Header list of 1j0s.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 21-NOV-02 1J0S
TITLE SOLUTION STRUCTURE OF THE HUMAN INTERLEUKIN-18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-18;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA TREFOIL, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.KATO,J.JEE,H.SHIKANO,M.MISHIMA,I.OHKI,T.YONEDA,T.HARA,K.TORIGOE,
AUTHOR 2 N.KONDO,M.SHIRAKAWA
REVDAT 3 23-FEB-22 1J0S 1 REMARK
REVDAT 2 24-FEB-09 1J0S 1 VERSN
REVDAT 1 11-NOV-03 1J0S 0
JRNL AUTH Z.KATO,J.JEE,H.SHIKANO,M.MISHIMA,I.OHKI,H.OHNISHI,A.LI,
JRNL AUTH 2 K.HASHIMOTO,E.MATSUKUMA,K.OMOYA,Y.YAMAMOTO,T.YONEDA,T.HARA,
JRNL AUTH 3 N.KONDO,M.SHIRAKAWA
JRNL TITL THE STRUCTURE AND BINDING MODE OF INTERLEUKIN-18
JRNL REF NAT.STRUCT.BIOL. V. 10 966 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 14528293
JRNL DOI 10.1038/NSB993
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J0S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000005486.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 150MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM INTERLEUKIN-18 U-15N,13C;
REMARK 210 50MM PHOSPHATE BUFFER K
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 1
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 1 GLU A 6 136.53 -175.18
REMARK 500 1 ASP A 17 38.03 74.87
REMARK 500 1 SER A 36 -62.46 -97.51
REMARK 500 1 ASP A 40 87.14 -61.52
REMARK 500 1 SER A 55 59.53 -97.59
REMARK 500 1 ARG A 58 102.98 -160.10
REMARK 500 1 CYS A 68 -82.76 179.31
REMARK 500 1 GLU A 77 -97.73 -53.78
REMARK 500 1 ASN A 78 -70.23 -98.04
REMARK 500 1 GLU A 85 97.91 -67.34
REMARK 500 1 MET A 86 137.57 -179.90
REMARK 500 1 ASN A 111 39.19 -160.01
REMARK 500 1 SER A 119 -74.51 -60.10
REMARK 500 1 GLU A 121 -173.91 -69.72
REMARK 500 1 ARG A 131 -115.59 60.59
REMARK 500 2 GLU A 6 139.53 -177.30
REMARK 500 2 SER A 36 -66.48 -97.35
REMARK 500 2 ILE A 46 -161.56 -66.67
REMARK 500 2 SER A 55 -70.67 -83.06
REMARK 500 2 ARG A 58 95.95 -161.61
REMARK 500 2 CYS A 68 -82.08 177.44
REMARK 500 2 GLU A 77 -98.85 -52.62
REMARK 500 2 ASN A 78 -73.82 -97.97
REMARK 500 2 GLU A 85 97.98 -67.88
REMARK 500 2 MET A 86 134.24 -174.34
REMARK 500 2 ASN A 111 50.94 -106.29
REMARK 500 2 SER A 119 -75.76 -60.58
REMARK 500 2 GLU A 121 -173.21 -68.36
REMARK 500 2 ARG A 131 -105.05 61.37
REMARK 500 3 ASN A 14 -165.17 -117.54
REMARK 500 3 THR A 34 -81.66 -136.66
REMARK 500 3 ALA A 42 132.85 -170.26
REMARK 500 3 ARG A 44 96.84 61.07
REMARK 500 3 ARG A 58 87.02 -164.94
REMARK 500 3 CYS A 68 -68.53 175.96
REMARK 500 3 GLU A 77 -100.87 -54.19
REMARK 500 3 ASN A 78 -72.62 -98.05
REMARK 500 3 GLU A 85 97.96 -68.08
REMARK 500 3 MET A 86 126.25 -176.66
REMARK 500 3 HIS A 109 -50.33 -136.27
REMARK 500 3 SER A 119 -73.50 -64.00
REMARK 500 3 ARG A 131 -118.30 59.00
REMARK 500 4 PHE A 2 156.91 -45.66
REMARK 500 4 GLU A 6 142.59 -171.13
REMARK 500 4 ASP A 17 32.59 73.19
REMARK 500 4 MET A 33 78.99 -101.02
REMARK 500 4 SER A 36 -66.95 -97.47
REMARK 500 4 ARG A 44 78.93 58.41
REMARK 500 4 CYS A 68 -141.49 -179.38
REMARK 500 4 GLU A 77 -101.01 -55.35
REMARK 500
REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1J0S A 1 157 UNP Q14116 IL18_HUMAN 37 193
SEQRES 1 A 157 TYR PHE GLY LYS LEU GLU SER LYS LEU SER VAL ILE ARG
SEQRES 2 A 157 ASN LEU ASN ASP GLN VAL LEU PHE ILE ASP GLN GLY ASN
SEQRES 3 A 157 ARG PRO LEU PHE GLU ASP MET THR ASP SER ASP CYS ARG
SEQRES 4 A 157 ASP ASN ALA PRO ARG THR ILE PHE ILE ILE SER MET TYR
SEQRES 5 A 157 LYS ASP SER GLN PRO ARG GLY MET ALA VAL THR ILE SER
SEQRES 6 A 157 VAL LYS CYS GLU LYS ILE SER THR LEU SER CYS GLU ASN
SEQRES 7 A 157 LYS ILE ILE SER PHE LYS GLU MET ASN PRO PRO ASP ASN
SEQRES 8 A 157 ILE LYS ASP THR LYS SER ASP ILE ILE PHE PHE GLN ARG
SEQRES 9 A 157 SER VAL PRO GLY HIS ASP ASN LYS MET GLN PHE GLU SER
SEQRES 10 A 157 SER SER TYR GLU GLY TYR PHE LEU ALA CYS GLU LYS GLU
SEQRES 11 A 157 ARG ASP LEU PHE LYS LEU ILE LEU LYS LYS GLU ASP GLU
SEQRES 12 A 157 LEU GLY ASP ARG SER ILE MET PHE THR VAL GLN ASN GLU
SEQRES 13 A 157 ASP
HELIX 1 1 ASP A 146 MET A 150 5 5
SHEET 1 A 6 ILE A 81 LYS A 84 0
SHEET 2 A 6 SER A 72 CYS A 76 -1 N SER A 75 O SER A 82
SHEET 3 A 6 ILE A 64 VAL A 66 -1 N VAL A 66 O SER A 72
SHEET 4 A 6 ILE A 48 TYR A 52 -1 N ILE A 48 O SER A 65
SHEET 5 A 6 LYS A 4 ARG A 13 -1 N GLU A 6 O MET A 51
SHEET 6 A 6 THR A 152 ASN A 155 -1 O GLN A 154 N VAL A 11
SHEET 1 B 2 VAL A 19 ILE A 22 0
SHEET 2 B 2 PRO A 28 GLU A 31 -1 O LEU A 29 N PHE A 21
SHEET 1 C 3 MET A 60 VAL A 62 0
SHEET 2 C 3 PHE A 101 SER A 105 -1 O GLN A 103 N MET A 60
SHEET 3 C 3 MET A 113 SER A 117 -1 O GLU A 116 N PHE A 102
SHEET 1 D 2 PHE A 124 GLU A 130 0
SHEET 2 D 2 LEU A 133 LYS A 139 -1 O ILE A 137 N ALA A 126
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 - b 23 2 Bytes