HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-AUG-12 4GKM
TITLE BIANTHRANILATE-LIKE ANALOGUE BOUND IN THE OUTER SITE OF ANTHRANILATE
TITLE 2 PHOSPHORIBOSYLTRANSFERASE (ANPRT; TRPD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: MT2248, MTCY190.03C, RV2192C, TRPD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PGROESL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS MAGNESIUM BINDING, PHOSPHORIBOSYLPYROPHOSPHATE, PRPP, INHIBITOR
KEYWDS 2 COMPLEX, BI-ANTHRANILATE-LIKE ANALOGUE, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC, PHOSPHORIBOSYLTRANSFERASE, TRANSFERASE-
KEYWDS 4 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.EVANS,E.N.BAKER,J.S.LOTT,TB STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 2 (TBSGC)
REVDAT 5 13-SEP-23 4GKM 1 HETSYN
REVDAT 4 29-JUL-20 4GKM 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 15-NOV-17 4GKM 1 REMARK
REVDAT 2 21-MAY-14 4GKM 1 JRNL
REVDAT 1 14-AUG-13 4GKM 0
JRNL AUTH G.L.EVANS,S.A.GAMAGE,E.M.BULLOCH,E.N.BAKER,W.A.DENNY,
JRNL AUTH 2 J.S.LOTT
JRNL TITL REPURPOSING THE CHEMICAL SCAFFOLD OF THE ANTI-ARTHRITIC DRUG
JRNL TITL 2 LOBENZARIT TO TARGET TRYPTOPHAN BIOSYNTHESIS IN
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF CHEMBIOCHEM V. 15 852 2014
JRNL REFN ISSN 1439-4227
JRNL PMID 24623674
JRNL DOI 10.1002/CBIC.201300628
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 81000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3799
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 56.5063 - 3.1912 0.96 11225 647 0.1761 0.1821
REMARK 3 2 3.1912 - 2.5329 0.98 11165 593 0.1943 0.2225
REMARK 3 3 2.5329 - 2.2127 0.99 11191 602 0.1914 0.2297
REMARK 3 4 2.2127 - 2.0104 0.99 11142 594 0.2027 0.2399
REMARK 3 5 2.0104 - 1.8663 1.00 11206 548 0.2117 0.2457
REMARK 3 6 1.8663 - 1.7563 1.00 11190 568 0.2338 0.2793
REMARK 3 7 1.7563 - 1.6683 0.88 9836 493 0.3040 0.3421
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 36.46
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.89360
REMARK 3 B22 (A**2) : 3.99480
REMARK 3 B33 (A**2) : -3.10120
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 5241
REMARK 3 ANGLE : 1.211 7244
REMARK 3 CHIRALITY : 0.260 824
REMARK 3 PLANARITY : 0.005 936
REMARK 3 DIHEDRAL : 13.774 1814
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.991841
REMARK 200 MONOCHROMATOR : SILICON DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (KABSCH
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81071
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.667
REMARK 200 RESOLUTION RANGE LOW (A) : 111.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: CHAIN A OF PDB ENTRY 3QR9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M IMIDAZOLE.MALATE, 13% PEG-4000,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 55.58350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.67100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.58350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.67100
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: 6080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 MET A 0
REMARK 465 VAL A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 ARG A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 PRO A 17
REMARK 465 LYS A 18
REMARK 465 ALA A 19
REMARK 465 GLU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 VAL A 24
REMARK 465 LEU A 371
REMARK 465 GLU A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 MET B 0
REMARK 465 VAL B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 ARG B 13
REMARK 465 GLY B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 PRO B 17
REMARK 465 LYS B 18
REMARK 465 ALA B 19
REMARK 465 GLU B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 SER B 23
REMARK 465 VAL B 24
REMARK 465 LEU B 371
REMARK 465 GLU B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
REMARK 465 HIS B 377
REMARK 465 HIS B 378
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 ASP A 100 CG OD1 OD2
REMARK 470 VAL A 113 CG1 CG2
REMARK 470 SER A 142 OG
REMARK 470 LEU A 144 CG CD1 CD2
REMARK 470 GLN A 285 CG CD OE1 NE2
REMARK 470 ASP A 287 CG OD1 OD2
REMARK 470 SER A 332 OG
REMARK 470 ARG A 333 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 335 CG CD OE1 OE2
REMARK 470 GLN A 369 CG CD OE1 NE2
REMARK 470 ASP B 100 CG OD1 OD2
REMARK 470 SER B 142 OG
REMARK 470 LEU B 144 CG CD1 CD2
REMARK 470 ASP B 287 CG OD1 OD2
REMARK 470 SER B 332 OG
REMARK 470 ARG B 333 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 335 CG CD OE1 OE2
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 727 O HOH B 751 2.17
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 73 103.70 92.22
REMARK 500 ASN A 114 71.61 41.44
REMARK 500 ASP A 251 43.71 -88.62
REMARK 500 THR A 257 -158.90 -162.97
REMARK 500 ALA B 73 101.54 91.91
REMARK 500 ASP B 251 44.48 -88.35
REMARK 500 THR B 257 -162.84 -171.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 119 OG
REMARK 620 2 GLU A 252 OE2 101.4
REMARK 620 3 PRP A 401 O3B 88.8 94.3
REMARK 620 4 PRP A 401 O2A 97.7 160.2 80.7
REMARK 620 5 HOH A 677 O 80.7 85.4 169.2 103.0
REMARK 620 6 HOH A 679 O 177.4 76.4 92.8 84.7 97.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 251 OD1
REMARK 620 2 GLU A 252 OE2 89.4
REMARK 620 3 HOH A 679 O 82.7 74.3
REMARK 620 4 HOH A 680 O 90.9 163.1 88.9
REMARK 620 5 HOH A 681 O 169.3 81.9 100.8 99.2
REMARK 620 6 HOH A 682 O 81.7 103.1 164.2 93.7 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 119 OG
REMARK 620 2 GLU B 252 OE2 101.5
REMARK 620 3 PRP B 401 O2B 89.3 94.5
REMARK 620 4 PRP B 401 O2A 96.2 162.1 83.8
REMARK 620 5 HOH B 702 O 177.2 79.4 93.3 82.9
REMARK 620 6 HOH B 703 O 80.1 86.4 169.3 98.7 97.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 251 OD1
REMARK 620 2 GLU B 252 OE2 91.3
REMARK 620 3 HOH B 702 O 87.1 76.5
REMARK 620 4 HOH B 704 O 80.4 107.9 166.8
REMARK 620 5 HOH B 705 O 87.7 162.4 85.9 89.2
REMARK 620 6 HOH B 706 O 172.6 86.1 99.0 93.8 96.8
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GIU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR.
REMARK 900 RELATED ID: TB-RV2192C RELATED DB: TARGETTRACK
DBREF 4GKM A 0 370 UNP P66992 TRPD_MYCTU 1 370
DBREF 4GKM B 0 370 UNP P66992 TRPD_MYCTU 1 370
SEQADV 4GKM VAL A 1 UNP P66992 EXPRESSION TAG
SEQADV 4GKM LEU A 371 UNP P66992 EXPRESSION TAG
SEQADV 4GKM GLU A 372 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 373 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 374 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 375 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 376 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 377 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS A 378 UNP P66992 EXPRESSION TAG
SEQADV 4GKM VAL B 1 UNP P66992 EXPRESSION TAG
SEQADV 4GKM LEU B 371 UNP P66992 EXPRESSION TAG
SEQADV 4GKM GLU B 372 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 373 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 374 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 375 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 376 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 377 UNP P66992 EXPRESSION TAG
SEQADV 4GKM HIS B 378 UNP P66992 EXPRESSION TAG
SEQRES 1 A 379 MET VAL ALA LEU SER ALA GLU GLY SER SER GLY GLY SER
SEQRES 2 A 379 ARG GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO
SEQRES 3 A 379 SER TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG
SEQRES 4 A 379 ASP LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN
SEQRES 5 A 379 ILE MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA
SEQRES 6 A 379 PHE ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP
SEQRES 7 A 379 GLU VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA
SEQRES 8 A 379 HIS PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL
SEQRES 9 A 379 ASP VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL
SEQRES 10 A 379 ASN LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA
SEQRES 11 A 379 GLY VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER
SEQRES 12 A 379 SER LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY
SEQRES 13 A 379 VAL ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER
SEQRES 14 A 379 LEU ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG
SEQRES 15 A 379 PHE HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG
SEQRES 16 A 379 GLU ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO
SEQRES 17 A 379 LEU THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY
SEQRES 18 A 379 CYS ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL
SEQRES 19 A 379 PHE ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY
SEQRES 20 A 379 ASP ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER
SEQRES 21 A 379 THR ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU
SEQRES 22 A 379 THR PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN
SEQRES 23 A 379 LEU ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA
SEQRES 24 A 379 ALA ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO
SEQRES 25 A 379 VAL ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE
SEQRES 26 A 379 VAL ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU
SEQRES 27 A 379 PRO ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA
SEQRES 28 A 379 ILE ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP
SEQRES 29 A 379 VAL ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS
SEQRES 30 A 379 HIS HIS
SEQRES 1 B 379 MET VAL ALA LEU SER ALA GLU GLY SER SER GLY GLY SER
SEQRES 2 B 379 ARG GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO
SEQRES 3 B 379 SER TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG
SEQRES 4 B 379 ASP LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN
SEQRES 5 B 379 ILE MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA
SEQRES 6 B 379 PHE ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP
SEQRES 7 B 379 GLU VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA
SEQRES 8 B 379 HIS PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL
SEQRES 9 B 379 ASP VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL
SEQRES 10 B 379 ASN LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA
SEQRES 11 B 379 GLY VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER
SEQRES 12 B 379 SER LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY
SEQRES 13 B 379 VAL ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER
SEQRES 14 B 379 LEU ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG
SEQRES 15 B 379 PHE HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG
SEQRES 16 B 379 GLU ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO
SEQRES 17 B 379 LEU THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY
SEQRES 18 B 379 CYS ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL
SEQRES 19 B 379 PHE ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY
SEQRES 20 B 379 ASP ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER
SEQRES 21 B 379 THR ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU
SEQRES 22 B 379 THR PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN
SEQRES 23 B 379 LEU ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA
SEQRES 24 B 379 ALA ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO
SEQRES 25 B 379 VAL ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE
SEQRES 26 B 379 VAL ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU
SEQRES 27 B 379 PRO ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA
SEQRES 28 B 379 ILE ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP
SEQRES 29 B 379 VAL ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS
SEQRES 30 B 379 HIS HIS
HET PRP A 401 22
HET MG A 402 1
HET MG A 403 1
HET 683 A 404 20
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET DMS A 408 4
HET PRP B 401 22
HET MG B 402 1
HET MG B 403 1
HET 683 B 404 20
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HET GOL B 408 6
HET DMS B 409 4
HET DMS B 410 4
HETNAM PRP 1-O-PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETNAM MG MAGNESIUM ION
HETNAM 683 2-[(2-CARBOXYPHENYL)AMINO]-5-METHYLBENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN PRP ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID; 1-O-
HETSYN 2 PRP PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOSE; 1-O-
HETSYN 3 PRP PYROPHOSPHONO-5-O-PHOSPHONO-D-RIBOSE; 1-O-
HETSYN 4 PRP PYROPHOSPHONO-5-O-PHOSPHONO-RIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PRP 2(C5 H13 O14 P3)
FORMUL 4 MG 4(MG 2+)
FORMUL 6 683 2(C15 H13 N O4)
FORMUL 7 GOL 7(C3 H8 O3)
FORMUL 10 DMS 3(C2 H6 O S)
FORMUL 21 HOH *485(H2 O)
HELIX 1 1 SER A 26 ASP A 36 1 11
HELIX 2 2 GLY A 43 THR A 54 1 12
HELIX 3 3 ARG A 58 ALA A 73 1 16
HELIX 4 4 THR A 75 ALA A 90 1 16
HELIX 5 5 ASN A 117 ALA A 129 1 13
HELIX 6 6 GLY A 146 GLY A 155 1 10
HELIX 7 7 GLY A 161 GLY A 173 1 13
HELIX 8 8 ALA A 179 HIS A 183 1 5
HELIX 9 9 TYR A 186 GLY A 197 1 12
HELIX 10 10 THR A 200 ASN A 203 5 4
HELIX 11 11 LEU A 204 THR A 209 1 6
HELIX 12 12 LEU A 226 ARG A 237 1 12
HELIX 13 13 ASP A 275 GLY A 280 5 6
HELIX 14 14 GLN A 285 ALA A 290 5 6
HELIX 15 15 ASP A 293 GLY A 306 1 14
HELIX 16 16 GLY A 310 GLY A 329 1 20
HELIX 17 17 GLU A 335 THR A 353 1 19
HELIX 18 18 GLY A 354 GLN A 369 1 16
HELIX 19 19 SER B 26 ASP B 36 1 11
HELIX 20 20 GLY B 43 THR B 54 1 12
HELIX 21 21 ARG B 58 ALA B 73 1 16
HELIX 22 22 THR B 75 ALA B 90 1 16
HELIX 23 23 ASN B 117 ALA B 129 1 13
HELIX 24 24 GLY B 146 LEU B 154 1 9
HELIX 25 25 GLY B 161 GLY B 173 1 13
HELIX 26 26 ALA B 179 HIS B 183 1 5
HELIX 27 27 TYR B 186 GLY B 197 1 12
HELIX 28 28 THR B 200 ASN B 203 5 4
HELIX 29 29 LEU B 204 THR B 209 1 6
HELIX 30 30 LEU B 226 ARG B 237 1 12
HELIX 31 31 ASP B 275 GLY B 280 5 6
HELIX 32 32 GLN B 285 ALA B 290 5 6
HELIX 33 33 ASP B 293 GLY B 306 1 14
HELIX 34 34 GLY B 310 GLY B 329 1 20
HELIX 35 35 GLU B 335 THR B 353 1 19
HELIX 36 36 GLY B 354 GLN B 369 1 16
SHEET 1 A 5 VAL A 103 GLY A 107 0
SHEET 2 A 5 ALA A 216 GLY A 220 1 O LEU A 218 N ASP A 104
SHEET 3 A 5 SER A 240 GLY A 246 1 O VAL A 244 N ILE A 219
SHEET 4 A 5 SER A 259 ALA A 265 -1 O THR A 260 N HIS A 245
SHEET 5 A 5 SER A 268 PHE A 274 -1 O PHE A 274 N SER A 259
SHEET 1 B 2 VAL A 133 GLY A 137 0
SHEET 2 B 2 ILE A 174 PHE A 178 1 O CYS A 177 N LYS A 135
SHEET 1 C 5 VAL B 103 GLY B 107 0
SHEET 2 C 5 ALA B 216 GLY B 220 1 O LEU B 218 N ASP B 104
SHEET 3 C 5 SER B 240 GLY B 246 1 O VAL B 244 N ILE B 219
SHEET 4 C 5 SER B 259 ALA B 265 -1 O THR B 260 N HIS B 245
SHEET 5 C 5 SER B 268 PHE B 274 -1 O PHE B 274 N SER B 259
SHEET 1 D 2 VAL B 133 GLY B 137 0
SHEET 2 D 2 ILE B 174 PHE B 178 1 O CYS B 177 N LYS B 135
LINK OG SER A 119 MG MG A 402 1555 1555 2.11
LINK OD1 ASP A 251 MG MG A 403 1555 1555 2.21
LINK OE2 GLU A 252 MG MG A 402 1555 1555 2.09
LINK OE2 GLU A 252 MG MG A 403 1555 1555 2.18
LINK O3B PRP A 401 MG MG A 402 1555 1555 2.01
LINK O2A PRP A 401 MG MG A 402 1555 1555 2.03
LINK MG MG A 402 O HOH A 677 1555 1555 2.09
LINK MG MG A 402 O HOH A 679 1555 1555 2.10
LINK MG MG A 403 O HOH A 679 1555 1555 2.11
LINK MG MG A 403 O HOH A 680 1555 1555 2.07
LINK MG MG A 403 O HOH A 681 1555 1555 2.12
LINK MG MG A 403 O HOH A 682 1555 1555 2.04
LINK OG SER B 119 MG MG B 402 1555 1555 2.09
LINK OD1 ASP B 251 MG MG B 403 1555 1555 2.17
LINK OE2 GLU B 252 MG MG B 402 1555 1555 2.04
LINK OE2 GLU B 252 MG MG B 403 1555 1555 2.15
LINK O2B PRP B 401 MG MG B 402 1555 1555 1.95
LINK O2A PRP B 401 MG MG B 402 1555 1555 2.09
LINK MG MG B 402 O HOH B 702 1555 1555 2.11
LINK MG MG B 402 O HOH B 703 1555 1555 2.05
LINK MG MG B 403 O HOH B 702 1555 1555 2.13
LINK MG MG B 403 O HOH B 704 1555 1555 2.04
LINK MG MG B 403 O HOH B 705 1555 1555 2.08
LINK MG MG B 403 O HOH B 706 1555 1555 2.09
CRYST1 111.167 81.342 78.468 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 0.008995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
