HEADER LIGASE/LIGASE INHIBITOR 22-SEP-13 4MUK
TITLE CRYSTAL STRUCTURE OF PANTOTHENATE SYNTHETASE IN COMPLEX WITH 2-(5-
TITLE 2 METHOXY-2-(4-(TRIFLUOROMETHYL)BENZYLSULFONYLCARBAMOYL)-1H-INDOL-1-
TITLE 3 YL)ACETIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANTOTHENATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PS, PANTOATE--BETA-ALANINE LIGASE, PANTOATE-ACTIVATING
COMPND 5 ENZYME;
COMPND 6 EC: 6.3.2.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: ROSETTA2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS ALPHA BETA 3-LAYER(ABA) SANDWICH ROSSMANN FOLD, PANTOATE-LIGASE, ATP
KEYWDS 2 BINDING, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.SILVESTRE,T.L.BLUNDELL
REVDAT 3 20-SEP-23 4MUK 1 REMARK SEQADV
REVDAT 2 23-NOV-16 4MUK 1 JRNL
REVDAT 1 27-AUG-14 4MUK 0
JRNL AUTH A.W.HUNG,H.L.SILVESTRE,S.WEN,G.P.GEORGE,J.BOLAND,
JRNL AUTH 2 T.L.BLUNDELL,A.CIULLI,C.ABELL
JRNL TITL OPTIMIZATION OF INHIBITORS OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 PANTOTHENATE SYNTHETASE BASED ON GROUP EFFICIENCY ANALYSIS.
JRNL REF CHEMMEDCHEM V. 11 38 2016
JRNL REFN ISSN 1860-7179
JRNL PMID 26486566
JRNL DOI 10.1002/CMDC.201500414
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 39100
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2088
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2704
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 363
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 1.61000
REMARK 3 B33 (A**2) : -1.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.492
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4301 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5887 ; 1.973 ; 2.015
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 564 ; 6.331 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;38.908 ;22.609
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 629 ;15.534 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.060 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 703 ; 0.145 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3274 ; 0.011 ; 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): 2805 ; 1.297 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4501 ; 2.143 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1496 ; 3.167 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1384 ; 5.032 ; 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 4MUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41188
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 80.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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 3LE8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-14% W/V PEG3000, 150 MM LITHIUM
REMARK 280 SULFATE, 100 MM IMIDAZOLE, 2% V/V ETHANOL, 10% V/V GLYCEROL, 20
REMARK 280 MM MAGNESIUM CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 35.45500
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: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 13.51663
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -80.68567
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 MET A 71
REMARK 465 GLN A 72
REMARK 465 PHE A 73
REMARK 465 GLY A 74
REMARK 465 ALA A 75
REMARK 465 GLY A 76
REMARK 465 GLY A 77
REMARK 465 ASP A 78
REMARK 465 LEU A 79
REMARK 465 ASP A 80
REMARK 465 ALA A 81
REMARK 465 TYR A 82
REMARK 465 PRO A 83
REMARK 465 ARG A 84
REMARK 465 THR A 85
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 ASN B 69
REMARK 465 PRO B 70
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 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 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 ARG A 25 NE CZ NH1 NH2
REMARK 470 MET A 260 CG SD CE
REMARK 470 MET B 1 CG SD CE
REMARK 470 ARG B 33 CD NE CZ NH1 NH2
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 671 O HOH A 679 1.77
REMARK 500 O HOH B 653 O HOH B 656 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 161 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 PRO A 243 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG B 151 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 278 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
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 HIS A 44 -169.68 -126.44
REMARK 500 ASP A 88 -76.64 -59.44
REMARK 500 ASP A 89 -67.30 -27.67
REMARK 500 ARG A 115 -93.13 -131.83
REMARK 500 LEU A 127 -122.11 53.79
REMARK 500 ASN A 263 -109.63 -101.58
REMARK 500 PHE B 67 48.19 -141.68
REMARK 500 ARG B 115 -99.28 -139.56
REMARK 500 LEU B 127 -108.05 53.08
REMARK 500 SER B 196 148.31 -172.19
REMARK 500 LEU B 257 11.52 81.64
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 2DV A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2DV B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MQ6 RELATED DB: PDB
REMARK 900 RELATED ID: 4MUE RELATED DB: PDB
REMARK 900 RELATED ID: 4MUF RELATED DB: PDB
REMARK 900 RELATED ID: 4MUG RELATED DB: PDB
REMARK 900 RELATED ID: 4MUH RELATED DB: PDB
REMARK 900 RELATED ID: 4MUI RELATED DB: PDB
REMARK 900 RELATED ID: 4MUL RELATED DB: PDB
REMARK 900 RELATED ID: 4MUN RELATED DB: PDB
DBREF 4MUK A 1 300 UNP P0A5R0 PANC_MYCTU 1 300
DBREF 4MUK B 1 300 UNP P0A5R0 PANC_MYCTU 1 300
SEQADV 4MUK ALA A 2 UNP P0A5R0 THR 2 ENGINEERED MUTATION
SEQADV 4MUK GLY A 77 UNP P0A5R0 GLU 77 ENGINEERED MUTATION
SEQADV 4MUK ALA B 2 UNP P0A5R0 THR 2 ENGINEERED MUTATION
SEQADV 4MUK GLY B 77 UNP P0A5R0 GLU 77 ENGINEERED MUTATION
SEQRES 1 A 300 MET ALA ILE PRO ALA PHE HIS PRO GLY GLU LEU ASN VAL
SEQRES 2 A 300 TYR SER ALA PRO GLY ASP VAL ALA ASP VAL SER ARG ALA
SEQRES 3 A 300 LEU ARG LEU THR GLY ARG ARG VAL MET LEU VAL PRO THR
SEQRES 4 A 300 MET GLY ALA LEU HIS GLU GLY HIS LEU ALA LEU VAL ARG
SEQRES 5 A 300 ALA ALA LYS ARG VAL PRO GLY SER VAL VAL VAL VAL SER
SEQRES 6 A 300 ILE PHE VAL ASN PRO MET GLN PHE GLY ALA GLY GLY ASP
SEQRES 7 A 300 LEU ASP ALA TYR PRO ARG THR PRO ASP ASP ASP LEU ALA
SEQRES 8 A 300 GLN LEU ARG ALA GLU GLY VAL GLU ILE ALA PHE THR PRO
SEQRES 9 A 300 THR THR ALA ALA MET TYR PRO ASP GLY LEU ARG THR THR
SEQRES 10 A 300 VAL GLN PRO GLY PRO LEU ALA ALA GLU LEU GLU GLY GLY
SEQRES 11 A 300 PRO ARG PRO THR HIS PHE ALA GLY VAL LEU THR VAL VAL
SEQRES 12 A 300 LEU LYS LEU LEU GLN ILE VAL ARG PRO ASP ARG VAL PHE
SEQRES 13 A 300 PHE GLY GLU LYS ASP TYR GLN GLN LEU VAL LEU ILE ARG
SEQRES 14 A 300 GLN LEU VAL ALA ASP PHE ASN LEU ASP VAL ALA VAL VAL
SEQRES 15 A 300 GLY VAL PRO THR VAL ARG GLU ALA ASP GLY LEU ALA MET
SEQRES 16 A 300 SER SER ARG ASN ARG TYR LEU ASP PRO ALA GLN ARG ALA
SEQRES 17 A 300 ALA ALA VAL ALA LEU SER ALA ALA LEU THR ALA ALA ALA
SEQRES 18 A 300 HIS ALA ALA THR ALA GLY ALA GLN ALA ALA LEU ASP ALA
SEQRES 19 A 300 ALA ARG ALA VAL LEU ASP ALA ALA PRO GLY VAL ALA VAL
SEQRES 20 A 300 ASP TYR LEU GLU LEU ARG ASP ILE GLY LEU GLY PRO MET
SEQRES 21 A 300 PRO LEU ASN GLY SER GLY ARG LEU LEU VAL ALA ALA ARG
SEQRES 22 A 300 LEU GLY THR THR ARG LEU LEU ASP ASN ILE ALA ILE GLU
SEQRES 23 A 300 ILE GLY THR PHE ALA GLY THR ASP ARG PRO ASP GLY TYR
SEQRES 24 A 300 ARG
SEQRES 1 B 300 MET ALA ILE PRO ALA PHE HIS PRO GLY GLU LEU ASN VAL
SEQRES 2 B 300 TYR SER ALA PRO GLY ASP VAL ALA ASP VAL SER ARG ALA
SEQRES 3 B 300 LEU ARG LEU THR GLY ARG ARG VAL MET LEU VAL PRO THR
SEQRES 4 B 300 MET GLY ALA LEU HIS GLU GLY HIS LEU ALA LEU VAL ARG
SEQRES 5 B 300 ALA ALA LYS ARG VAL PRO GLY SER VAL VAL VAL VAL SER
SEQRES 6 B 300 ILE PHE VAL ASN PRO MET GLN PHE GLY ALA GLY GLY ASP
SEQRES 7 B 300 LEU ASP ALA TYR PRO ARG THR PRO ASP ASP ASP LEU ALA
SEQRES 8 B 300 GLN LEU ARG ALA GLU GLY VAL GLU ILE ALA PHE THR PRO
SEQRES 9 B 300 THR THR ALA ALA MET TYR PRO ASP GLY LEU ARG THR THR
SEQRES 10 B 300 VAL GLN PRO GLY PRO LEU ALA ALA GLU LEU GLU GLY GLY
SEQRES 11 B 300 PRO ARG PRO THR HIS PHE ALA GLY VAL LEU THR VAL VAL
SEQRES 12 B 300 LEU LYS LEU LEU GLN ILE VAL ARG PRO ASP ARG VAL PHE
SEQRES 13 B 300 PHE GLY GLU LYS ASP TYR GLN GLN LEU VAL LEU ILE ARG
SEQRES 14 B 300 GLN LEU VAL ALA ASP PHE ASN LEU ASP VAL ALA VAL VAL
SEQRES 15 B 300 GLY VAL PRO THR VAL ARG GLU ALA ASP GLY LEU ALA MET
SEQRES 16 B 300 SER SER ARG ASN ARG TYR LEU ASP PRO ALA GLN ARG ALA
SEQRES 17 B 300 ALA ALA VAL ALA LEU SER ALA ALA LEU THR ALA ALA ALA
SEQRES 18 B 300 HIS ALA ALA THR ALA GLY ALA GLN ALA ALA LEU ASP ALA
SEQRES 19 B 300 ALA ARG ALA VAL LEU ASP ALA ALA PRO GLY VAL ALA VAL
SEQRES 20 B 300 ASP TYR LEU GLU LEU ARG ASP ILE GLY LEU GLY PRO MET
SEQRES 21 B 300 PRO LEU ASN GLY SER GLY ARG LEU LEU VAL ALA ALA ARG
SEQRES 22 B 300 LEU GLY THR THR ARG LEU LEU ASP ASN ILE ALA ILE GLU
SEQRES 23 B 300 ILE GLY THR PHE ALA GLY THR ASP ARG PRO ASP GLY TYR
SEQRES 24 B 300 ARG
HET 2DV A 401 64
HET EOH A 402 3
HET EOH A 403 3
HET EOH A 404 3
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EOH A 409 3
HET 2DV B 401 32
HET EDO B 402 4
HET EOH B 403 3
HETNAM 2DV [5-METHOXY-2-({[4-(TRIFLUOROMETHYL)
HETNAM 2 2DV BENZYL]SULFONYL}CARBAMOYL)-1H-INDOL-1-YL]ACETIC ACID
HETNAM EOH ETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 2DV 2(C20 H17 F3 N2 O6 S)
FORMUL 4 EOH 5(C2 H6 O)
FORMUL 7 EDO 5(C2 H6 O2)
FORMUL 15 HOH *363(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 ASP A 87 GLU A 96 1 10
HELIX 4 4 THR A 105 TYR A 110 1 6
HELIX 5 5 GLY A 121 GLY A 130 5 10
HELIX 6 6 THR A 134 ARG A 151 1 18
HELIX 7 7 ASP A 161 PHE A 175 1 15
HELIX 8 8 SER A 196 LEU A 202 5 7
HELIX 9 9 ASP A 203 ALA A 210 1 8
HELIX 10 10 VAL A 211 ALA A 224 1 14
HELIX 11 11 GLY A 227 ALA A 241 1 15
HELIX 12 12 GLY A 288 ALA A 291 5 4
HELIX 13 13 ALA B 16 THR B 30 1 15
HELIX 14 14 HIS B 44 ARG B 56 1 13
HELIX 15 15 PRO B 86 GLU B 96 1 11
HELIX 16 16 THR B 105 TYR B 110 1 6
HELIX 17 17 GLY B 121 GLY B 130 5 10
HELIX 18 18 THR B 134 ARG B 151 1 18
HELIX 19 19 ASP B 161 PHE B 175 1 15
HELIX 20 20 SER B 196 LEU B 202 5 7
HELIX 21 21 ASP B 203 VAL B 211 1 9
HELIX 22 22 VAL B 211 ALA B 224 1 14
HELIX 23 23 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 TYR A 14
SHEET 3 A 6 SER A 60 ILE A 66 1 N ILE A 66 O PHE A 102
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 GLN B 119 N THR A 117
SHEET 1 C 3 VAL A 245 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 ILE B 100
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 SER B 265 LEU B 274 -1 O LEU B 269 N GLU B 251
SHEET 3 E 3 THR B 277 GLU B 286 -1 O LEU B 279 N ALA B 272
CISPEP 1 GLY A 258 PRO A 259 0 -0.52
SITE 1 AC1 23 PRO A 38 THR A 39 MET A 40 HIS A 44
SITE 2 AC1 23 GLY A 46 HIS A 47 PHE A 67 VAL A 139
SITE 3 AC1 23 VAL A 142 VAL A 143 LEU A 146 LYS A 160
SITE 4 AC1 23 ASP A 161 GLN A 164 PRO A 185 THR A 186
SITE 5 AC1 23 VAL A 187 MET A 195 SER A 196 SER A 197
SITE 6 AC1 23 HOH A 562 HOH A 603 HOH A 664
SITE 1 AC2 5 ARG A 115 THR A 117 HOH A 592 GLN B 119
SITE 2 AC2 5 PRO B 120
SITE 1 AC3 3 THR A 218 HIS B 222 THR B 225
SITE 1 AC4 3 ASN A 176 GLY B 18 ALA B 21
SITE 1 AC5 7 MET A 109 TYR A 110 LEU A 114 ARG A 115
SITE 2 AC5 7 THR A 116 LYS A 145 ASP B 174
SITE 1 AC6 3 PRO A 111 ASP A 112 HOH A 631
SITE 1 AC7 2 LEU A 114 GLY A 138
SITE 1 AC8 5 ALA A 226 ALA B 208 ALA B 241 ALA B 242
SITE 2 AC8 5 PRO B 243
SITE 1 AC9 3 ALA A 21 HOH A 658 ASN B 176
SITE 1 BC1 17 PRO B 38 THR B 39 MET B 40 HIS B 44
SITE 2 BC1 17 GLY B 46 HIS B 47 VAL B 142 VAL B 143
SITE 3 BC1 17 GLN B 164 VAL B 184 PRO B 185 THR B 186
SITE 4 BC1 17 VAL B 187 MET B 195 HOH B 537 HOH B 639
SITE 5 BC1 17 HOH B 678
SITE 1 BC2 7 ASP A 174 TYR B 110 GLY B 113 LEU B 114
SITE 2 BC2 7 ARG B 115 THR B 116 LYS B 145
SITE 1 BC3 5 GLN B 206 ALA B 209 PRO B 243 GLY B 244
SITE 2 BC3 5 HOH B 684
CRYST1 48.620 70.910 81.810 90.00 99.51 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 0.020568 0.000000 0.003446 0.00000
SCALE2 0.000000 0.014102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
