HEADER TRANSFERASE 27-MAY-11 2YKH
TITLE SENSOR REGION OF A SENSOR HISTIDINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SENSOR HISTIDINE KINASE PDTAS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: GAF AND PAS DOMAINS, RESIDUES 1-303;
COMPND 5 SYNONYM: PDTAS;
COMPND 6 EC: 2.7.13.3;
COMPND 7 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: CC1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM11RV3320CN-TERM
KEYWDS TRANSFERASE, TWO-COMPONENT SYSTEM, GAF DOMAIN, PAS DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PREU,S.PANJIKAR,P.MORTH,R.JAISWAL,P.KARUNAKAR,P.A.TUCKER
REVDAT 4 20-DEC-23 2YKH 1 REMARK
REVDAT 3 17-JUL-19 2YKH 1 REMARK
REVDAT 2 27-JUN-12 2YKH 1 JRNL
REVDAT 1 06-JUN-12 2YKH 0
JRNL AUTH J.PREU,S.PANJIKAR,P.MORTH,R.JAISWAL,P.KARUNAKAR,P.A.TUCKER
JRNL TITL THE SENSOR REGION OF THE UBIQUITOUS CYTOSOLIC SENSOR KINASE,
JRNL TITL 2 PDTAS, CONTAINS PAS AND GAF DOMAIN SENSING MODULES.
JRNL REF J.STRUCT.BIOL. V. 177 498 2012
JRNL REFN ISSN 1047-8477
JRNL PMID 22115998
JRNL DOI 10.1016/J.JSB.2011.11.012
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 14178
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) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.200
REMARK 3 FREE R VALUE TEST SET COUNT : 932
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) : 2.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 855
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3971
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.457
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.349
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.880
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.826
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4045 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5515 ; 1.412 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 528 ; 8.131 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;35.018 ;22.832
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 628 ;19.071 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;19.343 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 661 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3068 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2629 ; 0.781 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4223 ; 1.449 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1416 ; 1.333 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1291 ; 2.409 ; 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 : 1
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 1 A 286 2
REMARK 3 1 B 1 B 286 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1053 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1053 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 914 ; 0.05 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 914 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1053 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1053 ; 0.09 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 914 ; 0.11 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 914 ; 0.11 ; 2.00
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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 2YKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1290048454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8501
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR555 FLAT PANEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15488
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: PDB ENTRY 2YKF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 36.46000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.31650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.76750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.31650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.46000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.76750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 GLY A 89
REMARK 465 GLY A 90
REMARK 465 VAL A 91
REMARK 465 PRO A 92
REMARK 465 GLY A 93
REMARK 465 ARG A 94
REMARK 465 GLU A 95
REMARK 465 GLY A 96
REMARK 465 ALA A 97
REMARK 465 VAL A 98
REMARK 465 GLY A 99
REMARK 465 GLN A 100
REMARK 465 GLN A 101
REMARK 465 ASN A 102
REMARK 465 SER A 103
REMARK 465 CYS A 104
REMARK 465 GLN A 105
REMARK 465 HIS A 106
REMARK 465 ASP A 107
REMARK 465 GLY A 108
REMARK 465 ARG A 287
REMARK 465 ASP A 288
REMARK 465 ARG A 289
REMARK 465 ALA A 290
REMARK 465 LEU A 291
REMARK 465 ILE A 292
REMARK 465 SER A 293
REMARK 465 LYS A 294
REMARK 465 ASP A 295
REMARK 465 ALA A 296
REMARK 465 THR A 297
REMARK 465 ILE A 298
REMARK 465 ARG A 299
REMARK 465 GLU A 300
REMARK 465 ILE A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 GLY B 89
REMARK 465 GLY B 90
REMARK 465 VAL B 91
REMARK 465 PRO B 92
REMARK 465 GLY B 93
REMARK 465 ARG B 94
REMARK 465 GLU B 95
REMARK 465 GLY B 96
REMARK 465 ALA B 97
REMARK 465 VAL B 98
REMARK 465 GLY B 99
REMARK 465 GLN B 100
REMARK 465 GLN B 101
REMARK 465 ASN B 102
REMARK 465 SER B 103
REMARK 465 CYS B 104
REMARK 465 GLN B 105
REMARK 465 HIS B 106
REMARK 465 ASP B 107
REMARK 465 GLY B 108
REMARK 465 ARG B 287
REMARK 465 ASP B 288
REMARK 465 ARG B 289
REMARK 465 ALA B 290
REMARK 465 LEU B 291
REMARK 465 ILE B 292
REMARK 465 SER B 293
REMARK 465 LYS B 294
REMARK 465 ASP B 295
REMARK 465 ALA B 296
REMARK 465 THR B 297
REMARK 465 ILE B 298
REMARK 465 ARG B 299
REMARK 465 GLU B 300
REMARK 465 ILE B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
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 SER A 88 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASN A 60 O HOH A 2004 2.13
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 PRO A 163 C - N - CD ANGL. DEV. = -14.2 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 ASP A 48 -19.17 -42.51
REMARK 500 PRO A 131 157.64 -49.06
REMARK 500 PRO A 163 175.80 -24.73
REMARK 500 ASP A 164 -179.30 145.11
REMARK 500 ALA A 165 120.15 -19.00
REMARK 500 ASP A 167 63.07 -162.42
REMARK 500 MET A 170 -19.81 68.35
REMARK 500 SER A 171 142.33 -170.06
REMARK 500 LYS A 285 57.16 -100.41
REMARK 500 ASP B 48 -30.90 -30.31
REMARK 500 PRO B 163 -167.51 -66.57
REMARK 500 ASP B 164 -141.79 -167.80
REMARK 500 ALA B 165 115.74 -19.98
REMARK 500 ASP B 167 60.73 -162.91
REMARK 500 MET B 170 -17.73 65.87
REMARK 500 SER B 171 138.09 -172.14
REMARK 500 SER B 174 142.75 -34.17
REMARK 500 THR B 208 -159.85 -97.47
REMARK 500 LYS B 285 58.10 -100.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 162 PRO A 163 -85.35
REMARK 500 PRO A 163 ASP A 164 -66.92
REMARK 500 PRO B 163 ASP B 164 -141.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YKF RELATED DB: PDB
REMARK 900 SENSOR REGION OF A SENSOR HISTIDINE KINASE
DBREF 2YKH A 1 303 UNP O05846 PDTAS_MYCTU 1 303
DBREF 2YKH B 1 303 UNP O05846 PDTAS_MYCTU 1 303
SEQADV 2YKH GLY A -1 UNP O05846 EXPRESSION TAG
SEQADV 2YKH ALA A 0 UNP O05846 EXPRESSION TAG
SEQADV 2YKH GLY B -1 UNP O05846 EXPRESSION TAG
SEQADV 2YKH ALA B 0 UNP O05846 EXPRESSION TAG
SEQRES 1 A 305 GLY ALA MET SER THR LEU GLY ASP LEU LEU ALA GLU HIS
SEQRES 2 A 305 THR VAL LEU PRO GLY SER ALA VAL ASP HIS LEU HIS ALA
SEQRES 3 A 305 VAL VAL GLY GLU TRP GLN LEU LEU ALA ASP LEU SER PHE
SEQRES 4 A 305 ALA ASP TYR LEU MET TRP VAL ARG ARG ASP ASP GLY VAL
SEQRES 5 A 305 LEU VAL CYS VAL ALA GLN CYS ARG PRO ASN THR GLY PRO
SEQRES 6 A 305 THR VAL VAL HIS THR ASP ALA VAL GLY THR VAL VAL ALA
SEQRES 7 A 305 ALA ASN SER MET PRO LEU VAL ALA ALA THR PHE SER GLY
SEQRES 8 A 305 GLY VAL PRO GLY ARG GLU GLY ALA VAL GLY GLN GLN ASN
SEQRES 9 A 305 SER CYS GLN HIS ASP GLY HIS SER VAL GLU VAL SER PRO
SEQRES 10 A 305 VAL ARG PHE GLY ASP GLN VAL VAL ALA VAL LEU THR ARG
SEQRES 11 A 305 HIS GLN PRO GLU LEU ALA ALA ARG ARG ARG SER GLY HIS
SEQRES 12 A 305 LEU GLU THR ALA TYR ARG LEU CYS ALA THR ASP LEU LEU
SEQRES 13 A 305 ARG MET LEU ALA GLU GLY THR PHE PRO ASP ALA GLY ASP
SEQRES 14 A 305 VAL ALA MET SER ARG SER SER PRO ARG ALA GLY ASP GLY
SEQRES 15 A 305 PHE ILE ARG LEU ASP VAL ASP GLY VAL VAL SER TYR ALA
SEQRES 16 A 305 SER PRO ASN ALA LEU SER ALA TYR HIS ARG MET GLY LEU
SEQRES 17 A 305 THR THR GLU LEU GLU GLY VAL ASN LEU ILE ASP ALA THR
SEQRES 18 A 305 ARG PRO LEU ILE SER ASP PRO PHE GLU ALA HIS GLU VAL
SEQRES 19 A 305 ASP GLU HIS VAL GLN ASP LEU LEU ALA GLY ASP GLY LYS
SEQRES 20 A 305 GLY MET ARG MET GLU VAL ASP ALA GLY GLY ALA THR VAL
SEQRES 21 A 305 LEU LEU ARG THR LEU PRO LEU VAL VAL ALA GLY ARG ASN
SEQRES 22 A 305 VAL GLY ALA ALA ILE LEU ILE ARG ASP VAL THR GLU VAL
SEQRES 23 A 305 LYS ARG ARG ASP ARG ALA LEU ILE SER LYS ASP ALA THR
SEQRES 24 A 305 ILE ARG GLU ILE HIS HIS
SEQRES 1 B 305 GLY ALA MET SER THR LEU GLY ASP LEU LEU ALA GLU HIS
SEQRES 2 B 305 THR VAL LEU PRO GLY SER ALA VAL ASP HIS LEU HIS ALA
SEQRES 3 B 305 VAL VAL GLY GLU TRP GLN LEU LEU ALA ASP LEU SER PHE
SEQRES 4 B 305 ALA ASP TYR LEU MET TRP VAL ARG ARG ASP ASP GLY VAL
SEQRES 5 B 305 LEU VAL CYS VAL ALA GLN CYS ARG PRO ASN THR GLY PRO
SEQRES 6 B 305 THR VAL VAL HIS THR ASP ALA VAL GLY THR VAL VAL ALA
SEQRES 7 B 305 ALA ASN SER MET PRO LEU VAL ALA ALA THR PHE SER GLY
SEQRES 8 B 305 GLY VAL PRO GLY ARG GLU GLY ALA VAL GLY GLN GLN ASN
SEQRES 9 B 305 SER CYS GLN HIS ASP GLY HIS SER VAL GLU VAL SER PRO
SEQRES 10 B 305 VAL ARG PHE GLY ASP GLN VAL VAL ALA VAL LEU THR ARG
SEQRES 11 B 305 HIS GLN PRO GLU LEU ALA ALA ARG ARG ARG SER GLY HIS
SEQRES 12 B 305 LEU GLU THR ALA TYR ARG LEU CYS ALA THR ASP LEU LEU
SEQRES 13 B 305 ARG MET LEU ALA GLU GLY THR PHE PRO ASP ALA GLY ASP
SEQRES 14 B 305 VAL ALA MET SER ARG SER SER PRO ARG ALA GLY ASP GLY
SEQRES 15 B 305 PHE ILE ARG LEU ASP VAL ASP GLY VAL VAL SER TYR ALA
SEQRES 16 B 305 SER PRO ASN ALA LEU SER ALA TYR HIS ARG MET GLY LEU
SEQRES 17 B 305 THR THR GLU LEU GLU GLY VAL ASN LEU ILE ASP ALA THR
SEQRES 18 B 305 ARG PRO LEU ILE SER ASP PRO PHE GLU ALA HIS GLU VAL
SEQRES 19 B 305 ASP GLU HIS VAL GLN ASP LEU LEU ALA GLY ASP GLY LYS
SEQRES 20 B 305 GLY MET ARG MET GLU VAL ASP ALA GLY GLY ALA THR VAL
SEQRES 21 B 305 LEU LEU ARG THR LEU PRO LEU VAL VAL ALA GLY ARG ASN
SEQRES 22 B 305 VAL GLY ALA ALA ILE LEU ILE ARG ASP VAL THR GLU VAL
SEQRES 23 B 305 LYS ARG ARG ASP ARG ALA LEU ILE SER LYS ASP ALA THR
SEQRES 24 B 305 ILE ARG GLU ILE HIS HIS
FORMUL 3 HOH *57(H2 O)
HELIX 1 1 THR A 3 THR A 12 1 10
HELIX 2 2 PRO A 15 TRP A 29 1 15
HELIX 3 3 TRP A 29 PHE A 37 1 9
HELIX 4 4 ALA A 76 SER A 79 5 4
HELIX 5 5 MET A 80 PHE A 87 1 8
HELIX 6 6 GLU A 132 ARG A 136 5 5
HELIX 7 7 GLY A 140 GLU A 159 1 20
HELIX 8 8 ARG A 176 ASP A 179 5 4
HELIX 9 9 SER A 194 MET A 204 1 11
HELIX 10 10 ASN A 214 ARG A 220 1 7
HELIX 11 11 ASP A 225 LEU A 240 1 16
HELIX 12 12 THR B 3 THR B 12 1 10
HELIX 13 13 PRO B 15 TRP B 29 1 15
HELIX 14 14 TRP B 29 PHE B 37 1 9
HELIX 15 15 ALA B 76 SER B 79 5 4
HELIX 16 16 MET B 80 SER B 88 1 9
HELIX 17 17 GLU B 132 ARG B 136 5 5
HELIX 18 18 GLY B 140 GLU B 159 1 20
HELIX 19 19 ARG B 176 ASP B 179 5 4
HELIX 20 20 SER B 194 GLY B 205 1 12
HELIX 21 21 ASN B 214 ARG B 220 1 7
HELIX 22 22 ASP B 225 LEU B 240 1 16
SHEET 1 AA 5 VAL A 74 VAL A 75 0
SHEET 2 AA 5 LEU A 51 CYS A 57 -1 O LEU A 51 N VAL A 75
SHEET 3 AA 5 ASP A 39 ARG A 45 -1 O TYR A 40 N CYS A 57
SHEET 4 AA 5 GLN A 121 GLN A 130 -1 O VAL A 125 N TRP A 43
SHEET 5 AA 5 SER A 110 PHE A 118 -1 O SER A 110 N GLN A 130
SHEET 1 AB 5 VAL A 190 ALA A 193 0
SHEET 2 AB 5 PHE A 181 LEU A 184 -1 O ARG A 183 N SER A 191
SHEET 3 AB 5 ARG A 270 ASP A 280 -1 O ALA A 274 N LEU A 184
SHEET 4 AB 5 ALA A 256 VAL A 267 -1 O LEU A 259 N ARG A 279
SHEET 5 AB 5 ARG A 248 ALA A 253 -1 O MET A 249 N LEU A 260
SHEET 1 BA 5 VAL B 74 VAL B 75 0
SHEET 2 BA 5 LEU B 51 CYS B 57 -1 O LEU B 51 N VAL B 75
SHEET 3 BA 5 ASP B 39 ARG B 45 -1 O TYR B 40 N CYS B 57
SHEET 4 BA 5 GLN B 121 GLN B 130 -1 O VAL B 125 N TRP B 43
SHEET 5 BA 5 SER B 110 PHE B 118 -1 O SER B 110 N GLN B 130
SHEET 1 BB 5 VAL B 190 ALA B 193 0
SHEET 2 BB 5 PHE B 181 LEU B 184 -1 O ARG B 183 N SER B 191
SHEET 3 BB 5 ARG B 270 ASP B 280 -1 O ALA B 274 N LEU B 184
SHEET 4 BB 5 ALA B 256 VAL B 267 -1 O LEU B 259 N ARG B 279
SHEET 5 BB 5 ARG B 248 ALA B 253 -1 O MET B 249 N LEU B 260
CISPEP 1 PHE B 162 PRO B 163 0 -27.06
CRYST1 72.920 79.535 102.633 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 0.013714 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009743 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
