Header list of 1k0s.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 20-SEP-01 1K0S
TITLE SOLUTION STRUCTURE OF THE CHEMOTAXIS PROTEIN CHEW FROM THE
TITLE 2 THERMOPHILIC ORGANISM THERMOTOGA MARITIMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS PROTEIN CHEW;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHEW;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: CHEW;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 594;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS CHEW, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.J.GRISWOLD,H.ZHOU,R.V.SWANSON,M.I.SIMON,F.W.DAHLQUIST
REVDAT 3 23-FEB-22 1K0S 1 REMARK
REVDAT 2 24-FEB-09 1K0S 1 VERSN
REVDAT 1 06-FEB-02 1K0S 0
JRNL AUTH I.J.GRISWOLD,H.ZHOU,M.MATISON,R.V.SWANSON,L.P.MCINTOSH,
JRNL AUTH 2 M.I.SIMON,F.W.DAHLQUIST
JRNL TITL THE SOLUTION STRUCTURE AND INTERACTIONS OF CHEW FROM
JRNL TITL 2 THERMOTOGA MARITIMA.
JRNL REF NAT.STRUCT.BIOL. V. 9 121 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11799399
JRNL DOI 10.1038/NSB753
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, ARIA 1.0
REMARK 3 AUTHORS : BRUNGER (CNS), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K0S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014416.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 50MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM TMW U-15N,13C; 50MM ACETATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_15N_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.0, FELIX 98
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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: 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
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 THR A 3 -55.86 65.73
REMARK 500 1 ALA A 5 134.85 62.39
REMARK 500 1 ASP A 6 140.40 -178.60
REMARK 500 1 ALA A 7 143.85 64.01
REMARK 500 1 LEU A 8 44.75 -147.50
REMARK 500 1 GLU A 20 -39.99 83.73
REMARK 500 1 ASP A 26 100.95 -44.20
REMARK 500 1 THR A 40 78.83 38.49
REMARK 500 1 LYS A 44 159.48 -46.46
REMARK 500 1 SER A 45 -53.26 -174.75
REMARK 500 1 ARG A 46 -118.31 -76.06
REMARK 500 1 HIS A 47 -49.95 -169.33
REMARK 500 1 ILE A 71 178.81 45.19
REMARK 500 1 PHE A 73 143.92 -31.07
REMARK 500 1 ASP A 74 39.71 -169.84
REMARK 500 1 LYS A 79 -48.63 -159.46
REMARK 500 1 ASP A 88 33.65 70.41
REMARK 500 1 ASP A 96 -75.95 -81.27
REMARK 500 1 ASP A 110 -52.61 -172.90
REMARK 500 1 THR A 112 44.77 176.52
REMARK 500 1 ASN A 113 125.12 62.87
REMARK 500 1 VAL A 114 113.50 -174.01
REMARK 500 1 SER A 115 130.96 -172.85
REMARK 500 1 PHE A 118 38.94 -165.19
REMARK 500 1 LYS A 121 32.99 -156.90
REMARK 500 1 SER A 122 -160.74 178.25
REMARK 500 1 ASP A 137 33.99 -97.20
REMARK 500 1 ILE A 138 20.43 42.40
REMARK 500 2 LYS A 2 60.80 62.16
REMARK 500 2 GLU A 20 -39.63 86.60
REMARK 500 2 LYS A 36 66.77 -169.18
REMARK 500 2 SER A 37 -168.34 -55.74
REMARK 500 2 ASP A 38 46.54 38.74
REMARK 500 2 THR A 40 91.57 34.57
REMARK 500 2 PRO A 43 5.16 -67.97
REMARK 500 2 SER A 45 60.28 174.92
REMARK 500 2 ARG A 46 -31.24 -170.46
REMARK 500 2 HIS A 47 146.98 73.73
REMARK 500 2 PHE A 48 -46.74 83.52
REMARK 500 2 ILE A 71 165.91 47.66
REMARK 500 2 PHE A 73 141.52 -28.08
REMARK 500 2 ASP A 74 37.03 -166.79
REMARK 500 2 LYS A 79 39.20 -179.64
REMARK 500 2 ASP A 88 32.13 71.00
REMARK 500 2 ASP A 96 -73.33 -92.96
REMARK 500 2 ASP A 110 -46.89 -175.74
REMARK 500 2 THR A 112 43.48 177.28
REMARK 500 2 ASN A 113 120.54 61.65
REMARK 500 2 SER A 115 133.83 175.34
REMARK 500 2 ASP A 116 -70.10 -71.29
REMARK 500
REMARK 500 THIS ENTRY HAS 592 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K0S A 1 151 UNP Q56311 CHEW_THEMA 1 151
SEQRES 1 A 151 MET LYS THR LEU ALA ASP ALA LEU LYS GLU PHE GLU VAL
SEQRES 2 A 151 LEU SER PHE GLU ILE ASP GLU GLN ALA LEU ALA PHE ASP
SEQRES 3 A 151 VAL ASP ASN ILE GLU MET VAL ILE GLU LYS SER ASP ILE
SEQRES 4 A 151 THR PRO VAL PRO LYS SER ARG HIS PHE VAL GLU GLY VAL
SEQRES 5 A 151 ILE ASN LEU ARG GLY ARG ILE ILE PRO VAL VAL ASN LEU
SEQRES 6 A 151 ALA LYS ILE LEU GLY ILE SER PHE ASP GLU GLN LYS MET
SEQRES 7 A 151 LYS SER ILE ILE VAL ALA ARG THR LYS ASP VAL GLU VAL
SEQRES 8 A 151 GLY PHE LEU VAL ASP ARG VAL LEU GLY VAL LEU ARG ILE
SEQRES 9 A 151 THR GLU ASN GLN LEU ASP LEU THR ASN VAL SER ASP LYS
SEQRES 10 A 151 PHE GLY LYS LYS SER LYS GLY LEU VAL LYS THR ASP GLY
SEQRES 11 A 151 ARG LEU ILE ILE TYR LEU ASP ILE ASP LYS ILE ILE GLU
SEQRES 12 A 151 GLU ILE THR VAL LYS GLU GLY VAL
HELIX 1 1 ASN A 64 GLY A 70 1 7
HELIX 2 2 ILE A 138 LYS A 148 1 11
SHEET 1 A 5 ARG A 97 THR A 105 0
SHEET 2 A 5 GLU A 10 ILE A 18 -1 N SER A 15 O GLY A 100
SHEET 3 A 5 GLN A 21 PHE A 25 -1 O GLN A 21 N ILE A 18
SHEET 4 A 5 ARG A 131 LEU A 136 1 O ILE A 134 N ALA A 24
SHEET 5 A 5 GLY A 124 THR A 128 -1 N VAL A 126 O ILE A 133
SHEET 1 B 5 ILE A 30 GLU A 35 0
SHEET 2 B 5 SER A 80 ARG A 85 -1 O ILE A 81 N ILE A 34
SHEET 3 B 5 GLU A 90 VAL A 95 -1 O VAL A 91 N ALA A 84
SHEET 4 B 5 ARG A 58 VAL A 63 1 N VAL A 63 O GLY A 92
SHEET 5 B 5 GLY A 51 LEU A 55 -1 N GLY A 51 O VAL A 62
CRYST1 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 - b 23 2 Bytes