HEADER TRANSFERASE 22-MAR-13 4BFV
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX WITH A
TITLE 2 TRIAZOLE INHIBITORY COMPOUND (1D) AND PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANTOTHENATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PANTOTHENIC ACID KINASE;
COMPND 5 EC: 2.7.1.33;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS TRANSFERASE, COA PATHWAY, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BJORKELID,T.BERGFORS,T.A.JONES
REVDAT 6 20-DEC-23 4BFV 1 REMARK
REVDAT 5 15-MAY-19 4BFV 1 REMARK
REVDAT 4 06-MAR-19 4BFV 1 REMARK
REVDAT 3 10-JUL-13 4BFV 1 JRNL
REVDAT 2 22-MAY-13 4BFV 1 JRNL
REVDAT 1 15-MAY-13 4BFV 0
JRNL AUTH C.BJORKELID,T.BERGFORS,A.K.V.RAICHURKAR,K.MUKHERJEE,
JRNL AUTH 2 M.KRISHNAN,B.BANDODKAR,T.A.JONES
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF COMPOUNDS
JRNL TITL 2 INHIBITING MYCOBACTERIUM TUBERCULOSIS PANK
JRNL REF J.BIOL.CHEM. V. 288 18260 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23661699
JRNL DOI 10.1074/JBC.M113.476473
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36854
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1946
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) : 2.29
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.35
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2677
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4942
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 213
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.97000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : 3.18000
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): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.920
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5138 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6996 ; 1.612 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 610 ; 6.760 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 252 ;31.869 ;22.063
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 830 ;20.365 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;19.280 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3970 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2446 ; 2.004 ; 3.073
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3054 ; 3.363 ; 4.602
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2692 ; 2.424 ; 3.331
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 4BFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38852
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BFS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR-DIFFUSION METHOD AT
REMARK 280 293 K. 1.8 M SODIUM/POTASSIUM PHOSPHATE, PH 8.2, VAPOR DIFFUSION,
REMARK 280 SITTING DROP
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 44.16500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.16500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.88500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.7 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2018 O HOH B 2019 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 28 109.31 43.46
REMARK 500 THR A 30 -119.40 -68.77
REMARK 500 GLU A 31 -23.18 -156.04
REMARK 500 GLU A 32 -72.99 84.56
REMARK 500 GLU A 42 59.65 -66.90
REMARK 500 HIS A 120 66.54 -156.61
REMARK 500 PRO A 134 151.10 -45.16
REMARK 500 HIS A 194 65.74 32.13
REMARK 500 THR A 211 -147.73 -128.51
REMARK 500 THR A 245 -105.82 -118.45
REMARK 500 ASP A 249 110.80 -30.01
REMARK 500 GLU A 251 -29.53 97.01
REMARK 500 ILE A 276 -61.08 -121.96
REMARK 500 ARG A 306 125.02 -178.30
REMARK 500 SER B 24 -70.47 -32.24
REMARK 500 THR B 25 -80.62 -177.85
REMARK 500 PRO B 26 -138.58 -81.71
REMARK 500 ALA B 28 147.04 44.29
REMARK 500 GLU B 31 -74.78 -24.56
REMARK 500 GLU B 32 -71.85 131.21
REMARK 500 GLU B 42 76.26 -56.25
REMARK 500 VAL B 52 -61.37 -124.07
REMARK 500 GLU B 80 61.88 39.16
REMARK 500 HIS B 120 71.81 -152.17
REMARK 500 THR B 211 -162.28 -122.15
REMARK 500 THR B 245 -88.41 -92.56
REMARK 500 ILE B 276 -63.07 -121.31
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 PRO B 7 SER B 8 -147.94
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 PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZVV A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZVV B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BFS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A TRIAZOLE INHIBITORY COMPOUND (1A)
REMARK 900 RELATED ID: 4BFT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A TRIAZOLE INHIBITORY COMPOUND (1B) AND PHOSPHATE
REMARK 900 RELATED ID: 4BFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A TRIAZOLE INHIBITORY COMPOUND (1C) AND PHOSPHATE
REMARK 900 RELATED ID: 4BFW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A TRIAZOLE INHIBITORY COMPOUND (1E) AND PHOSPHATE
REMARK 900 RELATED ID: 4BFX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A TRIAZOLE INHIBITORY COMPOUND (1F) AND PHOSPHATE
REMARK 900 RELATED ID: 4BFY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A BIARYL INHIBITORY COMPOUND (2A) AND PHOSPHATE
REMARK 900 RELATED ID: 4BFZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK IN COMPLEX
REMARK 900 WITH A BIARYL INHIBITORY COMPOUND (2B) AND PHOSPHATE
DBREF 4BFV A 1 312 UNP P63810 COAA_MYCTU 1 312
DBREF 4BFV B 1 312 UNP P63810 COAA_MYCTU 1 312
SEQADV 4BFV HIS A -5 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS A -4 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS A -3 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS A -2 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS A -1 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS A 0 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B -5 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B -4 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B -3 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B -2 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B -1 UNP P63810 EXPRESSION TAG
SEQADV 4BFV HIS B 0 UNP P63810 EXPRESSION TAG
SEQRES 1 A 318 HIS HIS HIS HIS HIS HIS MET SER ARG LEU SER GLU PRO
SEQRES 2 A 318 SER PRO TYR VAL GLU PHE ASP ARG ARG GLN TRP ARG ALA
SEQRES 3 A 318 LEU ARG MET SER THR PRO LEU ALA LEU THR GLU GLU GLU
SEQRES 4 A 318 LEU VAL GLY LEU ARG GLY LEU GLY GLU GLN ILE ASP LEU
SEQRES 5 A 318 LEU GLU VAL GLU GLU VAL TYR LEU PRO LEU ALA ARG LEU
SEQRES 6 A 318 ILE HIS LEU GLN VAL ALA ALA ARG GLN ARG LEU PHE ALA
SEQRES 7 A 318 ALA THR ALA GLU PHE LEU GLY GLU PRO GLN GLN ASN PRO
SEQRES 8 A 318 ASP ARG PRO VAL PRO PHE ILE ILE GLY VAL ALA GLY SER
SEQRES 9 A 318 VAL ALA VAL GLY LYS SER THR THR ALA ARG VAL LEU GLN
SEQRES 10 A 318 ALA LEU LEU ALA ARG TRP ASP HIS HIS PRO ARG VAL ASP
SEQRES 11 A 318 LEU VAL THR THR ASP GLY PHE LEU TYR PRO ASN ALA GLU
SEQRES 12 A 318 LEU GLN ARG ARG ASN LEU MET HIS ARG LYS GLY PHE PRO
SEQRES 13 A 318 GLU SER TYR ASN ARG ARG ALA LEU MET ARG PHE VAL THR
SEQRES 14 A 318 SER VAL LYS SER GLY SER ASP TYR ALA CYS ALA PRO VAL
SEQRES 15 A 318 TYR SER HIS LEU HIS TYR ASP ILE ILE PRO GLY ALA GLU
SEQRES 16 A 318 GLN VAL VAL ARG HIS PRO ASP ILE LEU ILE LEU GLU GLY
SEQRES 17 A 318 LEU ASN VAL LEU GLN THR GLY PRO THR LEU MET VAL SER
SEQRES 18 A 318 ASP LEU PHE ASP PHE SER LEU TYR VAL ASP ALA ARG ILE
SEQRES 19 A 318 GLU ASP ILE GLU GLN TRP TYR VAL SER ARG PHE LEU ALA
SEQRES 20 A 318 MET ARG THR THR ALA PHE ALA ASP PRO GLU SER HIS PHE
SEQRES 21 A 318 HIS HIS TYR ALA ALA PHE SER ASP SER GLN ALA VAL VAL
SEQRES 22 A 318 ALA ALA ARG GLU ILE TRP ARG THR ILE ASN ARG PRO ASN
SEQRES 23 A 318 LEU VAL GLU ASN ILE LEU PRO THR ARG PRO ARG ALA THR
SEQRES 24 A 318 LEU VAL LEU ARG LYS ASP ALA ASP HIS SER ILE ASN ARG
SEQRES 25 A 318 LEU ARG LEU ARG LYS LEU
SEQRES 1 B 318 HIS HIS HIS HIS HIS HIS MET SER ARG LEU SER GLU PRO
SEQRES 2 B 318 SER PRO TYR VAL GLU PHE ASP ARG ARG GLN TRP ARG ALA
SEQRES 3 B 318 LEU ARG MET SER THR PRO LEU ALA LEU THR GLU GLU GLU
SEQRES 4 B 318 LEU VAL GLY LEU ARG GLY LEU GLY GLU GLN ILE ASP LEU
SEQRES 5 B 318 LEU GLU VAL GLU GLU VAL TYR LEU PRO LEU ALA ARG LEU
SEQRES 6 B 318 ILE HIS LEU GLN VAL ALA ALA ARG GLN ARG LEU PHE ALA
SEQRES 7 B 318 ALA THR ALA GLU PHE LEU GLY GLU PRO GLN GLN ASN PRO
SEQRES 8 B 318 ASP ARG PRO VAL PRO PHE ILE ILE GLY VAL ALA GLY SER
SEQRES 9 B 318 VAL ALA VAL GLY LYS SER THR THR ALA ARG VAL LEU GLN
SEQRES 10 B 318 ALA LEU LEU ALA ARG TRP ASP HIS HIS PRO ARG VAL ASP
SEQRES 11 B 318 LEU VAL THR THR ASP GLY PHE LEU TYR PRO ASN ALA GLU
SEQRES 12 B 318 LEU GLN ARG ARG ASN LEU MET HIS ARG LYS GLY PHE PRO
SEQRES 13 B 318 GLU SER TYR ASN ARG ARG ALA LEU MET ARG PHE VAL THR
SEQRES 14 B 318 SER VAL LYS SER GLY SER ASP TYR ALA CYS ALA PRO VAL
SEQRES 15 B 318 TYR SER HIS LEU HIS TYR ASP ILE ILE PRO GLY ALA GLU
SEQRES 16 B 318 GLN VAL VAL ARG HIS PRO ASP ILE LEU ILE LEU GLU GLY
SEQRES 17 B 318 LEU ASN VAL LEU GLN THR GLY PRO THR LEU MET VAL SER
SEQRES 18 B 318 ASP LEU PHE ASP PHE SER LEU TYR VAL ASP ALA ARG ILE
SEQRES 19 B 318 GLU ASP ILE GLU GLN TRP TYR VAL SER ARG PHE LEU ALA
SEQRES 20 B 318 MET ARG THR THR ALA PHE ALA ASP PRO GLU SER HIS PHE
SEQRES 21 B 318 HIS HIS TYR ALA ALA PHE SER ASP SER GLN ALA VAL VAL
SEQRES 22 B 318 ALA ALA ARG GLU ILE TRP ARG THR ILE ASN ARG PRO ASN
SEQRES 23 B 318 LEU VAL GLU ASN ILE LEU PRO THR ARG PRO ARG ALA THR
SEQRES 24 B 318 LEU VAL LEU ARG LYS ASP ALA ASP HIS SER ILE ASN ARG
SEQRES 25 B 318 LEU ARG LEU ARG LYS LEU
HET PO4 A 401 5
HET ZVV A 501 32
HET PO4 B 401 5
HET ZVV B 501 32
HETNAM PO4 PHOSPHATE ION
HETNAM ZVV N-[1-(4-METHYL-5-{[2-(2-METHYLPHENOXY)ETHYL]SULFANYL}-
HETNAM 2 ZVV 4H-1,2,4-TRIAZOL-3-YL)ETHYL]-2-(TRIFLUOROMETHYL)
HETNAM 3 ZVV BENZAMIDE
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 ZVV 2(C22 H23 F3 N4 O2 S)
FORMUL 7 HOH *213(H2 O)
HELIX 1 1 ARG A 15 ALA A 20 1 6
HELIX 2 2 GLU A 33 LEU A 40 1 8
HELIX 3 3 ASP A 45 VAL A 52 1 8
HELIX 4 4 VAL A 52 GLY A 79 1 28
HELIX 5 5 GLY A 102 ALA A 115 1 14
HELIX 6 6 ASP A 129 PHE A 131 5 3
HELIX 7 7 PRO A 134 ARG A 141 1 8
HELIX 8 8 LEU A 143 LYS A 147 5 5
HELIX 9 9 PHE A 149 SER A 152 5 4
HELIX 10 10 ASN A 154 SER A 167 1 14
HELIX 11 11 MET A 213 PHE A 218 5 6
HELIX 12 12 ARG A 227 ARG A 243 1 17
HELIX 13 13 PHE A 254 ALA A 258 5 5
HELIX 14 14 SER A 261 ILE A 276 1 16
HELIX 15 15 ILE A 276 ILE A 285 1 10
HELIX 16 16 LEU A 286 ALA A 292 5 7
HELIX 17 17 ARG B 15 ALA B 20 1 6
HELIX 18 18 GLU B 32 GLY B 39 1 8
HELIX 19 19 ASP B 45 VAL B 52 1 8
HELIX 20 20 VAL B 52 LEU B 78 1 27
HELIX 21 21 GLY B 102 ALA B 115 1 14
HELIX 22 22 ASP B 129 PHE B 131 5 3
HELIX 23 23 PRO B 134 ARG B 141 1 8
HELIX 24 24 LEU B 143 LYS B 147 5 5
HELIX 25 25 PHE B 149 SER B 152 5 4
HELIX 26 26 ASN B 154 SER B 167 1 14
HELIX 27 27 MET B 213 PHE B 218 5 6
HELIX 28 28 ARG B 227 ARG B 243 1 17
HELIX 29 29 PHE B 254 ALA B 258 5 5
HELIX 30 30 SER B 261 ILE B 276 1 16
HELIX 31 31 ILE B 276 ILE B 285 1 10
HELIX 32 32 LEU B 286 ALA B 292 5 7
SHEET 1 AA 7 TYR A 10 ASP A 14 0
SHEET 2 AA 7 ILE A 304 ARG A 310 -1 O LEU A 307 N PHE A 13
SHEET 3 AA 7 LEU A 294 LYS A 298 -1 O VAL A 295 N ARG A 308
SHEET 4 AA 7 PHE A 220 ALA A 226 1 O SER A 221 N LEU A 294
SHEET 5 AA 7 PHE A 91 GLY A 97 1 O GLY A 94 N LEU A 222
SHEET 6 AA 7 ILE A 197 GLU A 201 1 O LEU A 198 N ILE A 93
SHEET 7 AA 7 VAL A 123 THR A 127 1 O ASP A 124 N ILE A 199
SHEET 1 AB 2 ALA A 172 SER A 178 0
SHEET 2 AB 2 ASP A 183 VAL A 192 -1 O ASP A 183 N SER A 178
SHEET 1 BA 7 TYR B 10 ASP B 14 0
SHEET 2 BA 7 ILE B 304 ARG B 310 -1 O LEU B 307 N PHE B 13
SHEET 3 BA 7 LEU B 294 LYS B 298 -1 O VAL B 295 N ARG B 308
SHEET 4 BA 7 PHE B 220 ALA B 226 1 O SER B 221 N LEU B 294
SHEET 5 BA 7 PHE B 91 GLY B 97 1 O GLY B 94 N LEU B 222
SHEET 6 BA 7 ILE B 197 GLU B 201 1 O LEU B 198 N ILE B 93
SHEET 7 BA 7 VAL B 123 THR B 127 1 O ASP B 124 N ILE B 199
SHEET 1 BB 2 ALA B 172 SER B 178 0
SHEET 2 BB 2 ASP B 183 VAL B 192 -1 O ASP B 183 N SER B 178
CISPEP 1 GLU A 31 GLU A 32 0 12.90
CISPEP 2 PRO B 26 LEU B 27 0 -16.25
CISPEP 3 GLU B 31 GLU B 32 0 6.75
SITE 1 AC1 9 SER A 98 VAL A 99 ALA A 100 VAL A 101
SITE 2 AC1 9 GLY A 102 LYS A 103 SER A 104 ARG A 238
SITE 3 AC1 9 HOH A2035
SITE 1 AC2 13 VAL A 99 ASP A 129 LEU A 132 HIS A 179
SITE 2 AC2 13 TYR A 182 TYR A 235 ARG A 238 PHE A 239
SITE 3 AC2 13 MET A 242 PHE A 254 ASN A 277 HOH A2058
SITE 4 AC2 13 HOH A2068
SITE 1 AC3 9 SER B 98 ALA B 100 VAL B 101 GLY B 102
SITE 2 AC3 9 LYS B 103 SER B 104 ARG B 238 HOH B2026
SITE 3 AC3 9 HOH B2094
SITE 1 AC4 14 VAL B 99 LEU B 132 GLY B 148 HIS B 179
SITE 2 AC4 14 TYR B 182 LEU B 203 TYR B 235 PHE B 239
SITE 3 AC4 14 MET B 242 PHE B 254 ILE B 276 ASN B 277
SITE 4 AC4 14 HOH B2050 HOH B2063
CRYST1 88.330 151.770 63.130 90.00 90.00 90.00 P 21 21 2 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 0.011321 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006589 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015840 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
