HEADER TRANSFERASE 02-FEB-14 4OWM
TITLE ANTHRANILATE PHOSPHORIBOSYL TRANSFERASE FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS IN COMPLEX WITH 3-FLUOROANTHRANILATE, PRPP AND MAGNESIUM
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: 1773;
SOURCE 4 GENE: MT2248,MTCY190.03C,RV2192C,TRPD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS ANTHRANILIC ACIDS, MAGNESIUM, TRYPTOPHAN, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CASTELL,T.V.M.COOKSON,F.L.SHORT,J.S.LOTT
REVDAT 7 27-DEC-23 4OWM 1 HETSYN
REVDAT 6 29-JUL-20 4OWM 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 07-MAR-18 4OWM 1 REMARK
REVDAT 4 27-SEP-17 4OWM 1 SOURCE JRNL REMARK
REVDAT 3 17-DEC-14 4OWM 1 REMARK
REVDAT 2 01-OCT-14 4OWM 1 JRNL
REVDAT 1 23-APR-14 4OWM 0
JRNL AUTH T.V.COOKSON,A.CASTELL,E.M.BULLOCH,G.L.EVANS,F.L.SHORT,
JRNL AUTH 2 E.N.BAKER,J.S.LOTT,E.J.PARKER
JRNL TITL ALTERNATIVE SUBSTRATES REVEAL CATALYTIC CYCLE AND KEY
JRNL TITL 2 BINDING EVENTS IN THE REACTION CATALYSED BY ANTHRANILATE
JRNL TITL 3 PHOSPHORIBOSYLTRANSFERASE FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF BIOCHEM.J. V. 461 87 2014
JRNL REFN ESSN 1470-8728
JRNL PMID 24712732
JRNL DOI 10.1042/BJ20140209
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 52819
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2677
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3797
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4988
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 453
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18000
REMARK 3 B22 (A**2) : 1.72000
REMARK 3 B33 (A**2) : -0.54000
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): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.072
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5196 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4980 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7106 ; 1.454 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11342 ; 0.770 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 700 ; 5.314 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 204 ;32.925 ;22.549
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 722 ;12.876 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;20.438 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 825 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6048 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1197 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 25 A 405
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7223 -21.1150 9.2075
REMARK 3 T TENSOR
REMARK 3 T11: 0.0124 T22: 0.0242
REMARK 3 T33: 0.0052 T12: 0.0105
REMARK 3 T13: -0.0027 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.9015 L22: 0.2534
REMARK 3 L33: 0.5921 L12: -0.2039
REMARK 3 L13: 0.5578 L23: -0.2912
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: -0.1312 S13: 0.0183
REMARK 3 S21: 0.0006 S22: 0.0319 S23: 0.0089
REMARK 3 S31: 0.0166 S32: -0.0725 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 24 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4067 -24.2893 51.3319
REMARK 3 T TENSOR
REMARK 3 T11: 0.0073 T22: 0.0082
REMARK 3 T33: 0.0163 T12: 0.0042
REMARK 3 T13: 0.0016 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.0573 L22: 0.1219
REMARK 3 L33: 0.5091 L12: -0.2295
REMARK 3 L13: 0.4396 L23: -0.0194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0714 S13: 0.0710
REMARK 3 S21: -0.0161 S22: -0.0299 S23: -0.0379
REMARK 3 S31: -0.0487 S32: 0.0034 S33: 0.0394
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4OWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200142.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 120.892
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48500
REMARK 200 R SYM FOR SHELL (I) : 0.48500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE/MALATE, PEG 4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.63700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.44600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.99500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.44600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.63700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.99500
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: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 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 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 SER B 142
REMARK 465 SER B 143
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 ARG A 238 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 333 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 24 CG1 CG2
REMARK 470 LEU B 144 CG CD1 CD2
REMARK 470 ASP B 225 CG OD1 OD2
REMARK 470 ARG B 333 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 335 CG CD OE1 OE2
REMARK 470 GLU B 372 CG CD OE1 OE2
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 73 104.88 88.97
REMARK 500 ARG A 139 170.42 -58.05
REMARK 500 ASP A 159 34.84 -98.60
REMARK 500 ASP A 159 45.19 -105.98
REMARK 500 ASP A 251 49.04 -88.26
REMARK 500 THR A 257 -166.62 -171.39
REMARK 500 LEU A 330 -70.21 -77.89
REMARK 500 GLN A 369 49.56 -89.35
REMARK 500 ALA B 73 102.49 101.93
REMARK 500 ASP B 159 62.01 -103.74
REMARK 500 HIS B 183 52.92 -118.95
REMARK 500 ASP B 251 44.88 -89.31
REMARK 500 THR B 257 -160.90 -168.15
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 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 119 OG
REMARK 620 2 GLU A 252 OE2 93.9
REMARK 620 3 PRP A 403 O2A 94.4 171.3
REMARK 620 4 PRP A 403 O2B 89.2 88.4 94.0
REMARK 620 5 HOH A 672 O 172.2 82.8 88.6 97.7
REMARK 620 6 HOH A 715 O 80.1 84.5 94.6 166.7 92.6
REMARK 620 N 1 2 3 4 5
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 ASP A 251 OD1
REMARK 620 2 GLU A 252 OE2 99.7
REMARK 620 3 HOH A 672 O 90.2 75.1
REMARK 620 4 HOH A 730 O 84.6 110.1 173.2
REMARK 620 5 HOH A 731 O 82.5 160.9 86.0 88.9
REMARK 620 6 HOH A 732 O 169.3 80.5 100.1 85.4 100.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 119 OG
REMARK 620 2 GLU B 252 OE2 98.7
REMARK 620 3 PRP B 403 O1A 92.0 168.8
REMARK 620 4 PRP B 403 O3B 95.6 90.1 92.2
REMARK 620 5 HOH B 595 O 170.7 82.0 86.9 93.7
REMARK 620 6 HOH B 602 O 79.2 84.2 94.6 171.6 91.7
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 ASP B 251 OD1
REMARK 620 2 GLU B 252 OE2 95.2
REMARK 620 3 HOH B 595 O 81.8 71.0
REMARK 620 4 HOH B 698 O 169.6 74.5 93.2
REMARK 620 5 HOH B 699 O 85.6 113.2 167.0 99.7
REMARK 620 6 HOH B 700 O 85.6 156.2 85.6 103.1 90.6
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OWN RELATED DB: PDB
REMARK 900 RELATED ID: 4OWO RELATED DB: PDB
REMARK 900 RELATED ID: 4OWQ RELATED DB: PDB
REMARK 900 RELATED ID: 4OWS RELATED DB: PDB
REMARK 900 RELATED ID: 4OWU RELATED DB: PDB
REMARK 900 RELATED ID: 4OWV RELATED DB: PDB
DBREF 4OWM A 1 370 UNP P66992 TRPD_MYCTU 1 370
DBREF 4OWM B 1 370 UNP P66992 TRPD_MYCTU 1 370
SEQADV 4OWM LEU A 371 UNP P66992 EXPRESSION TAG
SEQADV 4OWM GLU A 372 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 373 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 374 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 375 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 376 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 377 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS A 378 UNP P66992 EXPRESSION TAG
SEQADV 4OWM LEU B 371 UNP P66992 EXPRESSION TAG
SEQADV 4OWM GLU B 372 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 373 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 374 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 375 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 376 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 377 UNP P66992 EXPRESSION TAG
SEQADV 4OWM HIS B 378 UNP P66992 EXPRESSION TAG
SEQRES 1 A 378 MET ALA LEU SER ALA GLU GLY SER SER GLY GLY SER ARG
SEQRES 2 A 378 GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO SER
SEQRES 3 A 378 TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG ASP
SEQRES 4 A 378 LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN ILE
SEQRES 5 A 378 MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA PHE
SEQRES 6 A 378 ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP GLU
SEQRES 7 A 378 VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA HIS
SEQRES 8 A 378 PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL ASP
SEQRES 9 A 378 VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL ASN
SEQRES 10 A 378 LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA GLY
SEQRES 11 A 378 VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER SER
SEQRES 12 A 378 LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY VAL
SEQRES 13 A 378 ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER LEU
SEQRES 14 A 378 ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG PHE
SEQRES 15 A 378 HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG GLU
SEQRES 16 A 378 ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO LEU
SEQRES 17 A 378 THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY CYS
SEQRES 18 A 378 ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL PHE
SEQRES 19 A 378 ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY ASP
SEQRES 20 A 378 ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER THR
SEQRES 21 A 378 ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU THR
SEQRES 22 A 378 PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN LEU
SEQRES 23 A 378 ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA ALA
SEQRES 24 A 378 ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO VAL
SEQRES 25 A 378 ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE VAL
SEQRES 26 A 378 ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU PRO
SEQRES 27 A 378 ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA ILE
SEQRES 28 A 378 ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP VAL
SEQRES 29 A 378 ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 30 A 378 HIS
SEQRES 1 B 378 MET ALA LEU SER ALA GLU GLY SER SER GLY GLY SER ARG
SEQRES 2 B 378 GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO SER
SEQRES 3 B 378 TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG ASP
SEQRES 4 B 378 LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN ILE
SEQRES 5 B 378 MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA PHE
SEQRES 6 B 378 ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP GLU
SEQRES 7 B 378 VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA HIS
SEQRES 8 B 378 PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL ASP
SEQRES 9 B 378 VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL ASN
SEQRES 10 B 378 LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA GLY
SEQRES 11 B 378 VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER SER
SEQRES 12 B 378 LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY VAL
SEQRES 13 B 378 ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER LEU
SEQRES 14 B 378 ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG PHE
SEQRES 15 B 378 HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG GLU
SEQRES 16 B 378 ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO LEU
SEQRES 17 B 378 THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY CYS
SEQRES 18 B 378 ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL PHE
SEQRES 19 B 378 ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY ASP
SEQRES 20 B 378 ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER THR
SEQRES 21 B 378 ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU THR
SEQRES 22 B 378 PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN LEU
SEQRES 23 B 378 ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA ALA
SEQRES 24 B 378 ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO VAL
SEQRES 25 B 378 ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE VAL
SEQRES 26 B 378 ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU PRO
SEQRES 27 B 378 ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA ILE
SEQRES 28 B 378 ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP VAL
SEQRES 29 B 378 ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 30 B 378 HIS
HET MG A 401 1
HET MG A 402 1
HET PRP A 403 22
HET 3F0 A 404 11
HET GOL A 405 6
HET MG B 401 1
HET MG B 402 1
HET PRP B 403 22
HET 3F0 B 404 11
HET IMD B 405 5
HETNAM MG MAGNESIUM ION
HETNAM PRP 1-O-PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETNAM 3F0 2-AZANYL-3-FLUORANYL-BENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM IMD IMIDAZOLE
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 3F0 3-FLUOROANTHRANILATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG 4(MG 2+)
FORMUL 5 PRP 2(C5 H13 O14 P3)
FORMUL 6 3F0 2(C7 H6 F N O2)
FORMUL 7 GOL C3 H8 O3
FORMUL 12 IMD C3 H5 N2 1+
FORMUL 13 HOH *453(H2 O)
HELIX 1 AA1 SER A 26 ASP A 36 1 11
HELIX 2 AA2 GLY A 43 THR A 54 1 12
HELIX 3 AA3 ARG A 58 ALA A 73 1 16
HELIX 4 AA4 THR A 75 HIS A 89 1 15
HELIX 5 AA5 ASN A 117 ALA A 129 1 13
HELIX 6 AA6 GLY A 146 GLY A 155 1 10
HELIX 7 AA7 GLY A 161 GLY A 173 1 13
HELIX 8 AA8 ALA A 179 HIS A 183 1 5
HELIX 9 AA9 TYR A 186 GLY A 197 1 12
HELIX 10 AB1 THR A 200 ASN A 203 5 4
HELIX 11 AB2 LEU A 204 THR A 209 1 6
HELIX 12 AB3 PHE A 223 ALA A 236 1 14
HELIX 13 AB4 ASP A 275 GLY A 280 5 6
HELIX 14 AB5 GLN A 285 ALA A 290 5 6
HELIX 15 AB6 ASP A 293 GLY A 306 1 14
HELIX 16 AB7 GLY A 310 GLY A 329 1 20
HELIX 17 AB8 GLU A 335 THR A 353 1 19
HELIX 18 AB9 GLY A 354 GLN A 369 1 16
HELIX 19 AC1 SER B 26 ASP B 36 1 11
HELIX 20 AC2 GLY B 43 THR B 54 1 12
HELIX 21 AC3 ARG B 58 ALA B 73 1 16
HELIX 22 AC4 THR B 75 ALA B 90 1 16
HELIX 23 AC5 ASN B 117 ALA B 129 1 13
HELIX 24 AC6 GLY B 146 LEU B 154 1 9
HELIX 25 AC7 GLY B 161 GLY B 173 1 13
HELIX 26 AC8 ALA B 179 HIS B 183 1 5
HELIX 27 AC9 TYR B 186 GLY B 197 1 12
HELIX 28 AD1 THR B 200 ASN B 203 5 4
HELIX 29 AD2 LEU B 204 THR B 209 1 6
HELIX 30 AD3 PHE B 223 ARG B 237 1 15
HELIX 31 AD4 ASP B 275 GLY B 280 5 6
HELIX 32 AD5 GLN B 285 ALA B 290 5 6
HELIX 33 AD6 ASP B 293 GLY B 306 1 14
HELIX 34 AD7 GLY B 310 GLY B 329 1 20
HELIX 35 AD8 GLU B 335 THR B 353 1 19
HELIX 36 AD9 GLY B 354 ILE B 370 1 17
SHEET 1 AA1 5 VAL A 103 GLY A 107 0
SHEET 2 AA1 5 ALA A 216 GLY A 220 1 O LEU A 218 N ASP A 104
SHEET 3 AA1 5 SER A 240 GLY A 246 1 O LEU A 242 N ILE A 219
SHEET 4 AA1 5 SER A 259 ALA A 265 -1 O VAL A 264 N VAL A 241
SHEET 5 AA1 5 SER A 268 PHE A 274 -1 O PHE A 274 N SER A 259
SHEET 1 AA2 2 VAL A 133 GLY A 137 0
SHEET 2 AA2 2 ILE A 174 PHE A 178 1 O CYS A 177 N LYS A 135
SHEET 1 AA3 5 VAL B 103 GLY B 107 0
SHEET 2 AA3 5 ALA B 216 GLY B 220 1 O LEU B 218 N ASP B 104
SHEET 3 AA3 5 SER B 240 GLY B 246 1 O VAL B 244 N ILE B 219
SHEET 4 AA3 5 SER B 259 ALA B 265 -1 O VAL B 264 N VAL B 241
SHEET 5 AA3 5 SER B 268 PHE B 274 -1 O PHE B 274 N SER B 259
SHEET 1 AA4 2 VAL B 133 GLY B 137 0
SHEET 2 AA4 2 ILE B 174 PHE B 178 1 O CYS B 177 N LYS B 135
LINK OG SER A 119 MG MG A 401 1555 1555 2.12
LINK OD1 ASP A 251 MG MG A 402 1555 1555 2.24
LINK OE2 GLU A 252 MG MG A 401 1555 1555 2.17
LINK OE2 GLU A 252 MG MG A 402 1555 1555 2.15
LINK MG MG A 401 O2A PRP A 403 1555 1555 1.96
LINK MG MG A 401 O2B PRP A 403 1555 1555 2.04
LINK MG MG A 401 O HOH A 672 1555 1555 2.04
LINK MG MG A 401 O HOH A 715 1555 1555 2.09
LINK MG MG A 402 O HOH A 672 1555 1555 2.41
LINK MG MG A 402 O HOH A 730 1555 1555 1.93
LINK MG MG A 402 O HOH A 731 1555 1555 2.16
LINK MG MG A 402 O HOH A 732 1555 1555 2.50
LINK OG SER B 119 MG MG B 401 1555 1555 2.16
LINK OD1 ASP B 251 MG MG B 402 1555 1555 2.40
LINK OE2 GLU B 252 MG MG B 401 1555 1555 2.18
LINK OE2 GLU B 252 MG MG B 402 1555 1555 2.24
LINK MG MG B 401 O1A PRP B 403 1555 1555 2.11
LINK MG MG B 401 O3B PRP B 403 1555 1555 2.02
LINK MG MG B 401 O HOH B 595 1555 1555 2.05
LINK MG MG B 401 O HOH B 602 1555 1555 2.12
LINK MG MG B 402 O HOH B 595 1555 1555 2.53
LINK MG MG B 402 O HOH B 698 1555 1555 2.60
LINK MG MG B 402 O HOH B 699 1555 1555 2.06
LINK MG MG B 402 O HOH B 700 1555 1555 2.03
CRYST1 79.274 91.990 120.892 90.00 90.00 90.00 P 21 21 21 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 0.012614 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008272 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
