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Database: PDB
Entry: 6CEN
LinkDB: 6CEN
Original site: 6CEN 
HEADER    TRANSFERASE/INHIBITOR                   12-FEB-18   6CEN              
TITLE     CRYSTAL STRUCTURE OF WHSC1L1 IN COMPLEX WITH INHIBITOR PEP21          
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;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: ACE-GLY-VAL-NLE-ARG-ILE-NH2;                               
COMPND  12 CHAIN: D;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NSD3, WHSC1L1, DC28;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    HISTONE-LYSINE N-METHYLTRANSFERASE NSD3, TRANSFERASE, TRANSFERASE-    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.BORIACK-SJODIN,K.SWINGER,N.A.FARROW                               
REVDAT   2   23-MAY-18 6CEN    1       JRNL                                     
REVDAT   1   09-MAY-18 6CEN    0                                                
JRNL        AUTH   M.J.MORRISON,P.A.BORIACK-SJODIN,K.K.SWINGER,T.J.WIGLE,       
JRNL        AUTH 2 D.SADALGE,K.W.KUNTZ,M.P.SCOTT,W.P.JANZEN,R.CHESWORTH,        
JRNL        AUTH 3 K.W.DUNCAN,D.M.HARVEY,J.W.LAMPE,L.H.MITCHELL,R.A.COPELAND    
JRNL        TITL   IDENTIFICATION OF A PEPTIDE INHIBITOR FOR THE HISTONE        
JRNL        TITL 2 METHYLTRANSFERASE WHSC1.                                     
JRNL        REF    PLOS ONE                      V.  13 97082 2018              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   29742153                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0197082                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28299                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1491                            
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) : 1.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1820                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1836                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.99000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.09000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.098         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.109         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1948 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1857 ; 0.020 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2627 ; 1.644 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4274 ; 1.766 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   240 ; 6.241 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;30.380 ;24.105       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   351 ;14.623 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;16.798 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   279 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2205 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   450 ; 0.008 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                                                 
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6CEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232598.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29790                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 3.720                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20% W/V           
REMARK 280  PEG5000MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K         
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       31.33000            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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  1267                                                      
REMARK 465     ASN A  1268                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1445     O    HOH A  1465              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY D   1   N   -  CA  -  C   ANGL. DEV. = -24.6 DEGREES          
REMARK 500    GLY D   1   CA  -  C   -  O   ANGL. DEV. =  15.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A1063       76.71    -65.51                                   
REMARK 500    ASN A1136       51.24   -118.73                                   
REMARK 500    ASN A1217     -161.57   -116.46                                   
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 A1302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1098   SG                                                     
REMARK 620 2 CYS A1100   SG  108.3                                              
REMARK 620 3 CYS A1108   SG  105.2 103.1                                        
REMARK 620 4 CYS A1114   SG  116.1 109.5 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1108   SG                                                     
REMARK 620 2 CYS A1123   SG  116.5                                              
REMARK 620 3 CYS A1128   SG  101.1 115.0                                        
REMARK 620 4 CYS A1134   SG  108.7 101.4 114.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1226   SG                                                     
REMARK 620 2 CYS A1273   SG  116.9                                              
REMARK 620 3 CYS A1275   SG  106.1 106.2                                        
REMARK 620 4 CYS A1280   SG  108.8 108.2 110.6                                  
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 1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1304                 
DBREF  6CEN A 1058  1285  UNP    Q9BZ95   NSD3_HUMAN    1058   1285             
DBREF  6CEN D    0     6  PDB    6CEN     6CEN             0      6             
SEQRES   1 A  228  LYS GLU ALA LEU GLU ILE GLU LYS ASN SER ARG LYS PRO          
SEQRES   2 A  228  PRO PRO TYR LYS HIS ILE LYS ALA ASN LYS VAL ILE GLY          
SEQRES   3 A  228  LYS VAL GLN ILE GLN VAL ALA ASP LEU SER GLU ILE PRO          
SEQRES   4 A  228  ARG CYS ASN CYS LYS PRO ALA ASP GLU ASN PRO CYS GLY          
SEQRES   5 A  228  LEU GLU SER GLU CYS LEU ASN ARG MET LEU GLN TYR GLU          
SEQRES   6 A  228  CYS HIS PRO GLN VAL CYS PRO ALA GLY ASP ARG CYS GLN          
SEQRES   7 A  228  ASN GLN CYS PHE THR LYS ARG LEU TYR PRO ASP ALA GLU          
SEQRES   8 A  228  ILE ILE LYS THR GLU ARG ARG GLY TRP GLY LEU ARG THR          
SEQRES   9 A  228  LYS ARG SER ILE LYS LYS GLY GLU PHE VAL ASN GLU TYR          
SEQRES  10 A  228  VAL GLY GLU LEU ILE ASP GLU GLU GLU CYS ARG LEU ARG          
SEQRES  11 A  228  ILE LYS ARG ALA HIS GLU ASN SER VAL THR ASN PHE TYR          
SEQRES  12 A  228  MET LEU THR VAL THR LYS ASP ARG ILE ILE ASP ALA GLY          
SEQRES  13 A  228  PRO LYS GLY ASN TYR SER ARG PHE MET ASN HIS SER CYS          
SEQRES  14 A  228  ASN PRO ASN CYS GLU THR GLN LYS TRP THR VAL ASN GLY          
SEQRES  15 A  228  ASP VAL ARG VAL GLY LEU PHE ALA LEU CYS ASP ILE PRO          
SEQRES  16 A  228  ALA GLY MET GLU LEU THR PHE ASN TYR ASN LEU ASP CYS          
SEQRES  17 A  228  LEU GLY ASN GLY ARG THR GLU CYS HIS CYS GLY ALA ASP          
SEQRES  18 A  228  ASN CYS SER GLY PHE LEU GLY                                  
SEQRES   1 D    7  ACE GLY VAL NLE ARG ILE NH2                                  
HET    ACE  D   0       3                                                       
HET    NLE  D   3       8                                                       
HET    NH2  D   6       1                                                       
HET    SAM  A1301      27                                                       
HET     ZN  A1302       1                                                       
HET     ZN  A1303       1                                                       
HET     ZN  A1304       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NLE NORLEUCINE                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  NLE    C6 H13 N O2                                                  
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  SAM    C15 H22 N6 O5 S                                              
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *226(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 ALA A 1130  CYS A 1134  5                                   5    
HELIX    4 AA4 GLN A 1137  ARG A 1142  1                                   6    
HELIX    5 AA5 ASP A 1180  ASN A 1194  1                                  15    
HELIX    6 AA6 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 5 LYS A1080  VAL A1081  0                                        
SHEET    2 AA2 5 GLU A1177  ILE A1179  1  O  LEU A1178   N  LYS A1080           
SHEET    3 AA2 5 ARG A1208  ASP A1211 -1  O  ASP A1211   N  GLU A1177           
SHEET    4 AA2 5 MET A1201  THR A1205 -1  N  LEU A1202   O  ILE A1210           
SHEET    5 AA2 5 NLE D   3  ARG D   4  1  O  NLE D   3   N  MET A1201           
SHEET    1 AA3 2 ALA A1147  LYS A1151  0                                        
SHEET    2 AA3 2 TRP A1157  THR A1161 -1  O  GLY A1158   N  ILE A1150           
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 A1302     1555   1555  2.32  
LINK         SG  CYS A1100                ZN    ZN A1302     1555   1555  2.35  
LINK         SG  CYS A1108                ZN    ZN A1302     1555   1555  2.31  
LINK         SG  CYS A1108                ZN    ZN A1303     1555   1555  2.34  
LINK         SG  CYS A1114                ZN    ZN A1302     1555   1555  2.33  
LINK         SG  CYS A1123                ZN    ZN A1303     1555   1555  2.32  
LINK         SG  CYS A1128                ZN    ZN A1303     1555   1555  2.29  
LINK         SG  CYS A1134                ZN    ZN A1303     1555   1555  2.31  
LINK         SG  CYS A1226                ZN    ZN A1304     1555   1555  2.34  
LINK         SG  CYS A1273                ZN    ZN A1304     1555   1555  2.34  
LINK         SG  CYS A1275                ZN    ZN A1304     1555   1555  2.35  
LINK         SG  CYS A1280                ZN    ZN A1304     1555   1555  2.31  
LINK         C   ACE D   0                 N   GLY D   1     1555   1555  1.32  
LINK         C   VAL D   2                 N   NLE D   3     1555   1555  1.34  
LINK         C   NLE D   3                 N   ARG D   4     1555   1555  1.32  
LINK         C   ILE D   5                 N   NH2 D   6     1555   1555  1.28  
SITE     1 AC1 21 ARG A1155  GLY A1156  TRP A1157  THR A1197                    
SITE     2 AC1 21 ASN A1198  PHE A1199  TYR A1200  ARG A1220                    
SITE     3 AC1 21 ASN A1223  HIS A1224  TYR A1261  GLU A1272                    
SITE     4 AC1 21 CYS A1273  HIS A1274  LEU A1284  HOH A1439                    
SITE     5 AC1 21 HOH A1446  HOH A1447  HOH A1486  HOH A1488                    
SITE     6 AC1 21 HOH A1524                                                     
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   42.870   62.660   48.600  90.00 107.92  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      0.023326  0.000000  0.007543        0.00000                         
SCALE2      0.000000  0.015959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021625        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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