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Database: PDB
Entry: 4JT9
LinkDB: 4JT9
Original site: 4JT9 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           22-MAR-13   4JT9              
TITLE     CRYSTAL STRUCTURE OF HUMAN SIRT3 WITH ELT INHIBITOR 3 [14-(4-{2-      
TITLE    2 [(METHYLSULFONYL)AMINO]ETHYL}PIPERIDIN-1-YL)THIENO[3,2-D]PYRIMIDINE- 
TITLE    3 6-CARBOXAMIDE]                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL;
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 118-399;                                      
COMPND   5 SYNONYM: HSIRT3, REGULATORY PROTEIN SIR2 HOMOLOG 3, SIR2-LIKE PROTEIN
COMPND   6 3;                                                                   
COMPND   7 EC: 3.5.1.-;                                                         
COMPND   8 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: SIRT3, SIR2L3;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEACETYLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.DAI                                                                 
REVDAT   2   03-JUL-13 4JT9    1       JRNL                                     
REVDAT   1   24-APR-13 4JT9    0                                                
JRNL        AUTH   J.S.DISCH,G.EVINDAR,C.H.CHIU,C.A.BLUM,H.DAI,L.JIN,E.SCHUMAN, 
JRNL        AUTH 2 K.E.LIND,S.L.BELYANSKAYA,J.DENG,F.COPPO,L.AQUILANI,          
JRNL        AUTH 3 T.L.GRAYBILL,J.W.CUOZZO,S.LAVU,C.MAO,G.P.VLASUK,R.B.PERNI    
JRNL        TITL   DISCOVERY OF THIENO[3,2-D]PYRIMIDINE-6-CARBOXAMIDES AS       
JRNL        TITL 2 POTENT INHIBITORS OF SIRT1, SIRT2, AND SIRT3.                
JRNL        REF    J.MED.CHEM.                   V.  56  3666 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23570514                                                     
JRNL        DOI    10.1021/JM400204K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 16756                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 900                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1151                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2145                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.263         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.215         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.990         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2269 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3093 ; 1.270 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   279 ; 5.527 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;34.589 ;22.828       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   361 ;14.176 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.413 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   343 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1738 ; 0.005 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1390 ; 0.599 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2262 ; 1.137 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   879 ; 1.618 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   831 ; 2.708 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4JT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078475.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16756                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.64533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       14.82267            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       22.23400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        7.41133            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.05667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   115                                                      
REMARK 465     ASN A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     ASP A   395                                                      
REMARK 465     GLY A   396                                                      
REMARK 465     PRO A   397                                                      
REMARK 465     ASP A   398                                                      
REMARK 465     LYS A   399                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   681     O    HOH A   687              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 167       51.93   -119.76                                   
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 A 646        DISTANCE =  5.31 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                              NA A 405  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 653   O                                                      
REMARK 620 2 HOH A 629   O    95.4                                              
REMARK 620 3 HOH A 628   O    67.3  66.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 280   SG                                                     
REMARK 620 2 CYS A 256   SG  110.6                                              
REMARK 620 3 CYS A 283   SG  117.0  93.6                                        
REMARK 620 4 CYS A 259   SG  108.5 108.7 117.3                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JSR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JT8   RELATED DB: PDB                                   
DBREF  4JT9 A  118   399  UNP    Q9NTG7   SIR3_HUMAN     118    399             
SEQADV 4JT9 SER A  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 4JT9 ASN A  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 4JT9 ALA A  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQRES   1 A  285  SER ASN ALA SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 A  285  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 A  285  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 A  285  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 A  285  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 A  285  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 A  285  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 A  285  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 A  285  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 A  285  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 A  285  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 A  285  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 A  285  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 A  285  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 A  285  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 A  285  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 A  285  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 A  285  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 A  285  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 A  285  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 A  285  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 A  285  GLN ARG GLU THR GLY LYS LEU ASP GLY PRO ASP LYS              
HET     ZN  A 401       1                                                       
HET    1NS  A 402      25                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET     NA  A 405       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     1NS 4-(4-{2-[(METHYLSULFONYL)AMINO]ETHYL}PIPERIDIN-1-YL)             
HETNAM   2 1NS  THIENO[3,2-D]PYRIMIDINE-6-CARBOXAMIDE                           
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  1NS    C15 H21 N5 O3 S2                                             
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6   NA    NA 1+                                                        
FORMUL   7  HOH   *191(H2 O)                                                    
HELIX    1   1 SER A  124  ALA A  134  1                                  11    
HELIX    2   2 ALA A  146  GLY A  153  5                                   8    
HELIX    3   3 GLY A  163  SER A  166  5                                   4    
HELIX    4   4 ASN A  167  ASP A  172  1                                   6    
HELIX    5   5 TYR A  175  PHE A  180  5                                   6    
HELIX    6   6 GLU A  181  ASN A  188  1                                   8    
HELIX    7   7 PRO A  189  TYR A  200  1                                  12    
HELIX    8   8 ASN A  207  LYS A  219  1                                  13    
HELIX    9   9 GLY A  232  SER A  237  1                                   6    
HELIX   10  10 PRO A  240  SER A  242  5                                   3    
HELIX   11  11 ILE A  268  ALA A  274  1                                   7    
HELIX   12  12 PRO A  299  LEU A  303  5                                   5    
HELIX   13  13 LEU A  304  ALA A  312  1                                   9    
HELIX   14  14 PRO A  326  THR A  331  1                                   6    
HELIX   15  15 GLY A  349  HIS A  354  1                                   6    
HELIX   16  16 ASP A  365  GLY A  378  1                                  14    
HELIX   17  17 TRP A  379  GLY A  392  1                                  14    
SHEET    1   A 6 LEU A 244  GLU A 246  0                                        
SHEET    2   A 6 LEU A 222  THR A 227  1  N  LEU A 225   O  VAL A 245           
SHEET    3   A 6 VAL A 140  VAL A 144  1  N  VAL A 142   O  TYR A 226           
SHEET    4   A 6 LEU A 314  LEU A 318  1  O  LEU A 316   N  VAL A 141           
SHEET    5   A 6 ARG A 340  ASN A 344  1  O  ILE A 343   N  ILE A 317           
SHEET    6   A 6 ASP A 359  LEU A 363  1  O  GLN A 362   N  LEU A 342           
SHEET    1   B 3 PRO A 262  PRO A 264  0                                        
SHEET    2   B 3 GLY A 249  CYS A 256 -1  N  ALA A 254   O  PHE A 263           
SHEET    3   B 3 VAL A 287  ILE A 291 -1  O  ASP A 290   N  SER A 253           
LINK        NA    NA A 405                 O   HOH A 653     1555   1555  2.10  
LINK         SG  CYS A 280                ZN    ZN A 401     1555   1555  2.26  
LINK         SG  CYS A 256                ZN    ZN A 401     1555   1555  2.31  
LINK         SG  CYS A 283                ZN    ZN A 401     1555   1555  2.34  
LINK         SG  CYS A 259                ZN    ZN A 401     1555   1555  2.35  
LINK        NA    NA A 405                 O   HOH A 629     1555   1555  2.79  
LINK        NA    NA A 405                 O   HOH A 628     1555   1555  2.84  
CISPEP   1 GLU A  325    PRO A  326          0         7.69                     
SITE     1 AC1  4 CYS A 256  CYS A 259  CYS A 280  CYS A 283                    
SITE     1 AC2 14 ILE A 154  ASP A 156  PHE A 157  GLN A 228                    
SITE     2 AC2 14 ASN A 229  ILE A 230  ASP A 231  HIS A 248                    
SITE     3 AC2 14 VAL A 292  PHE A 294  GOL A 403  GOL A 404                    
SITE     4 AC2 14 HOH A 522  HOH A 614                                          
SITE     1 AC3  5 PHE A 294  GLY A 295  GLU A 296  LEU A 298                    
SITE     2 AC3  5 1NS A 402                                                     
SITE     1 AC4  5 GLY A 145  ALA A 146  GLN A 228  ASN A 229                    
SITE     2 AC4  5 1NS A 402                                                     
SITE     1 AC5  6 HIS A 187  HIS A 354  HOH A 611  HOH A 628                    
SITE     2 AC5  6 HOH A 629  HOH A 653                                          
CRYST1  120.464  120.464   44.468  90.00  90.00 120.00 P 65          6          
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      0.008301  0.004793  0.000000        0.00000                         
SCALE2      0.000000  0.009585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022488        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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