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Database: PDB
Entry: 4BVG
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Original site: 4BVG 
HEADER    HYDROLASE/LIGASE                        25-JUN-13   4BVG              
TITLE     CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH NATIVE ALKYLIMIDATE  
TITLE    2 FORMED FROM ACETYL-LYSINE ACS2-PEPTIDE CRYSTALLIZED IN PRESENCE OF   
TITLE    3 THE INHIBITOR EX-527                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL;
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 116-399;                                          
COMPND   5 SYNONYM: SIRT3, HSIRT3, REGULATORY PROTEIN SIR2 HOMOLOG 3, SIR2-LIKE 
COMPND   6 PROTEIN 3;                                                           
COMPND   7 EC: 3.5.1.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ACETYL-COENZYME A SYNTHETASE 2-LIKE, MITOCHONDRIAL;        
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RESIDUES 638-647;                                          
COMPND  13 SYNONYM: ACETYL-LYSINE ACS2-PEPTIDE, ACETATE--COA LIGASE 2, ACETYL-C 
COMPND  14 ACECS2, ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 1;             
COMPND  15 EC: 6.2.1.1;                                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVFT3S;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    HYDROLASE-LIGASE COMPLEX, NAD-DEPENDENT DEACETYLASE, NATIVE           
KEYWDS   2 INTERMEDIATE                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.T.T.NGUYEN,M.GERTZ,M.WEYAND,C.STEEGBORN                             
REVDAT   3   30-JAN-19 4BVG    1       COMPND JRNL   REMARK HET                 
REVDAT   3 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   3 3                   1       SITE   ATOM                              
REVDAT   2   07-AUG-13 4BVG    1       JRNL                                     
REVDAT   1   17-JUL-13 4BVG    0                                                
JRNL        AUTH   M.GERTZ,F.FISCHER,G.T.NGUYEN,M.LAKSHMINARASIMHAN,            
JRNL        AUTH 2 M.SCHUTKOWSKI,M.WEYAND,C.STEEGBORN                           
JRNL        TITL   EX-527 INHIBITS SIRTUINS BY EXPLOITING THEIR UNIQUE          
JRNL        TITL 2 NAD+-DEPENDENT DEACETYLATION MECHANISM.                      
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 110 E2772 2013              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   23840057                                                     
JRNL        DOI    10.1073/PNAS.1303628110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12267                          
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 646                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 911                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2207                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.438         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.285         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.264         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2356 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3188 ; 1.936 ; 2.025       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   279 ; 6.484 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;35.028 ;22.551       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   368 ;17.410 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;18.704 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   364 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1736 ; 0.009 ; 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):  1122 ; 3.395 ; 3.981       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1399 ; 5.349 ; 5.954       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1233 ; 4.031 ; 4.405       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U      
REMARK   3  VALUES REFINED INDIVIDUALLY                                         
REMARK   4                                                                      
REMARK   4 4BVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290057457.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : COLLIMATOR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12915                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3GLT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M (NH4)2SO4, 0.1M BISTRIS PH 5.5,    
REMARK 280  21% PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.25400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.25400            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.01150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.66450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.01150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.66450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.25400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.01150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.66450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.25400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.01150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.66450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     GLY A   116                                                      
REMARK 465     SER A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     GLY A   121                                                      
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 465     ARG B     4                                                      
REMARK 465     LEU B     5                                                      
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  2026     O    HOH A  2045              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 216   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 156     -155.52    -85.62                                   
REMARK 500    LEU A 168       14.57   -164.08                                   
REMARK 500    GLN A 169      131.82    -37.32                                   
REMARK 500    PRO A 201      118.09    -30.81                                   
REMARK 500    GLN A 260       14.98     58.00                                   
REMARK 500    ASP A 267        0.25    -61.75                                   
REMARK 500    THR A 284       -3.08     73.19                                   
REMARK 500    PRO A 289      152.08    -48.19                                   
REMARK 500    ASP A 290       48.09    -76.94                                   
REMARK 500    HIS A 354       79.28   -154.11                                   
REMARK 500    GLN A 388      -76.35    -30.79                                   
REMARK 500    ARG A 389       -5.62    -52.88                                   
REMARK 500    GLU A 390      -79.66   -107.50                                   
REMARK 500    LYS A 393       35.13    -77.20                                   
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 A1409  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 256   SG                                                     
REMARK 620 2 CYS A 280   SG  106.5                                              
REMARK 620 3 CYS A 259   SG  101.4 106.0                                        
REMARK 620 4 CYS A 283   SG   96.9 120.4 122.0                                  
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 OAD B 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1396                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1397                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1398                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1399                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1400                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1403                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1404                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1405                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1406                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1407                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1408                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1409                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BV2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH EX-527 AND 2'-O-ACETYL-    
REMARK 900 ADP-RIBOSE                                                           
REMARK 900 RELATED ID: 4BV3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SIRT3 IN COMPLEX WITH EX-527 AND NAD            
REMARK 900 RELATED ID: 4BVB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH EX- 527 AND ADP-    
REMARK 900 RIBOSE                                                               
REMARK 900 RELATED ID: 4BVE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH THIOALKYLIMIDATE    
REMARK 900 FORMED FROM THIO-ACETYL-LYSINE ACS2- PEPTIDE                         
REMARK 900 RELATED ID: 4BVF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH THIOALKYLIMIDATE    
REMARK 900 FORMED FROM THIO-ACETYL-LYSINE ACS2- PEPTIDE CRYSTALLIZED IN         
REMARK 900 PRESENCE OF THE INHIBITOR EX- 527                                    
REMARK 900 RELATED ID: 4BVH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH THE INHIBITOR EX-   
REMARK 900 527 AND 2'-O-ACETYL-ADP-RIBOSE                                       
REMARK 900 RELATED ID: 4BUZ   RELATED DB: PDB                                   
REMARK 900 SIR2 COMPLEX STRUCTURE MIXTURE OF EX-527 INHIBITOR AND REACTION      
REMARK 900 PRODUCTS OR OF REACTION SUBSTRATES P53 PEPTIDE AND NAD               
DBREF  4BVG A  116   399  UNP    Q9NTG7   SIR3_HUMAN     116    399             
DBREF  4BVG B   -4     5  UNP    Q9NUB1   ACS2L_HUMAN    638    647             
SEQRES   1 A  284  GLY SER SER ASP LYS GLY LYS LEU SER LEU GLN ASP VAL          
SEQRES   2 A  284  ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL VAL          
SEQRES   3 A  284  VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY ILE          
SEQRES   4 A  284  PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER ASN          
SEQRES   5 A  284  LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE PHE          
SEQRES   6 A  284  GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE PHE          
SEQRES   7 A  284  THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS PRO          
SEQRES   8 A  284  ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP LYS          
SEQRES   9 A  284  GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP GLY          
SEQRES  10 A  284  LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU VAL          
SEQRES  11 A  284  GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR VAL          
SEQRES  12 A  284  CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA ASP          
SEQRES  13 A  284  VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS THR          
SEQRES  14 A  284  GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU PRO          
SEQRES  15 A  284  LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE PRO          
SEQRES  16 A  284  MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU GLU          
SEQRES  17 A  284  VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG SER          
SEQRES  18 A  284  SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL GLY          
SEQRES  19 A  284  PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA GLN          
SEQRES  20 A  284  LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL GLU          
SEQRES  21 A  284  LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL GLN          
SEQRES  22 A  284  ARG GLU THR GLY LYS LEU ASP GLY PRO ASP LYS                  
SEQRES   1 B   10  THR ARG SER GLY LYS VAL MET ARG ARG LEU                      
HET    EDO  A1396       4                                                       
HET    EDO  A1397       4                                                       
HET    EDO  A1398       4                                                       
HET    EDO  A1399       4                                                       
HET    GOL  A1400       6                                                       
HET    GOL  A1401       6                                                       
HET    GOL  A1402       6                                                       
HET    EDO  A1403       4                                                       
HET    EDO  A1404       4                                                       
HET    SO4  A1405       5                                                       
HET    SO4  A1406       5                                                       
HET    EDO  A1407       4                                                       
HET    PEG  A1408       7                                                       
HET     ZN  A1409       1                                                       
HET    XYQ  B1000      38                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      ZN ZINC ION                                                         
HETNAM     XYQ (2R,3R,4S,5R)-5-({[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-               
HETNAM   2 XYQ  AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-            
HETNAM   3 XYQ  YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)                    
HETNAM   4 XYQ  PHOSPHORYL]OXY}METHYL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-          
HETNAM   5 XYQ  YL ACETATE                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     XYQ ACETYL-RIBOSYL-ADP                                               
FORMUL   3  EDO    7(C2 H6 O2)                                                  
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL  12  SO4    2(O4 S 2-)                                                   
FORMUL  15  PEG    C4 H10 O3                                                    
FORMUL  16   ZN    ZN 2+                                                        
FORMUL  17  XYQ    C17 H25 N5 O15 P2                                            
FORMUL  18  HOH   *56(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 TYR A  175  PHE A  180  5                                   6    
HELIX    4   4 GLU A  181  ASN A  188  1                                   8    
HELIX    5   5 PRO A  189  LEU A  199  1                                  11    
HELIX    6   6 ASN A  207  LYS A  219  1                                  13    
HELIX    7   7 GLY A  232  SER A  237  1                                   6    
HELIX    8   8 PRO A  240  SER A  242  5                                   3    
HELIX    9   9 ILE A  268  ALA A  274  1                                   7    
HELIX   10  10 PRO A  299  LEU A  303  5                                   5    
HELIX   11  11 LEU A  304  ALA A  312  1                                   9    
HELIX   12  12 PHE A  327  VAL A  334  5                                   8    
HELIX   13  13 GLY A  349  HIS A  354  1                                   6    
HELIX   14  14 ASP A  365  LEU A  377  1                                  13    
HELIX   15  15 TRP A  379  GLY A  392  1                                  14    
SHEET    1  AA 6 LEU A 244  GLU A 246  0                                        
SHEET    2  AA 6 LEU A 222  THR A 227  1  O  LEU A 225   N  VAL A 245           
SHEET    3  AA 6 VAL A 140  VAL A 144  1  O  VAL A 140   N  LEU A 223           
SHEET    4  AA 6 LEU A 314  LEU A 318  1  O  LEU A 314   N  VAL A 141           
SHEET    5  AA 6 ARG A 340  ASN A 344  1  O  LEU A 341   N  ILE A 317           
SHEET    6  AA 6 ASP A 359  LEU A 363  1  O  VAL A 360   N  LEU A 342           
SHEET    1  AB 3 PRO A 262  PRO A 264  0                                        
SHEET    2  AB 3 GLY A 249  CYS A 256 -1  O  ALA A 254   N  PHE A 263           
SHEET    3  AB 3 VAL A 287  ILE A 291 -1  O  LYS A 288   N  THR A 255           
SHEET    1  AC 2 VAL A 324  GLU A 325  0                                        
SHEET    2  AC 2 VAL B   1  MET B   2 -1  O  VAL B   1   N  GLU A 325           
LINK        ZN    ZN A1409                 SG  CYS A 256     1555   1555  2.43  
LINK        ZN    ZN A1409                 SG  CYS A 280     1555   1555  2.23  
LINK        ZN    ZN A1409                 SG  CYS A 259     1555   1555  2.14  
LINK        ZN    ZN A1409                 SG  CYS A 283     1555   1555  2.26  
LINK         CH  XYQ B1000                 NZ  LYS B   0     1555   1555  1.37  
CISPEP   1 GLU A  325    PRO A  326          0         2.59                     
SITE     1 AC1 26 GLY A 145  ALA A 146  GLY A 147  THR A 150                    
SITE     2 AC1 26 ASP A 156  PHE A 157  ARG A 158  TYR A 165                    
SITE     3 AC1 26 PHE A 180  GLN A 228  HIS A 248  VAL A 292                    
SITE     4 AC1 26 GLY A 319  THR A 320  SER A 321  VAL A 324                    
SITE     5 AC1 26 ASN A 344  ARG A 345  ASP A 346  GLY A 364                    
SITE     6 AC1 26 ASP A 365  VAL A 366  PEG A1408  HOH A2007                    
SITE     7 AC1 26 HOH A2019  LYS B   0                                          
SITE     1 AC2  5 GLU A 181  VAL A 258  CYS A 259  GLN A 260                    
SITE     2 AC2  5 MET B   2                                                     
SITE     1 AC3  5 TYR A 200  PRO A 201  PHE A 251  GLY A 265                    
SITE     2 AC3  5 ARG A 269                                                     
SITE     1 AC4  1 HIS A 187                                                     
SITE     1 AC5  7 ASN A 229  ILE A 230  GLY A 232  GLU A 246                    
SITE     2 AC5  7 GLY A 249  THR A 250  PHE A 251                               
SITE     1 AC6  4 LYS A 190  VAL A 277  ARG A 279  ARG A 384                    
SITE     1 AC7  9 ALA A 146  SER A 149  ILE A 154  PHE A 157                    
SITE     2 AC7  9 ASN A 229  ILE A 230  ASP A 231  HOH A2019                    
SITE     3 AC7  9 HOH A2053                                                     
SITE     1 AC8  3 LYS A 205  THR A 391  HOH A2054                               
SITE     1 AC9  4 SER A 152  ASN A 203  TYR A 204  LYS A 205                    
SITE     1 BC1  5 GLN A 138  GLY A 220  LEU A 221  LEU A 222                    
SITE     2 BC1  5 LYS A 243                                                     
SITE     1 BC2  4 ARG A 276  GLY A 364  ASP A 365  HIS A 368                    
SITE     1 BC3  3 ARG A 224  SER A 242  ARG A 301                               
SITE     1 BC4  4 CYS A 283  ARG A 384  GLN A 388  HOH A2056                    
SITE     1 BC5  6 ARG A 158  SER A 159  PRO A 160  ARG A 345                    
SITE     2 BC5  6 ASP A 346  XYQ B1000                                          
SITE     1 BC6  4 CYS A 256  CYS A 259  CYS A 280  CYS A 283                    
CRYST1   78.023  131.329   76.508  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012817  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007614  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013071        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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