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Database: PDB
Entry: 4HQ6
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Original site: 4HQ6 
HEADER    LIGASE                                  25-OCT-12   4HQ6              
TITLE     BC DOMAIN IN THE PRESENCE OF CITRATE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE 2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 217-776;                                      
COMPND   5 SYNONYM: ACC-BETA, BIOTIN CARBOXYLASE;                               
COMPND   6 EC: 6.4.1.2, 6.3.4.14;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    ACETYL-COA CARBOXYLATION, LIGASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.HEO                                                               
REVDAT   2   17-SEP-14 4HQ6    1       JRNL                                     
REVDAT   1   09-OCT-13 4HQ6    0                                                
JRNL        AUTH   S.J.KWON,Y.S.CHO,Y.S.HEO                                     
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE REGULATION OF ACC2 BY CITRATE   
JRNL        REF    BULL.KOREAN CHEM.SOC.         V.  34   565 2013              
JRNL        REFN                   ISSN 0253-2964                               
JRNL        DOI    10.5012/BKCS.2013.34.2.565                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 232867.600                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15395                          
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                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 760                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1845                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3710                       
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 85                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.045                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3871                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 44                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.34000                                             
REMARK   3    B22 (A**2) : 11.34000                                             
REMARK   3    B33 (A**2) : -22.68000                                            
REMARK   3    B12 (A**2) : 15.47000                                             
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) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.55                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.62                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.600                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.910                           
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        : 0.32                                                 
REMARK   3   BSOL        : 26.91                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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  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  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HQ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075781.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16550                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 1.8M AMMONIUM SULFATE, PH      
REMARK 280  6.5, 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      125.85533            
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       62.92767            
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       62.92767            
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      125.85533            
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   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     SEP 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     ILE A   236                                                      
REMARK 465     ASP A   237                                                      
REMARK 465     LEU A   238                                                      
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     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   687                                                      
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     SER A   698                                                      
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 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   OG   SER A   403     O    GLY A   432              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 257       38.58   -142.65                                   
REMARK 500    ARG A 258      127.36   -179.21                                   
REMARK 500    ASN A 267     -175.07   -179.52                                   
REMARK 500    ARG A 288       18.97     51.65                                   
REMARK 500    ASN A 328      -97.52   -146.95                                   
REMARK 500    HIS A 353     -131.45     51.42                                   
REMARK 500    ASP A 384     -164.92    -73.54                                   
REMARK 500    LYS A 420      119.22     72.82                                   
REMARK 500    ILE A 422      154.66    -47.22                                   
REMARK 500    ILE A 484       66.66   -118.49                                   
REMARK 500    HIS A 497       98.72     25.40                                   
REMARK 500    GLN A 509       43.36   -104.04                                   
REMARK 500    TYR A 510       12.48   -140.44                                   
REMARK 500    PHE A 517     -163.98     57.59                                   
REMARK 500    SER A 562     -144.72     83.07                                   
REMARK 500    ASP A 573      -85.24    -53.01                                   
REMARK 500    PRO A 583       29.28    -77.14                                   
REMARK 500    SER A 676      -76.68    -64.04                                   
REMARK 500    THR A 732      -59.06   -149.76                                   
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 623         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4HQ6 A  217   776  UNP    O00763   ACACB_HUMAN    217    776             
SEQADV 4HQ6 MET A  211  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 ARG A  212  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 GLY A  213  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 SER A  214  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 GLY A  215  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 SER A  216  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 ILE A  236  UNP  O00763    LEU   236 ENGINEERED MUTATION            
SEQADV 4HQ6 LEU A  776  UNP  O00763    VAL   776 ENGINEERED MUTATION            
SEQADV 4HQ6 GLU A  777  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  778  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  779  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  780  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  781  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  782  UNP  O00763              EXPRESSION TAG                 
SEQADV 4HQ6 HIS A  783  UNP  O00763              EXPRESSION TAG                 
SEQRES   1 A  573  MET ARG GLY SER GLY SER MET ARG PRO SER MET SEP GLY          
SEQRES   2 A  573  LEU HIS LEU VAL LYS ARG GLY ARG GLU HIS LYS LYS ILE          
SEQRES   3 A  573  ASP LEU HIS ARG ASP PHE THR VAL ALA SER PRO ALA GLU          
SEQRES   4 A  573  PHE VAL THR ARG PHE GLY GLY ASP ARG VAL ILE GLU LYS          
SEQRES   5 A  573  VAL LEU ILE ALA ASN ASN GLY ILE ALA ALA VAL LYS CYS          
SEQRES   6 A  573  MET ARG SER ILE ARG ARG TRP ALA TYR GLU MET PHE ARG          
SEQRES   7 A  573  ASN GLU ARG ALA ILE ARG PHE VAL VAL MET VAL THR PRO          
SEQRES   8 A  573  GLU ASP LEU LYS ALA ASN ALA GLU TYR ILE LYS MET ALA          
SEQRES   9 A  573  ASP HIS TYR VAL PRO VAL PRO GLY GLY PRO ASN ASN ASN          
SEQRES  10 A  573  ASN TYR ALA ASN VAL GLU LEU ILE VAL ASP ILE ALA LYS          
SEQRES  11 A  573  ARG ILE PRO VAL GLN ALA VAL TRP ALA GLY TRP GLY HIS          
SEQRES  12 A  573  ALA SER GLU ASN PRO LYS LEU PRO GLU LEU LEU CYS LYS          
SEQRES  13 A  573  ASN GLY VAL ALA PHE LEU GLY PRO PRO SER GLU ALA MET          
SEQRES  14 A  573  TRP ALA LEU GLY ASP LYS ILE ALA SER THR VAL VAL ALA          
SEQRES  15 A  573  GLN THR LEU GLN VAL PRO THR LEU PRO TRP SER GLY SER          
SEQRES  16 A  573  GLY LEU THR VAL GLU TRP THR GLU ASP ASP LEU GLN GLN          
SEQRES  17 A  573  GLY LYS ARG ILE SER VAL PRO GLU ASP VAL TYR ASP LYS          
SEQRES  18 A  573  GLY CYS VAL LYS ASP VAL ASP GLU GLY LEU GLU ALA ALA          
SEQRES  19 A  573  GLU ARG ILE GLY PHE PRO LEU MET ILE LYS ALA SER GLU          
SEQRES  20 A  573  GLY GLY GLY GLY LYS GLY ILE ARG LYS ALA GLU SER ALA          
SEQRES  21 A  573  GLU ASP PHE PRO ILE LEU PHE ARG GLN VAL GLN SER GLU          
SEQRES  22 A  573  ILE PRO GLY SER PRO ILE PHE LEU MET LYS LEU ALA GLN          
SEQRES  23 A  573  HIS ALA ARG HIS LEU GLU VAL GLN ILE LEU ALA ASP GLN          
SEQRES  24 A  573  TYR GLY ASN ALA VAL SER LEU PHE GLY ARG ASP CYS SER          
SEQRES  25 A  573  ILE GLN ARG ARG HIS GLN LYS ILE VAL GLU GLU ALA PRO          
SEQRES  26 A  573  ALA THR ILE ALA PRO LEU ALA ILE PHE GLU PHE MET GLU          
SEQRES  27 A  573  GLN CYS ALA ILE ARG LEU ALA LYS THR VAL GLY TYR VAL          
SEQRES  28 A  573  SER ALA GLY THR VAL GLU TYR LEU TYR SER GLN ASP GLY          
SEQRES  29 A  573  SER PHE HIS PHE LEU GLU LEU ASN PRO ARG LEU GLN VAL          
SEQRES  30 A  573  GLU HIS PRO CYS THR GLU MET ILE ALA ASP VAL ASN LEU          
SEQRES  31 A  573  PRO ALA ALA GLN LEU GLN ILE ALA MET GLY VAL PRO LEU          
SEQRES  32 A  573  HIS ARG LEU LYS ASP ILE ARG LEU LEU TYR GLY GLU SER          
SEQRES  33 A  573  PRO TRP GLY VAL THR PRO ILE SER PHE GLU THR PRO SER          
SEQRES  34 A  573  ASN PRO PRO LEU ALA ARG GLY HIS VAL ILE ALA ALA ARG          
SEQRES  35 A  573  ILE THR SER GLU ASN PRO ASP GLU GLY PHE LYS PRO SER          
SEQRES  36 A  573  SER GLY THR VAL GLN GLU LEU ASN PHE ARG SER SER LYS          
SEQRES  37 A  573  ASN VAL TRP GLY TYR PHE SER VAL ALA ALA THR GLY GLY          
SEQRES  38 A  573  LEU HIS GLU PHE ALA ASP SER GLN PHE GLY HIS CYS PHE          
SEQRES  39 A  573  SER TRP GLY GLU ASN ARG GLU GLU ALA ILE SER ASN MET          
SEQRES  40 A  573  VAL VAL ALA LEU LYS GLU LEU SER ILE ARG GLY ASP PHE          
SEQRES  41 A  573  ARG THR THR VAL GLU TYR LEU ILE ASN LEU LEU GLU THR          
SEQRES  42 A  573  GLU SER PHE GLN ASN ASN ASP ILE ASP THR GLY TRP LEU          
SEQRES  43 A  573  ASP TYR LEU ILE ALA GLU LYS VAL GLN ALA GLU LYS PRO          
SEQRES  44 A  573  ASP ILE MET LEU GLY VAL LEU GLU HIS HIS HIS HIS HIS          
SEQRES  45 A  573  HIS                                                          
FORMUL   2  HOH   *44(H2 O)                                                     
HELIX    1   1 SER A  246  PHE A  254  1                                   9    
HELIX    2   2 ASN A  268  PHE A  287  1                                  20    
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 GLY A  352  ASN A  357  5                                   6    
HELIX    8   8 PRO A  358  ASN A  367  1                                  10    
HELIX    9   9 PRO A  375  ALA A  381  1                                   7    
HELIX   10  10 ASP A  384  LEU A  395  1                                  12    
HELIX   11  11 PRO A  425  LYS A  431  1                                   7    
HELIX   12  12 ASP A  436  GLY A  448  1                                  13    
HELIX   13  13 ASP A  472  ILE A  484  1                                  13    
HELIX   14  14 PRO A  540  VAL A  558  1                                  19    
HELIX   15  15 HIS A  589  ASP A  597  1                                   9    
HELIX   16  16 ASN A  599  MET A  609  1                                  11    
HELIX   17  17 PRO A  612  ARG A  615  5                                   4    
HELIX   18  18 LEU A  616  TYR A  623  1                                   8    
HELIX   19  19 ASN A  709  ARG A  727  1                                  19    
HELIX   20  20 GLY A  728  ARG A  731  5                                   4    
HELIX   21  21 VAL A  734  THR A  743  1                                  10    
HELIX   22  22 THR A  743  ASN A  749  1                                   7    
HELIX   23  23 THR A  753  ASP A  757  5                                   5    
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  PHE A 490   N  LYS A 454           
SHEET    1   C 4 ALA A 513  ASP A 520  0                                        
SHEET    2   C 4 ARG A 499  ALA A 507 -1  N  LEU A 506   O  VAL A 514           
SHEET    3   C 4 SER A 562  TYR A 570 -1  O  TYR A 568   N  LEU A 501           
SHEET    4   C 4 PHE A 576  ASN A 582 -1  O  GLU A 580   N  GLU A 567           
SHEET    1   D 5 VAL A 531  ALA A 534  0                                        
SHEET    2   D 5 HIS A 647  THR A 654 -1  O  ALA A 650   N  GLU A 532           
SHEET    3   D 5 PHE A 700  GLY A 707 -1  O  SER A 705   N  ILE A 649           
SHEET    4   D 5 VAL A 680  SER A 685 -1  N  TRP A 681   O  PHE A 704           
SHEET    5   D 5 VAL A 669  LEU A 672 -1  N  GLN A 670   O  PHE A 684           
CISPEP   1 ILE A  342    PRO A  343          0        -0.16                     
CISPEP   2 PHE A  449    PRO A  450          0        -0.58                     
CISPEP   3 ALA A  534    PRO A  535          0        -0.52                     
CRYST1   75.595   75.595  188.783  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      0.013228  0.007637  0.000000        0.00000                         
SCALE2      0.000000  0.015275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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