HEADER TRANSCRIPTION 14-JUL-09 3IAO
TITLE CONFORMATIONAL PLASTICITY OF THE COILED COIL DOMAIN OF BMRR IS
TITLE 2 REQUIRED FOR BMR PROMOTER BINDING-THE UNLIGANDED STRUCTURE OF BMRR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG-EFFLUX TRANSPORTER 1 REGULATOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: BMR1R, BMRR, BSU24020;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS MULTIDRUG RESISTANCE, TRANSCRIPTION REGULATION, DNA-BINDING. WINGED
KEYWDS 2 HELIX-TURN-HELIX MOTIF, ACTIVATOR, DNA-BINDING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUMARASWAMI,K.J.NEWBERRY,R.G.BRENNAN
REVDAT 4 06-SEP-23 3IAO 1 REMARK
REVDAT 3 13-OCT-21 3IAO 1 SEQADV ATOM
REVDAT 2 19-MAY-10 3IAO 1 JRNL
REVDAT 1 14-APR-10 3IAO 0
JRNL AUTH M.KUMARASWAMI,K.J.NEWBERRY,R.G.BRENNAN
JRNL TITL CONFORMATIONAL PLASTICITY OF THE COILED-COIL DOMAIN OF BMRR
JRNL TITL 2 IS REQUIRED FOR BMR OPERATOR BINDING: THE STRUCTURE OF
JRNL TITL 3 UNLIGANDED BMRR.
JRNL REF J.MOL.BIOL. V. 398 264 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20230832
JRNL DOI 10.1016/J.JMB.2010.03.011
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 11322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1749
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2233
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 167
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.78000
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : 5.78000
REMARK 3 B13 (A**2) : -11.57000
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.43
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11336
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.3000
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) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 3D71
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2 M LITHIUM SULFATE,
REMARK 280 0.1M TRIS HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 84.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 84.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.55000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 15.77500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.32500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.32500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 15.77500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 84.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.55000
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 84.00000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 84.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 31.55000
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 84.00000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 47.32500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 15.77500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 84.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 15.77500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 47.32500
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 84.00000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 84.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 31.55000
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: 6830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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 84.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 84.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 31.55000
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 ASN A 197
REMARK 465 LYS A 198
REMARK 465 GLN A 199
REMARK 465 ILE A 200
REMARK 465 GLU A 278
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 MET A 1 CG SD CE
REMARK 470 LYS A 2 CG CD CE NZ
REMARK 470 TYR A 42 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 244 CG CD OE1 NE2
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 A 229 NE2 GLN A 253 2.18
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 O HOH A 391 O HOH A 391 5555 0.51
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 ASN A 16 64.69 -101.69
REMARK 500 ILE A 19 23.53 -74.66
REMARK 500 GLU A 67 -6.65 -58.38
REMARK 500 THR A 104 -8.28 -57.78
REMARK 500 GLU A 117 39.68 -89.65
REMARK 500 GLU A 131 106.43 -52.26
REMARK 500 ALA A 139 48.89 -90.91
REMARK 500 ASN A 146 -42.02 -136.48
REMARK 500 SER A 153 -73.79 -73.49
REMARK 500 LYS A 157 27.36 -76.32
REMARK 500 PHE A 158 -57.81 -132.52
REMARK 500 ALA A 162 -43.30 -133.34
REMARK 500 THR A 166 -154.73 -109.69
REMARK 500 THR A 210 -152.93 -151.67
REMARK 500 PRO A 213 173.41 -48.22
REMARK 500 PHE A 224 151.32 -43.00
REMARK 500 SER A 225 133.58 -170.80
REMARK 500 PRO A 226 4.50 -54.11
REMARK 500 ASP A 242 -5.96 -57.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D71 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH DNA
REMARK 900 RELATED ID: 3D70 RELATED DB: PDB
REMARK 900 E253A MUTANT PROTEIN OF THE SAME PROTEIN COMPLEXED WITH DNA
REMARK 900 RELATED ID: 1R8E RELATED DB: PDB
REMARK 900 BMRR BOUND TO DNA
DBREF 3IAO A 1 278 UNP P39075 BMRR_BACSU 1 278
SEQADV 3IAO GLN A 253 UNP P39075 GLU 253 ENGINEERED MUTATION
SEQADV 3IAO GLU A 275 UNP P39075 ARG 275 ENGINEERED MUTATION
SEQRES 1 A 278 MET LYS GLU SER TYR TYR SER ILE GLY GLU VAL SER LYS
SEQRES 2 A 278 LEU ALA ASN VAL SER ILE LYS ALA LEU ARG TYR TYR ASP
SEQRES 3 A 278 LYS ILE ASP LEU PHE LYS PRO ALA TYR VAL ASP PRO ASP
SEQRES 4 A 278 THR SER TYR ARG TYR TYR THR ASP SER GLN LEU ILE HIS
SEQRES 5 A 278 LEU ASP LEU ILE LYS SER LEU LYS TYR ILE GLY THR PRO
SEQRES 6 A 278 LEU GLU GLU MET LYS LYS ALA GLN ASP LEU GLU MET GLU
SEQRES 7 A 278 GLU LEU PHE ALA PHE TYR THR GLU GLN GLU ARG GLN ILE
SEQRES 8 A 278 ARG GLU LYS LEU ASP PHE LEU SER ALA LEU GLU GLN THR
SEQRES 9 A 278 ILE SER LEU VAL LYS LYS ARG MET LYS ARG GLN MET GLU
SEQRES 10 A 278 TYR PRO ALA LEU GLY GLU VAL PHE VAL LEU ASP GLU GLU
SEQRES 11 A 278 GLU ILE ARG ILE ILE GLN THR GLU ALA GLU GLY ILE GLY
SEQRES 12 A 278 PRO GLU ASN VAL LEU ASN ALA SER TYR SER LYS LEU LYS
SEQRES 13 A 278 LYS PHE ILE GLU SER ALA ASP GLY PHE THR ASN ASN SER
SEQRES 14 A 278 TYR GLY ALA THR PHE SER PHE GLN PRO TYR THR SER ILE
SEQRES 15 A 278 ASP GLU MET THR TYR ARG HIS ILE PHE THR PRO VAL LEU
SEQRES 16 A 278 THR ASN LYS GLN ILE SER SER ILE THR PRO ASP MET GLU
SEQRES 17 A 278 ILE THR THR ILE PRO LYS GLY ARG TYR ALA CYS ILE ALA
SEQRES 18 A 278 TYR ASN PHE SER PRO GLU HIS TYR PHE LEU ASN LEU GLN
SEQRES 19 A 278 LYS LEU ILE LYS TYR ILE ALA ASP ARG GLN LEU THR VAL
SEQRES 20 A 278 VAL SER ASP VAL TYR GLN LEU ILE ILE PRO ILE HIS TYR
SEQRES 21 A 278 SER PRO LYS LYS GLN GLU GLU TYR ARG VAL GLU MET LYS
SEQRES 22 A 278 ILE GLU ILE ALA GLU
FORMUL 2 HOH *167(H2 O)
HELIX 1 1 SER A 7 ALA A 15 1 9
HELIX 2 2 LYS A 20 ILE A 28 1 9
HELIX 3 3 LEU A 50 ILE A 62 1 13
HELIX 4 4 PRO A 65 ASP A 74 1 10
HELIX 5 5 GLU A 76 GLU A 86 1 11
HELIX 6 6 GLU A 86 GLU A 117 1 32
HELIX 7 7 LEU A 148 SER A 151 5 4
HELIX 8 8 TYR A 152 GLY A 164 1 13
HELIX 9 9 SER A 181 MET A 185 5 5
HELIX 10 10 GLU A 227 ASP A 242 1 16
SHEET 1 A 3 TYR A 5 TYR A 6 0
SHEET 2 A 3 ARG A 43 THR A 46 -1 O TYR A 45 N TYR A 6
SHEET 3 A 3 TYR A 35 VAL A 36 -1 N TYR A 35 O TYR A 44
SHEET 1 B 8 VAL A 124 ASP A 128 0
SHEET 2 B 8 ARG A 216 ASN A 223 -1 O CYS A 219 N PHE A 125
SHEET 3 B 8 TYR A 268 LYS A 273 -1 O VAL A 270 N TYR A 222
SHEET 4 B 8 VAL A 251 PRO A 257 -1 N TYR A 252 O LYS A 273
SHEET 5 B 8 TYR A 170 PHE A 174 -1 N PHE A 174 O VAL A 251
SHEET 6 B 8 HIS A 189 PRO A 193 -1 O PHE A 191 N GLY A 171
SHEET 7 B 8 ILE A 132 GLU A 138 -1 N ILE A 135 O THR A 192
SHEET 8 B 8 GLU A 208 ILE A 212 -1 O GLU A 208 N GLN A 136
SHEET 1 C 2 THR A 246 VAL A 247 0
SHEET 2 C 2 ILE A 276 ALA A 277 -1 O ALA A 277 N THR A 246
CRYST1 168.000 168.000 63.100 90.00 90.00 90.00 I 41 2 2 16
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 0.005952 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015848 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
