GenomeNet

Database: PDB
Entry: 5LSU
LinkDB: 5LSU
Original site: 5LSU 
HEADER    TRANSFERASE                             05-SEP-16   5LSU              
TITLE     STRUCTURE OF THE EPIGENETIC ONCOGENE MMSET AND INHIBITION BY N-ALKYL  
TITLE    2 SINEFUNGIN DERIVATIVES                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE NSD2;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MULTIPLE MYELOMA SET DOMAIN-CONTAINING PROTEIN,MMSET,NUCLEAR
COMPND   5 SET DOMAIN-CONTAINING PROTEIN 2,NSD2,PROTEIN TRITHORAX-5,WOLF-       
COMPND   6 HIRSCHHORN SYNDROME CANDIDATE 1 PROTEIN,WHSC1;                       
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: WHSC1, KIAA1090, MMSET, NSD2, TRX5;                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    LYSINE METHYLTRANSFERASE MMSET SET DOMAIN, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TISI,P.PATHURI,T.HEIGHTMAN                                          
REVDAT   2   21-DEC-16 5LSU    1       JRNL                                     
REVDAT   1   05-OCT-16 5LSU    0                                                
JRNL        AUTH   D.TISI,E.CHIARPARIN,E.TAMANINI,P.PATHURI,J.E.COYLE,A.HOLD,   
JRNL        AUTH 2 F.P.HOLDING,N.AMIN,A.C.MARTIN,S.J.RICH,V.BERDINI,J.YON,      
JRNL        AUTH 3 P.ACKLAM,R.BURKE,L.DROUIN,J.E.HARMER,F.JEGANATHAN,           
JRNL        AUTH 4 R.L.VAN MONTFORT,Y.NEWBATT,M.TORTORICI,M.WESTLAKE,A.WOOD,    
JRNL        AUTH 5 S.HOELDER,T.D.HEIGHTMAN                                      
JRNL        TITL   STRUCTURE OF THE EPIGENETIC ONCOGENE MMSET AND INHIBITION BY 
JRNL        TITL 2 N-ALKYL SINEFUNGIN DERIVATIVES.                              
JRNL        REF    ACS CHEM. BIOL.               V.  11  3093 2016              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   27571355                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.6B00308                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27404                          
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)  : 0.175                          
REMARK   3   R VALUE            (WORKING SET)  : 0.171                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1384                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.14                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.22                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.93                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2813                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2450                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2664                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2430                   
REMARK   3   BIN FREE R VALUE                        : 0.2800                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.30                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 149                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3562                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 528                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.03                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -18.83030                                            
REMARK   3    B22 (A**2) : 6.58740                                              
REMARK   3    B33 (A**2) : 12.24290                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.270               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.283               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.211               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.229               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.197               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3763   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5127   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1323   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 100    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 559    ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3763   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 489    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4527   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.012                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.47                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.21                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|973 - A|1206 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    7.2855   58.4780   12.3833           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0521 T22:   -0.1407                                    
REMARK   3     T33:   -0.1646 T12:    0.0376                                    
REMARK   3     T13:   -0.0273 T23:    0.0057                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9573 L22:    2.2280                                    
REMARK   3     L33:    3.6371 L12:    0.0006                                    
REMARK   3     L13:   -0.4705 L23:    0.0232                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0125 S12:    0.0718 S13:    0.0320                     
REMARK   3     S21:    0.3654 S22:   -0.0857 S23:   -0.1123                     
REMARK   3     S31:    0.1812 S32:    0.3013 S33:    0.0732                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|976 - B|1206 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.4414   62.9493   54.2972           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1881 T22:   -0.1348                                    
REMARK   3     T33:   -0.0620 T12:   -0.0046                                    
REMARK   3     T13:   -0.0068 T23:   -0.0216                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8748 L22:    4.3172                                    
REMARK   3     L33:    2.4844 L12:   -0.5887                                    
REMARK   3     L13:    0.3958 L23:    0.4637                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0450 S12:    0.0062 S13:   -0.1076                     
REMARK   3     S21:   -0.1196 S22:   -0.2003 S23:    0.5442                     
REMARK   3     S31:    0.0555 S32:   -0.1665 S33:    0.1553                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5LSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001301.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27812                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 3OOI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.0%W/V PEG 3350, 0.1M NH4CL, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.29150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.54700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.55700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.54700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.29150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.55700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   952                                                      
REMARK 465     GLY A   953                                                      
REMARK 465     SER A   954                                                      
REMARK 465     SER A   955                                                      
REMARK 465     HIS A   956                                                      
REMARK 465     HIS A   957                                                      
REMARK 465     HIS A   958                                                      
REMARK 465     HIS A   959                                                      
REMARK 465     HIS A   960                                                      
REMARK 465     HIS A   961                                                      
REMARK 465     SER A   962                                                      
REMARK 465     SER A   963                                                      
REMARK 465     GLY A   964                                                      
REMARK 465     LEU A   965                                                      
REMARK 465     VAL A   966                                                      
REMARK 465     PRO A   967                                                      
REMARK 465     ARG A   968                                                      
REMARK 465     GLY A   969                                                      
REMARK 465     SER A   970                                                      
REMARK 465     HIS A   971                                                      
REMARK 465     MET A   972                                                      
REMARK 465     MET B   952                                                      
REMARK 465     GLY B   953                                                      
REMARK 465     SER B   954                                                      
REMARK 465     SER B   955                                                      
REMARK 465     HIS B   956                                                      
REMARK 465     HIS B   957                                                      
REMARK 465     HIS B   958                                                      
REMARK 465     HIS B   959                                                      
REMARK 465     HIS B   960                                                      
REMARK 465     HIS B   961                                                      
REMARK 465     SER B   962                                                      
REMARK 465     SER B   963                                                      
REMARK 465     GLY B   964                                                      
REMARK 465     LEU B   965                                                      
REMARK 465     VAL B   966                                                      
REMARK 465     PRO B   967                                                      
REMARK 465     ARG B   968                                                      
REMARK 465     GLY B   969                                                      
REMARK 465     SER B   970                                                      
REMARK 465     HIS B   971                                                      
REMARK 465     MET B   972                                                      
REMARK 465     LYS B   973                                                      
REMARK 465     LEU B   974                                                      
REMARK 465     LEU B   975                                                      
REMARK 465     LYS B  1019                                                      
REMARK 465     PRO B  1020                                                      
REMARK 465     THR B  1021                                                      
REMARK 465     ASP B  1022                                                      
REMARK 465     GLU B  1023                                                      
REMARK 465     ASN B  1024                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 974    CG   CD1  CD2                                       
REMARK 470     LEU A 975    CG   CD1  CD2                                       
REMARK 470     LEU A 978    CG   CD1  CD2                                       
REMARK 470     THR A 981    OG1  CG2                                            
REMARK 470     GLN A 982    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 983    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 986    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 977    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 979    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 980    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 982    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 983    CG   CD   OE1  OE2                                  
REMARK 470     SER B 984    OG                                                  
REMARK 470     GLU B 985    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1031    CG   CD   OE1  OE2                                  
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    GLN A 982       56.76     20.04                                   
REMARK 500    GLU A 983     -160.26    -75.40                                   
REMARK 500    GLU A1031       31.47    -91.73                                   
REMARK 500    GLN A1055       28.48   -141.42                                   
REMARK 500    ASN A1135     -155.47   -120.05                                   
REMARK 500    ASP A1182       -8.26   -149.78                                   
REMARK 500    GLN B 982       60.83     29.95                                   
REMARK 500    CYS B1026       -2.47     60.41                                   
REMARK 500    ASP B1125        3.58     58.80                                   
REMARK 500    ASN B1135     -157.70   -110.97                                   
REMARK 500    ASP B1182       -7.99   -149.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1648        DISTANCE =  5.95 ANGSTROMS                       
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 A1016   SG                                                     
REMARK 620 2 CYS A1018   SG  110.3                                              
REMARK 620 3 CYS A1026   SG   95.7 100.5                                        
REMARK 620 4 CYS A1032   SG  117.0 118.5 111.2                                  
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 A1026   SG                                                     
REMARK 620 2 CYS A1041   SG  120.3                                              
REMARK 620 3 CYS A1046   SG  100.3 119.9                                        
REMARK 620 4 CYS A1052   SG  108.0 101.5 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1144   SG                                                     
REMARK 620 2 CYS A1191   SG  115.0                                              
REMARK 620 3 CYS A1193   SG  103.9 110.2                                        
REMARK 620 4 CYS A1198   SG  105.8 106.9 115.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1016   SG                                                     
REMARK 620 2 CYS B1018   SG  115.6                                              
REMARK 620 3 CYS B1026   SG  107.4  98.9                                        
REMARK 620 4 CYS B1032   SG  119.7 106.6 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1026   SG                                                     
REMARK 620 2 CYS B1041   SG  122.4                                              
REMARK 620 3 CYS B1046   SG   96.9 117.6                                        
REMARK 620 4 CYS B1052   SG  105.3 105.7 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1144   SG                                                     
REMARK 620 2 CYS B1191   SG  117.7                                              
REMARK 620 3 CYS B1193   SG  105.1 107.7                                        
REMARK 620 4 CYS B1198   SG  109.7 107.0 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 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 SAM A 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1304                
DBREF  5LSU A  973  1203  UNP    O96028   NSD2_HUMAN     973   1203             
DBREF  5LSU B  973  1203  UNP    O96028   NSD2_HUMAN     973   1203             
SEQADV 5LSU MET A  952  UNP  O96028              INITIATING METHIONINE          
SEQADV 5LSU GLY A  953  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER A  954  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER A  955  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  956  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  957  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  958  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  959  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  960  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  961  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER A  962  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER A  963  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU GLY A  964  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU LEU A  965  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU VAL A  966  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU PRO A  967  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU ARG A  968  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU GLY A  969  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER A  970  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS A  971  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU MET A  972  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU LEU A  975  UNP  O96028    GLN   975 ENGINEERED MUTATION            
SEQADV 5LSU LEU A  978  UNP  O96028    ALA   978 ENGINEERED MUTATION            
SEQADV 5LSU LEU A 1071  UNP  O96028    ASP  1071 ENGINEERED MUTATION            
SEQADV 5LSU GLN A 1072  UNP  O96028    GLY  1072 ENGINEERED MUTATION            
SEQADV 5LSU ARG A 1073  UNP  O96028    LYS  1073 ENGINEERED MUTATION            
SEQADV 5LSU MET B  952  UNP  O96028              INITIATING METHIONINE          
SEQADV 5LSU GLY B  953  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER B  954  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER B  955  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  956  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  957  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  958  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  959  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  960  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  961  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER B  962  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER B  963  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU GLY B  964  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU LEU B  965  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU VAL B  966  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU PRO B  967  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU ARG B  968  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU GLY B  969  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU SER B  970  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU HIS B  971  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU MET B  972  UNP  O96028              EXPRESSION TAG                 
SEQADV 5LSU LEU B  975  UNP  O96028    GLN   975 ENGINEERED MUTATION            
SEQADV 5LSU LEU B  978  UNP  O96028    ALA   978 ENGINEERED MUTATION            
SEQADV 5LSU LEU B 1071  UNP  O96028    ASP  1071 ENGINEERED MUTATION            
SEQADV 5LSU GLN B 1072  UNP  O96028    GLY  1072 ENGINEERED MUTATION            
SEQADV 5LSU ARG B 1073  UNP  O96028    LYS  1073 ENGINEERED MUTATION            
SEQRES   1 A  252  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  252  LEU VAL PRO ARG GLY SER HIS MET LYS LEU LEU ARG GLU          
SEQRES   3 A  252  LEU ARG GLU THR GLN GLU SER GLU ARG LYS PRO PRO PRO          
SEQRES   4 A  252  TYR LYS HIS ILE LYS VAL ASN LYS PRO TYR GLY LYS VAL          
SEQRES   5 A  252  GLN ILE TYR THR ALA ASP ILE SER GLU ILE PRO LYS CYS          
SEQRES   6 A  252  ASN CYS LYS PRO THR ASP GLU ASN PRO CYS GLY PHE ASP          
SEQRES   7 A  252  SER GLU CYS LEU ASN ARG MET LEU MET PHE GLU CYS HIS          
SEQRES   8 A  252  PRO GLN VAL CYS PRO ALA GLY GLU PHE CYS GLN ASN GLN          
SEQRES   9 A  252  CYS PHE THR LYS ARG GLN TYR PRO GLU THR LYS ILE ILE          
SEQRES  10 A  252  LYS THR LEU GLN ARG GLY TRP GLY LEU VAL ALA LYS ARG          
SEQRES  11 A  252  ASP ILE ARG LYS GLY GLU PHE VAL ASN GLU TYR VAL GLY          
SEQRES  12 A  252  GLU LEU ILE ASP GLU GLU GLU CYS MET ALA ARG ILE LYS          
SEQRES  13 A  252  HIS ALA HIS GLU ASN ASP ILE THR HIS PHE TYR MET LEU          
SEQRES  14 A  252  THR ILE ASP LYS ASP ARG ILE ILE ASP ALA GLY PRO LYS          
SEQRES  15 A  252  GLY ASN TYR SER ARG PHE MET ASN HIS SER CYS GLN PRO          
SEQRES  16 A  252  ASN CYS GLU THR LEU LYS TRP THR VAL ASN GLY ASP THR          
SEQRES  17 A  252  ARG VAL GLY LEU PHE ALA VAL CYS ASP ILE PRO ALA GLY          
SEQRES  18 A  252  THR GLU LEU THR PHE ASN TYR ASN LEU ASP CYS LEU GLY          
SEQRES  19 A  252  ASN GLU LYS THR VAL CYS ARG CYS GLY ALA SER ASN CYS          
SEQRES  20 A  252  SER GLY PHE LEU GLY                                          
SEQRES   1 B  252  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  252  LEU VAL PRO ARG GLY SER HIS MET LYS LEU LEU ARG GLU          
SEQRES   3 B  252  LEU ARG GLU THR GLN GLU SER GLU ARG LYS PRO PRO PRO          
SEQRES   4 B  252  TYR LYS HIS ILE LYS VAL ASN LYS PRO TYR GLY LYS VAL          
SEQRES   5 B  252  GLN ILE TYR THR ALA ASP ILE SER GLU ILE PRO LYS CYS          
SEQRES   6 B  252  ASN CYS LYS PRO THR ASP GLU ASN PRO CYS GLY PHE ASP          
SEQRES   7 B  252  SER GLU CYS LEU ASN ARG MET LEU MET PHE GLU CYS HIS          
SEQRES   8 B  252  PRO GLN VAL CYS PRO ALA GLY GLU PHE CYS GLN ASN GLN          
SEQRES   9 B  252  CYS PHE THR LYS ARG GLN TYR PRO GLU THR LYS ILE ILE          
SEQRES  10 B  252  LYS THR LEU GLN ARG GLY TRP GLY LEU VAL ALA LYS ARG          
SEQRES  11 B  252  ASP ILE ARG LYS GLY GLU PHE VAL ASN GLU TYR VAL GLY          
SEQRES  12 B  252  GLU LEU ILE ASP GLU GLU GLU CYS MET ALA ARG ILE LYS          
SEQRES  13 B  252  HIS ALA HIS GLU ASN ASP ILE THR HIS PHE TYR MET LEU          
SEQRES  14 B  252  THR ILE ASP LYS ASP ARG ILE ILE ASP ALA GLY PRO LYS          
SEQRES  15 B  252  GLY ASN TYR SER ARG PHE MET ASN HIS SER CYS GLN PRO          
SEQRES  16 B  252  ASN CYS GLU THR LEU LYS TRP THR VAL ASN GLY ASP THR          
SEQRES  17 B  252  ARG VAL GLY LEU PHE ALA VAL CYS ASP ILE PRO ALA GLY          
SEQRES  18 B  252  THR GLU LEU THR PHE ASN TYR ASN LEU ASP CYS LEU GLY          
SEQRES  19 B  252  ASN GLU LYS THR VAL CYS ARG CYS GLY ALA SER ASN CYS          
SEQRES  20 B  252  SER GLY PHE LEU GLY                                          
HET     ZN  A1301       1                                                       
HET     ZN  A1302       1                                                       
HET     ZN  A1303       1                                                       
HET    SAM  A1304      50                                                       
HET     ZN  B1301       1                                                       
HET     ZN  B1302       1                                                       
HET     ZN  B1303       1                                                       
HET    SAM  B1304      50                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  11  HOH   *528(H2 O)                                                    
HELIX    1 AA1 LYS A  973  GLN A  982  1                                  10    
HELIX    2 AA2 ASP A 1009  ILE A 1013  5                                   5    
HELIX    3 AA3 CYS A 1032  LEU A 1037  1                                   6    
HELIX    4 AA4 GLN A 1055  ARG A 1060  1                                   6    
HELIX    5 AA5 ASP A 1098  ASN A 1112  1                                  15    
HELIX    6 AA6 ASN A 1135  MET A 1140  5                                   6    
HELIX    7 AA7 ASN A 1178  LEU A 1181  5                                   4    
HELIX    8 AA8 GLU B  977  GLN B  982  1                                   6    
HELIX    9 AA9 ASP B 1009  ILE B 1013  5                                   5    
HELIX   10 AB1 CYS B 1032  LEU B 1037  1                                   6    
HELIX   11 AB2 GLN B 1055  ARG B 1060  1                                   6    
HELIX   12 AB3 ASP B 1098  ASN B 1112  1                                  15    
HELIX   13 AB4 TYR B 1136  MET B 1140  5                                   5    
HELIX   14 AB5 ASN B 1178  ASP B 1182  5                                   5    
SHEET    1 AA1 2 LYS A 992  HIS A 993  0                                        
SHEET    2 AA1 2 LYS A1133  GLY A1134  1  O  GLY A1134   N  LYS A 992           
SHEET    1 AA2 5 LYS A 998  PRO A 999  0                                        
SHEET    2 AA2 5 GLU A1095  ILE A1097  1  O  LEU A1096   N  LYS A 998           
SHEET    3 AA2 5 ARG A1126  ASP A1129 -1  O  ASP A1129   N  GLU A1095           
SHEET    4 AA2 5 MET A1119  ASP A1123 -1  N  LEU A1120   O  ILE A1128           
SHEET    5 AA2 5 CYS A1183  LEU A1184 -1  O  LEU A1184   N  MET A1119           
SHEET    1 AA3 2 THR A1065  LYS A1069  0                                        
SHEET    2 AA3 2 TRP A1075  ALA A1079 -1  O  GLY A1076   N  ILE A1068           
SHEET    1 AA4 3 PHE A1088  TYR A1092  0                                        
SHEET    2 AA4 3 ASP A1158  ALA A1165 -1  O  LEU A1163   N  VAL A1089           
SHEET    3 AA4 3 CYS A1148  VAL A1155 -1  N  VAL A1155   O  ASP A1158           
SHEET    1 AA5 2 ASN A1141  HIS A1142  0                                        
SHEET    2 AA5 2 THR A1176  PHE A1177  1  O  PHE A1177   N  ASN A1141           
SHEET    1 AA6 4 LYS B 992  HIS B 993  0                                        
SHEET    2 AA6 4 ARG B1126  GLY B1134  1  O  PRO B1132   N  LYS B 992           
SHEET    3 AA6 4 GLY B1094  ILE B1097 -1  N  GLU B1095   O  ASP B1129           
SHEET    4 AA6 4 LYS B 998  PRO B 999  1  N  LYS B 998   O  LEU B1096           
SHEET    1 AA7 3 LYS B 992  HIS B 993  0                                        
SHEET    2 AA7 3 ARG B1126  GLY B1134  1  O  PRO B1132   N  LYS B 992           
SHEET    3 AA7 3 MET B1119  ASP B1123 -1  N  LEU B1120   O  ILE B1128           
SHEET    1 AA8 2 THR B1065  LYS B1069  0                                        
SHEET    2 AA8 2 TRP B1075  ALA B1079 -1  O  GLY B1076   N  ILE B1068           
SHEET    1 AA9 3 PHE B1088  TYR B1092  0                                        
SHEET    2 AA9 3 ASP B1158  ALA B1165 -1  O  LEU B1163   N  VAL B1089           
SHEET    3 AA9 3 CYS B1148  VAL B1155 -1  N  TRP B1153   O  ARG B1160           
SHEET    1 AB1 2 ASN B1141  HIS B1142  0                                        
SHEET    2 AB1 2 THR B1176  PHE B1177  1  O  PHE B1177   N  ASN B1141           
LINK         SG  CYS A1016                ZN    ZN A1302     1555   1555  2.47  
LINK         SG  CYS A1018                ZN    ZN A1302     1555   1555  2.31  
LINK         SG  CYS A1026                ZN    ZN A1302     1555   1555  2.58  
LINK         SG  CYS A1026                ZN    ZN A1303     1555   1555  2.18  
LINK         SG  CYS A1032                ZN    ZN A1302     1555   1555  2.15  
LINK         SG  CYS A1041                ZN    ZN A1303     1555   1555  2.27  
LINK         SG  CYS A1046                ZN    ZN A1303     1555   1555  2.36  
LINK         SG  CYS A1052                ZN    ZN A1303     1555   1555  2.42  
LINK         SG  CYS A1144                ZN    ZN A1301     1555   1555  2.51  
LINK         SG  CYS A1191                ZN    ZN A1301     1555   1555  2.32  
LINK         SG  CYS A1193                ZN    ZN A1301     1555   1555  2.39  
LINK         SG  CYS A1198                ZN    ZN A1301     1555   1555  2.37  
LINK         SG  CYS B1016                ZN    ZN B1302     1555   1555  2.18  
LINK         SG  CYS B1018                ZN    ZN B1302     1555   1555  2.50  
LINK         SG  CYS B1026                ZN    ZN B1302     1555   1555  2.66  
LINK         SG  CYS B1026                ZN    ZN B1303     1555   1555  2.27  
LINK         SG  CYS B1032                ZN    ZN B1302     1555   1555  2.28  
LINK         SG  CYS B1041                ZN    ZN B1303     1555   1555  2.59  
LINK         SG  CYS B1046                ZN    ZN B1303     1555   1555  2.42  
LINK         SG  CYS B1052                ZN    ZN B1303     1555   1555  2.37  
LINK         SG  CYS B1144                ZN    ZN B1301     1555   1555  2.43  
LINK         SG  CYS B1191                ZN    ZN B1301     1555   1555  2.23  
LINK         SG  CYS B1193                ZN    ZN B1301     1555   1555  2.47  
LINK         SG  CYS B1198                ZN    ZN B1301     1555   1555  2.35  
SITE     1 AC1  4 CYS A1144  CYS A1191  CYS A1193  CYS A1198                    
SITE     1 AC2  4 CYS A1016  CYS A1018  CYS A1026  CYS A1032                    
SITE     1 AC3  4 CYS A1026  CYS A1041  CYS A1046  CYS A1052                    
SITE     1 AC4 18 ARG A1073  TRP A1075  THR A1115  HIS A1116                    
SITE     2 AC4 18 PHE A1117  TYR A1118  ARG A1138  PHE A1139                    
SITE     3 AC4 18 ASN A1141  HIS A1142  TYR A1179  ASN A1186                    
SITE     4 AC4 18 VAL A1190  CYS A1191  ARG A1192  HOH A1447                    
SITE     5 AC4 18 HOH A1471  HOH A1579                                          
SITE     1 AC5  4 CYS B1144  CYS B1191  CYS B1193  CYS B1198                    
SITE     1 AC6  4 CYS B1016  CYS B1018  CYS B1026  CYS B1032                    
SITE     1 AC7  4 CYS B1026  CYS B1041  CYS B1046  CYS B1052                    
SITE     1 AC8 20 ARG B1073  TRP B1075  THR B1115  HIS B1116                    
SITE     2 AC8 20 PHE B1117  TYR B1118  ARG B1138  PHE B1139                    
SITE     3 AC8 20 ASN B1141  HIS B1142  TYR B1179  ASN B1186                    
SITE     4 AC8 20 VAL B1190  CYS B1191  ARG B1192  CYS B1193                    
SITE     5 AC8 20 HOH B1407  HOH B1479  HOH B1492  HOH B1503                    
CRYST1   94.583   63.114   81.094  90.00  90.00  90.00 P 21 21 21    8          
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      0.010573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015844  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system