HEADER OXIDOREDUCTASE 05-AUG-14 4UVD
TITLE DISCOVERY OF PYRIMIDINE ISOXAZOLES INHA IN COMPLEX WITH
TITLE 2 COMPOUND 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENOYL-ACYL CARRIER PROTEIN REDUCTASE;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR
KEYWDS OXIDOREDUCTASE, INHA, ACP ENOYL REDUCTASE, FBLG, PYRIMIDINE ISOXAZOLE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.READ,H.GINGELL,P.MADHAVAPEDDI,S.GHORPADE,S.COWAN
REVDAT 1 30-SEP-15 4UVD 0
JRNL AUTH P.MADHAVAPEDDI,R.R.KALE,S.D.COWEN,S.R.GHORPADE,G.DAVIES,
JRNL AUTH 2 E.V.BELLALE,M.G.KALE,A.SRIVASTAVA,L.SPADOLA,A.KAWATKAR,
JRNL AUTH 3 A.V.RAICHURKAR,M.TONGE,R.NANDISHAIAH,S.GUPTHA,A.NARAYAN,
JRNL AUTH 4 H.GINGELL,D.PLANT,S.LANDGE,S.MENASINAKAI,K.R.PRABHAKAR,
JRNL AUTH 5 V.ACHAR,A.AMBADY,V.K.SAMBANDAMURTHY,V.RAMACHANDRAN,
JRNL AUTH 6 V.PANDUGA,J.REDDY,C.N.N.KUMAR,P.KAUR,R.SHANDIL,P.S.IYER,
JRNL AUTH 7 S.NARAYANAN,J.A.READ
JRNL TITL HITTING THE TARGET IN MORE THAN ONE WAY: NOVEL, DIRECT
JRNL TITL 2 INHIBITORS OF MYCOBACTERIUM TUBERCULOSIS ENOYL ACP
JRNL TITL 3 REDUCTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.87
REMARK 3 NUMBER OF REFLECTIONS : 33797
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) : 0.16147
REMARK 3 R VALUE (WORKING SET) : 0.16039
REMARK 3 FREE R VALUE : 0.18224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
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) : 1.823
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.870
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2437
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.209
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.254
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.736
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52
REMARK 3 B22 (A**2) : 0.52
REMARK 3 B33 (A**2) : -1.70
REMARK 3 B12 (A**2) : 0.52
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.092
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.094
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2135 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2045 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2913 ; 1.483 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4690 ; 0.826 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 5.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;33.736 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 334 ;12.759 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.007 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2428 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 476 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 1
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 2 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4861 47.5557 18.4002
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: 0.0786
REMARK 3 T33: 0.0285 T12: 0.0019
REMARK 3 T13: -0.0082 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 0.1507 L22: 0.0612
REMARK 3 L33: 0.2209 L12: 0.0037
REMARK 3 L13: 0.0767 L23: 0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: 0.0182 S13: -0.0086
REMARK 3 S21: 0.0091 S22: -0.0245 S23: -0.0092
REMARK 3 S31: -0.0362 S32: -0.0874 S33: 0.0588
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS.
REMARK 3 U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4UVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-AUG-14.
REMARK 100 THE PDBE ID CODE IS EBI-61449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-12
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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35577
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.82
REMARK 200 RESOLUTION RANGE LOW (A) : 72.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.1
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.3
REMARK 200 R MERGE FOR SHELL (I) : 0.49
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.40
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 40DR
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.81933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.90967
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.81933
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.90967
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.81933
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 46.90967
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 93.81933
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 46.90967
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.1 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 BIOMT1 2 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.90967
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 145.62600
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 84.07721
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 -0.866025 0.000000 145.62600
REMARK 350 BIOMT2 4 -0.866025 0.500000 0.000000 84.07721
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 46.90967
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2142 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2238 LIES ON A SPECIAL POSITION.
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 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 GLU A 210 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CZ A ARG A 153 CZ A ARG A 153 4765 1.90
REMARK 500 CZ A ARG A 153 NH1A ARG A 153 4765 1.91
REMARK 500 CZ A ARG A 153 NH2A ARG A 153 4765 1.69
REMARK 500 NH1A ARG A 153 NH2A ARG A 153 4765 1.22
REMARK 500 NH2A ARG A 153 NH2A ARG A 153 4765 1.85
REMARK 500 CZ B ARG A 153 NH1B ARG A 153 4765 2.19
REMARK 500 NH1B ARG A 153 NH1B ARG A 153 4765 1.32
REMARK 500 NH2B ARG A 153 O HOH A 2173 4765 2.01
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 LEU A 269 CA - CB - CG ANGL. DEV. = 14.6 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 ILE A 16 -38.57 -130.46
REMARK 500 ASP A 42 -60.69 67.17
REMARK 500 ALA A 124 -57.52 -123.16
REMARK 500 ALA A 157 -45.05 78.83
REMARK 500 ASN A 159 -116.08 44.53
REMARK 500 ALA A 260 72.57 -106.51
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 A1271 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2249 O
REMARK 620 2 HOH A2076 O 81.2
REMARK 620 3 HOH A2248 O 113.7 96.7
REMARK 620 4 HOH A2250 O 61.6 140.7 109.0
REMARK 620 5 ASP A 52 O 99.3 76.3 145.0 96.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HRW A1272
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UVE RELATED DB: PDB
REMARK 900 DISCOVERY OF PYRIMIDINE ISOXAZOLES INHA IN COMPLEX WITH
REMARK 900 COMPOUND 9
REMARK 900 RELATED ID: 4UVG RELATED DB: PDB
REMARK 900 DISCOVERY OF PYRIMIDINE ISOXAZOLES INHA IN COMPLEX WITH
REMARK 900 COMPOUND 15
REMARK 900 RELATED ID: 4UVH RELATED DB: PDB
REMARK 900 DISCOVERY OF PYRIMIDINE ISOXAZOLES INHA IN COMPLEX WITH
REMARK 900 COMPOUND 10
REMARK 900 RELATED ID: 4UVI RELATED DB: PDB
REMARK 900 DISCOVERY OF PYRIMIDINE ISOXAZOLES INHA IN COMPLEX WITH
REMARK 900 COMPOUND 23
DBREF 4UVD A 1 269 UNP M9TGV3 M9TGV3_MYCTX 1 269
SEQRES 1 A 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 A 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 A 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 A 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 A 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 A 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 A 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 A 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 A 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 A 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 A 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 A 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 A 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 A 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 A 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 A 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 A 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 A 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 A 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 A 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 A 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
HET NAD A1270 44
HET MG A1271 1
HET HRW A1272 29
HETNAM HRW 2-[(4,6-DIMETHYLPYRIMIDIN-2-YL)SULFANYL]-N-
HETNAM 2 HRW [(2Z)-5-[3-(TRIFLUOROMETHYL)BENZYL]-1,3-
HETNAM 3 HRW THIAZOL-2(3H)-YLIDENE]ACETAMIDE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM MG MAGNESIUM ION
FORMUL 2 HRW C19 H17 F3 N4 O S2
FORMUL 3 NAD C21 H27 N7 O14 P2
FORMUL 4 MG MG 2+
FORMUL 5 HOH *251(H2 O)
HELIX 1 1 SER A 20 GLN A 32 1 13
HELIX 2 2 ARG A 43 ASP A 52 1 10
HELIX 3 3 ASN A 67 GLY A 83 1 17
HELIX 4 4 PRO A 99 MET A 103 5 5
HELIX 5 5 PRO A 107 ALA A 111 5 5
HELIX 6 6 PRO A 112 ALA A 124 1 13
HELIX 7 7 ALA A 124 LEU A 135 1 12
HELIX 8 8 TYR A 158 LYS A 181 1 24
HELIX 9 9 THR A 196 GLY A 204 1 9
HELIX 10 10 GLY A 208 ALA A 226 1 19
HELIX 11 11 ALA A 235 SER A 247 1 13
HELIX 12 12 GLY A 263 GLN A 267 5 5
SHEET 1 AA 7 LEU A 60 GLU A 62 0
SHEET 2 AA 7 GLN A 35 GLY A 40 1 O LEU A 38 N LEU A 61
SHEET 3 AA 7 ARG A 9 SER A 13 1 O ILE A 10 N VAL A 37
SHEET 4 AA 7 LEU A 88 HIS A 93 1 N ASP A 89 O ARG A 9
SHEET 5 AA 7 MET A 138 ASP A 148 1 N ASN A 139 O LEU A 88
SHEET 6 AA 7 ARG A 185 ALA A 191 1 O ARG A 185 N ILE A 144
SHEET 7 AA 7 ASP A 256 ALA A 260 1 O ASP A 256 N LEU A 188
LINK MG MG A1271 O HOH A2249 1555 1555 2.78
LINK MG MG A1271 O HOH A2076 1555 1555 2.57
LINK MG MG A1271 O HOH A2248 1555 1555 2.85
LINK MG MG A1271 O HOH A2250 1555 1555 2.88
LINK MG MG A1271 O ASP A 52 1555 1555 2.30
SITE 1 AC1 33 GLY A 14 ILE A 15 ILE A 16 SER A 20
SITE 2 AC1 33 ILE A 21 PHE A 41 LEU A 63 ASP A 64
SITE 3 AC1 33 VAL A 65 SER A 94 ILE A 95 GLY A 96
SITE 4 AC1 33 ILE A 122 MET A 147 ASP A 148 LYS A 165
SITE 5 AC1 33 ALA A 191 GLY A 192 PRO A 193 ILE A 194
SITE 6 AC1 33 THR A 196 HRW A1272 HOH A2019 HOH A2020
SITE 7 AC1 33 HOH A2021 HOH A2023 HOH A2081 HOH A2123
SITE 8 AC1 33 HOH A2176 HOH A2195 HOH A2245 HOH A2246
SITE 9 AC1 33 HOH A2247
SITE 1 AC2 5 ASP A 52 HOH A2076 HOH A2248 HOH A2249
SITE 2 AC2 5 HOH A2250
SITE 1 AC3 10 GLY A 96 PHE A 97 MET A 98 GLN A 100
SITE 2 AC3 10 ALA A 198 MET A 199 ALA A 201 ILE A 202
SITE 3 AC3 10 ALA A 206 NAD A1270
CRYST1 97.084 97.084 140.729 90.00 90.00 120.00 P 62 2 2 12
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 0.010300 0.005947 0.000000 0.00000
SCALE2 0.000000 0.011894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
