HEADER TRANSCRIPTION/DNA 06-MAY-05 1ZLK
TITLE CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS HYPOXIC
TITLE 2 RESPONSE REGULATOR DOSR C-TERMINAL DOMAIN-DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-
COMPND 3 D(*GP*GP*CP*CP*CP*GP*CP*GP*CP*TP*TP*TP*GP*GP*GP*GP*AP*CP*TP
COMPND 4 *AP*AP*AP*GP*TP*CP*CP*CP*TP*AP*AP*CP*CP*CP*TP*GP*GP*CP*CP*A
COMPND 5 P*CP*GP*AP*T)-3';
COMPND 6 CHAIN: C;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5'-
COMPND 10 D(*CP*GP*TP*GP*GP*CP*CP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*AP*CP
COMPND 11 *TP*TP*TP*AP*GP*TP*CP*CP*CP*CP*AP*AP*AP*GP*CP*GP*CP*GP*GP*G
COMPND 12 P*CP*CP*AP*T)-3';
COMPND 13 CHAIN: D;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DORMANCY SURVIVAL REGULATOR;
COMPND 17 CHAIN: A, B;
COMPND 18 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 19 SYNONYM: DOSR;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 7 ORGANISM_TAXID: 1773;
SOURCE 8 GENE: DOSR, DEVR, RV3133C;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET28(+)
KEYWDS HELIX-TURN-HELIX, PROTEIN-DNA COMPLEX, TRANSCRIPTION/DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.WISEDCHAISRI,M.WU,A.E.RICE,D.M.ROBERTS,D.R.SHERMAN,
AUTHOR 2 W.G.J.HOL
REVDAT 2 24-FEB-09 1ZLK 1 VERSN
REVDAT 1 31-JAN-06 1ZLK 0
JRNL AUTH G.WISEDCHAISRI,M.WU,A.E.RICE,D.M.ROBERTS,
JRNL AUTH 2 D.R.SHERMAN,W.G.J.HOL
JRNL TITL STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS DOSR AND
JRNL TITL 2 DOSR-DNA COMPLEX INVOLVED IN GENE ACTIVATION
JRNL TITL 3 DURING ADAPTATION TO HYPOXIC LATENCY.
JRNL REF J.MOL.BIOL. V. 354 630 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16246368
JRNL DOI 10.1016/J.JMB.2005.09.048
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.7
REMARK 3 NUMBER OF REFLECTIONS : 7800
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) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 407
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4270
REMARK 3 BIN FREE R VALUE SET COUNT : 15
REMARK 3 BIN FREE R VALUE : 0.5690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1010
REMARK 3 NUCLEIC ACID ATOMS : 1008
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : -4.00000
REMARK 3 B33 (A**2) : 8.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.86000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.996
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.499
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.394
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.638
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.892
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.865
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2148 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1471 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3104 ; 1.086 ; 2.565
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3503 ; 0.841 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 4.242 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 313 ; 0.048 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1622 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 206 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 524 ; 0.220 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1961 ; 0.258 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1001 ; 0.088 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 67 ; 0.227 ; 0.500
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): 7 ; 0.254 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 29 ; 0.262 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.087 ; 0.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 145 A 209 2
REMARK 3 1 B 145 B 209 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 C (A): 384 ; 0.05 ; 0.10
REMARK 3 MEDIUM POSITIONAL 1 C (A): 619 ; 0.19 ; 0.40
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 14 C 19 4
REMARK 3 1 D 14 D 19 4
REMARK 3 2 C 22 C 27 4
REMARK 3 2 D 22 D 27 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 360 ; 0.14 ; 0.40
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1ZLK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032860.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96411
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8211
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 79.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ZLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, HEPES, CALCIUM CHLORIDE,
REMARK 280 PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 71.19850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.39550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.19850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.39550
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS 2 BIOLOGICAL PROTEIN
REMARK 300 MONOMERS FORMING ONE FUNCTIONAL DIMER BOUND TO DOUBLE-STRANDED
REMARK 300 OLIGONUCLEOTIDE.
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 APPLY THE FOLLOWING TO CHAINS: C, D, 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 DG C 1
REMARK 465 DG C 2
REMARK 465 DC C 3
REMARK 465 DC C 4
REMARK 465 DC C 5
REMARK 465 DG C 6
REMARK 465 DC C 7
REMARK 465 DC C 32
REMARK 465 DC C 33
REMARK 465 DT C 34
REMARK 465 DG C 35
REMARK 465 DG C 36
REMARK 465 DC C 37
REMARK 465 DC C 38
REMARK 465 DA C 39
REMARK 465 DC C 40
REMARK 465 DG C 41
REMARK 465 DA C 42
REMARK 465 DT C 43
REMARK 465 DC D 0
REMARK 465 DG D 1
REMARK 465 DT D 2
REMARK 465 DG D 3
REMARK 465 DG D 4
REMARK 465 DC D 5
REMARK 465 DC D 6
REMARK 465 DG D 32
REMARK 465 DC D 33
REMARK 465 DG D 34
REMARK 465 DC D 35
REMARK 465 DG D 36
REMARK 465 DG D 37
REMARK 465 DG D 38
REMARK 465 DC D 39
REMARK 465 DC D 40
REMARK 465 DA D 41
REMARK 465 DT D 42
REMARK 465 MET A 123
REMARK 465 GLY A 124
REMARK 465 SER A 125
REMARK 465 SER A 126
REMARK 465 HIS A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 SER A 133
REMARK 465 SER A 134
REMARK 465 GLY A 135
REMARK 465 LEU A 136
REMARK 465 VAL A 137
REMARK 465 PRO A 138
REMARK 465 ARG A 139
REMARK 465 GLY A 140
REMARK 465 SER A 141
REMARK 465 HIS A 142
REMARK 465 MET A 143
REMARK 465 GLN A 144
REMARK 465 SER A 210
REMARK 465 ARG A 211
REMARK 465 PRO A 212
REMARK 465 PRO A 213
REMARK 465 GLY A 214
REMARK 465 ASP A 215
REMARK 465 GLY A 216
REMARK 465 PRO A 217
REMARK 465 MET B 123
REMARK 465 GLY B 124
REMARK 465 SER B 125
REMARK 465 SER B 126
REMARK 465 HIS B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 SER B 133
REMARK 465 SER B 134
REMARK 465 GLY B 135
REMARK 465 LEU B 136
REMARK 465 VAL B 137
REMARK 465 PRO B 138
REMARK 465 ARG B 139
REMARK 465 GLY B 140
REMARK 465 SER B 141
REMARK 465 HIS B 142
REMARK 465 MET B 143
REMARK 465 GLN B 144
REMARK 465 SER B 210
REMARK 465 ARG B 211
REMARK 465 PRO B 212
REMARK 465 PRO B 213
REMARK 465 GLY B 214
REMARK 465 ASP B 215
REMARK 465 GLY B 216
REMARK 465 PRO B 217
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 209 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 209 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 DC C 9 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG C 14 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA C 17 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA C 20 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA C 21 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DC C 26 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DC C 26 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DC C 27 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DT C 28 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT D 11 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG D 14 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA D 17 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC D 26 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DC D 27 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DC D 28 O4' - C1' - N1 ANGL. DEV. = 2.7 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 THR A 151 -174.27 -61.98
REMARK 500 THR B 151 -173.30 -64.48
REMARK 500 ASP B 152 -70.67 -45.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZLJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS HYPOXIC
REMARK 900 RESPONSE REGULATOR DOSR C-TERMINAL DOMAIN
DBREF 1ZLK A 144 217 GB 15610269 NP_217649 144 217
DBREF 1ZLK B 144 217 GB 15610269 NP_217649 144 217
DBREF 1ZLK C 1 43 PDB 1ZLK 1ZLK 1 43
DBREF 1ZLK D 0 42 PDB 1ZLK 1ZLK 0 42
SEQADV 1ZLK MET A 123 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY A 124 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER A 125 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER A 126 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK HIS A 127 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS A 128 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS A 129 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS A 130 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS A 131 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS A 132 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK SER A 133 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER A 134 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY A 135 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK LEU A 136 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK VAL A 137 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK PRO A 138 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK ARG A 139 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY A 140 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER A 141 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK HIS A 142 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK MET A 143 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK MET B 123 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY B 124 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER B 125 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER B 126 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK HIS B 127 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS B 128 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS B 129 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS B 130 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS B 131 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK HIS B 132 GB 15610269 EXPRESSION TAG
SEQADV 1ZLK SER B 133 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER B 134 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY B 135 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK LEU B 136 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK VAL B 137 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK PRO B 138 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK ARG B 139 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK GLY B 140 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK SER B 141 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK HIS B 142 GB 15610269 CLONING ARTIFACT
SEQADV 1ZLK MET B 143 GB 15610269 CLONING ARTIFACT
SEQRES 1 C 43 DG DG DC DC DC DG DC DG DC DT DT DT DG
SEQRES 2 C 43 DG DG DG DA DC DT DA DA DA DG DT DC DC
SEQRES 3 C 43 DC DT DA DA DC DC DC DT DG DG DC DC DA
SEQRES 4 C 43 DC DG DA DT
SEQRES 1 D 43 DC DG DT DG DG DC DC DA DG DG DG DT DT
SEQRES 2 D 43 DA DG DG DG DA DC DT DT DT DA DG DT DC
SEQRES 3 D 43 DC DC DC DA DA DA DG DC DG DC DG DG DG
SEQRES 4 D 43 DC DC DA DT
SEQRES 1 A 95 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 95 LEU VAL PRO ARG GLY SER HIS MET GLN ASP PRO LEU SER
SEQRES 3 A 95 GLY LEU THR ASP GLN GLU ARG THR LEU LEU GLY LEU LEU
SEQRES 4 A 95 SER GLU GLY LEU THR ASN LYS GLN ILE ALA ASP ARG MET
SEQRES 5 A 95 PHE LEU ALA GLU LYS THR VAL LYS ASN TYR VAL SER ARG
SEQRES 6 A 95 LEU LEU ALA LYS LEU GLY MET GLU ARG ARG THR GLN ALA
SEQRES 7 A 95 ALA VAL PHE ALA THR GLU LEU LYS ARG SER ARG PRO PRO
SEQRES 8 A 95 GLY ASP GLY PRO
SEQRES 1 B 95 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 95 LEU VAL PRO ARG GLY SER HIS MET GLN ASP PRO LEU SER
SEQRES 3 B 95 GLY LEU THR ASP GLN GLU ARG THR LEU LEU GLY LEU LEU
SEQRES 4 B 95 SER GLU GLY LEU THR ASN LYS GLN ILE ALA ASP ARG MET
SEQRES 5 B 95 PHE LEU ALA GLU LYS THR VAL LYS ASN TYR VAL SER ARG
SEQRES 6 B 95 LEU LEU ALA LYS LEU GLY MET GLU ARG ARG THR GLN ALA
SEQRES 7 B 95 ALA VAL PHE ALA THR GLU LEU LYS ARG SER ARG PRO PRO
SEQRES 8 B 95 GLY ASP GLY PRO
HELIX 1 1 LEU A 160 GLY A 164 5 5
HELIX 2 2 THR A 166 ARG A 173 1 8
HELIX 3 3 ALA A 177 GLY A 193 1 17
HELIX 4 4 ARG A 196 ARG A 209 1 14
HELIX 5 5 ARG B 155 LEU B 160 1 6
HELIX 6 6 LEU B 161 GLY B 164 5 4
HELIX 7 7 THR B 166 ARG B 173 1 8
HELIX 8 8 ALA B 177 GLY B 193 1 17
HELIX 9 9 ARG B 196 ARG B 209 1 14
CRYST1 142.397 58.791 82.933 90.00 125.50 90.00 C 1 2 1 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 0.007023 0.000000 0.005009 0.00000
SCALE2 0.000000 0.017009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014811 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
