HEADER LYASE,ISOMERASE 25-MAR-11 3R9Q
TITLE STRUCTURE OF A PROBABLE ENOYL-COA HYDRATASE/ISOMERASE FROM
TITLE 2 MYCOBACTERIUM ABSCESSUS ATCC 19977 / DSM 44196
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-COA HYDRATASE/ISOMERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 4.2.1.17, 5.3.3.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM ABSCESSUS;
SOURCE 3 ORGANISM_TAXID: 561007;
SOURCE 4 STRAIN: ATCC 19977 / DSM 44196;
SOURCE 5 GENE: MAB_3857C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,
KEYWDS 2 ENOYL-COA HYDRATASE/ISOMERASE, LYASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 13-SEP-23 3R9Q 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3R9Q 1 REMARK
REVDAT 2 22-APR-15 3R9Q 1 JRNL VERSN
REVDAT 1 13-APR-11 3R9Q 0
JRNL AUTH L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,
JRNL AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,
JRNL AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,
JRNL AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,
JRNL AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,
JRNL AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,
JRNL AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER
JRNL TITL INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG
JRNL TITL 2 TARGETS.
JRNL REF TUBERCULOSIS (EDINB) V. 95 142 2015
JRNL REFN ISSN 1472-9792
JRNL PMID 25613812
JRNL DOI 10.1016/J.TUBE.2014.12.003
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 58337
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2964
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3829
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.1760
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 721
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.49000
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): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.990
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5378 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3579 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7336 ; 1.482 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8687 ; 0.956 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 5.315 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 231 ;38.031 ;23.117
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 798 ;14.023 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;21.411 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 839 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6205 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1086 ; 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): 3556 ; 0.630 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1463 ; 0.136 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5646 ; 1.193 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1822 ; 2.101 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1685 ; 3.341 ; 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 : 3
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 6 A 238
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7055 52.0535 -7.7808
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: 0.0102
REMARK 3 T33: 0.0379 T12: -0.0009
REMARK 3 T13: 0.0098 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.2000 L22: 0.4614
REMARK 3 L33: 0.2173 L12: -0.0946
REMARK 3 L13: -0.0279 L23: -0.2555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0011 S13: 0.0209
REMARK 3 S21: 0.0400 S22: 0.0341 S23: 0.0684
REMARK 3 S31: -0.0393 S32: -0.0071 S33: -0.0418
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 6 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3150 26.9383 3.6172
REMARK 3 T TENSOR
REMARK 3 T11: 0.0068 T22: 0.0166
REMARK 3 T33: 0.0121 T12: 0.0007
REMARK 3 T13: 0.0016 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.3909 L22: 0.2038
REMARK 3 L33: 0.3412 L12: -0.0239
REMARK 3 L13: -0.1560 L23: -0.0356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: -0.0637 S13: -0.0301
REMARK 3 S21: 0.0248 S22: 0.0037 S23: 0.0152
REMARK 3 S31: 0.0091 S32: 0.0158 S33: 0.0107
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 6 C 247
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7409 41.7850 -23.7535
REMARK 3 T TENSOR
REMARK 3 T11: 0.0127 T22: 0.0144
REMARK 3 T33: 0.0067 T12: -0.0031
REMARK 3 T13: 0.0069 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.2511 L22: 0.4225
REMARK 3 L33: 0.2143 L12: -0.0727
REMARK 3 L13: -0.0169 L23: -0.0764
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: 0.0281 S13: -0.0007
REMARK 3 S21: -0.0474 S22: -0.0122 S23: -0.0350
REMARK 3 S31: 0.0040 S32: 0.0185 S33: -0.0048
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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3R9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-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 : ALS
REMARK 200 BEAMLINE : 5.0.1
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 : ASYMMETRIC CURVED CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58642
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 3QKA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CHLORIDE, 20% PEG6000,
REMARK 280 0.1 M HEPES, PH 7.0, CRYOPROTECTANT: 25% ETHYLENE GLYCOL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 49.15900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.97550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.10650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.97550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.15900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.10650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 MET A 5
REMARK 465 GLU A 239
REMARK 465 ALA A 240
REMARK 465 LEU A 241
REMARK 465 GLU A 242
REMARK 465 GLY A 243
REMARK 465 ALA A 244
REMARK 465 GLY A 245
REMARK 465 ARG A 246
REMARK 465 PHE A 247
REMARK 465 ALA A 248
REMARK 465 ALA A 249
REMARK 465 GLY A 250
REMARK 465 GLU A 251
REMARK 465 GLY A 252
REMARK 465 ARG A 253
REMARK 465 HIS A 254
REMARK 465 GLY A 255
REMARK 465 ALA A 256
REMARK 465 GLY A 257
REMARK 465 VAL A 258
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 MET B 5
REMARK 465 ARG B 246
REMARK 465 PHE B 247
REMARK 465 ALA B 248
REMARK 465 ALA B 249
REMARK 465 GLY B 250
REMARK 465 GLU B 251
REMARK 465 GLY B 252
REMARK 465 ARG B 253
REMARK 465 HIS B 254
REMARK 465 GLY B 255
REMARK 465 ALA B 256
REMARK 465 GLY B 257
REMARK 465 VAL B 258
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 GLU C 4
REMARK 465 MET C 5
REMARK 465 ALA C 248
REMARK 465 ALA C 249
REMARK 465 GLY C 250
REMARK 465 GLU C 251
REMARK 465 GLY C 252
REMARK 465 ARG C 253
REMARK 465 HIS C 254
REMARK 465 GLY C 255
REMARK 465 ALA C 256
REMARK 465 GLY C 257
REMARK 465 VAL C 258
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 GLN A 6 CG CD OE1 NE2
REMARK 470 ARG A 28 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 THR A 238 OG1 CG2
REMARK 470 ARG B 95 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 28 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 234 CG CD OE1 OE2
REMARK 470 ARG C 246 CG CD NE CZ NH1 NH2
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 ARG A 157 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 189 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 189 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 MET C 159 CG - SD - CE ANGL. DEV. = -25.6 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 PHE A 64 -71.33 -86.56
REMARK 500 CYS A 65 123.89 -170.13
REMARK 500 ALA A 110 -130.66 54.00
REMARK 500 PHE B 64 -73.16 -87.09
REMARK 500 ALA B 110 -129.55 56.15
REMARK 500 PHE C 64 -74.71 -85.63
REMARK 500 ALA C 110 -128.96 56.64
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 CL A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 260
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYABA.00386.A RELATED DB: TARGETDB
DBREF 3R9Q A 1 258 UNP B1MGI6 B1MGI6_MYCA9 1 258
DBREF 3R9Q B 1 258 UNP B1MGI6 B1MGI6_MYCA9 1 258
DBREF 3R9Q C 1 258 UNP B1MGI6 B1MGI6_MYCA9 1 258
SEQADV 3R9Q GLY A -3 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q PRO A -2 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q GLY A -1 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q SER A 0 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q GLY B -3 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q PRO B -2 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q GLY B -1 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q SER B 0 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q GLY C -3 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q PRO C -2 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q GLY C -1 UNP B1MGI6 EXPRESSION TAG
SEQADV 3R9Q SER C 0 UNP B1MGI6 EXPRESSION TAG
SEQRES 1 A 262 GLY PRO GLY SER MET SER GLU GLU MET GLN PRO ALA VAL
SEQRES 2 A 262 ARG VAL GLU LYS ALA GLY PRO VAL THR THR VAL ILE LEU
SEQRES 3 A 262 ASN ARG PRO HIS ALA ARG ASN ALA VAL ASP GLY PRO THR
SEQRES 4 A 262 ALA ALA ALA LEU LEU ALA ALA PHE THR GLU PHE ASP ALA
SEQRES 5 A 262 ASP PRO GLU ALA SER VAL ALA VAL LEU TRP GLY ASP ASN
SEQRES 6 A 262 GLY THR PHE CYS ALA GLY ALA ASP LEU LYS ALA MET GLY
SEQRES 7 A 262 THR ASP ARG GLY ASN GLU LEU HIS PRO HIS GLY PRO GLY
SEQRES 8 A 262 PRO MET GLY PRO SER ARG LEU ARG LEU SER LYS PRO VAL
SEQRES 9 A 262 ILE ALA ALA ILE SER GLY HIS ALA VAL ALA GLY GLY ILE
SEQRES 10 A 262 GLU LEU ALA LEU TRP CYS ASP LEU ARG VAL VAL GLU GLU
SEQRES 11 A 262 ASP ALA VAL LEU GLY VAL PHE CYS ARG ARG TRP GLY VAL
SEQRES 12 A 262 PRO LEU ILE ASP GLY GLY THR ILE ARG LEU PRO ARG LEU
SEQRES 13 A 262 ILE GLY HIS SER ARG ALA MET ASP LEU ILE LEU THR GLY
SEQRES 14 A 262 ARG PRO VAL HIS ALA ASN GLU ALA LEU ASP ILE GLY LEU
SEQRES 15 A 262 VAL ASN ARG VAL VAL ALA ARG GLY GLN ALA ARG GLU ALA
SEQRES 16 A 262 ALA GLU THR LEU ALA ALA GLU ILE ALA ALA PHE PRO GLN
SEQRES 17 A 262 GLN CYS VAL ARG ALA ASP ARG ASP SER ALA ILE ALA GLN
SEQRES 18 A 262 TRP GLY MET ALA GLU GLU ALA ALA LEU ASP ASN GLU PHE
SEQRES 19 A 262 GLY SER ILE GLU ARG VAL ALA THR GLU ALA LEU GLU GLY
SEQRES 20 A 262 ALA GLY ARG PHE ALA ALA GLY GLU GLY ARG HIS GLY ALA
SEQRES 21 A 262 GLY VAL
SEQRES 1 B 262 GLY PRO GLY SER MET SER GLU GLU MET GLN PRO ALA VAL
SEQRES 2 B 262 ARG VAL GLU LYS ALA GLY PRO VAL THR THR VAL ILE LEU
SEQRES 3 B 262 ASN ARG PRO HIS ALA ARG ASN ALA VAL ASP GLY PRO THR
SEQRES 4 B 262 ALA ALA ALA LEU LEU ALA ALA PHE THR GLU PHE ASP ALA
SEQRES 5 B 262 ASP PRO GLU ALA SER VAL ALA VAL LEU TRP GLY ASP ASN
SEQRES 6 B 262 GLY THR PHE CYS ALA GLY ALA ASP LEU LYS ALA MET GLY
SEQRES 7 B 262 THR ASP ARG GLY ASN GLU LEU HIS PRO HIS GLY PRO GLY
SEQRES 8 B 262 PRO MET GLY PRO SER ARG LEU ARG LEU SER LYS PRO VAL
SEQRES 9 B 262 ILE ALA ALA ILE SER GLY HIS ALA VAL ALA GLY GLY ILE
SEQRES 10 B 262 GLU LEU ALA LEU TRP CYS ASP LEU ARG VAL VAL GLU GLU
SEQRES 11 B 262 ASP ALA VAL LEU GLY VAL PHE CYS ARG ARG TRP GLY VAL
SEQRES 12 B 262 PRO LEU ILE ASP GLY GLY THR ILE ARG LEU PRO ARG LEU
SEQRES 13 B 262 ILE GLY HIS SER ARG ALA MET ASP LEU ILE LEU THR GLY
SEQRES 14 B 262 ARG PRO VAL HIS ALA ASN GLU ALA LEU ASP ILE GLY LEU
SEQRES 15 B 262 VAL ASN ARG VAL VAL ALA ARG GLY GLN ALA ARG GLU ALA
SEQRES 16 B 262 ALA GLU THR LEU ALA ALA GLU ILE ALA ALA PHE PRO GLN
SEQRES 17 B 262 GLN CYS VAL ARG ALA ASP ARG ASP SER ALA ILE ALA GLN
SEQRES 18 B 262 TRP GLY MET ALA GLU GLU ALA ALA LEU ASP ASN GLU PHE
SEQRES 19 B 262 GLY SER ILE GLU ARG VAL ALA THR GLU ALA LEU GLU GLY
SEQRES 20 B 262 ALA GLY ARG PHE ALA ALA GLY GLU GLY ARG HIS GLY ALA
SEQRES 21 B 262 GLY VAL
SEQRES 1 C 262 GLY PRO GLY SER MET SER GLU GLU MET GLN PRO ALA VAL
SEQRES 2 C 262 ARG VAL GLU LYS ALA GLY PRO VAL THR THR VAL ILE LEU
SEQRES 3 C 262 ASN ARG PRO HIS ALA ARG ASN ALA VAL ASP GLY PRO THR
SEQRES 4 C 262 ALA ALA ALA LEU LEU ALA ALA PHE THR GLU PHE ASP ALA
SEQRES 5 C 262 ASP PRO GLU ALA SER VAL ALA VAL LEU TRP GLY ASP ASN
SEQRES 6 C 262 GLY THR PHE CYS ALA GLY ALA ASP LEU LYS ALA MET GLY
SEQRES 7 C 262 THR ASP ARG GLY ASN GLU LEU HIS PRO HIS GLY PRO GLY
SEQRES 8 C 262 PRO MET GLY PRO SER ARG LEU ARG LEU SER LYS PRO VAL
SEQRES 9 C 262 ILE ALA ALA ILE SER GLY HIS ALA VAL ALA GLY GLY ILE
SEQRES 10 C 262 GLU LEU ALA LEU TRP CYS ASP LEU ARG VAL VAL GLU GLU
SEQRES 11 C 262 ASP ALA VAL LEU GLY VAL PHE CYS ARG ARG TRP GLY VAL
SEQRES 12 C 262 PRO LEU ILE ASP GLY GLY THR ILE ARG LEU PRO ARG LEU
SEQRES 13 C 262 ILE GLY HIS SER ARG ALA MET ASP LEU ILE LEU THR GLY
SEQRES 14 C 262 ARG PRO VAL HIS ALA ASN GLU ALA LEU ASP ILE GLY LEU
SEQRES 15 C 262 VAL ASN ARG VAL VAL ALA ARG GLY GLN ALA ARG GLU ALA
SEQRES 16 C 262 ALA GLU THR LEU ALA ALA GLU ILE ALA ALA PHE PRO GLN
SEQRES 17 C 262 GLN CYS VAL ARG ALA ASP ARG ASP SER ALA ILE ALA GLN
SEQRES 18 C 262 TRP GLY MET ALA GLU GLU ALA ALA LEU ASP ASN GLU PHE
SEQRES 19 C 262 GLY SER ILE GLU ARG VAL ALA THR GLU ALA LEU GLU GLY
SEQRES 20 C 262 ALA GLY ARG PHE ALA ALA GLY GLU GLY ARG HIS GLY ALA
SEQRES 21 C 262 GLY VAL
HET CL A 259 1
HET GOL B 259 6
HET CL B 260 1
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 CL 2(CL 1-)
FORMUL 5 GOL C3 H8 O3
FORMUL 7 HOH *721(H2 O)
HELIX 1 1 ARG A 24 ARG A 28 5 5
HELIX 2 2 ASP A 32 ASP A 49 1 18
HELIX 3 3 ALA A 110 CYS A 119 1 10
HELIX 4 4 PHE A 133 GLY A 138 1 6
HELIX 5 5 GLY A 144 GLY A 154 1 11
HELIX 6 6 GLY A 154 GLY A 165 1 12
HELIX 7 7 ALA A 170 ILE A 176 1 7
HELIX 8 8 GLN A 187 PHE A 202 1 16
HELIX 9 9 PRO A 203 GLN A 217 1 15
HELIX 10 10 ALA A 221 GLY A 231 1 11
HELIX 11 11 GLY A 231 THR A 238 1 8
HELIX 12 12 ARG B 24 ARG B 28 5 5
HELIX 13 13 ASP B 32 ASP B 49 1 18
HELIX 14 14 ALA B 110 CYS B 119 1 10
HELIX 15 15 PHE B 133 GLY B 138 1 6
HELIX 16 16 GLY B 144 GLY B 154 1 11
HELIX 17 17 GLY B 154 GLY B 165 1 12
HELIX 18 18 ALA B 170 ILE B 176 1 7
HELIX 19 19 GLN B 187 ALA B 201 1 15
HELIX 20 20 PRO B 203 GLN B 217 1 15
HELIX 21 21 ALA B 221 GLY B 231 1 11
HELIX 22 22 GLY B 231 GLY B 243 1 13
HELIX 23 23 ARG C 24 ARG C 28 5 5
HELIX 24 24 ASP C 32 ASP C 49 1 18
HELIX 25 25 ALA C 110 CYS C 119 1 10
HELIX 26 26 PHE C 133 GLY C 138 1 6
HELIX 27 27 GLY C 144 GLY C 154 1 11
HELIX 28 28 GLY C 154 GLY C 165 1 12
HELIX 29 29 ALA C 170 ILE C 176 1 7
HELIX 30 30 GLN C 187 ALA C 201 1 15
HELIX 31 31 PRO C 203 GLN C 217 1 15
HELIX 32 32 ALA C 221 GLY C 231 1 11
HELIX 33 33 GLY C 231 VAL C 236 1 6
HELIX 34 34 VAL C 236 GLY C 243 1 8
SHEET 1 A 6 VAL A 9 ALA A 14 0
SHEET 2 A 6 VAL A 17 LEU A 22 -1 O ILE A 21 N ARG A 10
SHEET 3 A 6 VAL A 54 GLY A 59 1 O VAL A 56 N VAL A 20
SHEET 4 A 6 VAL A 100 ILE A 104 1 O ALA A 103 N LEU A 57
SHEET 5 A 6 LEU A 121 GLU A 125 1 O LEU A 121 N ALA A 102
SHEET 6 A 6 ARG A 181 VAL A 183 1 O ARG A 181 N VAL A 124
SHEET 1 B 3 HIS A 107 VAL A 109 0
SHEET 2 B 3 VAL A 129 GLY A 131 1 O VAL A 129 N ALA A 108
SHEET 3 B 3 VAL A 168 HIS A 169 -1 O VAL A 168 N LEU A 130
SHEET 1 C 6 VAL B 9 ALA B 14 0
SHEET 2 C 6 VAL B 17 LEU B 22 -1 O THR B 19 N GLU B 12
SHEET 3 C 6 VAL B 54 GLY B 59 1 O VAL B 56 N VAL B 20
SHEET 4 C 6 VAL B 100 ILE B 104 1 O ALA B 103 N LEU B 57
SHEET 5 C 6 LEU B 121 GLU B 125 1 O VAL B 123 N ALA B 102
SHEET 6 C 6 ARG B 181 VAL B 183 1 O ARG B 181 N VAL B 124
SHEET 1 D 3 HIS B 107 VAL B 109 0
SHEET 2 D 3 VAL B 129 GLY B 131 1 O VAL B 129 N ALA B 108
SHEET 3 D 3 VAL B 168 HIS B 169 -1 O VAL B 168 N LEU B 130
SHEET 1 E 6 VAL C 9 ALA C 14 0
SHEET 2 E 6 VAL C 17 LEU C 22 -1 O THR C 19 N GLU C 12
SHEET 3 E 6 VAL C 54 GLY C 59 1 O VAL C 56 N VAL C 20
SHEET 4 E 6 VAL C 100 ILE C 104 1 O ALA C 103 N LEU C 57
SHEET 5 E 6 LEU C 121 GLU C 125 1 O LEU C 121 N ALA C 102
SHEET 6 E 6 ARG C 181 VAL C 183 1 O ARG C 181 N VAL C 124
SHEET 1 F 3 HIS C 107 VAL C 109 0
SHEET 2 F 3 VAL C 129 GLY C 131 1 O VAL C 129 N ALA C 108
SHEET 3 F 3 VAL C 168 HIS C 169 -1 O VAL C 168 N LEU C 130
CISPEP 1 GLY A 85 PRO A 86 0 5.36
CISPEP 2 GLY B 85 PRO B 86 0 0.34
CISPEP 3 GLY C 85 PRO C 86 0 1.37
SITE 1 AC1 5 ILE A 153 GLY A 154 SER A 156 ARG A 157
SITE 2 AC1 5 LEU C 152
SITE 1 AC2 10 ARG A 151 TRP A 218 GLY A 219 GLN B 217
SITE 2 AC2 10 TRP B 218 GLY B 219 MET B 220 ARG C 151
SITE 3 AC2 10 TRP C 218 GLY C 219
SITE 1 AC3 5 LEU A 152 ILE B 153 GLY B 154 SER B 156
SITE 2 AC3 5 ARG B 157
CRYST1 98.318 98.213 103.951 90.00 90.00 90.00 P 21 21 21 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 0.010171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010182 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
