Header list of 1qqi.pdb file
Complete list - 2 20 Bytes
HEADER TRANSCRIPTION 07-JUN-99 1QQI
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING AND TRANSACTIVATION DOMAIN OF
TITLE 2 PHOB FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATE REGULON TRANSCRIPTIONAL REGULATORY PROTEIN PHOB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PT7-7-CB
KEYWDS WINGED HELIX-TURN-HELIX, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, TRANSCRIPTION
EXPDTA SOLUTION NMR
AUTHOR H.OKAMURA,S.HANAOKA,A.NAGADOI,K.MAKINO,Y.NISHIMURA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1QQI 1 REMARK
REVDAT 3 24-FEB-09 1QQI 1 VERSN
REVDAT 2 14-JUN-00 1QQI 1 REMARK
REVDAT 1 07-JUN-00 1QQI 0
JRNL AUTH H.OKAMURA,S.HANAOKA,A.NAGADOI,K.MAKINO,Y.NISHIMURA
JRNL TITL STRUCTURAL COMPARISON OF THE PHOB AND OMPR
JRNL TITL 2 DNA-BINDING/TRANSACTIVATION DOMAINS AND THE ARRANGEMENT OF
JRNL TITL 3 PHOB MOLECULES ON THE PHOSPHATE BOX.
JRNL REF J.MOL.BIOL. V. 295 1225 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10653699
JRNL DOI 10.1006/JMBI.1999.3379
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.6, EMBOSS 5
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), NAKAI,T., KIDERA, A. AND
REMARK 3 NAKAMURA, H. (EMBOSS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1758 RESTRAINTS, 1719 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS AND 39 DIHEDRAL ANGLE RESTRAINTS. STRUCTURE
REMARK 3 CALCULATIONS
REMARK 3 WERE PERFORMED WITH EMBOSS BY USING A 4D SIMULATED ANNEALING
REMARK 3 PROTOCOL STARTING
REMARK 3 FROM A RANDOM COIL CONFORMATION. THE GENERATED STRUCTURES WERE
REMARK 3 FURTHER REFINED
REMARK 3 BY ENERGY MINIMIZATION USING THE AMBER FORCE FIELD. THE FINAL
REMARK 3 STRUCTURES WERE
REMARK 3 SELECTED BY HAVING NO DISTANCE VIOLATIONS GREATER THAN 0.3
REMARK 3 ANGSTROMS AND NO
REMARK 3 DIHEDRAL ANGLE VIOLATIONS GREATER THAN 5 DEGREES, AND A LOW TARGET
REMARK 3 ENERGY.
REMARK 4
REMARK 4 1QQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009148.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NACL 500MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM PROTEIN U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 500MM NACL; 1-
REMARK 210 2MM PROTEIN U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER, 500MM NACL; 1-
REMARK 210 2MM PROTEIN ; 50MM PHOSPHATE
REMARK 210 BUFFER, 500MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 3.9
REMARK 210 METHOD USED : 4D SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: MONOMERIC
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 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 ALA A 2 118.30 -167.68
REMARK 500 VAL A 3 107.79 -160.12
REMARK 500 GLU A 4 -119.16 50.18
REMARK 500 GLU A 25 -40.14 -155.84
REMARK 500 HIS A 57 -70.21 -117.73
REMARK 500 ARG A 94 -137.40 50.54
REMARK 500 ARG A 103 -53.39 -169.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TRT001000190.1 RELATED DB: TARGETDB
DBREF 1QQI A 1 104 UNP P08402 PHOB_ECOLI 126 229
SEQRES 1 A 104 MET ALA VAL GLU GLU VAL ILE GLU MET GLN GLY LEU SER
SEQRES 2 A 104 LEU ASP PRO THR SER HIS ARG VAL MET ALA GLY GLU GLU
SEQRES 3 A 104 PRO LEU GLU MET GLY PRO THR GLU PHE LYS LEU LEU HIS
SEQRES 4 A 104 PHE PHE MET THR HIS PRO GLU ARG VAL TYR SER ARG GLU
SEQRES 5 A 104 GLN LEU LEU ASN HIS VAL TRP GLY THR ASN VAL TYR VAL
SEQRES 6 A 104 GLU ASP ARG THR VAL ASP VAL HIS ILE ARG ARG LEU ARG
SEQRES 7 A 104 LYS ALA LEU GLU PRO GLY GLY HIS ASP ARG MET VAL GLN
SEQRES 8 A 104 THR VAL ARG GLY THR GLY TYR ARG PHE SER THR ARG PHE
HELIX 1 1 GLY A 31 HIS A 44 1 14
HELIX 2 2 ARG A 51 VAL A 58 1 8
HELIX 3 3 GLU A 66 GLU A 82 1 17
HELIX 4 4 GLY A 85 ARG A 88 5 4
SHEET 1 A 4 ILE A 7 MET A 9 0
SHEET 2 A 4 LEU A 12 ASP A 15 -1 N LEU A 12 O MET A 9
SHEET 3 A 4 ARG A 20 ALA A 23 -1 O ARG A 20 N ASP A 15
SHEET 4 A 4 GLU A 26 LEU A 28 -1 O GLU A 26 N ALA A 23
SHEET 1 B 3 TYR A 49 SER A 50 0
SHEET 2 B 3 GLY A 97 PHE A 100 -1 O TYR A 98 N TYR A 49
SHEET 3 B 3 VAL A 90 VAL A 93 -1 N GLN A 91 O ARG A 99
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
Complete list - 2 20 Bytes