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Database: PDB
Entry: 4C78
LinkDB: 4C78
Original site: 4C78 
HEADER    HYDROLASE                               19-SEP-13   4C78              
TITLE     COMPLEX OF HUMAN SIRT3 WITH BROMO-RESVERATROL AND ACS2 PEPTIDE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3,               
COMPND   3  MITOCHONDRIAL;                                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: RESIDUES 116-399;                                          
COMPND   6 EC: 3.5.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ACETYL-COENZYME A SYNTHETASE 2-LIKE, MITOCHONDRIAL;        
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: RESIDUES 638-647;                                          
COMPND  12 EC: 6.2.1.1                                                          
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, SIRTUIN, INHIBITOR, ACTIVATION, RESVERATROL, SIRT1,        
KEYWDS   2 METABOLIC SENSOR, METABOLISM, AGING                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.T.T.NGUYEN,M.GERTZ,M.WEYAND,C.STEEGBORN                             
REVDAT   3   11-DEC-13 4C78    1       JRNL                                     
REVDAT   2   27-NOV-13 4C78    1       JRNL                                     
REVDAT   1   20-NOV-13 4C78    0                                                
JRNL        AUTH   G.T.T.NGUYEN,M.GERTZ,C.STEEGBORN                             
JRNL        TITL   CRYSTAL STRUCTURES OF SIRT3 COMPLEXES WITH 4'-BROMO-         
JRNL        TITL 2 RESVERATROL REVEAL BINDING SITES AND INHIBITION MECHANISM.   
JRNL        REF    CHEM.BIOL.                    V.  20  1375 2013              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   24211137                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2013.09.019                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.58                          
REMARK   3   NUMBER OF REFLECTIONS             : 19507                          
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) : 0.19614                         
REMARK   3   R VALUE            (WORKING SET) : 0.19375                         
REMARK   3   FREE R VALUE                     : 0.24056                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1025                            
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) : 2.000                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.052                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1427                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.283                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.334                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.552                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07                                                 
REMARK   3    B22 (A**2) : 1.64                                                 
REMARK   3    B33 (A**2) : -1.71                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.167         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.553         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2191 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2146 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2977 ; 1.923 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4925 ; 0.952 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   267 ; 6.768 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;35.802 ;22.447       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;16.063 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;17.160 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   337 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2422 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   497 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1071 ; 1.016 ; 0.811       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1070 ; 1.014 ; 0.810       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1334 ; 1.729 ; 1.203       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1335 ; 1.729 ; 1.205       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1120 ; 1.221 ; 1.731       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1121 ; 1.220 ; 1.731       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1643 ; 1.918 ; 1.952       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2610 ; 8.066 ; 8.050       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2570 ; 8.015 ; 7.554       
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):     1 ;47.891 ; 5.000       
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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   122        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3608  35.9439 -11.3175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2384 T22:   0.2404                                     
REMARK   3      T33:   0.2498 T12:  -0.0687                                     
REMARK   3      T13:   0.0208 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1059 L22:   2.9326                                     
REMARK   3      L33:   8.1764 L12:  -0.6258                                     
REMARK   3      L13:   0.1628 L23:   2.5813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1286 S12:  -0.3987 S13:   0.5604                       
REMARK   3      S21:  -0.0808 S22:  -0.1106 S23:  -0.0968                       
REMARK   3      S31:  -0.8549 S32:  -0.0338 S33:  -0.0180                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   153        A   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2755  16.7542 -39.3275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4356 T22:   0.3222                                     
REMARK   3      T33:   0.2247 T12:  -0.0082                                     
REMARK   3      T13:  -0.0245 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6329 L22:   2.2252                                     
REMARK   3      L33:  10.9070 L12:   0.0726                                     
REMARK   3      L13:   0.6360 L23:   1.9798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1206 S12:   0.2072 S13:   0.0173                       
REMARK   3      S21:  -0.4887 S22:   0.3250 S23:  -0.1984                       
REMARK   3      S31:   0.2931 S32:   0.7321 S33:  -0.2044                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   190        A   311                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0646  14.7076 -22.7303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3944 T22:   0.3241                                     
REMARK   3      T33:   0.3047 T12:   0.0462                                     
REMARK   3      T13:  -0.1139 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2412 L22:   2.4628                                     
REMARK   3      L33:   4.8175 L12:   0.4181                                     
REMARK   3      L13:  -0.0715 L23:   2.2474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:  -0.0194 S13:  -0.0987                       
REMARK   3      S21:   0.1801 S22:   0.2763 S23:  -0.2132                       
REMARK   3      S31:   0.8918 S32:   0.3213 S33:  -0.3196                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   312        A   394                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0960  34.7840 -16.5729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2341 T22:   0.2283                                     
REMARK   3      T33:   0.2310 T12:  -0.0306                                     
REMARK   3      T13:   0.0540 T23:  -0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4865 L22:   1.7405                                     
REMARK   3      L33:   4.3914 L12:  -0.6432                                     
REMARK   3      L13:   0.9070 L23:   0.4339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1078 S12:   0.1182 S13:   0.2890                       
REMARK   3      S21:  -0.3094 S22:   0.0280 S23:  -0.0794                       
REMARK   3      S31:  -0.5758 S32:   0.2248 S33:  -0.1357                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C     9                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3307  24.5024 -36.0324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4482 T22:   0.2173                                     
REMARK   3      T33:   0.3254 T12:   0.0328                                     
REMARK   3      T13:  -0.0456 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4895 L22:  14.7773                                     
REMARK   3      L33:  20.9928 L12:   1.6376                                     
REMARK   3      L13:  -3.9265 L23:  -4.9381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1851 S12:   0.0195 S13:   0.4910                       
REMARK   3      S21:  -0.2521 S22:   0.4518 S23:   0.3606                       
REMARK   3      S31:  -1.1253 S32:  -0.5658 S33:  -0.6369                       
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              
REMARK   3  THE RIDING POSITIONS. U VALUES WITH TLS ADDED.                      
REMARK   4                                                                      
REMARK   4 4C78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58410.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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 (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37699                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.40                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 2.1                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.99                               
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 4H8D                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 250 MM (NH4)2SO4, 100 MM                 
REMARK 280  BISTRIS PH 6, 21% (W/V) PEG 3350                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.85000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.85000            
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: 1170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2039   LIES ON A SPECIAL POSITION.                         
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     PRO A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     TYR A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     ASN A   167                                                      
REMARK 465     LEU A   168                                                      
REMARK 465     GLN A   169                                                      
REMARK 465     GLN A   170                                                      
REMARK 465     TYR A   171                                                      
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     THR C     0                                                      
REMARK 465     ARG C     1                                                      
REMARK 465     SER C     2                                                      
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   OD2  ASP A   218     O    HOH A  2042              2.11            
REMARK 500   O    HOH A  2039     O    HOH A  2040              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2039     O    HOH A  2040     2565     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 381   CD    GLU A 381   OE2     0.087                       
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    ARG A 139   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A 313   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 384   NE  -  CZ  -  NH1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A 384   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 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    ALA A 134        9.74    -64.84                                   
REMARK 500    ARG A 135       21.90     44.96                                   
REMARK 500    ASN A 188       97.70   -165.23                                   
REMARK 500    ASN A 203      -71.11    -79.12                                   
REMARK 500    ASP A 290       47.88    -79.05                                   
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 A1396  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 283   SG                                                     
REMARK 620 2 CYS A 256   SG   94.3                                              
REMARK 620 3 CYS A 259   SG  126.2 111.2                                        
REMARK 620 4 CYS A 280   SG  113.8 102.0 106.3                                  
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 BVB A1395                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1396                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C7B   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF HUMAN SIRT3 WITH BROMO-RESVERATROL AND                   
REMARK 900  FLUOR-DE-LYS PEPTIDE                                                
DBREF  4C78 A  116   399  UNP    Q9NTG7   SIR3_HUMAN     116    399             
DBREF  4C78 C    0     9  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 C   10  THR ARG SER GLY ALY VAL MET ARG ARG LEU                      
MODRES 4C78 ALY C    4  LYS  ACETYLATED LYSINE                                  
HET    BVB  A1395      17                                                       
HET    ALY  C   4      12                                                       
HET     ZN  A1396       1                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     BVB 5-[(E)-2-(4-BROMOPHENYL)ETHENYL]BENZENE-1,3-                     
HETNAM   2 BVB  DIOL                                                            
FORMUL   3  ALY    C8 H16 N2 O3                                                 
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  BVB    C14 H11 BR O2                                                
FORMUL   6  HOH   *125(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  TYR A  200  1                                  12    
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 PRO A  326  GLU A  332  1                                   7    
HELIX   13  13 VAL A  348  HIS A  354  1                                   7    
HELIX   14  14 ASP A  365  GLY A  378  1                                  14    
HELIX   15  15 TRP A  379  LYS A  393  1                                  15    
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           
LINK        ZN    ZN A1396                 SG  CYS A 283     1555   1555  2.29  
LINK        ZN    ZN A1396                 SG  CYS A 280     1555   1555  2.34  
LINK        ZN    ZN A1396                 SG  CYS A 259     1555   1555  2.32  
LINK        ZN    ZN A1396                 SG  CYS A 256     1555   1555  2.29  
LINK         C   GLY C   3                 N   ALY C   4     1555   1555  1.34  
LINK         C   ALY C   4                 N   VAL C   5     1555   1555  1.32  
CISPEP   1 GLU A  325    PRO A  326          0         1.53                     
SITE     1 AC1  8 ARG A 139  MET A 311  ASP A 313  ARG A 335                    
SITE     2 AC1  8 GLU A 371  GLU A 381  ARG A 384  HOH A2122                    
SITE     1 AC2  4 CYS A 256  CYS A 259  CYS A 280  CYS A 283                    
CRYST1   34.700   52.600  159.700  90.00  90.00  90.00 P 2 21 21     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      0.028818  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019011  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006262        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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