HEADER TRANSCRIPTION,SIGNALING PROTEIN 01-FEB-07 2OQR
TITLE THE STRUCTURE OF THE RESPONSE REGULATOR REGX3 FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SENSORY TRANSDUCTION PROTEIN REGX3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: REGX3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS RESPONSE REGULATOR, WINGED-HELIX-TURN-HELIX, DNA-BINDING, 3D DOMAIN
KEYWDS 2 SWAPPING, REGX3, TWO COMPONENT SYSTEM, TRANSCRIPTION, SIGNALING
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KING-SCOTT
REVDAT 7 27-DEC-23 2OQR 1 REMARK SEQADV SHEET
REVDAT 6 18-OCT-17 2OQR 1 REMARK
REVDAT 5 13-JUL-11 2OQR 1 VERSN
REVDAT 4 24-FEB-09 2OQR 1 VERSN
REVDAT 3 08-JAN-08 2OQR 1 JRNL
REVDAT 2 30-OCT-07 2OQR 1 JRNL
REVDAT 1 16-OCT-07 2OQR 0
JRNL AUTH J.KING-SCOTT,E.NOWAK,E.MYLONAS,S.PANJIKAR,M.ROESSLE,
JRNL AUTH 2 D.I.SVERGUN,P.A.TUCKER
JRNL TITL THE STRUCTURE OF A FULL-LENGTH RESPONSE REGULATOR FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS IN A STABILIZED THREE-DIMENSIONAL
JRNL TITL 3 DOMAIN-SWAPPED, ACTIVATED STATE.
JRNL REF J.BIOL.CHEM. V. 282 37717 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17942407
JRNL DOI 10.1074/JBC.M705081200
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21964
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1543
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1734
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 163
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.07000
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): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.159
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1797 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1216 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2402 ; 1.548 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2958 ; 1.069 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 227 ;10.934 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 77 ;37.649 ;23.117
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 316 ;17.145 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;19.926 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 285 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1975 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 348 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 358 ; 0.243 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1268 ; 0.199 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 864 ; 0.175 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1014 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 127 ; 0.175 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.171 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 25 ; 0.299 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 53 ; 0.265 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.177 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 3 ; 0.354 ; 0.200
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): 1175 ; 1.000 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 461 ; 0.174 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1820 ; 1.557 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 678 ; 4.168 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 581 ; 6.355 ;10.000
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 1 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3320 -45.4840 5.2280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1574 T22: -0.1582
REMARK 3 T33: -0.2214 T12: -0.0158
REMARK 3 T13: -0.0080 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 2.1180 L22: 2.3943
REMARK 3 L33: 1.5414 L12: 1.8843
REMARK 3 L13: 0.0215 L23: -0.4309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1184 S12: -0.2230 S13: -0.2580
REMARK 3 S21: 0.1870 S22: -0.1115 S23: -0.2729
REMARK 3 S31: 0.1384 S32: 0.0244 S33: -0.0069
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 108 A 171
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4320 -13.8110 17.4470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0422 T22: -0.1771
REMARK 3 T33: -0.2104 T12: -0.0405
REMARK 3 T13: 0.1045 T23: 0.0996
REMARK 3 L TENSOR
REMARK 3 L11: 2.7184 L22: 4.4049
REMARK 3 L33: 7.9870 L12: -1.3853
REMARK 3 L13: 1.7207 L23: -0.6038
REMARK 3 S TENSOR
REMARK 3 S11: -0.0873 S12: -0.5366 S13: -0.3085
REMARK 3 S21: 0.5978 S22: 0.2083 S23: 0.6891
REMARK 3 S31: -0.2211 S32: -0.3437 S33: -0.1210
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 : A 172 A 226
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6890 -2.3810 10.4800
REMARK 3 T TENSOR
REMARK 3 T11: -0.0386 T22: -0.2032
REMARK 3 T33: -0.0878 T12: 0.0066
REMARK 3 T13: 0.1205 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 2.4363 L22: 5.8518
REMARK 3 L33: 3.6483 L12: -0.8496
REMARK 3 L13: -0.0533 L23: -0.6006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: -0.2071 S13: 0.0110
REMARK 3 S21: 0.6582 S22: 0.2558 S23: 0.9124
REMARK 3 S31: -0.2609 S32: -0.2897 S33: -0.1910
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
REMARK 4
REMARK 4 2OQR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.813
REMARK 200 MONOCHROMATOR : SI [111], HORIZONTALLY FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 19.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : 0.66400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 2-4% PEG 4000,
REMARK 280 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 62.17550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.17550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.17550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.17550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.17550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.17550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.17550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.17550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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
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 BIOLOGICAL DIMER IS GENERATED FROM THE MONOMER IN THE
REMARK 300 ASYMMETRIC UNIT BY THE OPERATION: -X+1/2, Y+1/2, -Z.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 GLY A 227
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 O HOH A 549 O HOH A 550 1.88
REMARK 500 O HOH A 463 O HOH A 464 2.16
REMARK 500 O HOH A 457 O HOH A 458 2.17
REMARK 500 O HOH A 463 O HOH A 465 2.17
REMARK 500 O HOH A 421 O HOH A 422 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 141 LA LA A 304 8556 1.84
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 ASP A 86 CB - CG - OD1 ANGL. DEV. = 6.5 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 PRO A 102 130.78 -30.37
REMARK 500 ASN A 148 -73.97 68.35
REMARK 500 ILE A 152 -155.14 -53.19
REMARK 500 ALA A 210 -51.10 -165.61
REMARK 500 LEU A 221 -70.11 -123.18
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 A 101 PRO A 102 -50.25
REMARK 500 THR A 153 LEU A 154 146.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700 THE BIOLOGICAL MOLECULE IS A 3D-DOMAIN SWAPPED DIMER.
REMARK 700 IN THIS DIMER THE BETA-SHEET A IS IN FACT 5-STRANDED
REMARK 700 WITH THE FIFTH STRAND COMING FROM THE SECOND MOLECULE.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700 THE BETA-SHEET B IS IN FACT AN ANTI-PARALLEL 4-STRANDED
REMARK 700 BETA-SHEET. IN ORDER TO REPRESENT THIS FEATURE S4
REMARK 700 HAS BEEN DEFINED BELOW.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 401
DBREF 2OQR A 2 227 UNP Q11156 REGX3_MYCTU 2 227
SEQADV 2OQR GLY A -2 UNP Q11156 EXPRESSION TAG
SEQADV 2OQR ALA A -1 UNP Q11156 EXPRESSION TAG
SEQADV 2OQR MET A 0 UNP Q11156 EXPRESSION TAG
SEQADV 2OQR ALA A 1 UNP Q11156 EXPRESSION TAG
SEQRES 1 A 230 GLY ALA MET ALA THR SER VAL LEU ILE VAL GLU ASP GLU
SEQRES 2 A 230 GLU SER LEU ALA ASP PRO LEU ALA PHE LEU LEU ARG LYS
SEQRES 3 A 230 GLU GLY PHE GLU ALA THR VAL VAL THR ASP GLY PRO ALA
SEQRES 4 A 230 ALA LEU ALA GLU PHE ASP ARG ALA GLY ALA ASP ILE VAL
SEQRES 5 A 230 LEU LEU ASP LEU MET LEU PRO GLY MET SER GLY THR ASP
SEQRES 6 A 230 VAL CYS LYS GLN LEU ARG ALA ARG SER SER VAL PRO VAL
SEQRES 7 A 230 ILE MET VAL THR ALA ARG ASP SER GLU ILE ASP LYS VAL
SEQRES 8 A 230 VAL GLY LEU GLU LEU GLY ALA ASP ASP TYR VAL THR LYS
SEQRES 9 A 230 PRO TYR SER ALA ARG GLU LEU ILE ALA ARG ILE ARG ALA
SEQRES 10 A 230 VAL LEU ARG ARG GLY GLY ASP ASP ASP SER GLU MET SER
SEQRES 11 A 230 ASP GLY VAL LEU GLU SER GLY PRO VAL ARG MET ASP VAL
SEQRES 12 A 230 GLU ARG HIS VAL VAL SER VAL ASN GLY ASP THR ILE THR
SEQRES 13 A 230 LEU PRO LEU LYS GLU PHE ASP LEU LEU GLU TYR LEU MET
SEQRES 14 A 230 ARG ASN SER GLY ARG VAL LEU THR ARG GLY GLN LEU ILE
SEQRES 15 A 230 ASP ARG VAL TRP GLY ALA ASP TYR VAL GLY ASP THR LYS
SEQRES 16 A 230 THR LEU ASP VAL HIS VAL LYS ARG LEU ARG SER LYS ILE
SEQRES 17 A 230 GLU ALA ASP PRO ALA ASN PRO VAL HIS LEU VAL THR VAL
SEQRES 18 A 230 ARG GLY LEU GLY TYR LYS LEU GLU GLY
HET ACT A 228 4
HET ACT A 229 4
HET LA A 301 1
HET LA A 302 1
HET LA A 303 1
HET LA A 304 1
HET LA A 305 1
HET BME A 401 4
HETNAM ACT ACETATE ION
HETNAM LA LANTHANUM (III) ION
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 LA 5(LA 3+)
FORMUL 9 BME C2 H6 O S
FORMUL 10 HOH *163(H2 O)
HELIX 1 1 GLU A 10 GLU A 24 1 15
HELIX 2 2 ASP A 33 GLY A 45 1 13
HELIX 3 3 SER A 59 SER A 71 1 13
HELIX 4 4 ARG A 81 GLY A 94 1 14
HELIX 5 5 SER A 104 ARG A 117 1 14
HELIX 6 6 PRO A 155 ASN A 168 1 14
HELIX 7 7 ARG A 175 TRP A 183 1 9
HELIX 8 8 GLY A 189 GLU A 206 1 18
SHEET 1 A 4 GLU A 27 VAL A 31 0
SHEET 2 A 4 SER A 3 VAL A 7 1 N ILE A 6 O THR A 29
SHEET 3 A 4 ILE A 48 ASP A 52 1 O LEU A 50 N VAL A 7
SHEET 4 A 4 VAL A 75 THR A 79 1 O VAL A 75 N VAL A 49
SHEET 1 B 4 LEU A 131 SER A 133 0
SHEET 2 B 4 VAL A 136 ASP A 139 -1 O MET A 138 N LEU A 131
SHEET 3 B 4 VAL A 144 VAL A 147 -1 O VAL A 144 N ASP A 139
SHEET 4 B 4 GLY A 149 THR A 151 -1 N GLY A 149 N THR A 151
SHEET 1 C 3 LEU A 173 THR A 174 0
SHEET 2 C 3 GLY A 222 LEU A 225 -1 O TYR A 223 N LEU A 173
SHEET 3 C 3 LEU A 215 VAL A 218 -1 N VAL A 218 O GLY A 222
SITE 1 AC1 4 MET A 77 ARG A 111 VAL A 115 HOH A 459
SITE 1 AC2 3 TYR A 164 HOH A 531 HOH A 537
SITE 1 AC3 8 ASP A 86 ASP A 97 TYR A 98 HOH A 460
SITE 2 AC3 8 HOH A 462 HOH A 463 HOH A 465 HOH A 466
SITE 1 AC4 8 GLU A 24 ASP A 180 ASP A 186 HOH A 548
SITE 2 AC4 8 HOH A 549 HOH A 550 HOH A 551 HOH A 552
SITE 1 AC5 8 GLU A 11 ASP A 15 ASP A 122 ASP A 123
SITE 2 AC5 8 ASP A 128 HOH A 432 HOH A 433 HOH A 439
SITE 1 AC6 8 GLU A 11 ASP A 121 ASP A 122 ASP A 123
SITE 2 AC6 8 GLU A 141 HOH A 434 HOH A 435 HOH A 509
SITE 1 AC7 7 ASP A 9 ASP A 52 MET A 54 GLU A 84
SITE 2 AC7 7 HOH A 420 HOH A 421 HOH A 422
SITE 1 AC8 3 TYR A 103 HOH A 423 HOH A 471
CRYST1 124.351 124.351 44.824 90.00 90.00 90.00 P 4 21 2 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 0.008042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022309 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
