HEADER TRANSCRIPTION 25-MAR-15 4UHS
TITLE CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF CPXR FROM E. COLI
TITLE 2 (TETRAGONAL FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATORY PROTEIN CPXR;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 1-123;
COMPND 5 SYNONYM: CPXR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLI5
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.MECHALY,P.M.A.ALZARI
REVDAT 4 10-JAN-24 4UHS 1 REMARK LINK
REVDAT 3 24-OCT-18 4UHS 1 JRNL
REVDAT 2 12-SEP-18 4UHS 1 JRNL
REVDAT 1 13-APR-16 4UHS 0
JRNL AUTH A.E.MECHALY,A.HAOUZ,N.SASSOON,A.BUSCHIAZZO,J.M.BETTON,
JRNL AUTH 2 P.M.ALZARI
JRNL TITL CONFORMATIONAL PLASTICITY OF THE RESPONSE REGULATOR CPXR, A
JRNL TITL 2 KEY PLAYER IN GAMMAPROTEOBACTERIA VIRULENCE AND
JRNL TITL 3 DRUG-RESISTANCE.
JRNL REF J. STRUCT. BIOL. V. 204 165 2018
JRNL REFN ESSN 1095-8657
JRNL PMID 30086390
JRNL DOI 10.1016/J.JSB.2018.08.001
REMARK 2
REMARK 2 RESOLUTION. 5.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 5453
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) : 0.261
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.490
REMARK 3 FREE R VALUE TEST SET COUNT : 245
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 5.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 5.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1499
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2807
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1433
REMARK 3 BIN R VALUE (WORKING SET) : 0.2833
REMARK 3 BIN FREE R VALUE : 0.2158
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 66
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 256.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 260.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -57.29820
REMARK 3 B22 (A**2) : -57.29820
REMARK 3 B33 (A**2) : 114.59640
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.993
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.890
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3033 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4095 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1500 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 93 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 423 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3033 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 396 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3359 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.24
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.01
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7808 45.7760 -17.3118
REMARK 3 T TENSOR
REMARK 3 T11: -0.9469 T22: 0.9471
REMARK 3 T33: 0.1659 T12: 0.5667
REMARK 3 T13: -0.4775 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 7.3429 L22: 7.6373
REMARK 3 L33: 29.0412 L12: 5.1467
REMARK 3 L13: 0.0002 L23: -9.4629
REMARK 3 S TENSOR
REMARK 3 S11: 0.5207 S12: 1.0333 S13: -1.5422
REMARK 3 S21: 0.3091 S22: -0.6108 S23: -0.5274
REMARK 3 S31: -0.8015 S32: -1.0364 S33: 0.0901
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6939 60.7168 -7.9931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2945 T22: 1.2160
REMARK 3 T33: -0.8488 T12: 0.6080
REMARK 3 T13: -0.0547 T23: -0.1742
REMARK 3 L TENSOR
REMARK 3 L11: 30.3962 L22: 23.2622
REMARK 3 L33: 33.2617 L12: 9.8079
REMARK 3 L13: 11.2347 L23: 4.8304
REMARK 3 S TENSOR
REMARK 3 S11: 0.3287 S12: -1.1585 S13: 1.4798
REMARK 3 S21: -0.5007 S22: 1.2133 S23: 1.6435
REMARK 3 S31: -0.9798 S32: -1.8219 S33: -1.5420
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8751 48.1813 -37.8843
REMARK 3 T TENSOR
REMARK 3 T11: -0.2233 T22: 1.2160
REMARK 3 T33: -0.2846 T12: 0.0948
REMARK 3 T13: -0.2186 T23: 0.5757
REMARK 3 L TENSOR
REMARK 3 L11: 6.5697 L22: 17.3435
REMARK 3 L33: 22.9209 L12: -1.3965
REMARK 3 L13: 11.4230 L23: 3.2590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: -0.0504 S13: -0.7150
REMARK 3 S21: -0.1612 S22: 1.2251 S23: 1.4182
REMARK 3 S31: -0.0137 S32: -1.2281 S33: -1.2873
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4UHS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063463.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5469
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4UHJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 57.11100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 57.11100
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 178.36700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 89.18350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 57.11100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 267.55050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 267.55050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.11100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 89.18350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 57.11100
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 178.36700
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 57.11100
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 178.36700
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 57.11100
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 267.55050
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 89.18350
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 57.11100
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 89.18350
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 267.55050
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 57.11100
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 57.11100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 178.36700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
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: 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 MET A 1
REMARK 465 ALA A 128
REMARK 465 LEU A 129
REMARK 465 GLU A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 MET B 1
REMARK 465 ALA B 128
REMARK 465 LEU B 129
REMARK 465 GLU B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 HIS B 133
REMARK 465 HIS B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 MET C 1
REMARK 465 ALA C 128
REMARK 465 LEU C 129
REMARK 465 GLU C 130
REMARK 465 HIS C 131
REMARK 465 HIS C 132
REMARK 465 HIS C 133
REMARK 465 HIS C 134
REMARK 465 HIS C 135
REMARK 465 HIS C 136
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 84 CB LEU A 84 CG -0.214
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 VAL A 52 -69.28 -104.20
REMARK 500 LYS A 56 -58.12 70.84
REMARK 500 LYS B 56 -59.37 72.05
REMARK 500 LYS C 56 -58.85 71.50
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 B1128 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 51 OD1
REMARK 620 2 ASP B 51 OD2 45.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1128
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UHJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF CPXR FROM E. COLI
REMARK 900 (ORTHORHOMBIC FORM)
REMARK 900 RELATED ID: 4UHK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF CPXR FROM E. COLI
REMARK 900 (PHOSPHORYLATED)
REMARK 900 RELATED ID: 4UHT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF CPXR FROM E. COLI
DBREF 4UHS A 1 123 UNP P0AE88 CPXR_ECOLI 1 123
DBREF 4UHS B 1 123 UNP P0AE88 CPXR_ECOLI 1 123
DBREF 4UHS C 1 123 UNP P0AE88 CPXR_ECOLI 1 123
SEQADV 4UHS LYS A 124 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU A 125 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA A 126 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA A 127 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA A 128 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU A 129 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS GLU A 130 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 131 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 132 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 133 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 134 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 135 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS A 136 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LYS B 124 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU B 125 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA B 126 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA B 127 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA B 128 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU B 129 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS GLU B 130 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 131 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 132 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 133 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 134 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 135 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS B 136 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LYS C 124 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU C 125 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA C 126 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA C 127 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS ALA C 128 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS LEU C 129 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS GLU C 130 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 131 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 132 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 133 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 134 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 135 UNP P0AE88 EXPRESSION TAG
SEQADV 4UHS HIS C 136 UNP P0AE88 EXPRESSION TAG
SEQRES 1 A 136 MET ASN LYS ILE LEU LEU VAL ASP ASP ASP ARG GLU LEU
SEQRES 2 A 136 THR SER LEU LEU LYS GLU LEU LEU GLU MET GLU GLY PHE
SEQRES 3 A 136 ASN VAL ILE VAL ALA HIS ASP GLY GLU GLN ALA LEU ASP
SEQRES 4 A 136 LEU LEU ASP ASP SER ILE ASP LEU LEU LEU LEU ASP VAL
SEQRES 5 A 136 MET MET PRO LYS LYS ASN GLY ILE ASP THR LEU LYS ALA
SEQRES 6 A 136 LEU ARG GLN THR HIS GLN THR PRO VAL ILE MET LEU THR
SEQRES 7 A 136 ALA ARG GLY SER GLU LEU ASP ARG VAL LEU GLY LEU GLU
SEQRES 8 A 136 LEU GLY ALA ASP ASP TYR LEU PRO LYS PRO PHE ASN ASP
SEQRES 9 A 136 ARG GLU LEU VAL ALA ARG ILE ARG ALA ILE LEU ARG ARG
SEQRES 10 A 136 SER HIS TRP SER GLU GLN LYS LEU ALA ALA ALA LEU GLU
SEQRES 11 A 136 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 136 MET ASN LYS ILE LEU LEU VAL ASP ASP ASP ARG GLU LEU
SEQRES 2 B 136 THR SER LEU LEU LYS GLU LEU LEU GLU MET GLU GLY PHE
SEQRES 3 B 136 ASN VAL ILE VAL ALA HIS ASP GLY GLU GLN ALA LEU ASP
SEQRES 4 B 136 LEU LEU ASP ASP SER ILE ASP LEU LEU LEU LEU ASP VAL
SEQRES 5 B 136 MET MET PRO LYS LYS ASN GLY ILE ASP THR LEU LYS ALA
SEQRES 6 B 136 LEU ARG GLN THR HIS GLN THR PRO VAL ILE MET LEU THR
SEQRES 7 B 136 ALA ARG GLY SER GLU LEU ASP ARG VAL LEU GLY LEU GLU
SEQRES 8 B 136 LEU GLY ALA ASP ASP TYR LEU PRO LYS PRO PHE ASN ASP
SEQRES 9 B 136 ARG GLU LEU VAL ALA ARG ILE ARG ALA ILE LEU ARG ARG
SEQRES 10 B 136 SER HIS TRP SER GLU GLN LYS LEU ALA ALA ALA LEU GLU
SEQRES 11 B 136 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 136 MET ASN LYS ILE LEU LEU VAL ASP ASP ASP ARG GLU LEU
SEQRES 2 C 136 THR SER LEU LEU LYS GLU LEU LEU GLU MET GLU GLY PHE
SEQRES 3 C 136 ASN VAL ILE VAL ALA HIS ASP GLY GLU GLN ALA LEU ASP
SEQRES 4 C 136 LEU LEU ASP ASP SER ILE ASP LEU LEU LEU LEU ASP VAL
SEQRES 5 C 136 MET MET PRO LYS LYS ASN GLY ILE ASP THR LEU LYS ALA
SEQRES 6 C 136 LEU ARG GLN THR HIS GLN THR PRO VAL ILE MET LEU THR
SEQRES 7 C 136 ALA ARG GLY SER GLU LEU ASP ARG VAL LEU GLY LEU GLU
SEQRES 8 C 136 LEU GLY ALA ASP ASP TYR LEU PRO LYS PRO PHE ASN ASP
SEQRES 9 C 136 ARG GLU LEU VAL ALA ARG ILE ARG ALA ILE LEU ARG ARG
SEQRES 10 C 136 SER HIS TRP SER GLU GLN LYS LEU ALA ALA ALA LEU GLU
SEQRES 11 C 136 HIS HIS HIS HIS HIS HIS
HET MG A1128 1
HET MG B1128 1
HET MG C1128 1
HETNAM MG MAGNESIUM ION
FORMUL 4 MG 3(MG 2+)
HELIX 1 1 ASP A 10 GLU A 24 1 15
HELIX 2 2 ASP A 33 LEU A 41 1 9
HELIX 3 3 ASN A 58 ARG A 67 1 10
HELIX 4 4 SER A 82 LEU A 92 1 11
HELIX 5 5 ASN A 103 ALA A 127 1 25
HELIX 6 6 ASP B 10 GLU B 24 1 15
HELIX 7 7 ASP B 33 LEU B 41 1 9
HELIX 8 8 ASN B 58 ARG B 67 1 10
HELIX 9 9 SER B 82 LEU B 92 1 11
HELIX 10 10 ASN B 103 ALA B 127 1 25
HELIX 11 11 ASP C 10 GLU C 24 1 15
HELIX 12 12 ASP C 33 LEU C 41 1 9
HELIX 13 13 ASN C 58 ARG C 67 1 10
HELIX 14 14 SER C 82 LEU C 92 1 11
HELIX 15 15 ASN C 103 ALA C 127 1 25
SHEET 1 AA 5 ASN A 27 ALA A 31 0
SHEET 2 AA 5 LYS A 3 VAL A 7 1 O ILE A 4 N ILE A 29
SHEET 3 AA 5 LEU A 47 LEU A 50 1 O LEU A 47 N LEU A 5
SHEET 4 AA 5 VAL A 74 THR A 78 1 O ILE A 75 N LEU A 50
SHEET 5 AA 5 ASP A 96 PRO A 99 1 O ASP A 96 N MET A 76
SHEET 1 BA 5 ASN B 27 ALA B 31 0
SHEET 2 BA 5 LYS B 3 VAL B 7 1 O ILE B 4 N ILE B 29
SHEET 3 BA 5 LEU B 47 ASP B 51 1 O LEU B 47 N LEU B 5
SHEET 4 BA 5 VAL B 74 THR B 78 1 O ILE B 75 N LEU B 50
SHEET 5 BA 5 ASP B 96 PRO B 99 1 O ASP B 96 N MET B 76
SHEET 1 CA 5 ASN C 27 ALA C 31 0
SHEET 2 CA 5 LYS C 3 VAL C 7 1 O ILE C 4 N ILE C 29
SHEET 3 CA 5 LEU C 47 ASP C 51 1 O LEU C 47 N LEU C 5
SHEET 4 CA 5 VAL C 74 THR C 78 1 O ILE C 75 N LEU C 50
SHEET 5 CA 5 ASP C 96 PRO C 99 1 O ASP C 96 N MET C 76
LINK OD2 ASP A 51 MG MG A1128 1555 1555 2.97
LINK OD1 ASP B 51 MG MG B1128 1555 1555 2.88
LINK OD2 ASP B 51 MG MG B1128 1555 1555 2.82
LINK OD1 ASP C 51 MG MG C1128 1555 1555 2.14
CISPEP 1 LYS A 100 PRO A 101 0 -2.81
CISPEP 2 LYS B 100 PRO B 101 0 1.87
CISPEP 3 LYS C 100 PRO C 101 0 -2.55
SITE 1 AC1 1 ASP A 51
SITE 1 AC2 3 ASP B 51 MET B 53 LYS B 100
SITE 1 AC3 4 ASP C 51 MET C 53 ALA C 79 LYS C 100
CRYST1 114.222 114.222 356.734 90.00 90.00 90.00 I 41 2 2 48
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 0.008755 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END