620 2 CYS A  60   SG  117.4                                              
REMARK 620 3 CYS A  54   SG  105.3 115.2                                        
REMARK 620 4 CYS A  46   SG  110.1 106.7 100.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 232  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 219   SG                                                     
REMARK 620 2 CYS A 221   SG  104.5                                              
REMARK 620 3 CYS A 226   SG  106.7 113.8                                        
REMARK 620 4 CYS A 172   SG  115.9 107.5 108.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 234  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  74   SG                                                     
REMARK 620 2 CYS A  69   SG  115.3                                              
REMARK 620 3 CYS A  80   SG  111.0 104.6                                        
REMARK 620 4 CYS A  54   SG  101.4 115.2 109.4                                  
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 232                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 233                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 234                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 235                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 236                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 237                 
DBREF  3OOI A    1   231  UNP    Q96L73   NSD1_HUMAN    1852   2082             
SEQADV 3OOI SER A    0  UNP  Q96L73              EXPRESSION TAG                 
SEQRES   1 A  232  SER LYS GLU LEU ARG GLN LEU GLN GLU ASP ARG LYS ASN          
SEQRES   2 A  232  ASP LYS LYS PRO PRO PRO TYR LYS HIS ILE LYS VAL ASN          
SEQRES   3 A  232  ARG PRO ILE GLY ARG VAL GLN ILE PHE THR ALA ASP LEU          
SEQRES   4 A  232  SER GLU ILE PRO ARG CYS ASN CYS LYS ALA THR ASP GLU          
SEQRES   5 A  232  ASN PRO CYS GLY ILE ASP SER GLU CYS ILE ASN ARG MET          
SEQRES   6 A  232  LEU LEU TYR GLU CYS HIS PRO THR VAL CYS PRO ALA GLY          
SEQRES   7 A  232  GLY ARG CYS GLN ASN GLN CYS PHE SER LYS ARG GLN TYR          
SEQRES   8 A  232  PRO GLU VAL GLU ILE PHE ARG THR LEU GLN ARG GLY TRP          
SEQRES   9 A  232  GLY LEU ARG THR LYS THR ASP ILE LYS LYS GLY GLU PHE          
SEQRES  10 A  232  VAL ASN GLU TYR VAL GLY GLU LEU ILE ASP GLU GLU GLU          
SEQRES  11 A  232  CYS ARG ALA ARG ILE ARG TYR ALA GLN GLU HIS ASP ILE          
SEQRES  12 A  232  THR ASN PHE TYR MET LEU THR LEU ASP LYS ASP ARG ILE          
SEQRES  13 A  232  ILE ASP ALA GLY PRO LYS GLY ASN TYR ALA ARG PHE MET          
SEQRES  14 A  232  ASN HIS CYS CYS GLN PRO ASN CYS GLU THR GLN LYS TRP          
SEQRES  15 A  232  SER VAL ASN GLY ASP THR ARG VAL GLY LEU PHE ALA LEU          
SEQRES  16 A  232  SER ASP ILE LYS ALA GLY THR GLU LEU THR PHE ASN TYR          
SEQRES  17 A  232  ASN LEU GLU CYS LEU GLY ASN GLY LYS THR VAL CYS LYS          
SEQRES  18 A  232  CYS GLY ALA PRO ASN CYS SER GLY PHE LEU GLY                  
HET     ZN  A 232       1                                                       
HET     ZN  A 233       1                                                       
HET     ZN  A 234       1                                                       
HET    SO4  A 235       5                                                       
HET    SO4  A 236       5                                                       
HET    SAM  A 237      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  SAM    C15 H22 N6 O5 S                                              
FORMUL   8  HOH   *288(H2 O)                                                    
HELIX    1   1 SER A    0  ASP A   13  1                                  14    
HELIX    2   2 ASP A   37  ILE A   41  5                                   5    
HELIX    3   3 CYS A   60  LEU A   65  1                                   6    
HELIX    4   4 ALA A   76  CYS A   80  5                                   5    
HELIX    5   5 GLN A   83  ARG A   88  1                                   6    
HELIX    6   6 ASP A  126  HIS A  140  1                                  15    
HELIX    7   7 TYR A  164  MET A  168  5                                   5    
SHEET    1   A 4 LYS A  20  HIS A  21  0                                        
SHEET    2   A 4 ARG A 154  GLY A 162  1  O  PRO A 160   N  LYS A  20           
SHEET    3   A 4 GLY A 122  ILE A 125 -1  N  GLU A 123   O  ASP A 157           
SHEET    4   A 4 ARG A  26  PRO A  27  1  N  ARG A  26   O  LEU A 124           
SHEET    1   B 3 LYS A  20  HIS A  21  0                                        
SHEET    2   B 3 ARG A 154  GLY A 162  1  O  PRO A 160   N  LYS A  20           
SHEET    3   B 3 MET A 147  ASP A 151 -1  N  LEU A 148   O  ILE A 156           
SHEET    1   C 2 VAL A  93  ARG A  97  0                                        
SHEET    2   C 2 TRP A 103  THR A 107 -1  O  GLY A 104   N  PHE A  96           
SHEET    1   D 3 PHE A 116  GLU A 119  0                                        
SHEET    2   D 3 ASP A 186  ALA A 193 -1  O  LEU A 191   N  ASN A 118           
SHEET    3   D 3 CYS A 176  VAL A 183 -1  N  VAL A 183   O  ASP A 186           
SHEET    1   E 2 ASN A 169  HIS A 170  0                                        
SHEET    2   E 2 THR A 204  PHE A 205  1  O  PHE A 205   N  ASN A 169           
LINK         SG  CYS A  44                ZN    ZN A 233     1555   1555  2.29  
LINK         SG  CYS A 219                ZN    ZN A 232     1555   1555  2.30  
LINK         SG  CYS A 221                ZN    ZN A 232     1555   1555  2.33  
LINK         SG  CYS A  74                ZN    ZN A 234     1555   1555  2.33  
LINK         SG  CYS A  60                ZN    ZN A 233     1555   1555  2.34  
LINK         SG  CYS A 226                ZN    ZN A 232     1555   1555  2.35  
LINK         SG  CYS A  54                ZN    ZN A 233     1555   1555  2.35  
LINK         SG  CYS A  69                ZN    ZN A 234     1555   1555  2.35  
LINK         SG  CYS A  80                ZN    ZN A 234     1555   1555  2.36  
LINK         SG  CYS A  54                ZN    ZN A 234     1555   1555  2.39  
LINK         SG  CYS A 172                ZN    ZN A 232     1555   1555  2.42  
LINK         SG  CYS A  46                ZN    ZN A 233     1555   1555  2.42  
SITE     1 AC1  4 CYS A 172  CYS A 219  CYS A 221  CYS A 226                    
SITE     1 AC2  4 CYS A  44  CYS A  46  CYS A  54  CYS A  60                    
SITE     1 AC3  4 CYS A  54  CYS A  69  CYS A  74  CYS A  80                    
SITE     1 AC4 10 GLY A  77  GLY A  78  THR A  98  LEU A  99                    
SITE     2 AC4 10 GLN A 100  ARG A 101  HOH A 322  HOH A 383                    
SITE     3 AC4 10 HOH A 585  HOH A 607                                          
SITE     1 AC5  5 ILE A  22  LYS A  23  VAL A  24  ARG A  26                    
SITE     2 AC5  5 HOH A 414                                                     
SITE     1 AC6 20 ARG A 101  TRP A 103  THR A 143  ASN A 144                    
SITE     2 AC6 20 PHE A 145  TYR A 146  ARG A 166  ASN A 169                    
SITE     3 AC6 20 HIS A 170  TYR A 207  ASN A 214  VAL A 218                    
SITE     4 AC6 20 CYS A 219  LYS A 220  LEU A 230  HOH A 277                    
SITE     5 AC6 20 HOH A 278  HOH A 366  HOH A 401  HOH A 458                    
CRYST1   65.875   67.751   69.086  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      0.015180  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014760  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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