GenomeNet

Database: PDB
Entry: 2VQD
LinkDB: 2VQD
Original site: 2VQD 
HEADER    LIGASE                                  13-MAR-08   2VQD              
TITLE     CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA   
TITLE    2 COMPLEXED WITH AMPCP                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIOTIN CARBOXYLASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACETYL-COA CARBOXYLASE SUBUNIT A, ACC;                      
COMPND   5 EC: 6.3.4.14;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOTIDE-BINDING, FATTY ACID BIOSYNTHESIS, LIPID SYNTHESIS, ATP-    
KEYWDS   2 GRASP DOMAIN, BIOTIN CARBOXYLASE, LIGASE, BIOTIN, BACTERIA, ATP-     
KEYWDS   3 BINDING                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN                                                           
REVDAT   5   05-JUL-17 2VQD    1       REMARK                                   
REVDAT   4   13-JUL-11 2VQD    1       VERSN                                    
REVDAT   3   24-FEB-09 2VQD    1       VERSN                                    
REVDAT   2   30-SEP-08 2VQD    1       JRNL                                     
REVDAT   1   09-SEP-08 2VQD    0                                                
JRNL        AUTH   I.MOCHALKIN,J.R.MILLER,A.EVDOKIMOV,S.LIGHTLE,C.YAN,          
JRNL        AUTH 2 C.K.STOVER,G.L.WALDROP                                       
JRNL        TITL   STRUCTURAL EVIDENCE FOR SUBSTRATE-INDUCED SYNERGISM AND      
JRNL        TITL 2 HALF-SITES REACTIVITY IN BIOTIN CARBOXYLASE.                 
JRNL        REF    PROTEIN SCI.                  V.  17  1706 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18725455                                                     
JRNL        DOI    10.1110/PS.035584.108                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14953                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 791                             
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) : 2.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 884                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 44                           
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3412                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 232                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.51000                                              
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : -1.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.859         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.311         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.229         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.358        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3514 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3247 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4756 ; 1.212 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7541 ; 0.758 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   448 ; 5.853 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;36.850 ;23.718       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   600 ;15.604 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   529 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3943 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   697 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   691 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3225 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1687 ; 0.165 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2141 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   176 ; 0.149 ; 0.200       
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):    17 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    84 ; 0.182 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.172 ; 0.200       
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):  2883 ; 0.543 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3558 ; 0.619 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1469 ; 1.021 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1198 ; 1.503 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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     1        A   447                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1219  20.3449  13.0923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0552 T22:  -0.0555                                     
REMARK   3      T33:  -0.0993 T12:  -0.0093                                     
REMARK   3      T13:  -0.0309 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5996 L22:   1.9352                                     
REMARK   3      L33:   0.3516 L12:   0.0165                                     
REMARK   3      L13:  -0.1497 L23:  -0.3972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0393 S12:   0.0107 S13:   0.0827                       
REMARK   3      S21:   0.2110 S22:  -0.0420 S23:  -0.1140                       
REMARK   3      S31:  -0.0783 S32:  -0.0012 S33:   0.0027                       
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  1448        A  1448                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3358  31.0848   9.8703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0057 T22:   0.0004                                     
REMARK   3      T33:   0.0031 T12:  -0.0160                                     
REMARK   3      T13:   0.0067 T23:  -0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.7093 L22:  30.0504                                     
REMARK   3      L33:  14.9986 L12:  -0.3605                                     
REMARK   3      L13:  17.1687 L23:   0.8228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6192 S12:  -0.5199 S13:   0.7931                       
REMARK   3      S21:  -0.1356 S22:  -0.8025 S23:   1.4562                       
REMARK   3      S31:  -0.2469 S32:   0.4023 S33:   0.1833                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2VQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035552.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15777                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.860                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.0), 0.2M MGCL2, 15      
REMARK 280  -20% PEG3350                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       32.11350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.39300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.11350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.39300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 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 A2176  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     LYS A   448                                                      
REMARK 465     HIS A   449                                                      
REMARK 465     GLY A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     GLU A   452                                                      
REMARK 465     ASN A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     TYR A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     GLN A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     HIS A   460                                                      
REMARK 465     HIS A   461                                                      
REMARK 465     HIS A   462                                                      
REMARK 465     HIS A   463                                                      
REMARK 465     HIS A   464                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   9     -168.39   -168.00                                   
REMARK 500    PRO A  53     -174.39    -69.66                                   
REMARK 500    SER A  59      -84.29   -136.11                                   
REMARK 500    PHE A  84     -111.93     44.21                                   
REMARK 500    ASN A 281       59.73     35.50                                   
REMARK 500    THR A 291       58.37   -101.55                                   
REMARK 500    TYR A 381     -169.28   -126.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  444     GLY A  445                   38.81                    
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 A2013        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH A2019        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A2023        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH A2056        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A2074        DISTANCE =  6.45 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER (AP2):                   
REMARK 600  NON-HYDROLYZABLE ADP ANALOG                                         
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                              MG A1449  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 276   OE1                                                    
REMARK 620 2 GLU A 288   OE2  78.2                                              
REMARK 620 3 AP2 A1448   O2A  80.2  71.8                                        
REMARK 620 4 HOH A2133   O    83.6 159.3  95.6                                  
REMARK 620 5 AP2 A1448   O1B 153.8  91.2  73.7 101.1                            
REMARK 620 6 HOH A2139   O    93.3  80.3 152.0 110.9 108.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AP2 A1448                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1449                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1450                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C00   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA  
REMARK 900 IN APO FORM                                                          
REMARK 900 RELATED ID: 2J9G   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX      
REMARK 900 WITH AMPPNP AND ADP                                                  
REMARK 900 RELATED ID: 2VPQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM S. AUREUS COMPLEXED     
REMARK 900 WITH AMPPNP                                                          
REMARK 900 RELATED ID: 2VR1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX      
REMARK 900 WITH ATP ANALOG, ADPCF2P.                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 C-TERMINAL HIS-TAG PRESENT                                           
DBREF  2VQD A    1   449  UNP    P37798   ACCC_PSEAE       1    449             
DBREF  2VQD A  450   464  PDB    2VQD     2VQD           450    464             
SEQRES   1 A  464  MET LEU GLU LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 A  464  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 A  464  LYS THR VAL ALA VAL HIS SER THR ALA ASP ARG GLU LEU          
SEQRES   4 A  464  MET HIS LEU SER LEU ALA ASP GLU SER VAL CYS ILE GLY          
SEQRES   5 A  464  PRO ALA PRO ALA THR GLN SER TYR LEU GLN ILE PRO ALA          
SEQRES   6 A  464  ILE ILE ALA ALA ALA GLU VAL THR GLY ALA THR ALA ILE          
SEQRES   7 A  464  HIS PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE          
SEQRES   8 A  464  ALA GLU GLN ILE GLU ARG SER GLY PHE THR PHE VAL GLY          
SEQRES   9 A  464  PRO THR ALA GLU VAL ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 A  464  SER ALA LYS ASP ALA MET LYS ARG ALA GLY VAL PRO THR          
SEQRES  11 A  464  VAL PRO GLY SER ASP GLY PRO LEU PRO GLU ASP GLU GLU          
SEQRES  12 A  464  THR ALA LEU ALA ILE ALA ARG GLU VAL GLY TYR PRO VAL          
SEQRES  13 A  464  ILE ILE LYS ALA ALA GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 A  464  ARG VAL VAL TYR ASP GLU SER GLU LEU ILE LYS SER ALA          
SEQRES  15 A  464  LYS LEU THR ARG THR GLU ALA GLY ALA ALA PHE GLY ASN          
SEQRES  16 A  464  PRO MET VAL TYR LEU GLU LYS PHE LEU THR ASN PRO ARG          
SEQRES  17 A  464  HIS VAL GLU VAL GLN VAL LEU SER ASP GLY GLN GLY ASN          
SEQRES  18 A  464  ALA ILE HIS LEU GLY ASP ARG ASP CYS SER LEU GLN ARG          
SEQRES  19 A  464  ARG HIS GLN LYS VAL ILE GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 A  464  ILE ASP GLU LYS ALA ARG GLN GLU VAL PHE ALA ARG CYS          
SEQRES  21 A  464  VAL GLN ALA CYS ILE GLU ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 A  464  THR PHE GLU PHE LEU TYR GLU ASN GLY ARG PHE TYR PHE          
SEQRES  23 A  464  ILE GLU MET ASN THR ARG VAL GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  464  SER GLU MET VAL THR GLY VAL ASP ILE VAL LYS GLU MET          
SEQRES  25 A  464  LEU ARG ILE ALA SER GLY GLU LYS LEU SER ILE ARG GLN          
SEQRES  26 A  464  GLU ASP VAL VAL ILE ARG GLY HIS ALA LEU GLU CYS ARG          
SEQRES  27 A  464  ILE ASN ALA GLU ASP PRO LYS THR PHE MET PRO SER PRO          
SEQRES  28 A  464  GLY LYS VAL LYS HIS PHE HIS ALA PRO GLY GLY ASN GLY          
SEQRES  29 A  464  VAL ARG VAL ASP SER HIS LEU TYR SER GLY TYR SER VAL          
SEQRES  30 A  464  PRO PRO ASN TYR ASP SER LEU VAL GLY LYS VAL ILE THR          
SEQRES  31 A  464  TYR GLY ALA ASP ARG ASP GLU ALA LEU ALA ARG MET ARG          
SEQRES  32 A  464  ASN ALA LEU ASP GLU LEU ILE VAL ASP GLY ILE LYS THR          
SEQRES  33 A  464  ASN THR GLU LEU HIS LYS ASP LEU VAL ARG ASP ALA ALA          
SEQRES  34 A  464  PHE CYS LYS GLY GLY VAL ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 A  464  LYS LEU GLY MET ASP LYS HIS GLY SER GLU ASN LEU TYR          
SEQRES  36 A  464  PHE GLN GLY HIS HIS HIS HIS HIS HIS                          
HET    AP2  A1448      27                                                       
HET     MG  A1449       1                                                       
HET    SO4  A1450       5                                                       
HETNAM     AP2 PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  AP2    C11 H17 N5 O9 P2                                             
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *232(H2 O)                                                    
HELIX    1   1 ARG A   10  LEU A   24  1                                  15    
HELIX    2   2 ALA A   35  ARG A   37  5                                   3    
HELIX    3   3 LEU A   39  ALA A   45  1                                   7    
HELIX    4   4 PRO A   55  SER A   59  5                                   5    
HELIX    5   5 GLN A   62  GLY A   74  1                                  13    
HELIX    6   6 ASN A   88  SER A   98  1                                  11    
HELIX    7   7 THR A  106  ASP A  115  1                                  10    
HELIX    8   8 ASP A  115  ALA A  126  1                                  12    
HELIX    9   9 ASP A  141  GLY A  153  1                                  13    
HELIX   10  10 ASP A  174  SER A  176  5                                   3    
HELIX   11  11 GLU A  177  GLY A  194  1                                  18    
HELIX   12  12 ASP A  249  GLY A  268  1                                  20    
HELIX   13  13 GLU A  296  GLY A  305  1                                  10    
HELIX   14  14 ASP A  307  SER A  317  1                                  11    
HELIX   15  15 ARG A  324  VAL A  328  5                                   5    
HELIX   16  16 ASP A  394  LEU A  409  1                                  16    
HELIX   17  17 ASN A  417  VAL A  425  1                                   9    
HELIX   18  18 ASP A  427  GLY A  433  1                                   7    
HELIX   19  19 HIS A  438  GLY A  445  1                                   8    
SHEET    1  AA 5 GLU A  47  GLY A  52  0                                        
SHEET    2  AA 5 LYS A  27  SER A  33  1  O  THR A  28   N  GLU A  47           
SHEET    3  AA 5 LYS A   4  ILE A   7  1  O  VAL A   5   N  VAL A  29           
SHEET    4  AA 5 ALA A  77  HIS A  79  1  O  ALA A  77   N  LEU A   6           
SHEET    5  AA 5 THR A 101  PHE A 102  1  O  THR A 101   N  ILE A  78           
SHEET    1  AB 3 MET A 169  VAL A 172  0                                        
SHEET    2  AB 3 VAL A 156  ALA A 160 -1  O  VAL A 156   N  VAL A 172           
SHEET    3  AB 3 VAL A 198  LYS A 202 -1  O  TYR A 199   N  LYS A 159           
SHEET    1  AC 4 ALA A 222  ASP A 229  0                                        
SHEET    2  AC 4 ARG A 208  ASP A 217 -1  O  GLU A 211   N  ARG A 228           
SHEET    3  AC 4 ARG A 270  GLU A 280 -1  O  GLY A 271   N  SER A 216           
SHEET    4  AC 4 ARG A 283  ASN A 290 -1  O  ARG A 283   N  GLU A 280           
SHEET    1  AD 2 GLN A 233  ARG A 234  0                                        
SHEET    2  AD 2 GLN A 237  LYS A 238 -1  O  GLN A 237   N  ARG A 234           
SHEET    1  AE 4 ILE A 240  ALA A 243  0                                        
SHEET    2  AE 4 HIS A 333  ASN A 340 -1  O  ALA A 334   N  ALA A 243           
SHEET    3  AE 4 LEU A 384  GLY A 392 -1  N  VAL A 385   O  ILE A 339           
SHEET    4  AE 4 VAL A 365  SER A 369 -1  O  ARG A 366   N  ILE A 389           
SHEET    1  AF 2 GLY A 352  VAL A 354  0                                        
SHEET    2  AF 2 TYR A 375  VAL A 377 -1  O  TYR A 375   N  VAL A 354           
SHEET    1  AG 2 HIS A 356  HIS A 358  0                                        
SHEET    2  AG 2 ILE A 410  ASP A 412 -1  O  ILE A 410   N  HIS A 358           
LINK        MG    MG A1449                 OE1 GLU A 276     1555   1555  2.36  
LINK        MG    MG A1449                 OE2 GLU A 288     1555   1555  1.89  
LINK        MG    MG A1449                 O2A AP2 A1448     1555   1555  2.37  
LINK        MG    MG A1449                 O   HOH A2133     1555   1555  2.20  
LINK        MG    MG A1449                 O1B AP2 A1448     1555   1555  2.01  
LINK        MG    MG A1449                 O   HOH A2139     1555   1555  2.00  
CISPEP   1 TYR A  154    PRO A  155          0         2.46                     
CISPEP   2 ALA A  243    PRO A  244          0       -10.32                     
SITE     1 AC1 22 LYS A 116  ILE A 157  LYS A 159  GLY A 163                    
SITE     2 AC1 22 GLY A 164  GLY A 165  GLY A 166  MET A 169                    
SITE     3 AC1 22 GLU A 201  LYS A 202  PHE A 203  LEU A 204                    
SITE     4 AC1 22 HIS A 209  GLN A 233  HIS A 236  GLU A 276                    
SITE     5 AC1 22 LEU A 278  GLU A 288  ILE A 437   MG A1449                    
SITE     6 AC1 22 HOH A2092  HOH A2231                                          
SITE     1 AC2  5 GLU A 276  GLU A 288  AP2 A1448  HOH A2133                    
SITE     2 AC2  5 HOH A2139                                                     
SITE     1 AC3  7 GLU A  87  MET A 113  GLY A 114  GLY A 163                    
SITE     2 AC3  7 GLU A 288  MET A 289  HOH A2140                               
CRYST1   64.227  126.786   49.878  90.00  90.00  90.00 P 21 21 2     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      0.015570  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007887  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020049        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system