HEADER LIGASE 10-AUG-09 3IMG
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE
TITLE 2 SYNTHETASE AT 1.8 ANG RESOLUTION IN A TERNARY COMPLEX WITH FRAGMENT
TITLE 3 COMPOUNDS 5-METHOXYINDOLE AND 1-BENZOFURAN-2-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANTOTHENATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-300;
COMPND 5 SYNONYM: PS, PANTOATE-BETA-ALANINE LIGASE, PANTOATE-ACTIVATING
COMPND 6 ENZYME;
COMPND 7 EC: 6.3.2.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MT3707, MTCY07H7B.20, PANC, RV3602C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS MYCOBACTERIUM TUBERCULOSIS, PANTOTHENATE BIOSYNTHESIS, ENZYMES,
KEYWDS 2 LIGASE, DRUG DESIGN, FRAGMENT-BASED, ATP-BINDING, MAGNESIUM, METAL-
KEYWDS 3 BINDING, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CIULLI,A.W.HUNG,H.L.SILVESTRE,S.WEN,T.L.BLUNDELL,C.ABELL
REVDAT 7 06-SEP-23 3IMG 1 REMARK
REVDAT 6 13-OCT-21 3IMG 1 REMARK SEQADV
REVDAT 5 01-NOV-17 3IMG 1 REMARK
REVDAT 4 13-JUL-11 3IMG 1 VERSN
REVDAT 3 02-MAR-11 3IMG 1 HETSYN
REVDAT 2 10-NOV-09 3IMG 1 JRNL
REVDAT 1 13-OCT-09 3IMG 0
JRNL AUTH A.W.HUNG,H.L.SILVESTRE,S.WEN,A.CIULLI,T.L.BLUNDELL,C.ABELL
JRNL TITL APPLICATION OF FRAGMENT GROWING AND FRAGMENT LINKING TO THE
JRNL TITL 2 DISCOVERY OF INHIBITORS OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 3 PANTOTHENATE SYNTHETASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 48 8452 2009
JRNL REFN ISSN 1433-7851
JRNL PMID 19780086
JRNL DOI 10.1002/ANIE.200903821
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 48270
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2543
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3487
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4126
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 382
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.669
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4281 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5845 ; 1.401 ; 2.004
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 559 ; 5.670 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;37.147 ;22.470
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 634 ;13.223 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;15.113 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 693 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3260 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2006 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2967 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 341 ; 0.150 ; 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): 89 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.096 ; 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): 2860 ; 2.815 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4469 ; 3.728 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1572 ; 3.550 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1375 ; 5.406 ; 7.000
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 3IMG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-RAY DETECTOR SOFTWARE (XDS)
REMARK 200 PROGRAM PACKAGE
REMARK 200 DATA SCALING SOFTWARE : X-RAY DETECTOR SOFTWARE (XDS)
REMARK 200 PROGRAM PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50816
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
REMARK 200 R SYM FOR SHELL (I) : 0.52900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.760
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3COV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-14% W/V PEG3000, 100-150 MM LITHIUM
REMARK 280 SULFATE, 100 MM IMIDAZOLE, PH 8.0, 2-4% V/V ETHANOL, 10% V/V
REMARK 280 GLYCEROL AND 20 MM MAGNESIUM CHLORIDE., VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 35.61000
REMARK 290 SMTRY3 2 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: DIMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 13.36006
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -80.70160
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 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 291
REMARK 465 GLY A 292
REMARK 465 THR A 293
REMARK 465 ASP A 294
REMARK 465 ARG A 295
REMARK 465 PRO A 296
REMARK 465 ASP A 297
REMARK 465 GLY A 298
REMARK 465 TYR A 299
REMARK 465 ARG A 300
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 MET B 71
REMARK 465 GLN B 72
REMARK 465 PHE B 73
REMARK 465 GLY B 74
REMARK 465 ALA B 75
REMARK 465 GLY B 76
REMARK 465 GLY B 77
REMARK 465 ASP B 78
REMARK 465 LEU B 79
REMARK 465 ASP B 80
REMARK 465 ALA B 81
REMARK 465 TYR B 82
REMARK 465 PRO B 83
REMARK 465 ARG B 84
REMARK 465 THR B 85
REMARK 465 THR B 289
REMARK 465 PHE B 290
REMARK 465 ALA B 291
REMARK 465 GLY B 292
REMARK 465 THR B 293
REMARK 465 ASP B 294
REMARK 465 ARG B 295
REMARK 465 PRO B 296
REMARK 465 ASP B 297
REMARK 465 GLY B 298
REMARK 465 TYR B 299
REMARK 465 ARG B 300
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 A 676 O HOH B 577 2.05
REMARK 500 NAG BZ3 A 401 O2 SO4 A 701 2.19
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 ARG A 115 -92.70 -118.82
REMARK 500 LEU A 127 -115.45 56.33
REMARK 500 ASN A 263 -115.16 -105.33
REMARK 500 ARG B 115 -91.99 -132.06
REMARK 500 LEU B 127 -106.86 52.55
REMARK 500 SER B 196 144.58 -171.73
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 BZ2 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZ3 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZ2 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZ3 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3COV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE
REMARK 900 SYNTHETASE AT 1.5 ANG RESOLUTION- APO FORM
REMARK 900 RELATED ID: 3IMC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE
REMARK 900 SYNTHETASE AT 1.6 ANG RESOLUTION IN COMPLEX WITH FRAGMENT COMPOUND
REMARK 900 5-METHOXYINDOLE, SULFATE AND GLYCEROL
REMARK 900 RELATED ID: 3IME RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE
REMARK 900 SYNTHETASE AT 2.40 ANG RESOLUTION IN COMPLEX WITH FRAGMENT COMPOUND
REMARK 900 1-BENZOFURAN-2-CARBOXYLIC ACID
DBREF 3IMG A 1 300 UNP P0A5R0 PANC_MYCTU 1 300
DBREF 3IMG B 1 300 UNP P0A5R0 PANC_MYCTU 1 300
SEQADV 3IMG ALA A 0 UNP P0A5R0 EXPRESSION TAG
SEQADV 3IMG ALA A 2 UNP P0A5R0 THR 2 ENGINEERED MUTATION
SEQADV 3IMG GLY A 77 UNP P0A5R0 GLU 77 ENGINEERED MUTATION
SEQADV 3IMG ALA B 0 UNP P0A5R0 EXPRESSION TAG
SEQADV 3IMG ALA B 2 UNP P0A5R0 THR 2 ENGINEERED MUTATION
SEQADV 3IMG GLY B 77 UNP P0A5R0 GLU 77 ENGINEERED MUTATION
SEQRES 1 A 301 ALA MET ALA ILE PRO ALA PHE HIS PRO GLY GLU LEU ASN
SEQRES 2 A 301 VAL TYR SER ALA PRO GLY ASP VAL ALA ASP VAL SER ARG
SEQRES 3 A 301 ALA LEU ARG LEU THR GLY ARG ARG VAL MET LEU VAL PRO
SEQRES 4 A 301 THR MET GLY ALA LEU HIS GLU GLY HIS LEU ALA LEU VAL
SEQRES 5 A 301 ARG ALA ALA LYS ARG VAL PRO GLY SER VAL VAL VAL VAL
SEQRES 6 A 301 SER ILE PHE VAL ASN PRO MET GLN PHE GLY ALA GLY GLY
SEQRES 7 A 301 ASP LEU ASP ALA TYR PRO ARG THR PRO ASP ASP ASP LEU
SEQRES 8 A 301 ALA GLN LEU ARG ALA GLU GLY VAL GLU ILE ALA PHE THR
SEQRES 9 A 301 PRO THR THR ALA ALA MET TYR PRO ASP GLY LEU ARG THR
SEQRES 10 A 301 THR VAL GLN PRO GLY PRO LEU ALA ALA GLU LEU GLU GLY
SEQRES 11 A 301 GLY PRO ARG PRO THR HIS PHE ALA GLY VAL LEU THR VAL
SEQRES 12 A 301 VAL LEU LYS LEU LEU GLN ILE VAL ARG PRO ASP ARG VAL
SEQRES 13 A 301 PHE PHE GLY GLU LYS ASP TYR GLN GLN LEU VAL LEU ILE
SEQRES 14 A 301 ARG GLN LEU VAL ALA ASP PHE ASN LEU ASP VAL ALA VAL
SEQRES 15 A 301 VAL GLY VAL PRO THR VAL ARG GLU ALA ASP GLY LEU ALA
SEQRES 16 A 301 MET SER SER ARG ASN ARG TYR LEU ASP PRO ALA GLN ARG
SEQRES 17 A 301 ALA ALA ALA VAL ALA LEU SER ALA ALA LEU THR ALA ALA
SEQRES 18 A 301 ALA HIS ALA ALA THR ALA GLY ALA GLN ALA ALA LEU ASP
SEQRES 19 A 301 ALA ALA ARG ALA VAL LEU ASP ALA ALA PRO GLY VAL ALA
SEQRES 20 A 301 VAL ASP TYR LEU GLU LEU ARG ASP ILE GLY LEU GLY PRO
SEQRES 21 A 301 MET PRO LEU ASN GLY SER GLY ARG LEU LEU VAL ALA ALA
SEQRES 22 A 301 ARG LEU GLY THR THR ARG LEU LEU ASP ASN ILE ALA ILE
SEQRES 23 A 301 GLU ILE GLY THR PHE ALA GLY THR ASP ARG PRO ASP GLY
SEQRES 24 A 301 TYR ARG
SEQRES 1 B 301 ALA MET ALA ILE PRO ALA PHE HIS PRO GLY GLU LEU ASN
SEQRES 2 B 301 VAL TYR SER ALA PRO GLY ASP VAL ALA ASP VAL SER ARG
SEQRES 3 B 301 ALA LEU ARG LEU THR GLY ARG ARG VAL MET LEU VAL PRO
SEQRES 4 B 301 THR MET GLY ALA LEU HIS GLU GLY HIS LEU ALA LEU VAL
SEQRES 5 B 301 ARG ALA ALA LYS ARG VAL PRO GLY SER VAL VAL VAL VAL
SEQRES 6 B 301 SER ILE PHE VAL ASN PRO MET GLN PHE GLY ALA GLY GLY
SEQRES 7 B 301 ASP LEU ASP ALA TYR PRO ARG THR PRO ASP ASP ASP LEU
SEQRES 8 B 301 ALA GLN LEU ARG ALA GLU GLY VAL GLU ILE ALA PHE THR
SEQRES 9 B 301 PRO THR THR ALA ALA MET TYR PRO ASP GLY LEU ARG THR
SEQRES 10 B 301 THR VAL GLN PRO GLY PRO LEU ALA ALA GLU LEU GLU GLY
SEQRES 11 B 301 GLY PRO ARG PRO THR HIS PHE ALA GLY VAL LEU THR VAL
SEQRES 12 B 301 VAL LEU LYS LEU LEU GLN ILE VAL ARG PRO ASP ARG VAL
SEQRES 13 B 301 PHE PHE GLY GLU LYS ASP TYR GLN GLN LEU VAL LEU ILE
SEQRES 14 B 301 ARG GLN LEU VAL ALA ASP PHE ASN LEU ASP VAL ALA VAL
SEQRES 15 B 301 VAL GLY VAL PRO THR VAL ARG GLU ALA ASP GLY LEU ALA
SEQRES 16 B 301 MET SER SER ARG ASN ARG TYR LEU ASP PRO ALA GLN ARG
SEQRES 17 B 301 ALA ALA ALA VAL ALA LEU SER ALA ALA LEU THR ALA ALA
SEQRES 18 B 301 ALA HIS ALA ALA THR ALA GLY ALA GLN ALA ALA LEU ASP
SEQRES 19 B 301 ALA ALA ARG ALA VAL LEU ASP ALA ALA PRO GLY VAL ALA
SEQRES 20 B 301 VAL ASP TYR LEU GLU LEU ARG ASP ILE GLY LEU GLY PRO
SEQRES 21 B 301 MET PRO LEU ASN GLY SER GLY ARG LEU LEU VAL ALA ALA
SEQRES 22 B 301 ARG LEU GLY THR THR ARG LEU LEU ASP ASN ILE ALA ILE
SEQRES 23 B 301 GLU ILE GLY THR PHE ALA GLY THR ASP ARG PRO ASP GLY
SEQRES 24 B 301 TYR ARG
HET BZ2 A 301 12
HET BZ3 A 401 11
HET SO4 A 701 5
HET SO4 A 703 5
HET GOL A 705 6
HET EOH A 710 3
HET EOH A 711 3
HET BZ2 B 302 12
HET BZ3 B 402 11
HET SO4 B 702 5
HETNAM BZ2 1-BENZOFURAN-2-CARBOXYLIC ACID
HETNAM BZ3 5-METHOXY-1H-INDOLE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM EOH ETHANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BZ2 2(C9 H6 O3)
FORMUL 4 BZ3 2(C9 H9 N O)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 EOH 2(C2 H6 O)
FORMUL 13 HOH *382(H2 O)
HELIX 1 1 ALA A 16 THR A 30 1 15
HELIX 2 2 HIS A 44 ARG A 56 1 13
HELIX 3 3 ASN A 69 PHE A 73 5 5
HELIX 4 4 GLY A 77 TYR A 82 1 6
HELIX 5 5 THR A 85 GLU A 96 1 12
HELIX 6 6 THR A 105 TYR A 110 1 6
HELIX 7 7 GLY A 121 GLY A 130 5 10
HELIX 8 8 THR A 134 ARG A 151 1 18
HELIX 9 9 ASP A 161 PHE A 175 1 15
HELIX 10 10 ARG A 198 LEU A 202 5 5
HELIX 11 11 ASP A 203 ALA A 210 1 8
HELIX 12 12 VAL A 211 ALA A 224 1 14
HELIX 13 13 GLY A 227 ALA A 241 1 15
HELIX 14 14 ALA B 16 THR B 30 1 15
HELIX 15 15 HIS B 44 ARG B 56 1 13
HELIX 16 16 PRO B 86 GLU B 96 1 11
HELIX 17 17 THR B 105 TYR B 110 1 6
HELIX 18 18 GLY B 121 GLY B 130 5 10
HELIX 19 19 THR B 134 ARG B 151 1 18
HELIX 20 20 ASP B 161 PHE B 175 1 15
HELIX 21 21 SER B 196 LEU B 202 5 7
HELIX 22 22 ASP B 203 ALA B 210 1 8
HELIX 23 23 VAL B 211 ALA B 224 1 14
HELIX 24 24 GLY B 227 ALA B 241 1 15
SHEET 1 A 6 ASN A 12 TYR A 14 0
SHEET 2 A 6 ILE A 100 PHE A 102 1 O ALA A 101 N ASN A 12
SHEET 3 A 6 SER A 60 ILE A 66 1 N VAL A 64 O ILE A 100
SHEET 4 A 6 ARG A 33 THR A 39 1 N MET A 35 O VAL A 63
SHEET 5 A 6 ARG A 154 GLY A 158 1 O ARG A 154 N LEU A 36
SHEET 6 A 6 ALA A 180 VAL A 184 1 O VAL A 182 N VAL A 155
SHEET 1 B 2 THR A 117 GLN A 119 0
SHEET 2 B 2 THR B 117 GLN B 119 -1 O THR B 117 N GLN A 119
SHEET 1 C 3 ALA A 246 ASP A 254 0
SHEET 2 C 3 SER A 265 LEU A 274 -1 O ARG A 273 N ALA A 246
SHEET 3 C 3 THR A 277 GLU A 286 -1 O LEU A 279 N ALA A 272
SHEET 1 D 6 ASN B 12 TYR B 14 0
SHEET 2 D 6 ILE B 100 PHE B 102 1 O ALA B 101 N TYR B 14
SHEET 3 D 6 SER B 60 ILE B 66 1 N VAL B 64 O PHE B 102
SHEET 4 D 6 ARG B 33 THR B 39 1 N MET B 35 O VAL B 63
SHEET 5 D 6 ARG B 154 GLY B 158 1 O ARG B 154 N LEU B 36
SHEET 6 D 6 ALA B 180 VAL B 184 1 O VAL B 182 N VAL B 155
SHEET 1 E 3 ALA B 246 ASP B 254 0
SHEET 2 E 3 GLY B 264 LEU B 274 -1 O ALA B 271 N ASP B 248
SHEET 3 E 3 THR B 277 ILE B 287 -1 O LEU B 279 N ALA B 272
CISPEP 1 ALA A 75 GLY A 76 0 5.07
CISPEP 2 GLY A 76 GLY A 77 0 9.10
SITE 1 AC1 10 PRO A 38 THR A 39 MET A 40 HIS A 47
SITE 2 AC1 10 VAL A 143 GLN A 164 BZ3 A 401 HOH A 627
SITE 3 AC1 10 HOH A 637 SO4 A 701
SITE 1 AC2 10 HIS A 44 GLY A 46 HIS A 47 LYS A 160
SITE 2 AC2 10 PRO A 185 THR A 186 VAL A 187 MET A 195
SITE 3 AC2 10 BZ2 A 301 SO4 A 701
SITE 1 AC3 7 HIS A 44 LYS A 160 MET A 195 SER A 196
SITE 2 AC3 7 SER A 197 BZ2 A 301 BZ3 A 401
SITE 1 AC4 3 PRO A 111 ASP A 112 HOH A 388
SITE 1 AC5 9 MET A 109 TYR A 110 PRO A 111 ASP A 112
SITE 2 AC5 9 GLY A 113 ARG A 115 THR A 116 LYS A 145
SITE 3 AC5 9 ASP B 174
SITE 1 AC6 6 LEU A 114 ARG A 115 THR A 117 HOH A 667
SITE 2 AC6 6 GLN B 119 PRO B 120
SITE 1 AC7 3 THR A 218 HIS B 222 THR B 225
SITE 1 AC8 8 PRO B 38 THR B 39 MET B 40 HIS B 47
SITE 2 AC8 8 VAL B 143 GLN B 164 BZ3 B 402 SO4 B 702
SITE 1 AC9 8 HIS B 44 GLY B 46 PRO B 185 THR B 186
SITE 2 AC9 8 VAL B 187 MET B 195 BZ2 B 302 SO4 B 702
SITE 1 BC1 6 HIS B 44 LYS B 160 SER B 196 SER B 197
SITE 2 BC1 6 BZ2 B 302 BZ3 B 402
CRYST1 48.480 71.220 81.800 90.00 99.40 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020627 0.000000 0.003415 0.00000
SCALE2 0.000000 0.014041 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
