Header list of 1z0r.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 02-MAR-05 1Z0R
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DNA RECOGNITION DOMAIN OF THE
TITLE 2 BACILLUS SUBTILIS TRANSCRIPTION-STATE REGULATOR ABRB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSITION STATE REGULATORY PROTEIN ABRB;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DIMER FROM RESIDUES 1-53 (OF 94);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ABRB;
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: PET-24
KEYWDS SCOP DATABASE, N-TERMINAL DNA-BINDING DOMAIN, TRANSITION STATE
KEYWDS 2 REGULATOR, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR B.G.BOBAY,A.ANDREEVA,G.A.MUELLER,J.CAVANAGH,A.G.MURZIN
REVDAT 4 02-MAR-22 1Z0R 1 REMARK
REVDAT 3 24-FEB-09 1Z0R 1 VERSN
REVDAT 2 01-NOV-05 1Z0R 1 JRNL
REVDAT 1 15-MAR-05 1Z0R 0
SPRSDE 15-MAR-05 1Z0R 1EKT
JRNL AUTH B.G.BOBAY,A.ANDREEVA,G.A.MUELLER,J.CAVANAGH,A.G.MURZIN
JRNL TITL REVISED STRUCTURE OF THE ABRB N-TERMINAL DOMAIN UNIFIES A
JRNL TITL 2 DIVERSE SUPERFAMILY OF PUTATIVE DNA-BINDING PROTEINS.
JRNL REF FEBS LETT. V. 579 5669 2005
JRNL REFN ISSN 0014-5793
JRNL PMID 16223496
JRNL DOI 10.1016/J.FEBSLET.2005.09.045
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 : DELAGLIO, F. (NMRPIPE), NILGES, M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z0R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032152.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 15MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM ABRB; 95% PURE; 20MM
REMARK 210 PHOSPHATE, 15MM KCL, 1MM EDTA,
REMARK 210 1MM DTT
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 : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: NEW RELATIONSHIPS FOUND IN PROCESS OF UPDATING THE SCOP
REMARK 210 DATABASE RESULTED IN REVISION OF THE STRUCTURE OF THE N-TERMINAL,
REMARK 210 DNA-BINDING DOMAIN OF THE TRANSITION STATE REGULATOR ABRB.
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 HD13 ILE A 28 HD23 LEU A 34 1.22
REMARK 500 HD13 ILE B 28 HD23 LEU B 34 1.32
REMARK 500 OE1 GLU B 35 HZ2 LYS B 46 1.56
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 LYS A 2 -124.51 -163.30
REMARK 500 1 ASP A 11 -91.81 73.32
REMARK 500 1 GLU A 12 -54.24 -161.12
REMARK 500 1 ASP A 40 -67.42 61.46
REMARK 500 1 PRO A 50 41.25 -75.74
REMARK 500 1 LYS B 2 -120.35 -168.98
REMARK 500 1 ASP B 11 -109.84 71.65
REMARK 500 1 GLU B 12 -42.23 -151.63
REMARK 500 1 ASP B 40 -70.46 62.72
REMARK 500 2 LYS A 2 -133.77 -146.60
REMARK 500 2 ASP A 11 -147.28 66.29
REMARK 500 2 ILE A 28 -157.66 -88.12
REMARK 500 2 ASP A 40 -79.37 60.79
REMARK 500 2 GLU A 41 20.82 -141.25
REMARK 500 2 LYS B 2 -104.25 -136.91
REMARK 500 2 ASP B 11 -148.43 70.17
REMARK 500 2 ILE B 28 -153.45 -78.34
REMARK 500 2 ALA B 29 -105.92 -153.44
REMARK 500 2 GLU B 30 -39.34 -154.70
REMARK 500 2 ASP B 40 -13.31 67.04
REMARK 500 2 GLU B 41 -15.46 -179.91
REMARK 500 3 LYS A 2 -151.08 63.22
REMARK 500 3 ASP A 11 -133.34 66.94
REMARK 500 3 GLU A 12 -37.13 -131.19
REMARK 500 3 ILE A 28 -153.75 -83.11
REMARK 500 3 ALA A 29 -168.61 -162.47
REMARK 500 3 ASP A 40 -73.82 67.87
REMARK 500 3 GLU A 41 17.88 -155.50
REMARK 500 3 LYS B 2 -148.00 62.93
REMARK 500 3 ASP B 11 -145.14 64.69
REMARK 500 3 ILE B 28 -157.95 -88.81
REMARK 500 3 ASP B 40 -69.47 69.73
REMARK 500 3 GLU B 41 20.82 -158.81
REMARK 500 4 LYS A 2 -151.01 64.68
REMARK 500 4 THR A 4 -34.51 -135.77
REMARK 500 4 ASP A 11 -135.62 66.35
REMARK 500 4 GLU A 12 -47.96 -130.25
REMARK 500 4 ILE A 28 -156.29 -81.10
REMARK 500 4 ASP A 40 -83.73 64.83
REMARK 500 4 GLU A 41 18.15 -143.97
REMARK 500 4 LYS B 2 -155.37 66.01
REMARK 500 4 THR B 4 -39.66 -137.86
REMARK 500 4 ASP B 11 -136.74 67.18
REMARK 500 4 GLU B 12 -42.33 -131.56
REMARK 500 4 ILE B 28 -156.36 -80.90
REMARK 500 4 ASP B 40 -87.11 60.85
REMARK 500 4 GLU B 41 29.81 -144.43
REMARK 500 5 LYS A 2 -140.28 -151.92
REMARK 500 5 ASP A 11 -124.45 68.51
REMARK 500 5 GLU A 12 -40.40 -142.90
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MVF RELATED DB: PDB
REMARK 900 MAZE ADDICTION ANTIDOTE
REMARK 900 RELATED ID: 1N0F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CELL DIVISION AND CELL WALL BIOSYNTHESIS
REMARK 900 PROTEIN UPF0040 FROM MYCOPLASMA PNEUMONIAE: INDICATION OF A NOVEL
REMARK 900 FOLD WITH A POSSIBLE NEW CONSERVED SEQUENCE MOTIF
DBREF 1Z0R A 1 53 UNP P08874 ABRB_BACSU 3 55
DBREF 1Z0R B 1 53 UNP P08874 ABRB_BACSU 3 55
SEQRES 1 A 53 MET LYS SER THR GLY ILE VAL ARG LYS VAL ASP GLU LEU
SEQRES 2 A 53 GLY ARG VAL VAL ILE PRO ILE GLU LEU ARG ARG THR LEU
SEQRES 3 A 53 GLY ILE ALA GLU LYS ASP ALA LEU GLU ILE TYR VAL ASP
SEQRES 4 A 53 ASP GLU LYS ILE ILE LEU LYS LYS TYR LYS PRO ASN MET
SEQRES 5 A 53 THR
SEQRES 1 B 53 MET LYS SER THR GLY ILE VAL ARG LYS VAL ASP GLU LEU
SEQRES 2 B 53 GLY ARG VAL VAL ILE PRO ILE GLU LEU ARG ARG THR LEU
SEQRES 3 B 53 GLY ILE ALA GLU LYS ASP ALA LEU GLU ILE TYR VAL ASP
SEQRES 4 B 53 ASP GLU LYS ILE ILE LEU LYS LYS TYR LYS PRO ASN MET
SEQRES 5 B 53 THR
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 ILE A 6 LYS A 9 0
SHEET 2 A 6 ALA B 33 ASP B 39 -1 O ILE B 36 N ILE A 6
SHEET 3 A 6 LYS B 42 LYS B 47 -1 O ILE B 44 N TYR B 37
SHEET 4 A 6 LYS A 42 LYS A 47 -1 N ILE A 43 O LEU B 45
SHEET 5 A 6 ALA A 33 ASP A 39 -1 N TYR A 37 O ILE A 44
SHEET 6 A 6 ILE B 6 LYS B 9 -1 O ILE B 6 N ILE A 36
SHEET 1 B 2 ARG A 15 VAL A 17 0
SHEET 2 B 2 ARG B 15 VAL B 17 -1 O VAL B 16 N VAL 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 2 2 Bytes