HEADER TRANSCRIPTION 08-MAY-08 2VT3
TITLE STRUCTURE AND FUNCTIONAL PROPERTIES OF THE BACILLUS SUBTILIS
TITLE 2 TRANSCRIPTIONAL REPRESSOR REX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REDOX-SENSING TRANSCRIPTIONAL REPRESSOR REX;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: REX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: 1A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: TUNER;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET101
KEYWDS TRANSCRIPTIONAL REGULATION, REDOX POISE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.WANG,M.C.BAUER,A.ROGSTAM,S.LINSE,D.LOGAN,C.VON WACHENFELDT
REVDAT 5 13-DEC-23 2VT3 1 REMARK
REVDAT 4 17-JAN-18 2VT3 1 SOURCE JRNL REMARK
REVDAT 3 13-JUL-11 2VT3 1 VERSN
REVDAT 2 24-FEB-09 2VT3 1 VERSN
REVDAT 1 09-SEP-08 2VT3 0
JRNL AUTH E.WANG,M.C.BAUER,A.ROGSTAM,S.LINSE,D.T.LOGAN,
JRNL AUTH 2 C.VON WACHENFELDT
JRNL TITL STRUCTURE AND FUNCTIONAL PROPERTIES OF THE BACILLUS SUBTILIS
JRNL TITL 2 TRANSCRIPTIONAL REPRESSOR REX.
JRNL REF MOL. MICROBIOL. V. 69 466 2008
JRNL REFN ESSN 1365-2958
JRNL PMID 18485070
JRNL DOI 10.1111/J.1365-2958.2008.06295.X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 30388
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1605
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2008
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3101
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 1.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.383
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3237 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2135 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4398 ; 1.554 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5208 ; 0.952 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 390 ; 7.469 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;39.372 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 546 ;16.461 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.990 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 508 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3523 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 666 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 637 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2089 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1530 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1680 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 0.173 ; 0.200
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): 17 ; 0.223 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 84 ; 0.274 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.182 ; 0.200
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): 2537 ; 0.982 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 799 ; 0.184 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3152 ; 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): 1491 ; 1.973 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1246 ; 2.714 ; 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 : 4
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 11 A 83
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4360 45.7910 -18.1260
REMARK 3 T TENSOR
REMARK 3 T11: -0.1401 T22: -0.1221
REMARK 3 T33: 0.0379 T12: -0.0112
REMARK 3 T13: -0.1156 T23: 0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 8.6716 L22: 12.6522
REMARK 3 L33: 8.1851 L12: -1.0663
REMARK 3 L13: 2.1006 L23: -7.6646
REMARK 3 S TENSOR
REMARK 3 S11: -0.4234 S12: 0.2443 S13: 1.3988
REMARK 3 S21: -0.0037 S22: -0.0252 S23: -0.1578
REMARK 3 S31: -0.2614 S32: 0.1391 S33: 0.4485
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 : A 87 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8540 20.9030 -27.4560
REMARK 3 T TENSOR
REMARK 3 T11: -0.0856 T22: -0.0674
REMARK 3 T33: -0.0763 T12: -0.0134
REMARK 3 T13: -0.0046 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 1.7767 L22: 1.3760
REMARK 3 L33: 3.6418 L12: -0.4866
REMARK 3 L13: 1.4515 L23: -0.3079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: 0.1413 S13: -0.0932
REMARK 3 S21: -0.1394 S22: -0.0212 S23: 0.0744
REMARK 3 S31: 0.0127 S32: -0.0005 S33: 0.0166
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 : B 7 B 85
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1030 1.6910 -0.1130
REMARK 3 T TENSOR
REMARK 3 T11: -0.0851 T22: -0.0254
REMARK 3 T33: -0.0823 T12: 0.0252
REMARK 3 T13: -0.0526 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 3.1542 L22: 1.6834
REMARK 3 L33: 2.4909 L12: 0.5898
REMARK 3 L13: -0.1589 L23: 0.0285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: 0.1270 S13: 0.1003
REMARK 3 S21: -0.0348 S22: 0.0358 S23: 0.2855
REMARK 3 S31: -0.1058 S32: -0.0586 S33: -0.0299
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 86 B 214
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3010 7.0880 -13.4540
REMARK 3 T TENSOR
REMARK 3 T11: -0.1016 T22: -0.1170
REMARK 3 T33: 0.0524 T12: -0.0162
REMARK 3 T13: -0.0129 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.6532 L22: 3.4068
REMARK 3 L33: 1.6477 L12: -1.0090
REMARK 3 L13: -0.2773 L23: 0.3473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0451 S12: -0.0014 S13: -0.3021
REMARK 3 S21: 0.1177 S22: 0.0683 S23: 0.0725
REMARK 3 S31: 0.1865 S32: 0.0485 S33: -0.0232
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2VT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1290036137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : OXFORD DANFYSIK DOUBLE CRYSTAL
REMARK 200 OPTICS : FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31994
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1XCB CHAIN F, C-TERMINAL DOMAIN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOAR SOLUTION OF 20% W/V PEG6000,
REMARK 280 0.2M NH4CL AND 0.1M HEPES PH 7.1
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 64.23000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.76000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.23000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.76000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 ASP A 4
REMARK 465 GLN A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ILE A 8
REMARK 465 PRO A 9
REMARK 465 GLN A 10
REMARK 465 GLY A 61
REMARK 465 LYS A 62
REMARK 465 LYS A 63
REMARK 465 GLY A 64
REMARK 465 TYR A 65
REMARK 465 GLU A 84
REMARK 465 MET A 85
REMARK 465 THR A 86
REMARK 465 PHE A 105
REMARK 465 THR A 106
REMARK 465 LYS A 107
REMARK 465 ASN A 108
REMARK 465 ASN A 109
REMARK 465 ASN A 110
REMARK 465 VAL A 210
REMARK 465 LEU A 211
REMARK 465 GLU A 212
REMARK 465 GLU A 213
REMARK 465 ILE A 214
REMARK 465 GLU A 215
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 GLN B 5
REMARK 465 SER B 6
REMARK 465 GLU B 215
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 OH TYR B 208 O HOH B 2124 2.08
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 ARG B 15 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 15 NE - CZ - NH2 ANGL. DEV. = -6.0 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 SER A 47 -59.31 -24.44
REMARK 500 VAL A 93 59.62 -94.20
REMARK 500 LYS A 144 -75.48 -129.40
REMARK 500 PHE A 176 61.28 -100.16
REMARK 500 ILE B 8 112.60 -34.84
REMARK 500 VAL B 45 -167.33 -126.23
REMARK 500 VAL B 93 60.29 -102.51
REMARK 500 LYS B 144 -84.53 -119.88
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 LYS B 7 ILE B 8 99.45
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 ATP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VT2 RELATED DB: PDB
REMARK 900 STRUCTURE AND FUNCTIONAL PROPERTIES OF THE BACILLUS SUBTILIS
REMARK 900 TRANSCRIPTIONAL REPRESSOR REX
DBREF 2VT3 A 1 215 UNP O05521 REX_BACSU 1 215
DBREF 2VT3 B 1 215 UNP O05521 REX_BACSU 1 215
SEQRES 1 A 215 MET ASN LYS ASP GLN SER LYS ILE PRO GLN ALA THR ALA
SEQRES 2 A 215 LYS ARG LEU PRO LEU TYR TYR ARG PHE LEU LYS ASN LEU
SEQRES 3 A 215 HIS ALA SER GLY LYS GLN ARG VAL SER SER ALA GLU LEU
SEQRES 4 A 215 SER ASP ALA VAL LYS VAL ASP SER ALA THR ILE ARG ARG
SEQRES 5 A 215 ASP PHE SER TYR PHE GLY ALA LEU GLY LYS LYS GLY TYR
SEQRES 6 A 215 GLY TYR ASN VAL ASP TYR LEU LEU SER PHE PHE ARG LYS
SEQRES 7 A 215 THR LEU ASP GLN ASP GLU MET THR ASP VAL ILE LEU ILE
SEQRES 8 A 215 GLY VAL GLY ASN LEU GLY THR ALA PHE LEU HIS TYR ASN
SEQRES 9 A 215 PHE THR LYS ASN ASN ASN THR LYS ILE SER MET ALA PHE
SEQRES 10 A 215 ASP ILE ASN GLU SER LYS ILE GLY THR GLU VAL GLY GLY
SEQRES 11 A 215 VAL PRO VAL TYR ASN LEU ASP ASP LEU GLU GLN HIS VAL
SEQRES 12 A 215 LYS ASP GLU SER VAL ALA ILE LEU THR VAL PRO ALA VAL
SEQRES 13 A 215 ALA ALA GLN SER ILE THR ASP ARG LEU VAL ALA LEU GLY
SEQRES 14 A 215 ILE LYS GLY ILE LEU ASN PHE THR PRO ALA ARG LEU ASN
SEQRES 15 A 215 VAL PRO GLU HIS ILE ARG ILE HIS HIS ILE ASP LEU ALA
SEQRES 16 A 215 VAL GLU LEU GLN SER LEU VAL TYR PHE LEU LYS HIS TYR
SEQRES 17 A 215 SER VAL LEU GLU GLU ILE GLU
SEQRES 1 B 215 MET ASN LYS ASP GLN SER LYS ILE PRO GLN ALA THR ALA
SEQRES 2 B 215 LYS ARG LEU PRO LEU TYR TYR ARG PHE LEU LYS ASN LEU
SEQRES 3 B 215 HIS ALA SER GLY LYS GLN ARG VAL SER SER ALA GLU LEU
SEQRES 4 B 215 SER ASP ALA VAL LYS VAL ASP SER ALA THR ILE ARG ARG
SEQRES 5 B 215 ASP PHE SER TYR PHE GLY ALA LEU GLY LYS LYS GLY TYR
SEQRES 6 B 215 GLY TYR ASN VAL ASP TYR LEU LEU SER PHE PHE ARG LYS
SEQRES 7 B 215 THR LEU ASP GLN ASP GLU MET THR ASP VAL ILE LEU ILE
SEQRES 8 B 215 GLY VAL GLY ASN LEU GLY THR ALA PHE LEU HIS TYR ASN
SEQRES 9 B 215 PHE THR LYS ASN ASN ASN THR LYS ILE SER MET ALA PHE
SEQRES 10 B 215 ASP ILE ASN GLU SER LYS ILE GLY THR GLU VAL GLY GLY
SEQRES 11 B 215 VAL PRO VAL TYR ASN LEU ASP ASP LEU GLU GLN HIS VAL
SEQRES 12 B 215 LYS ASP GLU SER VAL ALA ILE LEU THR VAL PRO ALA VAL
SEQRES 13 B 215 ALA ALA GLN SER ILE THR ASP ARG LEU VAL ALA LEU GLY
SEQRES 14 B 215 ILE LYS GLY ILE LEU ASN PHE THR PRO ALA ARG LEU ASN
SEQRES 15 B 215 VAL PRO GLU HIS ILE ARG ILE HIS HIS ILE ASP LEU ALA
SEQRES 16 B 215 VAL GLU LEU GLN SER LEU VAL TYR PHE LEU LYS HIS TYR
SEQRES 17 B 215 SER VAL LEU GLU GLU ILE GLU
HET ATP A 302 31
HET ATP B 302 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 5 HOH *224(H2 O)
HELIX 1 1 ALA A 11 SER A 29 1 19
HELIX 2 2 SER A 35 LYS A 44 1 10
HELIX 3 3 ASP A 46 PHE A 57 1 12
HELIX 4 4 VAL A 69 ASP A 83 1 15
HELIX 5 5 GLY A 94 TYR A 103 1 10
HELIX 6 6 ASP A 138 VAL A 143 1 6
HELIX 7 7 PRO A 154 LEU A 168 1 15
HELIX 8 8 ASP A 193 SER A 209 1 17
HELIX 9 9 PRO B 9 SER B 29 1 21
HELIX 10 10 SER B 35 LYS B 44 1 10
HELIX 11 11 ASP B 46 GLY B 58 1 13
HELIX 12 12 VAL B 69 MET B 85 1 17
HELIX 13 13 GLY B 94 HIS B 102 1 9
HELIX 14 14 ASP B 138 VAL B 143 1 6
HELIX 15 15 PRO B 154 LEU B 168 1 15
HELIX 16 16 ASP B 193 TYR B 208 1 16
SHEET 1 AA 2 ARG A 33 VAL A 34 0
SHEET 2 AA 2 TYR A 67 ASN A 68 -1 O TYR A 67 N VAL A 34
SHEET 1 AB 7 GLU A 127 VAL A 128 0
SHEET 2 AB 7 VAL A 131 ASN A 135 -1 O VAL A 131 N VAL A 128
SHEET 3 AB 7 ILE A 113 ASP A 118 1 O ALA A 116 N TYR A 134
SHEET 4 AB 7 VAL A 88 ILE A 91 1 O VAL A 88 N SER A 114
SHEET 5 AB 7 VAL A 148 LEU A 151 1 O VAL A 148 N ILE A 89
SHEET 6 AB 7 GLY A 172 ASN A 175 1 O GLY A 172 N ALA A 149
SHEET 7 AB 7 ARG A 188 HIS A 191 1 O ARG A 188 N ILE A 173
SHEET 1 BA 2 ARG B 33 VAL B 34 0
SHEET 2 BA 2 TYR B 67 ASN B 68 -1 O TYR B 67 N VAL B 34
SHEET 1 BB 7 GLU B 127 VAL B 128 0
SHEET 2 BB 7 VAL B 131 ASN B 135 -1 O VAL B 131 N VAL B 128
SHEET 3 BB 7 THR B 111 ASP B 118 1 O ALA B 116 N TYR B 134
SHEET 4 BB 7 THR B 86 ILE B 91 1 O THR B 86 N LYS B 112
SHEET 5 BB 7 VAL B 148 LEU B 151 1 O VAL B 148 N ILE B 89
SHEET 6 BB 7 GLY B 172 ASN B 175 1 O GLY B 172 N ALA B 149
SHEET 7 BB 7 ARG B 188 HIS B 191 1 O ARG B 188 N ILE B 173
SITE 1 AC1 18 GLY A 92 VAL A 93 GLY A 94 ASN A 95
SITE 2 AC1 18 ASP A 118 ILE A 119 LYS A 123 LEU A 136
SITE 3 AC1 18 VAL A 153 PRO A 154 ALA A 157 ILE A 161
SITE 4 AC1 18 HOH A2025 HOH A2031 HOH A2084 HOH A2085
SITE 5 AC1 18 HOH A2087 HOH A2088
SITE 1 AC2 18 LYS A 44 GLY B 92 VAL B 93 GLY B 94
SITE 2 AC2 18 ASN B 95 ASP B 118 ILE B 119 ASN B 120
SITE 3 AC2 18 LYS B 123 LEU B 136 THR B 152 PRO B 154
SITE 4 AC2 18 ALA B 157 ILE B 161 HOH B2133 HOH B2134
SITE 5 AC2 18 HOH B2135 HOH B2136
CRYST1 128.460 53.520 86.240 90.00 125.80 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 0.007785 0.000000 0.005614 0.00000
SCALE2 0.000000 0.018685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
