Header list of 2fy9.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 07-FEB-06 2FY9
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DNA RECOGNITION DOMAIN OF THE
TITLE 2 BACILLUS SUBTILIS TRANSCRIPTION-STATE REGULATOR ABH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE TRANSITION STATE REGULATOR ABH;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ABH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE)3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21-B
KEYWDS N-TERMINAL DNA-BINDING DOMAIN, TRANSITION STATE REGULATOR,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.CAVANAGH,B.G.BOBAY
REVDAT 4 09-MAR-22 2FY9 1 REMARK
REVDAT 3 24-FEB-09 2FY9 1 VERSN
REVDAT 2 08-AUG-06 2FY9 1 JRNL
REVDAT 1 23-MAY-06 2FY9 0
JRNL AUTH B.G.BOBAY,G.A.MUELLER,R.J.THOMPSON,A.G.MURZIN,R.A.VENTERS,
JRNL AUTH 2 M.A.STRAUCH,J.CAVANAGH
JRNL TITL NMR STRUCTURE OF ABHN AND COMPARISON WITH ABRBN: FIRST
JRNL TITL 2 INSIGHTS INTO THE DNA-BINDING PROMISCUITY AND SPECIFICITY OF
JRNL TITL 3 ABRB-LIKE TRANSITION-STATE REGULATOR PROTEINS
JRNL REF J.BIOL.CHEM. V. 281 21399 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16702211
JRNL DOI 10.1074/JBC.M601963200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE JULY 15TH 2004, ARIA 1.2
REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), JENS LINGE, MICHAEL
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2357 RESTRAINTS, 2191 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 96 DIHEDRAL ANGLE RESTRAINTS,70 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 2FY9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036453.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 10MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM ABHN, 15N,13C; 10MM KP04,
REMARK 210 15MM KCL, 1MM DTT, 1MM EDTA,
REMARK 210 0.02% NAN3; 95% H2O, 5% D2O; 1-
REMARK 210 2MM ABHN, 15N,13C; 10MM KP04,
REMARK 210 15MM KCL, 1MM DTT, 1MM EDTA,
REMARK 210 0.02% NAN3; 5% H2O, 95% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3-D 13C/15N
REMARK 210 SEQUENTIAL ASSIGNMENT PROTOCOLS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HD1 PHE A 36 HG LEU A 45 1.30
REMARK 500 HD22 LEU B 26 H LYS B 47 1.30
REMARK 500 HD23 LEU A 26 H LYS A 47 1.31
REMARK 500 H LYS A 2 HA2 GLY A 5 1.32
REMARK 500 OD1 ASP A 32 HZ1 LYS A 47 1.58
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 1 ASP A 11 -75.15 -60.85
REMARK 500 1 GLU A 12 -46.56 -151.25
REMARK 500 1 LEU A 26 -101.52 -85.19
REMARK 500 1 ASP A 27 50.93 -179.36
REMARK 500 1 ILE A 30 -32.36 -145.31
REMARK 500 1 LYS A 31 -50.41 -137.83
REMARK 500 1 ASP A 32 -118.84 35.91
REMARK 500 1 ASP B 11 -79.17 -53.86
REMARK 500 1 GLU B 12 -34.42 -154.70
REMARK 500 1 LEU B 26 -80.44 -92.93
REMARK 500 1 ASP B 27 16.49 177.40
REMARK 500 1 ILE B 30 -33.43 -166.05
REMARK 500 1 LYS B 31 -49.86 -136.58
REMARK 500 1 ASP B 32 -111.46 35.39
REMARK 500 2 LYS A 2 -170.44 55.00
REMARK 500 2 ASP A 11 -81.19 -60.88
REMARK 500 2 GLU A 12 -43.78 -154.30
REMARK 500 2 LEU A 26 -88.64 -93.67
REMARK 500 2 ASP A 27 23.85 177.27
REMARK 500 2 ILE A 30 -30.06 -151.15
REMARK 500 2 LYS A 31 -51.90 -137.03
REMARK 500 2 ASP A 32 -117.05 36.44
REMARK 500 2 HIS A 51 78.87 -166.54
REMARK 500 2 LYS B 2 -161.81 53.10
REMARK 500 2 ASP B 11 -82.84 -62.12
REMARK 500 2 GLU B 12 -41.78 -149.83
REMARK 500 2 LEU B 26 -93.90 -85.26
REMARK 500 2 ASP B 27 40.17 177.76
REMARK 500 2 ILE B 30 -30.61 -160.40
REMARK 500 2 LYS B 31 -52.45 -133.89
REMARK 500 2 ASP B 32 -117.83 39.45
REMARK 500 3 ASP A 11 -80.32 -61.32
REMARK 500 3 GLU A 12 -42.28 -153.82
REMARK 500 3 LEU A 26 -89.61 -89.45
REMARK 500 3 ASP A 27 58.78 168.52
REMARK 500 3 ILE A 30 -31.78 -142.62
REMARK 500 3 LYS A 31 -56.34 -134.63
REMARK 500 3 ASP A 32 -121.33 38.90
REMARK 500 3 HIS A 51 76.76 -117.00
REMARK 500 3 ASP B 11 -79.92 -57.19
REMARK 500 3 GLU B 12 -38.11 -152.92
REMARK 500 3 LEU B 26 -85.65 -90.83
REMARK 500 3 ASP B 27 55.45 169.05
REMARK 500 3 ILE B 30 -33.19 -140.85
REMARK 500 3 LYS B 31 -52.63 -133.98
REMARK 500 3 ASP B 32 -118.96 36.94
REMARK 500 4 LYS A 2 -162.28 -75.19
REMARK 500 4 ASP A 11 -77.87 -57.71
REMARK 500 4 GLU A 12 -45.87 -154.81
REMARK 500 4 LEU A 26 -89.87 -78.01
REMARK 500
REMARK 500 THIS ENTRY HAS 154 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z0R RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL DNA RECOGNITION DOMAIN OF THE
REMARK 900 BACILLUS SUBTILIS TRANSCRIPTION-STATE REGULATOR ABRB
REMARK 900 RELATED ID: 1YSF RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF THE N-DOMAIN OF THE TRANSCRIPTION FACTOR
REMARK 900 ABRB
DBREF 2FY9 A 1 54 UNP P39758 ABH_BACSU 1 54
DBREF 2FY9 B 1 54 UNP P39758 ABH_BACSU 1 54
SEQRES 1 A 54 MET LYS SER ILE GLY VAL VAL ARG LYS VAL ASP GLU LEU
SEQRES 2 A 54 GLY ARG ILE VAL MET PRO ILE GLU LEU ARG ARG ALA LEU
SEQRES 3 A 54 ASP ILE ALA ILE LYS ASP SER ILE GLU PHE PHE VAL ASP
SEQRES 4 A 54 GLY ASP LYS ILE ILE LEU LYS LYS TYR LYS PRO HIS GLY
SEQRES 5 A 54 VAL CYS
SEQRES 1 B 54 MET LYS SER ILE GLY VAL VAL ARG LYS VAL ASP GLU LEU
SEQRES 2 B 54 GLY ARG ILE VAL MET PRO ILE GLU LEU ARG ARG ALA LEU
SEQRES 3 B 54 ASP ILE ALA ILE LYS ASP SER ILE GLU PHE PHE VAL ASP
SEQRES 4 B 54 GLY ASP LYS ILE ILE LEU LYS LYS TYR LYS PRO HIS GLY
SEQRES 5 B 54 VAL CYS
HELIX 1 1 PRO A 19 LEU A 26 1 8
HELIX 2 2 PRO B 19 LEU B 26 1 8
SHEET 1 A 6 VAL A 7 ARG A 8 0
SHEET 2 A 6 ILE B 34 ASP B 39 -1 O ILE B 34 N ARG A 8
SHEET 3 A 6 LYS B 42 LYS B 46 -1 O LYS B 46 N GLU B 35
SHEET 4 A 6 LYS A 42 LYS A 46 -1 N ILE A 43 O LEU B 45
SHEET 5 A 6 ILE A 34 ASP A 39 -1 N GLU A 35 O LYS A 46
SHEET 6 A 6 VAL B 7 ARG B 8 -1 O ARG B 8 N ILE A 34
SHEET 1 B 2 ARG A 15 VAL A 17 0
SHEET 2 B 2 ARG B 15 VAL B 17 -1 O ILE B 16 N ILE A 16
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes