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Database: PDB
Entry: 3JRX
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Original site: 3JRX 
HEADER    LIGASE                                  09-SEP-09   3JRX              
TITLE     CRYSTAL STRUCTURE OF THE BC DOMAIN OF ACC2 IN COMPLEX WITH            
TITLE    2 SORAPHEN A                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE 2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BC DOMAIN, RESIDUES 217-775;                               
COMPND   5 SYNONYM: ACC-BETA, BIOTIN CARBOXYLASE, ACC2;                         
COMPND   6 EC: 6.4.1.2, 6.3.4.14;                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACACB, ACC2, ACCB;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET21B                           
KEYWDS    BC DOMAIN, SORAPHEN A, ALTERNATIVE SPLICING, ATP-BINDING,             
KEYWDS   2 BIOTIN, FATTY ACID BIOSYNTHESIS, LIGASE, LIPID SYNTHESIS,            
KEYWDS   3 MANGANESE, MEMBRANE, METAL-BINDING, MULTIFUNCTIONAL ENZYME,          
KEYWDS   4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.CHO,J.I.LEE,D.SHIN,H.T.KIM,T.G.LEE,Y.S.HEO                        
REVDAT   1   12-JAN-10 3JRX    0                                                
JRNL        AUTH   Y.S.CHO,J.I.LEE,D.SHIN,H.T.KIM,H.Y.JUNG,T.G.LEE,             
JRNL        AUTH 2 L.W.KANG,Y.J.AHN,H.S.CHO,Y.S.HEO                             
JRNL        TITL   MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN              
JRNL        TITL 2 ACC2 THROUGH PHOSPHORYLATION BY AMPK.                        
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 391   187 2010              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   19900410                                                     
JRNL        DOI    10.1016/J.BBRC.2009.11.029                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 305442.900                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19922                          
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 SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 961                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3020                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 153                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3881                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.91000                                              
REMARK   3    B22 (A**2) : 1.91000                                              
REMARK   3    B33 (A**2) : -3.82000                                             
REMARK   3    B12 (A**2) : 3.40000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 36.90                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SOR.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : SOR.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3JRX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055082.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20538                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2HJW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, PH 6.50,          
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.60933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.80467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.80467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      119.60933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   205                                                      
REMARK 465     ARG A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     MET A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     SER A   216                                                      
REMARK 465     MET A   217                                                      
REMARK 465     ARG A   218                                                      
REMARK 465     PRO A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     MET A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     GLY A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     LEU A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     GLY A   230                                                      
REMARK 465     ARG A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     THR A   412                                                      
REMARK 465     GLU A   413                                                      
REMARK 465     ASP A   414                                                      
REMARK 465     ASP A   415                                                      
REMARK 465     LEU A   416                                                      
REMARK 465     GLN A   417                                                      
REMARK 465     GLU A   656                                                      
REMARK 465     ASN A   657                                                      
REMARK 465     PRO A   658                                                      
REMARK 465     ASP A   659                                                      
REMARK 465     GLU A   660                                                      
REMARK 465     GLY A   661                                                      
REMARK 465     PHE A   662                                                      
REMARK 465     LYS A   663                                                      
REMARK 465     PRO A   664                                                      
REMARK 465     SER A   665                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     THR A   689                                                      
REMARK 465     GLY A   690                                                      
REMARK 465     GLY A   691                                                      
REMARK 465     LEU A   692                                                      
REMARK 465     HIS A   693                                                      
REMARK 465     GLU A   694                                                      
REMARK 465     PHE A   695                                                      
REMARK 465     ALA A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     LEU A   759                                                      
REMARK 465     ILE A   760                                                      
REMARK 465     ALA A   761                                                      
REMARK 465     GLU A   762                                                      
REMARK 465     LYS A   763                                                      
REMARK 465     VAL A   764                                                      
REMARK 465     GLN A   765                                                      
REMARK 465     ALA A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     LYS A   768                                                      
REMARK 465     PRO A   769                                                      
REMARK 465     ASP A   770                                                      
REMARK 465     ILE A   771                                                      
REMARK 465     MET A   772                                                      
REMARK 465     LEU A   773                                                      
REMARK 465     GLY A   774                                                      
REMARK 465     VAL A   775                                                      
REMARK 465     LEU A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     HIS A   778                                                      
REMARK 465     HIS A   779                                                      
REMARK 465     HIS A   780                                                      
REMARK 465     HIS A   781                                                      
REMARK 465     HIS A   782                                                      
REMARK 465     HIS A   783                                                      
REMARK 465     LEU A   784                                                      
REMARK 465     GLU A   785                                                      
REMARK 465     HIS A   786                                                      
REMARK 465     HIS A   787                                                      
REMARK 465     HIS A   788                                                      
REMARK 465     HIS A   789                                                      
REMARK 465     HIS A   790                                                      
REMARK 465     HIS A   791                                                      
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 266       59.93    -93.56                                   
REMARK 500    ASN A 328      -94.12   -154.18                                   
REMARK 500    HIS A 353     -124.10     54.63                                   
REMARK 500    ASP A 384     -145.86    -83.74                                   
REMARK 500    SER A 403       -3.77    -59.75                                   
REMARK 500    LYS A 420       94.72     62.62                                   
REMARK 500    GLN A 496     -109.18    -61.20                                   
REMARK 500    HIS A 497       64.78   -111.55                                   
REMARK 500    LEU A 516       60.53   -115.25                                   
REMARK 500    PHE A 517     -152.17     55.28                                   
REMARK 500    ARG A 526       72.41     55.72                                   
REMARK 500    SER A 562     -157.74     81.45                                   
REMARK 500    ASP A 573      -73.68    -64.71                                   
REMARK 500    LEU A 579      -70.45   -103.08                                   
REMARK 500    SER A 676      -78.47    -59.63                                   
REMARK 500    GLN A 699     -137.89   -150.31                                   
REMARK 500    THR A 732      -47.22   -172.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 683         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  12        DISTANCE =  6.77 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S1A A 1000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HJW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BC DOMAIN OF HUMAN ACC2                     
REMARK 900 RELATED ID: 3JRW   RELATED DB: PDB                                   
DBREF  3JRX A  217   775  UNP    O00763   ACACB_HUMAN    217    775             
SEQADV 3JRX MET A  205  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX ARG A  206  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLY A  207  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX SER A  208  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLY A  209  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX SER A  210  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX MET A  211  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX ARG A  212  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLY A  213  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX SER A  214  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLY A  215  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX SER A  216  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX LEU A  776  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLU A  777  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  778  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  779  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  780  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  781  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  782  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  783  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX LEU A  784  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX GLU A  785  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  786  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  787  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  788  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  789  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  790  UNP  O00763              EXPRESSION TAG                 
SEQADV 3JRX HIS A  791  UNP  O00763              EXPRESSION TAG                 
SEQRES   1 A  587  MET ARG GLY SER GLY SER MET ARG GLY SER GLY SER MET          
SEQRES   2 A  587  ARG PRO SER MET SER GLY LEU HIS LEU VAL LYS ARG GLY          
SEQRES   3 A  587  ARG GLU HIS LYS LYS LEU ASP LEU HIS ARG ASP PHE THR          
SEQRES   4 A  587  VAL ALA SER PRO ALA GLU PHE VAL THR ARG PHE GLY GLY          
SEQRES   5 A  587  ASP ARG VAL ILE GLU LYS VAL LEU ILE ALA ASN ASN GLY          
SEQRES   6 A  587  ILE ALA ALA VAL LYS CYS MET ARG SER ILE ARG ARG TRP          
SEQRES   7 A  587  ALA TYR GLU MET PHE ARG ASN GLU ARG ALA ILE ARG PHE          
SEQRES   8 A  587  VAL VAL MET VAL THR PRO GLU ASP LEU LYS ALA ASN ALA          
SEQRES   9 A  587  GLU TYR ILE LYS MET ALA ASP HIS TYR VAL PRO VAL PRO          
SEQRES  10 A  587  GLY GLY PRO ASN ASN ASN ASN TYR ALA ASN VAL GLU LEU          
SEQRES  11 A  587  ILE VAL ASP ILE ALA LYS ARG ILE PRO VAL GLN ALA VAL          
SEQRES  12 A  587  TRP ALA GLY TRP GLY HIS ALA SER GLU ASN PRO LYS LEU          
SEQRES  13 A  587  PRO GLU LEU LEU CYS LYS ASN GLY VAL ALA PHE LEU GLY          
SEQRES  14 A  587  PRO PRO SER GLU ALA MET TRP ALA LEU GLY ASP LYS ILE          
SEQRES  15 A  587  ALA SER THR VAL VAL ALA GLN THR LEU GLN VAL PRO THR          
SEQRES  16 A  587  LEU PRO TRP SER GLY SER GLY LEU THR VAL GLU TRP THR          
SEQRES  17 A  587  GLU ASP ASP LEU GLN GLN GLY LYS ARG ILE SER VAL PRO          
SEQRES  18 A  587  GLU ASP VAL TYR ASP LYS GLY CYS VAL LYS ASP VAL ASP          
SEQRES  19 A  587  GLU GLY LEU GLU ALA ALA GLU ARG ILE GLY PHE PRO LEU          
SEQRES  20 A  587  MET ILE LYS ALA SER GLU GLY GLY GLY GLY LYS GLY ILE          
SEQRES  21 A  587  ARG LYS ALA GLU SER ALA GLU ASP PHE PRO ILE LEU PHE          
SEQRES  22 A  587  ARG GLN VAL GLN SER GLU ILE PRO GLY SER PRO ILE PHE          
SEQRES  23 A  587  LEU MET LYS LEU ALA GLN HIS ALA ARG HIS LEU GLU VAL          
SEQRES  24 A  587  GLN ILE LEU ALA ASP GLN TYR GLY ASN ALA VAL SER LEU          
SEQRES  25 A  587  PHE GLY ARG ASP CYS SER ILE GLN ARG ARG HIS GLN LYS          
SEQRES  26 A  587  ILE VAL GLU GLU ALA PRO ALA THR ILE ALA PRO LEU ALA          
SEQRES  27 A  587  ILE PHE GLU PHE MET GLU GLN CYS ALA ILE ARG LEU ALA          
SEQRES  28 A  587  LYS THR VAL GLY TYR VAL SER ALA GLY THR VAL GLU TYR          
SEQRES  29 A  587  LEU TYR SER GLN ASP GLY SER PHE HIS PHE LEU GLU LEU          
SEQRES  30 A  587  ASN PRO ARG LEU GLN VAL GLU HIS PRO CYS THR GLU MET          
SEQRES  31 A  587  ILE ALA ASP VAL ASN LEU PRO ALA ALA GLN LEU GLN ILE          
SEQRES  32 A  587  ALA MET GLY VAL PRO LEU HIS ARG LEU LYS ASP ILE ARG          
SEQRES  33 A  587  LEU LEU TYR GLY GLU SER PRO TRP GLY VAL THR PRO ILE          
SEQRES  34 A  587  SER PHE GLU THR PRO SER ASN PRO PRO LEU ALA ARG GLY          
SEQRES  35 A  587  HIS VAL ILE ALA ALA ARG ILE THR SER GLU ASN PRO ASP          
SEQRES  36 A  587  GLU GLY PHE LYS PRO SER SER GLY THR VAL GLN GLU LEU          
SEQRES  37 A  587  ASN PHE ARG SER SER LYS ASN VAL TRP GLY TYR PHE SER          
SEQRES  38 A  587  VAL ALA ALA THR GLY GLY LEU HIS GLU PHE ALA ASP SER          
SEQRES  39 A  587  GLN PHE GLY HIS CYS PHE SER TRP GLY GLU ASN ARG GLU          
SEQRES  40 A  587  GLU ALA ILE SER ASN MET VAL VAL ALA LEU LYS GLU LEU          
SEQRES  41 A  587  SER ILE ARG GLY ASP PHE ARG THR THR VAL GLU TYR LEU          
SEQRES  42 A  587  ILE ASN LEU LEU GLU THR GLU SER PHE GLN ASN ASN ASP          
SEQRES  43 A  587  ILE ASP THR GLY TRP LEU ASP TYR LEU ILE ALA GLU LYS          
SEQRES  44 A  587  VAL GLN ALA GLU LYS PRO ASP ILE MET LEU GLY VAL LEU          
SEQRES  45 A  587  GLU HIS HIS HIS HIS HIS HIS LEU GLU HIS HIS HIS HIS          
SEQRES  46 A  587  HIS HIS                                                      
HET    S1A  A1000      37                                                       
HETNAM     S1A SORAPHEN A                                                       
FORMUL   2  S1A    C29 H44 O8                                                   
FORMUL   3  HOH   *93(H2 O)                                                     
HELIX    1   1 SER A  246  PHE A  254  1                                   9    
HELIX    2   2 ASN A  268  ARG A  288  1                                  21    
HELIX    3   3 THR A  300  ALA A  306  1                                   7    
HELIX    4   4 ALA A  308  ALA A  314  1                                   7    
HELIX    5   5 PRO A  324  ASN A  328  5                                   5    
HELIX    6   6 ASN A  331  ILE A  342  1                                  12    
HELIX    7   7 PRO A  358  LYS A  366  1                                   9    
HELIX    8   8 PRO A  375  GLY A  383  1                                   9    
HELIX    9   9 ASP A  384  LEU A  395  1                                  12    
HELIX   10  10 PRO A  425  LYS A  431  1                                   7    
HELIX   11  11 ASP A  436  GLY A  448  1                                  13    
HELIX   12  12 ASP A  472  ILE A  484  1                                  13    
HELIX   13  13 PRO A  540  GLY A  559  1                                  20    
HELIX   14  14 GLU A  588  ASP A  597  1                                  10    
HELIX   15  15 ASN A  599  MET A  609  1                                  11    
HELIX   16  16 PRO A  612  ARG A  615  5                                   4    
HELIX   17  17 LEU A  616  TYR A  623  1                                   8    
HELIX   18  18 ASN A  709  ARG A  727  1                                  19    
HELIX   19  19 VAL A  734  GLU A  742  1                                   9    
HELIX   20  20 THR A  743  ASN A  748  1                                   6    
HELIX   21  21 THR A  753  TYR A  758  5                                   6    
SHEET    1   A 5 HIS A 316  PRO A 319  0                                        
SHEET    2   A 5 ARG A 294  VAL A 299  1  N  VAL A 297   O  VAL A 318           
SHEET    3   A 5 LYS A 262  ILE A 265  1  N  ILE A 265   O  VAL A 296           
SHEET    4   A 5 ALA A 346  TRP A 348  1  O  ALA A 346   N  LEU A 264           
SHEET    5   A 5 ALA A 370  PHE A 371  1  O  ALA A 370   N  VAL A 347           
SHEET    1   B 3 ILE A 464  ALA A 467  0                                        
SHEET    2   B 3 LEU A 451  ALA A 455 -1  N  ILE A 453   O  ARG A 465           
SHEET    3   B 3 ILE A 489  LYS A 493 -1  O  MET A 492   N  MET A 452           
SHEET    1   C 9 PHE A 576  ASN A 582  0                                        
SHEET    2   C 9 SER A 562  TYR A 570 -1  N  THR A 565   O  ASN A 582           
SHEET    3   C 9 ARG A 499  ALA A 507 -1  N  LEU A 501   O  TYR A 568           
SHEET    4   C 9 ALA A 513  GLN A 524 -1  O  ARG A 519   N  GLU A 502           
SHEET    5   C 9 LYS A 529  ALA A 534 -1  O  GLU A 533   N  ASP A 520           
SHEET    6   C 9 HIS A 647  THR A 654 -1  O  ALA A 650   N  GLU A 532           
SHEET    7   C 9 PHE A 700  GLY A 707 -1  O  SER A 705   N  ILE A 649           
SHEET    8   C 9 VAL A 680  PHE A 684 -1  N  TRP A 681   O  PHE A 704           
SHEET    9   C 9 GLN A 670  ASN A 673 -1  N  LEU A 672   O  GLY A 682           
CISPEP   1 ILE A  342    PRO A  343          0        -1.08                     
CISPEP   2 PHE A  449    PRO A  450          0        -0.85                     
CISPEP   3 ALA A  534    PRO A  535          0        -0.26                     
SITE     1 AC1  8 LYS A 274  ARG A 277  SER A 278  GLU A 593                    
SITE     2 AC1  8 MET A 594  VAL A 598  ASN A 599  PHE A 704                    
CRYST1   74.744   74.744  179.414  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013379  0.007724  0.000000        0.00000                         
SCALE2      0.000000  0.015449  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005574        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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