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Database: PDB
Entry: 5LT6
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HEADER    TRANSFERASE                             06-SEP-16   5LT6              
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 SETD2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1433-1711;                                    
COMPND   5 SYNONYM: HIF-1,HUNTINGTIN YEAST PARTNER B,HUNTINGTIN-INTERACTING     
COMPND   6 PROTEIN 1,HIP-1,HUNTINGTIN-INTERACTING PROTEIN B,LYSINE N-           
COMPND   7 METHYLTRANSFERASE 3A,SET DOMAIN-CONTAINING PROTEIN 2,HSET2,P231HBP;  
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069;             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RIL                            
KEYWDS    LYSINE METHYLTRANSFERASE SETD2 SET DOMAIN, SETD2#1, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TISI,P.PATHURI,T.HEIGHTMAN                                          
REVDAT   2   21-DEC-16 5LT6    1       JRNL                                     
REVDAT   1   05-OCT-16 5LT6    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.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 31328                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.231                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1565                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.05                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.12                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.03                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2855                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2390                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2715                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2370                   
REMARK   3   BIN FREE R VALUE                        : 0.2670                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.90                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 140                      
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            : 3630                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.16350                                              
REMARK   3    B22 (A**2) : -3.09560                                             
REMARK   3    B33 (A**2) : -5.06780                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -4.43480                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.260               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.195               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.171               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.191               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.170               
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      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3919   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5356   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1380   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 109    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 576    ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3919   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 3      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 485    ; 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   : 4398   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.012                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.10                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.77                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1446 - A|1690 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   28.0254   11.9648   64.7015           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0765 T22:   -0.1302                                    
REMARK   3     T33:   -0.1169 T12:    0.0148                                    
REMARK   3     T13:   -0.0290 T23:    0.0166                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4748 L22:    2.1647                                    
REMARK   3     L33:    2.0727 L12:    0.0885                                    
REMARK   3     L13:   -0.1510 L23:    0.5092                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0320 S12:    0.0039 S13:   -0.0430                     
REMARK   3     S21:   -0.0140 S22:    0.0182 S23:    0.0832                     
REMARK   3     S31:    0.0964 S32:    0.0654 S33:    0.0138                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1447 - B|1689 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   56.9668   15.8801   35.6808           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1674 T22:   -0.0861                                    
REMARK   3     T33:   -0.1914 T12:    0.0445                                    
REMARK   3     T13:    0.0577 T23:    0.0827                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4297 L22:    1.8825                                    
REMARK   3     L33:    3.0448 L12:    0.1755                                    
REMARK   3     L13:    0.9257 L23:    0.3511                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2962 S12:   -0.0094 S13:   -0.0544                     
REMARK   3     S21:    0.0687 S22:    0.1729 S23:    0.2104                     
REMARK   3     S31:   -0.1545 S32:    0.0262 S33:    0.1232                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5LT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001307.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-12                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1MHEPES,PH7.3, 0.1MKSCN, 25            
REMARK 280  -30%MPEG2000., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.35000            
REMARK 290   SMTRY3   2  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  1417                                                      
REMARK 465     HIS A  1418                                                      
REMARK 465     HIS A  1419                                                      
REMARK 465     HIS A  1420                                                      
REMARK 465     HIS A  1421                                                      
REMARK 465     HIS A  1422                                                      
REMARK 465     HIS A  1423                                                      
REMARK 465     SER A  1424                                                      
REMARK 465     SER A  1425                                                      
REMARK 465     GLY A  1426                                                      
REMARK 465     ARG A  1427                                                      
REMARK 465     GLU A  1428                                                      
REMARK 465     ASN A  1429                                                      
REMARK 465     LEU A  1430                                                      
REMARK 465     TYR A  1431                                                      
REMARK 465     PHE A  1432                                                      
REMARK 465     GLN A  1433                                                      
REMARK 465     GLY A  1434                                                      
REMARK 465     GLU A  1435                                                      
REMARK 465     THR A  1436                                                      
REMARK 465     SER A  1437                                                      
REMARK 465     VAL A  1438                                                      
REMARK 465     PRO A  1439                                                      
REMARK 465     PRO A  1440                                                      
REMARK 465     GLY A  1441                                                      
REMARK 465     SER A  1442                                                      
REMARK 465     ALA A  1443                                                      
REMARK 465     LEU A  1444                                                      
REMARK 465     VAL A  1445                                                      
REMARK 465     LYS A  1486                                                      
REMARK 465     LYS A  1487                                                      
REMARK 465     ASN A  1488                                                      
REMARK 465     LYS A  1489                                                      
REMARK 465     SER A  1490                                                      
REMARK 465     HIS A  1491                                                      
REMARK 465     ARG A  1492                                                      
REMARK 465     ASP A  1493                                                      
REMARK 465     ILE A  1494                                                      
REMARK 465     LYS A  1495                                                      
REMARK 465     ARG A  1496                                                      
REMARK 465     GLY A  1691                                                      
REMARK 465     GLU A  1692                                                      
REMARK 465     ASN A  1693                                                      
REMARK 465     ARG A  1694                                                      
REMARK 465     VAL A  1695                                                      
REMARK 465     SER A  1696                                                      
REMARK 465     ILE A  1697                                                      
REMARK 465     ARG A  1698                                                      
REMARK 465     ALA A  1699                                                      
REMARK 465     ALA A  1700                                                      
REMARK 465     GLY A  1701                                                      
REMARK 465     GLY A  1702                                                      
REMARK 465     LYS A  1703                                                      
REMARK 465     MET A  1704                                                      
REMARK 465     LYS A  1705                                                      
REMARK 465     LYS A  1706                                                      
REMARK 465     GLU A  1707                                                      
REMARK 465     ARG A  1708                                                      
REMARK 465     SER A  1709                                                      
REMARK 465     ARG A  1710                                                      
REMARK 465     LYS A  1711                                                      
REMARK 465     MET B  1417                                                      
REMARK 465     HIS B  1418                                                      
REMARK 465     HIS B  1419                                                      
REMARK 465     HIS B  1420                                                      
REMARK 465     HIS B  1421                                                      
REMARK 465     HIS B  1422                                                      
REMARK 465     HIS B  1423                                                      
REMARK 465     SER B  1424                                                      
REMARK 465     SER B  1425                                                      
REMARK 465     GLY B  1426                                                      
REMARK 465     ARG B  1427                                                      
REMARK 465     GLU B  1428                                                      
REMARK 465     ASN B  1429                                                      
REMARK 465     LEU B  1430                                                      
REMARK 465     TYR B  1431                                                      
REMARK 465     PHE B  1432                                                      
REMARK 465     GLN B  1433                                                      
REMARK 465     GLY B  1434                                                      
REMARK 465     GLU B  1435                                                      
REMARK 465     THR B  1436                                                      
REMARK 465     SER B  1437                                                      
REMARK 465     VAL B  1438                                                      
REMARK 465     PRO B  1439                                                      
REMARK 465     PRO B  1440                                                      
REMARK 465     GLY B  1441                                                      
REMARK 465     SER B  1442                                                      
REMARK 465     ALA B  1443                                                      
REMARK 465     LEU B  1444                                                      
REMARK 465     VAL B  1445                                                      
REMARK 465     GLY B  1446                                                      
REMARK 465     GLU B  1484                                                      
REMARK 465     ARG B  1485                                                      
REMARK 465     LYS B  1486                                                      
REMARK 465     LYS B  1487                                                      
REMARK 465     ASN B  1488                                                      
REMARK 465     LYS B  1489                                                      
REMARK 465     SER B  1490                                                      
REMARK 465     HIS B  1491                                                      
REMARK 465     ARG B  1492                                                      
REMARK 465     ASP B  1493                                                      
REMARK 465     ILE B  1494                                                      
REMARK 465     LYS B  1495                                                      
REMARK 465     TYR B  1671                                                      
REMARK 465     GLY B  1672                                                      
REMARK 465     LYS B  1673                                                      
REMARK 465     GLU B  1674                                                      
REMARK 465     GLY B  1690                                                      
REMARK 465     GLY B  1691                                                      
REMARK 465     GLU B  1692                                                      
REMARK 465     ASN B  1693                                                      
REMARK 465     ARG B  1694                                                      
REMARK 465     VAL B  1695                                                      
REMARK 465     SER B  1696                                                      
REMARK 465     ILE B  1697                                                      
REMARK 465     ARG B  1698                                                      
REMARK 465     ALA B  1699                                                      
REMARK 465     ALA B  1700                                                      
REMARK 465     GLY B  1701                                                      
REMARK 465     GLY B  1702                                                      
REMARK 465     LYS B  1703                                                      
REMARK 465     MET B  1704                                                      
REMARK 465     LYS B  1705                                                      
REMARK 465     LYS B  1706                                                      
REMARK 465     GLU B  1707                                                      
REMARK 465     ARG B  1708                                                      
REMARK 465     SER B  1709                                                      
REMARK 465     ARG B  1710                                                      
REMARK 465     LYS B  1711                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A1458    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1459    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A1478    CD   OE1  OE2                                       
REMARK 470     MET A1497    CG   SD   CE                                        
REMARK 470     LYS A1506    CG   CD   CE   NZ                                   
REMARK 470     ASP A1507    CG   OD1  OD2                                       
REMARK 470     GLN A1511    CG   CD   OE1  NE2                                  
REMARK 470     ILE A1514    CD1                                                 
REMARK 470     GLU A1518    CG   CD   OE1  OE2                                  
REMARK 470     ASN A1599    CG   OD1  ND2                                       
REMARK 470     LYS A1600    CG   CD   CE   NZ                                   
REMARK 470     ASN A1611    CG   OD1  ND2                                       
REMARK 470     LYS A1673    CG   CD   CE   NZ                                   
REMARK 470     GLU A1674    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1458    CG   CD   OE1  NE2                                  
REMARK 470     ARG B1459    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B1468    CG   CD   CE   NZ                                   
REMARK 470     ARG B1496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B1497    CG   SD   CE                                        
REMARK 470     LYS B1506    CG   CD   CE   NZ                                   
REMARK 470     ASP B1507    CG   OD1  OD2                                       
REMARK 470     GLN B1511    CG   CD   OE1  NE2                                  
REMARK 470     ILE B1514    CD1                                                 
REMARK 470     ARG B1598    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1670    CG   CD   NE   CZ   NH1  NH2                        
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    VAL A1576      -68.05    -91.33                                   
REMARK 500    ALA A1597       11.23    -69.89                                   
REMARK 500    ARG A1598      -51.95   -121.32                                   
REMARK 500    LYS A1600      -32.29     66.30                                   
REMARK 500    CYS B1471      133.20    -37.77                                   
REMARK 500    MET B1497      173.46    161.31                                   
REMARK 500    ASN B1541       40.01   -108.31                                   
REMARK 500    VAL B1576      -70.41    -90.53                                   
REMARK 500    ALA B1597       42.29    -75.82                                   
REMARK 500    ARG B1598       16.39   -157.55                                   
REMARK 500    ASN B1599      100.18   -163.56                                   
REMARK 500    ASP B1612       -2.18     80.15                                   
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 A1803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  110.3                                              
REMARK 620 3 CYS A1516   SG   99.6 106.6                                        
REMARK 620 4 CYS A1520   SG  117.4 114.6 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1516   SG                                                     
REMARK 620 2 CYS A1529   SG  113.2                                              
REMARK 620 3 CYS A1533   SG  101.1 111.3                                        
REMARK 620 4 CYS A1539   SG  117.1 106.7 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1631   SG                                                     
REMARK 620 2 CYS A1678   SG  113.0                                              
REMARK 620 3 CYS A1680   SG  106.7 106.3                                        
REMARK 620 4 CYS A1685   SG  113.4 106.5 110.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1499   SG                                                     
REMARK 620 2 CYS B1501   SG  111.1                                              
REMARK 620 3 CYS B1516   SG  101.0 109.2                                        
REMARK 620 4 CYS B1520   SG  115.9 111.6 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1516   SG                                                     
REMARK 620 2 CYS B1529   SG  112.8                                              
REMARK 620 3 CYS B1533   SG  103.4 114.3                                        
REMARK 620 4 CYS B1539   SG  113.5 106.5 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1631   SG                                                     
REMARK 620 2 CYS B1678   SG  113.1                                              
REMARK 620 3 CYS B1680   SG  108.5 107.2                                        
REMARK 620 4 CYS B1685   SG  117.5 111.3  97.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76J A 1805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76J B 1805                
DBREF  5LT6 A 1433  1711  UNP    Q9BYW2   SETD2_HUMAN   1433   1711             
DBREF  5LT6 B 1433  1711  UNP    Q9BYW2   SETD2_HUMAN   1433   1711             
SEQADV 5LT6 MET A 1417  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5LT6 HIS A 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS A 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS A 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS A 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS A 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS A 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 SER A 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 SER A 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 GLY A 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 ARG A 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 GLU A 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 ASN A 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 LEU A 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 TYR A 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 PHE A 1432  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 MET B 1417  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5LT6 HIS B 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS B 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS B 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS B 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS B 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 HIS B 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 SER B 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 SER B 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 GLY B 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 ARG B 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 GLU B 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 ASN B 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 LEU B 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 TYR B 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT6 PHE B 1432  UNP  Q9BYW2              EXPRESSION TAG                 
SEQRES   1 A  295  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  295  LEU TYR PHE GLN GLY GLU THR SER VAL PRO PRO GLY SER          
SEQRES   3 A  295  ALA LEU VAL GLY PRO SER CYS VAL MET ASP ASP PHE ARG          
SEQRES   4 A  295  ASP PRO GLN ARG TRP LYS GLU CYS ALA LYS GLN GLY LYS          
SEQRES   5 A  295  MET PRO CYS TYR PHE ASP LEU ILE GLU GLU ASN VAL TYR          
SEQRES   6 A  295  LEU THR GLU ARG LYS LYS ASN LYS SER HIS ARG ASP ILE          
SEQRES   7 A  295  LYS ARG MET GLN CYS GLU CYS THR PRO LEU SER LYS ASP          
SEQRES   8 A  295  GLU ARG ALA GLN GLY GLU ILE ALA CYS GLY GLU ASP CYS          
SEQRES   9 A  295  LEU ASN ARG LEU LEU MET ILE GLU CYS SER SER ARG CYS          
SEQRES  10 A  295  PRO ASN GLY ASP TYR CYS SER ASN ARG ARG PHE GLN ARG          
SEQRES  11 A  295  LYS GLN HIS ALA ASP VAL GLU VAL ILE LEU THR GLU LYS          
SEQRES  12 A  295  LYS GLY TRP GLY LEU ARG ALA ALA LYS ASP LEU PRO SER          
SEQRES  13 A  295  ASN THR PHE VAL LEU GLU TYR CYS GLY GLU VAL LEU ASP          
SEQRES  14 A  295  HIS LYS GLU PHE LYS ALA ARG VAL LYS GLU TYR ALA ARG          
SEQRES  15 A  295  ASN LYS ASN ILE HIS TYR TYR PHE MET ALA LEU LYS ASN          
SEQRES  16 A  295  ASP GLU ILE ILE ASP ALA THR GLN LYS GLY ASN CYS SER          
SEQRES  17 A  295  ARG PHE MET ASN HIS SER CYS GLU PRO ASN CYS GLU THR          
SEQRES  18 A  295  GLN LYS TRP THR VAL ASN GLY GLN LEU ARG VAL GLY PHE          
SEQRES  19 A  295  PHE THR THR LYS LEU VAL PRO SER GLY SER GLU LEU THR          
SEQRES  20 A  295  PHE ASP TYR GLN PHE GLN ARG TYR GLY LYS GLU ALA GLN          
SEQRES  21 A  295  LYS CYS PHE CYS GLY SER ALA ASN CYS ARG GLY TYR LEU          
SEQRES  22 A  295  GLY GLY GLU ASN ARG VAL SER ILE ARG ALA ALA GLY GLY          
SEQRES  23 A  295  LYS MET LYS LYS GLU ARG SER ARG LYS                          
SEQRES   1 B  295  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 B  295  LEU TYR PHE GLN GLY GLU THR SER VAL PRO PRO GLY SER          
SEQRES   3 B  295  ALA LEU VAL GLY PRO SER CYS VAL MET ASP ASP PHE ARG          
SEQRES   4 B  295  ASP PRO GLN ARG TRP LYS GLU CYS ALA LYS GLN GLY LYS          
SEQRES   5 B  295  MET PRO CYS TYR PHE ASP LEU ILE GLU GLU ASN VAL TYR          
SEQRES   6 B  295  LEU THR GLU ARG LYS LYS ASN LYS SER HIS ARG ASP ILE          
SEQRES   7 B  295  LYS ARG MET GLN CYS GLU CYS THR PRO LEU SER LYS ASP          
SEQRES   8 B  295  GLU ARG ALA GLN GLY GLU ILE ALA CYS GLY GLU ASP CYS          
SEQRES   9 B  295  LEU ASN ARG LEU LEU MET ILE GLU CYS SER SER ARG CYS          
SEQRES  10 B  295  PRO ASN GLY ASP TYR CYS SER ASN ARG ARG PHE GLN ARG          
SEQRES  11 B  295  LYS GLN HIS ALA ASP VAL GLU VAL ILE LEU THR GLU LYS          
SEQRES  12 B  295  LYS GLY TRP GLY LEU ARG ALA ALA LYS ASP LEU PRO SER          
SEQRES  13 B  295  ASN THR PHE VAL LEU GLU TYR CYS GLY GLU VAL LEU ASP          
SEQRES  14 B  295  HIS LYS GLU PHE LYS ALA ARG VAL LYS GLU TYR ALA ARG          
SEQRES  15 B  295  ASN LYS ASN ILE HIS TYR TYR PHE MET ALA LEU LYS ASN          
SEQRES  16 B  295  ASP GLU ILE ILE ASP ALA THR GLN LYS GLY ASN CYS SER          
SEQRES  17 B  295  ARG PHE MET ASN HIS SER CYS GLU PRO ASN CYS GLU THR          
SEQRES  18 B  295  GLN LYS TRP THR VAL ASN GLY GLN LEU ARG VAL GLY PHE          
SEQRES  19 B  295  PHE THR THR LYS LEU VAL PRO SER GLY SER GLU LEU THR          
SEQRES  20 B  295  PHE ASP TYR GLN PHE GLN ARG TYR GLY LYS GLU ALA GLN          
SEQRES  21 B  295  LYS CYS PHE CYS GLY SER ALA ASN CYS ARG GLY TYR LEU          
SEQRES  22 B  295  GLY GLY GLU ASN ARG VAL SER ILE ARG ALA ALA GLY GLY          
SEQRES  23 B  295  LYS MET LYS LYS GLU ARG SER ARG LYS                          
HET     ZN  A1801       1                                                       
HET     ZN  A1802       1                                                       
HET     ZN  A1803       1                                                       
HET    SCN  A1804       3                                                       
HET    76J  A1805      66                                                       
HET     ZN  B1801       1                                                       
HET     ZN  B1802       1                                                       
HET     ZN  B1803       1                                                       
HET    SCN  B1804       3                                                       
HET    76J  B1805      66                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     76J [(2~{S},5~{S})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-                
HETNAM   2 76J  AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]-5-               
HETNAM   3 76J  AZANIUMYL-6-OXIDANYL-6-OXIDANYLIDENE-HEXAN-2-YL]-               
HETNAM   4 76J  PENTYL-AZANIUM                                                  
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  SCN    2(C N S 1-)                                                  
FORMUL   7  76J    2(C20 H35 N7 O5 2+)                                          
FORMUL  13  HOH   *263(H2 O)                                                    
HELIX    1 AA1 ASP A 1452  ARG A 1455  5                                   4    
HELIX    2 AA2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3 AA3 SER A 1505  GLN A 1511  1                                   7    
HELIX    4 AA4 CYS A 1520  LEU A 1525  1                                   6    
HELIX    5 AA5 ASN A 1535  CYS A 1539  5                                   5    
HELIX    6 AA6 ASP A 1585  LYS A 1600  1                                  16    
HELIX    7 AA7 ASN A 1622  MET A 1627  5                                   6    
HELIX    8 AA8 ASP A 1665  GLN A 1669  5                                   5    
HELIX    9 AA9 ASP B 1452  ARG B 1455  5                                   4    
HELIX   10 AB1 ASP B 1456  GLN B 1466  1                                  11    
HELIX   11 AB2 SER B 1505  GLN B 1511  1                                   7    
HELIX   12 AB3 CYS B 1520  LEU B 1525  1                                   6    
HELIX   13 AB4 ASN B 1535  CYS B 1539  5                                   5    
HELIX   14 AB5 ASP B 1585  ALA B 1597  1                                  13    
HELIX   15 AB6 ASN B 1622  MET B 1627  5                                   6    
HELIX   16 AB7 ASP B 1665  GLN B 1669  5                                   5    
SHEET    1 AA1 5 SER A1448  CYS A1449  0                                        
SHEET    2 AA1 5 VAL A1552  LEU A1556 -1  O  VAL A1554   N  CYS A1449           
SHEET    3 AA1 5 TRP A1562  ALA A1566 -1  O  ARG A1565   N  GLU A1553           
SHEET    4 AA1 5 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    5 AA1 5 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
SHEET    1 AA2 2 ASP A1474  LEU A1475  0                                        
SHEET    2 AA2 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1 AA3 5 VAL A1480  TYR A1481  0                                        
SHEET    2 AA3 5 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3 AA3 5 GLU A1613  ASP A1616 -1  O  ASP A1616   N  GLU A1582           
SHEET    4 AA3 5 TYR A1605  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    5 AA3 5 ARG A1670  TYR A1671 -1  O  ARG A1670   N  PHE A1606           
SHEET    1 AA4 3 PHE A1575  GLU A1578  0                                        
SHEET    2 AA4 3 GLN A1645  THR A1652 -1  O  PHE A1650   N  VAL A1576           
SHEET    3 AA4 3 CYS A1635  VAL A1642 -1  N  TRP A1640   O  ARG A1647           
SHEET    1 AA5 2 GLN A1676  LYS A1677  0                                        
SHEET    2 AA5 2 TYR A1688  LEU A1689 -1  O  LEU A1689   N  GLN A1676           
SHEET    1 AA6 5 SER B1448  CYS B1449  0                                        
SHEET    2 AA6 5 VAL B1552  LEU B1556 -1  O  VAL B1554   N  CYS B1449           
SHEET    3 AA6 5 TRP B1562  ALA B1566 -1  O  ARG B1565   N  GLU B1553           
SHEET    4 AA6 5 GLU B1661  PHE B1664 -1  O  LEU B1662   N  LEU B1564           
SHEET    5 AA6 5 ASN B1628  HIS B1629  1  N  ASN B1628   O  PHE B1664           
SHEET    1 AA7 2 ASP B1474  LEU B1475  0                                        
SHEET    2 AA7 2 LYS B1620  GLY B1621  1  O  GLY B1621   N  ASP B1474           
SHEET    1 AA8 4 VAL B1480  TYR B1481  0                                        
SHEET    2 AA8 4 GLU B1582  LEU B1584  1  O  VAL B1583   N  VAL B1480           
SHEET    3 AA8 4 GLU B1613  ASP B1616 -1  O  ASP B1616   N  GLU B1582           
SHEET    4 AA8 4 PHE B1606  LYS B1610 -1  N  MET B1607   O  ILE B1615           
SHEET    1 AA9 3 PHE B1575  GLU B1578  0                                        
SHEET    2 AA9 3 GLN B1645  THR B1652 -1  O  PHE B1650   N  VAL B1576           
SHEET    3 AA9 3 CYS B1635  VAL B1642 -1  N  VAL B1642   O  GLN B1645           
LINK         SG  CYS A1499                ZN    ZN A1803     1555   1555  2.37  
LINK         SG  CYS A1501                ZN    ZN A1803     1555   1555  2.44  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.15  
LINK         SG  CYS A1516                ZN    ZN A1803     1555   1555  2.57  
LINK         SG  CYS A1520                ZN    ZN A1803     1555   1555  2.23  
LINK         SG  CYS A1529                ZN    ZN A1802     1555   1555  2.46  
LINK         SG  CYS A1533                ZN    ZN A1802     1555   1555  2.50  
LINK         SG  CYS A1539                ZN    ZN A1802     1555   1555  2.38  
LINK         SG  CYS A1631                ZN    ZN A1801     1555   1555  2.22  
LINK         SG  CYS A1678                ZN    ZN A1801     1555   1555  2.28  
LINK         SG  CYS A1680                ZN    ZN A1801     1555   1555  2.36  
LINK         SG  CYS A1685                ZN    ZN A1801     1555   1555  2.40  
LINK         SG  CYS B1499                ZN    ZN B1801     1555   1555  2.29  
LINK         SG  CYS B1501                ZN    ZN B1801     1555   1555  2.48  
LINK         SG  CYS B1516                ZN    ZN B1802     1555   1555  2.15  
LINK         SG  CYS B1516                ZN    ZN B1801     1555   1555  2.52  
LINK         SG  CYS B1520                ZN    ZN B1801     1555   1555  2.28  
LINK         SG  CYS B1529                ZN    ZN B1802     1555   1555  2.44  
LINK         SG  CYS B1533                ZN    ZN B1802     1555   1555  2.46  
LINK         SG  CYS B1539                ZN    ZN B1802     1555   1555  2.42  
LINK         SG  CYS B1631                ZN    ZN B1803     1555   1555  2.38  
LINK         SG  CYS B1678                ZN    ZN B1803     1555   1555  2.18  
LINK         SG  CYS B1680                ZN    ZN B1803     1555   1555  2.47  
LINK         SG  CYS B1685                ZN    ZN B1803     1555   1555  2.79  
SITE     1 AC1  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC2  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC3  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC4  6 MET A1497  CYS A1499  ASN A1522  CYS A1529                    
SITE     2 AC4  6 SER A1530  CYS A1533                                          
SITE     1 AC5 18 LYS A1560  GLY A1561  TRP A1562  TYR A1579                    
SITE     2 AC5 18 TYR A1605  SER A1624  ARG A1625  ASN A1628                    
SITE     3 AC5 18 HIS A1629  PHE A1664  TYR A1666  GLN A1676                    
SITE     4 AC5 18 LYS A1677  CYS A1678  PHE A1679  LEU A1689                    
SITE     5 AC5 18 HOH A1922  HOH A1928                                          
SITE     1 AC6  4 CYS B1499  CYS B1501  CYS B1516  CYS B1520                    
SITE     1 AC7  4 CYS B1516  CYS B1529  CYS B1533  CYS B1539                    
SITE     1 AC8  4 CYS B1631  CYS B1678  CYS B1680  CYS B1685                    
SITE     1 AC9  7 MET B1497  GLN B1498  CYS B1499  ASN B1522                    
SITE     2 AC9  7 CYS B1529  SER B1530  CYS B1533                               
SITE     1 AD1 19 LYS B1560  GLY B1561  TRP B1562  TYR B1579                    
SITE     2 AD1 19 TYR B1605  SER B1624  ARG B1625  MET B1627                    
SITE     3 AD1 19 ASN B1628  HIS B1629  TYR B1666  GLN B1669                    
SITE     4 AD1 19 GLN B1676  LYS B1677  CYS B1678  PHE B1679                    
SITE     5 AD1 19 HOH B1918  HOH B1940  HOH B1941                               
CRYST1   57.360   72.700   61.860  90.00  89.77  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017434  0.000000 -0.000070        0.00000                         
SCALE2      0.000000  0.013755  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016166        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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