Header list of 1fwp.pdb file
Complete list - 23 20 Bytes
HEADER CHEMOTAXIS 06-FEB-96 1FWP
TITLE CHEY-BINDING DOMAIN OF CHEA (RESIDUES 159-227), NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHEY-BINDING DOMAIN, RESIDUES 159 - 227;
COMPND 5 SYNONYM: P2 DOMAIN OF CHEA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CHEA (RESIDUES 124-257);
SOURCE 5 EXPRESSION_SYSTEM: TAC PROMOTER;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PTM22;
SOURCE 7 EXPRESSION_SYSTEM_GENE: CHEA (RESIDUES 124-257)
KEYWDS KINASE, SIGNAL TRANSDUCTION, CHEMOTAXIS
EXPDTA SOLUTION NMR
AUTHOR M.M.MCEVOY,F.W.DAHLQUIST
REVDAT 4 23-FEB-22 1FWP 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1FWP 1 VERSN
REVDAT 2 01-APR-03 1FWP 1 JRNL
REVDAT 1 11-JUL-96 1FWP 0
JRNL AUTH M.M.MCEVOY,D.R.MUHANDIRAM,L.E.KAY,F.W.DAHLQUIST
JRNL TITL STRUCTURE AND DYNAMICS OF A CHEY-BINDING DOMAIN OF THE
JRNL TITL 2 CHEMOTAXIS KINASE CHEA DETERMINED BY NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 35 5633 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8639521
JRNL DOI 10.1021/BI952707H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.MCEVOY,H.ZHOU,A.F.ROTH,D.F.LOWRY,T.B.MORRISON,L.E.KAY,
REMARK 1 AUTH 2 F.W.DAHLQUIST
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE ASSIGNMENTS AND GLOBAL FOLD OF A
REMARK 1 TITL 2 CHEY-BINDING DOMAIN IN CHEA, THE CHEMOTAXIS-SPECIFIC KINASE
REMARK 1 TITL 3 OF ESCHERICHIA COLI
REMARK 1 REF BIOCHEMISTRY V. 34 13871 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173452.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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: 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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ARG A -34
REMARK 465 GLN A -33
REMARK 465 LEU A -32
REMARK 465 ALA A -31
REMARK 465 LEU A -30
REMARK 465 GLU A -29
REMARK 465 ALA A -28
REMARK 465 LYS A -27
REMARK 465 GLY A -26
REMARK 465 GLU A -25
REMARK 465 THR A -24
REMARK 465 PRO A -23
REMARK 465 SER A -22
REMARK 465 ALA A -21
REMARK 465 VAL A -20
REMARK 465 THR A -19
REMARK 465 ARG A -18
REMARK 465 LEU A -17
REMARK 465 SER A -16
REMARK 465 VAL A -15
REMARK 465 VAL A -14
REMARK 465 ALA A -13
REMARK 465 LYS A -12
REMARK 465 SER A -11
REMARK 465 GLU A -10
REMARK 465 PRO A -9
REMARK 465 GLN A -8
REMARK 465 ASP A -7
REMARK 465 GLU A -6
REMARK 465 GLN A -5
REMARK 465 SER A -4
REMARK 465 ARG A -3
REMARK 465 SER A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 VAL A 70
REMARK 465 SER A 71
REMARK 465 PRO A 72
REMARK 465 LYS A 73
REMARK 465 ILE A 74
REMARK 465 SER A 75
REMARK 465 THR A 76
REMARK 465 PRO A 77
REMARK 465 PRO A 78
REMARK 465 VAL A 79
REMARK 465 LEU A 80
REMARK 465 LYS A 81
REMARK 465 LEU A 82
REMARK 465 ALA A 83
REMARK 465 ALA A 84
REMARK 465 GLU A 85
REMARK 465 GLN A 86
REMARK 465 ALA A 87
REMARK 465 PRO A 88
REMARK 465 THR A 89
REMARK 465 GLY A 90
REMARK 465 ARG A 91
REMARK 465 VAL A 92
REMARK 465 GLU A 93
REMARK 465 ARG A 94
REMARK 465 GLU A 95
REMARK 465 LYS A 96
REMARK 465 THR A 97
REMARK 465 THR A 98
REMARK 465 ARG A 99
REMARK 465 ILE A 100
REMARK 465 LYS A 101
REMARK 465 LEU A 102
REMARK 465 GLY A 103
REMARK 465 THR A 104
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 ARG A 8 -32.48 -171.61
REMARK 500 LEU A 9 -169.84 -61.74
REMARK 500 LYS A 10 -159.09 -128.13
REMARK 500 LEU A 27 -160.42 -56.85
REMARK 500 THR A 28 -42.91 -138.66
REMARK 500 ASP A 29 58.98 -173.47
REMARK 500 ASP A 35 12.85 -140.38
REMARK 500 PRO A 42 -164.46 -77.10
REMARK 500 ASP A 44 36.06 -146.93
REMARK 500 ILE A 45 -154.71 -119.53
REMARK 500 ALA A 46 49.57 -93.36
REMARK 500 ILE A 58 -57.63 -143.83
REMARK 500 GLU A 59 -145.51 -173.52
REMARK 500 ALA A 60 31.57 -147.37
REMARK 500 ASP A 61 15.09 -157.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 2 0.31 SIDE CHAIN
REMARK 500 ARG A 3 0.27 SIDE CHAIN
REMARK 500 ARG A 8 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FWP A -34 104 UNP P07363 CHEA_ECOLI 124 262
SEQADV 1FWP ILE A 100 UNP P07363 SER 258 CONFLICT
SEQADV 1FWP LYS A 101 UNP P07363 ASN 259 CONFLICT
SEQADV 1FWP LEU A 102 UNP P07363 GLU 260 CONFLICT
SEQADV 1FWP GLY A 103 UNP P07363 SER 261 CONFLICT
SEQRES 1 A 139 ARG GLN LEU ALA LEU GLU ALA LYS GLY GLU THR PRO SER
SEQRES 2 A 139 ALA VAL THR ARG LEU SER VAL VAL ALA LYS SER GLU PRO
SEQRES 3 A 139 GLN ASP GLU GLN SER ARG SER GLN SER PRO ARG ARG ILE
SEQRES 4 A 139 ILE LEU SER ARG LEU LYS ALA GLY GLU VAL ASP LEU LEU
SEQRES 5 A 139 GLU GLU GLU LEU GLY HIS LEU THR THR LEU THR ASP VAL
SEQRES 6 A 139 VAL LYS GLY ALA ASP SER LEU SER ALA ILE LEU PRO GLY
SEQRES 7 A 139 ASP ILE ALA GLU ASP ASP ILE THR ALA VAL LEU CYS PHE
SEQRES 8 A 139 VAL ILE GLU ALA ASP GLN ILE THR PHE GLU THR VAL GLU
SEQRES 9 A 139 VAL SER PRO LYS ILE SER THR PRO PRO VAL LEU LYS LEU
SEQRES 10 A 139 ALA ALA GLU GLN ALA PRO THR GLY ARG VAL GLU ARG GLU
SEQRES 11 A 139 LYS THR THR ARG ILE LYS LEU GLY THR
HELIX 1 1 VAL A 14 LEU A 24 1 11
HELIX 2 2 GLU A 47 VAL A 57 1 11
SHEET 1 A 3 SER A 36 LEU A 41 0
SHEET 2 A 3 ARG A 2 SER A 7 -1 N LEU A 6 O LEU A 37
SHEET 3 A 3 ILE A 63 THR A 67 -1 N GLU A 66 O ARG A 3
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 - 23 20 Bytes