HEADER LIGASE 02-OCT-08 2V5A
TITLE CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E.COLI IN COMPLEX WITH
TITLE 2 POTENT INHIBITOR 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACETYL-COA CARBOXYLASE SUBUNIT A;
COMPND 5 EC: 6.3.4.14;
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 FATTY ACID BIOSYNTHESIS, BIOTIN CARBOXYLASE, NUCLEOTIDE-BINDING, ATP-
KEYWDS 2 BINDING, ANTIBACTERIAL, LIPID SYNTHESIS, FAS, LIGASE, BIOTIN,
KEYWDS 3 BACTERIAL, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOCHALKIN,J.R.MILLER
REVDAT 4 13-DEC-23 2V5A 1 REMARK
REVDAT 3 24-FEB-09 2V5A 1 JRNL
REVDAT 2 03-FEB-09 2V5A 1 JRNL REMARK
REVDAT 1 13-JAN-09 2V5A 0
JRNL AUTH J.R.MILLER,S.DUNHAM,I.MOCHALKIN,C.BANOTAI,M.BOWMAN,S.BUIST,
JRNL AUTH 2 B.DUNKLE,D.HANNA,H.J.HARWOOD,M.D.HUBAND,A.KARNOVSKY,M.KUHN,
JRNL AUTH 3 C.LIMBERAKIS,J.Y.LIU,S.MEHRENS,W.T.MUELLER,L.NARASIMHAN,
JRNL AUTH 4 A.OGDEN,J.OHREN,J.V.PRASAD,J.A.SHELLY,L.SKERLOS,M.SULAVIK,
JRNL AUTH 5 V.H.THOMAS,S.VANDERROEST,L.WANG,Z.WANG,A.WHITTON,T.ZHU,
JRNL AUTH 6 C.K.STOVER
JRNL TITL A CLASS OF SELECTIVE ANTIBACTERIALS DERIVED FROM A PROTEIN
JRNL TITL 2 KINASE INHIBITOR PHARMACOPHORE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 1737 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19164768
JRNL DOI 10.1073/PNAS.0811275106
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.4
REMARK 3 NUMBER OF REFLECTIONS : 39547
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2120
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2710
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6860
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 339
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -0.90000
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): 0.411
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.251
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.208
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7043 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9503 ; 0.998 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 889 ; 4.916 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 319 ;34.995 ;23.668
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1243 ;13.908 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;16.775 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1038 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5355 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3185 ; 0.173 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4847 ; 0.293 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 366 ; 0.116 ; 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): 42 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.125 ; 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): 4581 ; 0.358 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7092 ; 0.610 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2797 ; 0.850 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2411 ; 1.464 ; 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 : 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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2V5A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1290037727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-05
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 : 41691
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
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 (%) : 85.3
REMARK 200 DATA REDUNDANCY : 3.210
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.740
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 (%): 54.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M POTASSIUM CHLORIDE, 4% (W/V) PEG
REMARK 280 8000
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 42.15750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.09200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.09200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.15750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.20500
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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
REMARK 470 GLN A 447 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 -88.56 -120.83
REMARK 500 PHE A 84 -110.99 36.14
REMARK 500 SER A 194 29.03 49.51
REMARK 500 ALA A 226 -158.12 57.91
REMARK 500 ASN B 9 -171.18 -170.52
REMARK 500 SER B 59 -84.15 -130.39
REMARK 500 PHE B 84 -115.92 45.46
REMARK 500 SER B 194 1.13 55.51
REMARK 500 ALA B 226 -155.86 56.42
REMARK 500 THR B 291 59.13 -92.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LZL A1447
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1446
REMARK 900
REMARK 900 RELATED ENTRIES
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: 2VR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX
REMARK 900 WITH ATP ANALOG, ADPCF2P.
REMARK 900 RELATED ID: 1K69 RELATED DB: PDB
REMARK 900 MODEL INTERACTION BETWEEN BCCP AND ATP-BOUND CARBOXYLASESUBUNIT OF
REMARK 900 ACETYL COA CARBOXYLASE
REMARK 900 RELATED ID: 2GPW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT, F363AMUTANT,
REMARK 900 OF ACETYL-COA CARBOXYLASE FROM ESCHERICHIA COLI.
REMARK 900 RELATED ID: 1DV1 RELATED DB: PDB
REMARK 900 STRUCTURE OF BIOTIN CARBOXYLASE (APO)
REMARK 900 RELATED ID: 1BNC RELATED DB: PDB
REMARK 900 RELATED ID: 2GPS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT, E23RMUTANT, OF
REMARK 900 ACETYL-COA CARBOXYLASE FROM ESCHERICHIA COLI.
REMARK 900 RELATED ID: 1DV2 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BIOTIN CARBOXYLASE, MUTANT E288K, COMPLEXED WITH
REMARK 900 ATP
REMARK 900 RELATED ID: 2V59 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E.COLI IN COMPLEX WITH
REMARK 900 POTENT INHIBITOR 2
REMARK 900 RELATED ID: 2V58 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E.COLI IN COMPLEX WITH
REMARK 900 POTENT INHIBITOR 1
DBREF 2V5A A 1 449 UNP P24182 ACCC_ECOLI 1 449
DBREF 2V5A 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 LZL A1447 22
HET CL A1448 1
HET CL B1446 1
HETNAM LZL 7-(2,5-DIHYDROPYRROL-1-YL)-6-PHENYL-PYRIDO[6,5-
HETNAM 2 LZL D]PYRIMIDIN-2-AMINE
HETNAM CL CHLORIDE ION
FORMUL 3 LZL C17 H15 N5
FORMUL 4 CL 2(CL 1-)
FORMUL 6 HOH *339(H2 O)
HELIX 1 1 ARG A 10 GLY A 25 1 16
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 ASN A 62 GLY A 74 1 13
HELIX 6 6 ASN A 88 SER A 98 1 11
HELIX 7 7 LYS A 106 GLY A 114 1 9
HELIX 8 8 ASP A 115 GLY A 127 1 13
HELIX 9 9 ASP A 141 GLY A 153 1 13
HELIX 10 10 GLY A 174 SER A 194 1 21
HELIX 11 11 THR A 249 GLY A 268 1 20
HELIX 12 12 GLU A 296 GLY A 305 1 10
HELIX 13 13 ASP A 307 GLY A 318 1 12
HELIX 14 14 LYS A 324 VAL A 328 5 5
HELIX 15 15 ASN A 394 LEU A 409 1 16
HELIX 16 16 ASN A 417 ASN A 426 1 10
HELIX 17 17 ASP A 427 GLY A 433 1 7
HELIX 18 18 HIS A 438 LEU A 446 1 9
HELIX 19 19 ARG B 10 GLY B 25 1 16
HELIX 20 20 SER B 33 ARG B 37 5 5
HELIX 21 21 LEU B 39 ALA B 45 1 7
HELIX 22 22 PRO B 55 SER B 59 5 5
HELIX 23 23 ASN B 62 THR B 73 1 12
HELIX 24 24 ASN B 88 SER B 98 1 11
HELIX 25 25 LYS B 106 ASP B 115 1 10
HELIX 26 26 ASP B 115 GLY B 127 1 13
HELIX 27 27 ASP B 141 GLY B 153 1 13
HELIX 28 28 GLU B 177 PHE B 193 1 17
HELIX 29 29 THR B 249 ILE B 267 1 19
HELIX 30 30 GLU B 296 GLY B 305 1 10
HELIX 31 31 ASP B 307 ALA B 317 1 11
HELIX 32 32 LYS B 324 VAL B 328 5 5
HELIX 33 33 ASN B 394 LEU B 409 1 16
HELIX 34 34 ASN B 417 ASN B 426 1 10
HELIX 35 35 ASP B 427 GLY B 433 1 7
HELIX 36 36 HIS B 438 LEU B 444 1 7
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 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 ALA A 216 -1 O GLU A 211 N ARG A 228
SHEET 3 AC 4 GLY A 271 GLU A 280 -1 O GLY A 271 N ALA A 216
SHEET 4 AC 4 GLU A 283 ASN A 290 -1 O GLU 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 VAL 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 MET A 384 GLY A 392 -1 N ILE 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 LYS A 353 0
SHEET 2 AF 2 THR A 376 VAL A 377 -1 O VAL A 377 N GLY A 352
SHEET 1 AG 2 ARG 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
SHEET 1 BA 5 GLU B 47 CYS B 50 0
SHEET 2 BA 5 LYS B 27 HIS B 32 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 4 ALA B 222 ASP B 229 0
SHEET 2 BC 4 ARG B 208 ASP B 217 -1 O GLU B 211 N ARG B 228
SHEET 3 BC 4 ARG B 270 GLU B 280 -1 O GLY B 271 N ALA B 216
SHEET 4 BC 4 GLU B 283 ASN B 290 -1 O GLU B 283 N GLU B 280
SHEET 1 BD 2 GLN B 233 ARG B 234 0
SHEET 2 BD 2 GLN B 237 LYS B 238 -1 O GLN B 237 N ARG B 234
SHEET 1 BE 4 VAL B 240 ALA B 243 0
SHEET 2 BE 4 HIS B 333 ASN B 340 -1 O ALA B 334 N ALA B 243
SHEET 3 BE 4 MET B 384 GLY B 392 -1 N ILE B 385 O ILE B 339
SHEET 4 BE 4 VAL B 365 GLU B 368 -1 O ARG B 366 N ILE B 389
SHEET 1 BF 2 GLY B 352 LYS B 353 0
SHEET 2 BF 2 THR B 376 VAL B 377 -1 O VAL B 377 N GLY B 352
SHEET 1 BG 2 ARG B 356 HIS B 358 0
SHEET 2 BG 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 0.93
CISPEP 2 ALA A 243 PRO A 244 0 -6.78
CISPEP 3 TYR B 154 PRO B 155 0 -0.62
CISPEP 4 ALA B 243 PRO B 244 0 -5.91
SITE 1 AC1 12 ILE A 157 LYS A 159 MET A 169 GLU A 201
SITE 2 AC1 12 LYS A 202 LEU A 204 GLN A 233 HIS A 236
SITE 3 AC1 12 LEU A 278 ILE A 287 GLU A 288 ILE A 437
SITE 1 AC2 3 ARG A 292 GLN A 294 VAL A 295
SITE 1 AC3 2 ARG B 292 VAL B 295
CRYST1 84.315 106.410 122.184 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 0.011860 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
