HEADER LIGASE 18-DEC-08 2W6Q
TITLE CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN
TITLE 2 COMPLEX WITH THE TRIAZINE-2,4-DIAMINE FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACETYL-COA CARBOXYLASE SUBUNIT A, ACC;
COMPND 5 EC: 6.3.4.14, 6.4.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGASE, ATP-BINDING, FATTY ACID BIOSYNTHESIS, NUCLEOTIDE-BINDING,
KEYWDS 2 LIPID SYNTHESIS, ATP-GRASP DOMAIN, FRAGMENT SCREENING
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOCHALKIN,J.R.MILLER
REVDAT 2 27-APR-11 2W6Q 1 KEYWDS JRNL REMARK HETNAM
REVDAT 2 2 FORMUL
REVDAT 1 19-MAY-09 2W6Q 0
JRNL AUTH I.MOCHALKIN,J.R.MILLER,L.S.NARASIMHAN,V.THANABAL,
JRNL AUTH 2 P.ERDMAN,P.COX,J.V.PRASAD,S.LIGHTLE,M.HUBAND,
JRNL AUTH 3 K.STOVER
JRNL TITL DISCOVERY OF ANTIBACTERIAL BIOTIN CARBOXYLASE
JRNL TITL 2 INHIBITORS BY VIRTUAL SCREENING AND FRAGMENT-BASED
JRNL TITL 3 APPROACHES.
JRNL REF ACS CHEM.BIOL. V. 4 473 2009
JRNL REFN ISSN 1554-8929
JRNL PMID 19413326
JRNL DOI 10.1021/CB9000102
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 62953
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3364
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4408
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 253
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.789
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7060 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9520 ; 1.057 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 889 ; 5.148 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 319 ;35.379 ;23.668
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1247 ;13.666 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;18.413 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1038 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5363 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3353 ; 0.178 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4873 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 609 ; 0.120 ; 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): 56 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.132 ; 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): 4575 ; 0.475 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7093 ; 0.819 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2802 ; 1.308 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2427 ; 2.202 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2W6Q COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-08.
REMARK 100 THE PDBE ID CODE IS EBI-38400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66405
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.05
REMARK 200 RESOLUTION RANGE LOW (A) : 100.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.99
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.22
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.0
REMARK 200 R MERGE FOR SHELL (I) : 0.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.50
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 2J9G
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M KCL AND 2-8% PEG-800
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 41.99800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.02250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.78650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.02250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.99800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.78650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 448
REMARK 465 LYS A 449
REMARK 465 GLN B 447
REMARK 465 GLU B 448
REMARK 465 LYS B 449
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 447 CA C O CB CG CD OE1 NE2
REMARK 470 LEU B 446 CA C O CB CG CD1 CD2
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 SER A 59 -87.10 -126.97
REMARK 500 PHE A 84 -111.78 38.92
REMARK 500 LEU A 225 61.57 -118.74
REMARK 500 ALA A 226 -155.74 56.02
REMARK 500 ASN B 9 -169.49 -170.65
REMARK 500 SER B 59 -85.56 -135.50
REMARK 500 PHE B 84 -115.01 43.78
REMARK 500 SER B 194 14.68 57.55
REMARK 500 LEU B 225 64.22 -119.59
REMARK 500 ALA B 226 -155.11 55.25
REMARK 500 THR B 291 57.97 -92.08
REMARK 500 TYR B 381 -167.85 -123.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 6-(2-PHENOXY-ETHOXY)-[1,3,5]TRIAZINE-2,4-DIAMINE (OA5):
REMARK 600 INITIAL FRAGMENT SCREENING HIT
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OA5 A1447
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OA5 B1446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1447
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2J9G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH AMPPNP AND ADP
REMARK 900 RELATED ID: 2VR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH ATP ANALOG, ADPCF2P.
REMARK 900 RELATED ID: 2V5A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E.COLI IN COMPLEX WITH POTENT INHIBITOR 3
REMARK 900 RELATED ID: 1K69 RELATED DB: PDB
REMARK 900 MODEL INTERACTION BETWEEN BCCP AND ATP-BOUND
REMARK 900 CARBOXYLASESUBUNIT OF ACETYL COA CARBOXYLASE
REMARK 900 RELATED ID: 2GPW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE
REMARK 900 SUBUNIT, F363AMUTANT, OF ACETYL-COA
REMARK 900 CARBOXYLASE FROM ESCHERICHIA COLI.
REMARK 900 RELATED ID: 2W6N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH AMINO-OXAZOLE
REMARK 900 FRAGMENT SERIES
REMARK 900 RELATED ID: 1BNC RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: BIOTIN CARBOXYLASE; CHAIN
REMARK 900 : A, B; EC: 6.3.4.14
REMARK 900 RELATED ID: 2W71 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH THE IMIDAZOLE-
REMARK 900 PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 2V59 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E.COLI IN COMPLEX WITH POTENT INHIBITOR 2
REMARK 900 RELATED ID: 2W6P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH 5-METHYL-6-
REMARK 900 PHENYL-QUINAZOLINE-2,4-DIAMINE
REMARK 900 RELATED ID: 2W7C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH THE 2-AMINO-
REMARK 900 PYRIMIDINE FRAGMENT
REMARK 900 RELATED ID: 2V58 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E.COLI IN COMPLEX WITH POTENT INHIBITOR 1
REMARK 900 RELATED ID: 2W6O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH 4-AMINO-7,7-
REMARK 900 DIMETHYL-7,8-DIHYDRO-QUINAZOLINONE FRAGMENT
REMARK 900 RELATED ID: 2W6Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH THE 3-(3-METHYL
REMARK 900 -BUT-2-ENYL)-3H-PURIN-6-YLAMINE FRAGMENT
REMARK 900 RELATED ID: 1DV1 RELATED DB: PDB
REMARK 900 STRUCTURE OF BIOTIN CARBOXYLASE (APO)
REMARK 900 RELATED ID: 2W6M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH AMINO-OXAZOLE
REMARK 900 FRAGMENT SERIES
REMARK 900 RELATED ID: 2GPS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE
REMARK 900 SUBUNIT, E23RMUTANT, OF ACETYL-COA CARBOXYLASE
REMARK 900 FROM ESCHERICHIA COLI.
REMARK 900 RELATED ID: 2W70 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM
REMARK 900 E. COLI IN COMPLEX WITH THE AMINO-THIAZOLE
REMARK 900 -PYRIMIDINE FRAGMENT
REMARK 900 RELATED ID: 1DV2 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BIOTIN CARBOXYLASE, MUTANT
REMARK 900 E288K, COMPLEXED WITH ATP
DBREF 2W6Q A 1 449 UNP P24182 ACCC_ECOLI 1 449
DBREF 2W6Q B 1 449 UNP P24182 ACCC_ECOLI 1 449
SEQRES 1 A 449 MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE
SEQRES 2 A 449 ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE
SEQRES 3 A 449 LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU
SEQRES 4 A 449 LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY
SEQRES 5 A 449 PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA
SEQRES 6 A 449 ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE
SEQRES 7 A 449 HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE
SEQRES 8 A 449 ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY
SEQRES 9 A 449 PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL
SEQRES 10 A 449 SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS
SEQRES 11 A 449 VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP
SEQRES 12 A 449 LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL
SEQRES 13 A 449 ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET
SEQRES 14 A 449 ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE
SEQRES 15 A 449 SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN
SEQRES 16 A 449 ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG
SEQRES 17 A 449 HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN
SEQRES 18 A 449 ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG
SEQRES 19 A 449 ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY
SEQRES 20 A 449 ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS
SEQRES 21 A 449 ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY
SEQRES 22 A 449 THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE
SEQRES 23 A 449 ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL
SEQRES 24 A 449 THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN
SEQRES 25 A 449 LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN
SEQRES 26 A 449 GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG
SEQRES 27 A 449 ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO
SEQRES 28 A 449 GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY
SEQRES 29 A 449 VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL
SEQRES 30 A 449 PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS
SEQRES 31 A 449 TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS
SEQRES 32 A 449 ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR
SEQRES 33 A 449 ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN
SEQRES 34 A 449 PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS
SEQRES 35 A 449 LYS LEU GLY LEU GLN GLU LYS
SEQRES 1 B 449 MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE
SEQRES 2 B 449 ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE
SEQRES 3 B 449 LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU
SEQRES 4 B 449 LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY
SEQRES 5 B 449 PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA
SEQRES 6 B 449 ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE
SEQRES 7 B 449 HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE
SEQRES 8 B 449 ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY
SEQRES 9 B 449 PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL
SEQRES 10 B 449 SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS
SEQRES 11 B 449 VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP
SEQRES 12 B 449 LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL
SEQRES 13 B 449 ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET
SEQRES 14 B 449 ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE
SEQRES 15 B 449 SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN
SEQRES 16 B 449 ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG
SEQRES 17 B 449 HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN
SEQRES 18 B 449 ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG
SEQRES 19 B 449 ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY
SEQRES 20 B 449 ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS
SEQRES 21 B 449 ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY
SEQRES 22 B 449 THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE
SEQRES 23 B 449 ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL
SEQRES 24 B 449 THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN
SEQRES 25 B 449 LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN
SEQRES 26 B 449 GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG
SEQRES 27 B 449 ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO
SEQRES 28 B 449 GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY
SEQRES 29 B 449 VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL
SEQRES 30 B 449 PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS
SEQRES 31 B 449 TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS
SEQRES 32 B 449 ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR
SEQRES 33 B 449 ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN
SEQRES 34 B 449 PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS
SEQRES 35 B 449 LYS LEU GLY LEU GLN GLU LYS
HET OA5 A1447 18
HET OA5 B1446 18
HET CL A1448 1
HET CL B1447 1
HETNAM OA5 6-(2-PHENOXYETHOXY)-1,3,5-TRIAZINE-2,4-DIAMINE
HETNAM CL CHLORIDE ION
FORMUL 3 OA5 2(C11 H13 N5 O2)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 HOH *699(H2 O)
HELIX 1 1 ARG A 10 LEU A 24 1 15
HELIX 2 2 LEU A 39 ALA A 45 1 7
HELIX 3 3 PRO A 55 SER A 59 5 5
HELIX 4 4 ASN A 62 GLY A 74 1 13
HELIX 5 5 ASN A 88 SER A 98 1 11
HELIX 6 6 LYS A 106 ASP A 115 1 10
HELIX 7 7 ASP A 115 GLY A 127 1 13
HELIX 8 8 ASP A 141 GLY A 153 1 13
HELIX 9 9 GLY A 174 SER A 194 1 21
HELIX 10 10 THR A 249 GLY A 268 1 20
HELIX 11 11 GLU A 296 GLY A 305 1 10
HELIX 12 12 ASP A 307 GLY A 318 1 12
HELIX 13 13 LYS A 324 VAL A 328 5 5
HELIX 14 14 ASN A 394 LEU A 409 1 16
HELIX 15 15 ASN A 417 ASN A 426 1 10
HELIX 16 16 ASP A 427 GLY A 433 1 7
HELIX 17 17 HIS A 438 LEU A 446 1 9
HELIX 18 18 ARG B 10 GLY B 25 1 16
HELIX 19 19 ALA B 35 ARG B 37 5 3
HELIX 20 20 LEU B 39 ALA B 45 1 7
HELIX 21 21 PRO B 55 SER B 59 5 5
HELIX 22 22 ASN B 62 THR B 73 1 12
HELIX 23 23 ASN B 88 SER B 98 1 11
HELIX 24 24 LYS B 106 ASP B 115 1 10
HELIX 25 25 ASP B 115 GLY B 127 1 13
HELIX 26 26 ASP B 141 GLY B 153 1 13
HELIX 27 27 GLY B 174 PHE B 193 1 20
HELIX 28 28 THR B 249 GLY B 268 1 20
HELIX 29 29 GLU B 296 GLY B 305 1 10
HELIX 30 30 ASP B 307 ALA B 317 1 11
HELIX 31 31 LYS B 324 VAL B 328 5 5
HELIX 32 32 ASN B 394 LEU B 409 1 16
HELIX 33 33 ASN B 417 ASP B 427 1 11
HELIX 34 34 ASP B 427 GLY B 433 1 7
HELIX 35 35 HIS B 438 GLY B 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 ILE A 5 N VAL A 29
SHEET 4 AA 5 ALA A 77 HIS A 79 1 O ALA A 77 N VAL A 6
SHEET 5 AA 5 ILE A 101 PHE A 102 1 O ILE A 101 N ILE A 78
SHEET 1 AB 3 ARG A 167 VAL A 172 0
SHEET 2 AB 3 VAL A 156 GLY A 164 -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 8 GLU A 283 ASN A 290 0
SHEET 2 AC 8 GLY A 271 GLU A 280 -1 O THR A 274 N ASN A 290
SHEET 3 AC 8 ARG A 208 ALA A 216 -1 O ARG A 208 N PHE A 279
SHEET 4 AC 8 ALA A 222 ARG A 234 -1 O ILE A 223 N LEU A 215
SHEET 5 AC 8 GLN A 237 ALA A 243 -1 O GLN A 237 N ARG A 234
SHEET 6 AC 8 HIS A 333 ASN A 340 -1 O ALA A 334 N ALA A 243
SHEET 7 AC 8 MET A 384 GLY A 392 -1 N ILE A 385 O ILE A 339
SHEET 8 AC 8 VAL A 365 SER A 369 -1 O ARG A 366 N ILE A 389
SHEET 1 AD 2 GLY A 352 LYS A 353 0
SHEET 2 AD 2 THR A 376 VAL A 377 -1 O VAL A 377 N GLY A 352
SHEET 1 AE 2 ARG A 356 HIS A 358 0
SHEET 2 AE 2 ILE A 410 ASP A 412 -1 O ILE A 410 N HIS A 358
SHEET 1 BA 5 GLU B 47 GLY B 52 0
SHEET 2 BA 5 LYS B 27 SER B 33 1 O THR B 28 N GLU B 47
SHEET 3 BA 5 LYS B 4 ILE B 7 1 O ILE B 5 N VAL B 29
SHEET 4 BA 5 ALA B 77 HIS B 79 1 O ALA B 77 N VAL B 6
SHEET 5 BA 5 ILE B 101 PHE B 102 1 O ILE B 101 N ILE B 78
SHEET 1 BB 3 MET B 169 VAL B 172 0
SHEET 2 BB 3 VAL B 156 ALA B 160 -1 O VAL B 156 N VAL B 172
SHEET 3 BB 3 VAL B 198 LYS B 202 -1 O TYR B 199 N LYS B 159
SHEET 1 BC 8 GLU B 283 ASN B 290 0
SHEET 2 BC 8 ARG B 270 GLU B 280 -1 O THR B 274 N ASN B 290
SHEET 3 BC 8 ARG B 208 ASP B 217 -1 O ARG B 208 N PHE B 279
SHEET 4 BC 8 ALA B 222 ARG B 234 -1 O ILE B 223 N LEU B 215
SHEET 5 BC 8 GLN B 237 ALA B 243 -1 O GLN B 237 N ARG B 234
SHEET 6 BC 8 HIS B 333 ASN B 340 -1 O ALA B 334 N ALA B 243
SHEET 7 BC 8 MET B 384 GLY B 392 -1 N ILE B 385 O ILE B 339
SHEET 8 BC 8 VAL B 365 SER B 369 -1 O ARG B 366 N ILE B 389
SHEET 1 BD 2 GLY B 352 LYS B 353 0
SHEET 2 BD 2 THR B 376 VAL B 377 -1 O VAL B 377 N GLY B 352
SHEET 1 BE 2 ARG B 356 HIS B 358 0
SHEET 2 BE 2 ILE B 410 ASP B 412 -1 O ILE B 410 N HIS B 358
CISPEP 1 TYR A 154 PRO A 155 0 -1.88
CISPEP 2 ALA A 243 PRO A 244 0 -9.37
CISPEP 3 TYR B 154 PRO B 155 0 -2.88
CISPEP 4 ALA B 243 PRO B 244 0 -8.80
SITE 1 AC1 11 ILE A 157 LYS A 159 MET A 169 GLU A 201
SITE 2 AC1 11 LYS A 202 TYR A 203 LEU A 204 HIS A 236
SITE 3 AC1 11 LEU A 278 HIS A 438 HOH A2214
SITE 1 AC2 9 LYS B 159 MET B 169 GLU B 201 LYS B 202
SITE 2 AC2 9 TYR B 203 LEU B 204 HIS B 236 LEU B 278
SITE 3 AC2 9 HOH B2299
SITE 1 AC3 3 ARG A 292 GLN A 294 VAL A 295
SITE 1 AC4 4 ARG B 292 GLN B 294 VAL B 295 HOH B2176
CRYST1 83.996 105.573 122.045 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011905 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
