HEADER TRANSFERASE 10-AUG-07 2QX1
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN MYCOBACTERIUM TUBERCULOSIS
TITLE 2 BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (FABH) AND DECYL-COA
TITLE 3 DISULFIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-KETOACYL-ACP SYNTHASE III;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 3-OXOACYL- [ACYL-CARRIER-PROTEIN] SYNTHASE III, 3-OXOACYL-
COMPND 5 [ACYL-CARRIER-PROTEIN] SYNTHASE 3, KAS III, MTFABH;
COMPND 6 EC: 2.3.1.41;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: FABH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FATTY ACID BIOSYNTHESIS, MYOBACTERIUM TUBERCULOSIS, STRUCTURAL BASIS
KEYWDS 2 FOR SUBSTRATE SPECIFICITY, ENZYME INHIBITOR COMPLEX, MECHANISM BASED
KEYWDS 3 INHIBITOR, ACYLTRANSFERASE, LIPID SYNTHESIS, MULTIFUNCTIONAL ENZYME,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SACHDEVA,F.MUSAYEV,M.ALHAMADSHEH,J.N.SCARSDALE,H.T.WRIGHT,
AUTHOR 2 K.A.REYNOLDS
REVDAT 5 30-AUG-23 2QX1 1 REMARK
REVDAT 4 24-JUL-19 2QX1 1 REMARK LINK
REVDAT 3 13-JUL-11 2QX1 1 VERSN
REVDAT 2 24-FEB-09 2QX1 1 VERSN
REVDAT 1 18-MAR-08 2QX1 0
JRNL AUTH S.SACHDEVA,F.MUSAYEV,M.M.ALHAMADSHEH,J.NEEL SCARSDALE,
JRNL AUTH 2 H.TONIE WRIGHT,K.A.REYNOLDS
JRNL TITL PROBING REACTIVITY AND SUBSTRATE SPECIFICITY OF BOTH
JRNL TITL 2 SUBUNITS OF THE DIMERIC MYCOBACTERIUM TUBERCULOSIS FABH
JRNL TITL 3 USING ALKYL-COA DISULFIDE INHIBITORS AND ACYL-COA SUBSTRATES
JRNL REF BIOORG.CHEM. V. 36 85 2008
JRNL REFN ISSN 0045-2068
JRNL PMID 18096200
JRNL DOI 10.1016/J.BIOORG.2007.11.001
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.N.SCARSDALE,G.KAZANINA,X.HE,K.A.REYNOLDS,H.T.WRIGHT
REMARK 1 TITL CRYSTAL STRUCTURE OF THE MYCOBACTERIUM BETA-KETO-ACYL ACYL
REMARK 1 TITL 2 CARRIER PROTEIN SYNTHASE III
REMARK 1 REF J.BIOL.CHEM. V. 276 20516 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11278743
REMARK 1 DOI 10.1074/JBC.M010762200
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.MUSAYEV,S.SACHDEVA,J.N.SCARSDALE,K.A.REYNOLDS,H.T.WRIGHT
REMARK 1 TITL CRYSTAL STRUCTURE OF A SUBSTRATE COMPLEX OF MYCOBACTERIUM
REMARK 1 TITL 2 TUBERCULOSIS BETA-KETO-ACYL ACYL CARRIER PROTEIN SYNTHASE
REMARK 1 TITL 3 III (FABH) WITH LAUROYL COENZYME A
REMARK 1 REF J.MOL.BIOL. V. 346 1313 2005
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15713483
REMARK 1 DOI 10.1016/J.JMB.2004.12.044
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 19381
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2178
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1432
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 186
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 37.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.43000
REMARK 3 B22 (A**2) : -1.25000
REMARK 3 B33 (A**2) : -1.19000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.440
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.343
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.633
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.894
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.822
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5032 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6842 ; 1.229 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 666 ; 5.699 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;37.350 ;23.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 745 ;17.090 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;18.882 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 781 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3825 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2646 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3504 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 256 ; 0.162 ; 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): 52 ; 0.174 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.237 ; 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): 3358 ; 0.273 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5248 ; 0.482 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1846 ; 0.705 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1594 ; 1.172 ; 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 317
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5245 28.0481 37.3931
REMARK 3 T TENSOR
REMARK 3 T11: -.1675 T22: -.0836
REMARK 3 T33: -.0928 T12: -.0358
REMARK 3 T13: .0060 T23: .0210
REMARK 3 L TENSOR
REMARK 3 L11: .8531 L22: 1.4911
REMARK 3 L33: 1.6539 L12: -.2187
REMARK 3 L13: .3296 L23: -.3773
REMARK 3 S TENSOR
REMARK 3 S11: .0107 S12: .0278 S13: .0218
REMARK 3 S21: .1470 S22: -.0132 S23: -.1164
REMARK 3 S31: .0126 S32: .1865 S33: .0025
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 : B 1 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0210 43.3905 20.8861
REMARK 3 T TENSOR
REMARK 3 T11: -.0860 T22: -.0872
REMARK 3 T33: -.0550 T12: .0042
REMARK 3 T13: -.0350 T23: -.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.4690 L22: .9882
REMARK 3 L33: 1.4482 L12: -.0182
REMARK 3 L13: .5200 L23: -.2038
REMARK 3 S TENSOR
REMARK 3 S11: .0073 S12: .0662 S13: .1046
REMARK 3 S21: -.1148 S22: .0146 S23: .1415
REMARK 3 S31: -.1143 S32: -.0891 S33: -.0219
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CNS AND REFMAC WERE USED FOR REFINEMENT
REMARK 4
REMARK 4 2QX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : RIGAKU VARIMAX CONFOCAL OPTICS
REMARK 200 OPTICS : RIGAKU VARIMAX CONFOCAL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21693
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.760
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.79
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1HZP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NA HEPES, 18% PEG-10K(W.V), PH
REMARK 280 7.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 116.00300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.00300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.82450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.68250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.82450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.68250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 116.00300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.82450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.68250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 116.00300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.82450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.68250
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A 318
REMARK 465 GLY B 318
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 CYS B 23 SG
REMARK 470 GLN B 24 CG CD OE1 NE2
REMARK 470 ILE B 26 CG1 CG2 CD1
REMARK 470 ASP B 27 CG OD1 OD2
REMARK 470 SER B 28 OG
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 THR A -9 95.47 51.69
REMARK 500 ALA A -1 128.80 -27.62
REMARK 500 PHE A 84 33.77 -90.95
REMARK 500 ALA A 100 57.24 -101.23
REMARK 500 ALA A 110 50.80 -151.95
REMARK 500 ALA A 113 21.35 -71.03
REMARK 500 ASN A 153 -3.31 -146.48
REMARK 500 GLU A 208 69.35 -103.62
REMARK 500 ASN A 247 122.25 177.74
REMARK 500 SER A 276 -118.63 41.51
REMARK 500 LEU A 308 81.49 61.81
REMARK 500 PRO A 317A -153.84 -87.56
REMARK 500 ILE B 26 -156.34 -112.08
REMARK 500 SER B 28 -144.09 -155.62
REMARK 500 THR B 37 -37.03 -130.84
REMARK 500 PHE B 84 32.01 -92.19
REMARK 500 ALA B 100 53.59 -101.34
REMARK 500 LYS B 101 -35.87 -38.67
REMARK 500 ALA B 110 57.97 -147.33
REMARK 500 ALA B 131 141.70 179.45
REMARK 500 ARG B 151 15.94 -68.76
REMARK 500 ASN B 247 119.32 -174.22
REMARK 500 ASN B 267 34.66 -140.85
REMARK 500 THR B 272 -37.73 -137.24
REMARK 500 SER B 276 -130.30 53.75
REMARK 500 ALA B 306 160.65 -44.22
REMARK 500 LEU B 308 80.72 44.56
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 GLY B 307 LEU B 308 -149.59
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 COA A 962
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1T A 963
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1T B 963
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U6S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN MYCOBACTERIUM TUBERCULOSIS
REMARK 900 BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III AND LAUROYL
REMARK 900 COENZYME A
REMARK 900 RELATED ID: 1HZP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-
REMARK 900 ACYL CARRIER PROTEIN SYNTHASE III
REMARK 900 RELATED ID: 1U6E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C112A MUTANT OF MYCOBACTERIUM TUBERCULOSIS
REMARK 900 BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III
REMARK 900 RELATED ID: 1HNJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI FABH + MALONYL COA
REMARK 900 RELATED ID: 1HNK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI BETA-KETO ACP SYNTHASE III, TETRAGONAL
REMARK 900 FORM
DBREF 2QX1 A -10 318 UNP P0A574 FABH_MYCTU 1 335
DBREF 2QX1 B -10 318 UNP P0A574 FABH_MYCTU 1 335
SEQRES 1 A 335 MET THR GLU ILE ALA THR THR SER GLY ALA ARG SER VAL
SEQRES 2 A 335 GLY LEU LEU SER VAL GLY ALA TYR ARG PRO GLU ARG VAL
SEQRES 3 A 335 VAL THR ASN ASP GLU ILE CYS GLN HIS ILE ASP SER SER
SEQRES 4 A 335 ASP GLU TRP ILE TYR THR ARG THR GLY ILE LYS THR ARG
SEQRES 5 A 335 ARG PHE ALA ALA ASP ASP GLU SER ALA ALA SER MET ALA
SEQRES 6 A 335 THR GLU ALA CYS ARG ARG ALA LEU SER ASN ALA GLY LEU
SEQRES 7 A 335 SER ALA ALA ASP ILE ASP GLY VAL ILE VAL THR THR ASN
SEQRES 8 A 335 THR HIS PHE LEU GLN THR PRO PRO ALA ALA PRO MET VAL
SEQRES 9 A 335 ALA ALA SER LEU GLY ALA LYS GLY ILE LEU GLY PHE ASP
SEQRES 10 A 335 LEU SER ALA GLY CYS ALA GLY PHE GLY TYR ALA LEU GLY
SEQRES 11 A 335 ALA ALA ALA ASP MET ILE ARG GLY GLY GLY ALA ALA THR
SEQRES 12 A 335 MET LEU VAL VAL GLY THR GLU LYS LEU SER PRO THR ILE
SEQRES 13 A 335 ASP MET TYR ASP ARG GLY ASN CYS PHE ILE PHE ALA ASP
SEQRES 14 A 335 GLY ALA ALA ALA VAL VAL VAL GLY GLU THR PRO PHE GLN
SEQRES 15 A 335 GLY ILE GLY PRO THR VAL ALA GLY SER ASP GLY GLU GLN
SEQRES 16 A 335 ALA ASP ALA ILE ARG GLN ASP ILE ASP TRP ILE THR PHE
SEQRES 17 A 335 ALA GLN ASN PRO SER GLY PRO ARG PRO PHE VAL ARG LEU
SEQRES 18 A 335 GLU GLY PRO ALA VAL PHE ARG TRP ALA ALA PHE LYS MET
SEQRES 19 A 335 GLY ASP VAL GLY ARG ARG ALA MET ASP ALA ALA GLY VAL
SEQRES 20 A 335 ARG PRO ASP GLN ILE ASP VAL PHE VAL PRO HIS GLN ALA
SEQRES 21 A 335 ASN SER ARG ILE ASN GLU LEU LEU VAL LYS ASN LEU GLN
SEQRES 22 A 335 LEU ARG PRO ASP ALA VAL VAL ALA ASN ASP ILE GLU HIS
SEQRES 23 A 335 THR GLY ASN THR SER ALA ALA SER ILE PRO LEU ALA MET
SEQRES 24 A 335 ALA GLU LEU LEU THR THR GLY ALA ALA LYS PRO GLY ASP
SEQRES 25 A 335 LEU ALA LEU LEU ILE GLY TYR GLY ALA GLY LEU SER TYR
SEQRES 26 A 335 ALA ALA GLN VAL VAL ARG MET PRO LYS GLY
SEQRES 1 B 335 MET THR GLU ILE ALA THR THR SER GLY ALA ARG SER VAL
SEQRES 2 B 335 GLY LEU LEU SER VAL GLY ALA TYR ARG PRO GLU ARG VAL
SEQRES 3 B 335 VAL THR ASN ASP GLU ILE CYS GLN HIS ILE ASP SER SER
SEQRES 4 B 335 ASP GLU TRP ILE TYR THR ARG THR GLY ILE LYS THR ARG
SEQRES 5 B 335 ARG PHE ALA ALA ASP ASP GLU SER ALA ALA SER MET ALA
SEQRES 6 B 335 THR GLU ALA CYS ARG ARG ALA LEU SER ASN ALA GLY LEU
SEQRES 7 B 335 SER ALA ALA ASP ILE ASP GLY VAL ILE VAL THR THR ASN
SEQRES 8 B 335 THR HIS PHE LEU GLN THR PRO PRO ALA ALA PRO MET VAL
SEQRES 9 B 335 ALA ALA SER LEU GLY ALA LYS GLY ILE LEU GLY PHE ASP
SEQRES 10 B 335 LEU SER ALA GLY CYS ALA GLY PHE GLY TYR ALA LEU GLY
SEQRES 11 B 335 ALA ALA ALA ASP MET ILE ARG GLY GLY GLY ALA ALA THR
SEQRES 12 B 335 MET LEU VAL VAL GLY THR GLU LYS LEU SER PRO THR ILE
SEQRES 13 B 335 ASP MET TYR ASP ARG GLY ASN CYS PHE ILE PHE ALA ASP
SEQRES 14 B 335 GLY ALA ALA ALA VAL VAL VAL GLY GLU THR PRO PHE GLN
SEQRES 15 B 335 GLY ILE GLY PRO THR VAL ALA GLY SER ASP GLY GLU GLN
SEQRES 16 B 335 ALA ASP ALA ILE ARG GLN ASP ILE ASP TRP ILE THR PHE
SEQRES 17 B 335 ALA GLN ASN PRO SER GLY PRO ARG PRO PHE VAL ARG LEU
SEQRES 18 B 335 GLU GLY PRO ALA VAL PHE ARG TRP ALA ALA PHE LYS MET
SEQRES 19 B 335 GLY ASP VAL GLY ARG ARG ALA MET ASP ALA ALA GLY VAL
SEQRES 20 B 335 ARG PRO ASP GLN ILE ASP VAL PHE VAL PRO HIS GLN ALA
SEQRES 21 B 335 ASN SER ARG ILE ASN GLU LEU LEU VAL LYS ASN LEU GLN
SEQRES 22 B 335 LEU ARG PRO ASP ALA VAL VAL ALA ASN ASP ILE GLU HIS
SEQRES 23 B 335 THR GLY ASN THR SER ALA ALA SER ILE PRO LEU ALA MET
SEQRES 24 B 335 ALA GLU LEU LEU THR THR GLY ALA ALA LYS PRO GLY ASP
SEQRES 25 B 335 LEU ALA LEU LEU ILE GLY TYR GLY ALA GLY LEU SER TYR
SEQRES 26 B 335 ALA ALA GLN VAL VAL ARG MET PRO LYS GLY
HET COA A 962 48
HET D1T A 963 11
HET D1T B 963 11
HETNAM COA COENZYME A
HETNAM D1T DECANE-1-THIOL
FORMUL 3 COA C21 H36 N7 O16 P3 S
FORMUL 4 D1T 2(C10 H22 S)
FORMUL 6 HOH *145(H2 O)
HELIX 1 1 ASN A 19 CYS A 23 1 5
HELIX 2 2 SER A 29 GLY A 38 1 10
HELIX 3 3 SER A 50 GLY A 67 1 18
HELIX 4 4 SER A 69 ILE A 73 5 5
HELIX 5 5 PRO A 89 GLY A 99 1 11
HELIX 6 6 ALA A 110 CYS A 112 5 3
HELIX 7 7 ALA A 113 GLY A 128 1 16
HELIX 8 8 SER A 143 ILE A 146 5 4
HELIX 9 9 GLY A 183 ALA A 186 5 4
HELIX 10 10 ASP A 194 GLN A 200 1 7
HELIX 11 11 GLU A 208 ALA A 231 1 24
HELIX 12 12 ARG A 234 ILE A 238 5 5
HELIX 13 13 ASN A 247 LEU A 258 1 12
HELIX 14 14 ASN A 267 THR A 272 5 6
HELIX 15 15 THR A 275 ALA A 277 5 3
HELIX 16 16 ALA A 278 THR A 290 1 13
HELIX 17 17 ASN B 19 GLN B 24 1 6
HELIX 18 18 SER B 29 GLY B 38 1 10
HELIX 19 19 SER B 50 ALA B 66 1 17
HELIX 20 20 SER B 69 ILE B 73 5 5
HELIX 21 21 PRO B 89 GLY B 99 1 11
HELIX 22 22 ALA B 110 CYS B 112 5 3
HELIX 23 23 ALA B 113 GLY B 128 1 16
HELIX 24 24 SER B 143 ILE B 146 5 4
HELIX 25 25 GLY B 183 ASP B 187 5 5
HELIX 26 26 ASP B 194 ASN B 201 1 8
HELIX 27 27 GLU B 208 GLY B 232 1 25
HELIX 28 28 ARG B 234 ILE B 238 5 5
HELIX 29 29 ASN B 247 GLN B 259 1 13
HELIX 30 30 ASN B 267 THR B 272 5 6
HELIX 31 31 THR B 275 ALA B 277 5 3
HELIX 32 32 ALA B 278 GLY B 291 1 14
SHEET 1 A10 VAL A 3 TYR A 11 0
SHEET 2 A10 ASP A 159 GLU A 168 -1 O ALA A 161 N TYR A 11
SHEET 3 A10 THR A 133 LYS A 141 -1 N MET A 134 O VAL A 166
SHEET 4 A10 GLY A 75 THR A 79 1 N THR A 79 O VAL A 137
SHEET 5 A10 LEU A 104 SER A 109 1 O LEU A 104 N VAL A 76
SHEET 6 A10 LEU B 104 SER B 109 -1 O ASP B 107 N SER A 109
SHEET 7 A10 GLY B 75 THR B 79 1 N VAL B 78 O PHE B 106
SHEET 8 A10 THR B 133 LYS B 141 1 O LEU B 135 N GLY B 75
SHEET 9 A10 ASP B 159 GLU B 168 -1 O VAL B 166 N MET B 134
SHEET 10 A10 VAL B 3 TYR B 11 -1 N LEU B 6 O VAL B 165
SHEET 1 B 2 VAL A 16 THR A 18 0
SHEET 2 B 2 THR A 41 ARG A 43 -1 O ARG A 42 N VAL A 17
SHEET 1 C 5 VAL A 178 SER A 181 0
SHEET 2 C 5 SER A 309 ARG A 316 -1 O ALA A 312 N VAL A 178
SHEET 3 C 5 LEU A 298 GLY A 305 -1 N ALA A 299 O VAL A 315
SHEET 4 C 5 VAL A 240 PRO A 243 1 N VAL A 242 O LEU A 300
SHEET 5 C 5 VAL A 264 VAL A 265 1 O VAL A 264 N PHE A 241
SHEET 1 D 2 ILE A 189 GLN A 191 0
SHEET 2 D 2 VAL A 205 LEU A 207 -1 O ARG A 206 N ARG A 190
SHEET 1 E 2 ARG B 15 THR B 18 0
SHEET 2 E 2 THR B 41 PHE B 44 -1 O ARG B 42 N VAL B 17
SHEET 1 F 5 VAL B 178 SER B 181 0
SHEET 2 F 5 SER B 309 ARG B 316 -1 O ALA B 312 N VAL B 178
SHEET 3 F 5 LEU B 298 GLY B 305 -1 N ALA B 299 O VAL B 315
SHEET 4 F 5 VAL B 240 PRO B 243 1 N VAL B 240 O LEU B 300
SHEET 5 F 5 VAL B 264 VAL B 265 1 O VAL B 264 N PHE B 241
SHEET 1 G 2 ILE B 189 GLN B 191 0
SHEET 2 G 2 VAL B 205 LEU B 207 -1 O ARG B 206 N ARG B 190
LINK SG CYS A 112 S1 D1T A 963 1555 1555 2.02
LINK SG CYS B 112 S1 D1T B 963 1555 1555 2.05
CISPEP 1 THR A 87 PRO A 88 0 -1.91
CISPEP 2 THR B 87 PRO B 88 0 -4.66
SITE 1 AC1 11 ASP A 27 SER A 28 TRP A 32 ARG A 151
SITE 2 AC1 11 GLY A 209 PRO A 210 PHE A 213 ARG A 214
SITE 3 AC1 11 ASN A 247 ILE A 250 HOH A1005
SITE 1 AC2 12 ASN A 81 CYS A 112 LEU A 142 THR A 145
SITE 2 AC2 12 PHE A 157 ILE A 189 GLN A 191 PHE A 204
SITE 3 AC2 12 SER A 276 ALA A 306 GLN B 86 THR B 87
SITE 1 AC3 8 THR A 87 CYS B 112 LEU B 142 THR B 145
SITE 2 AC3 8 GLN B 191 PHE B 204 SER B 276 ALA B 306
CRYST1 67.649 89.365 232.006 90.00 90.00 90.00 C 2 2 21 16
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 0.014782 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004310 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
