Header list of 1o7b.pdb file
Complete list - n 24 2 Bytes
HEADER CELL ADHESION 29-OCT-02 1O7B
TITLE REFINED SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6;
COMPND 3 CHAIN: T;
COMPND 4 FRAGMENT: LINK_MODULE, RESIDUES 36-133;
COMPND 5 SYNONYM: HUMAN TSG-6, HYALURONATE-BINDING PROTEIN, TNF-STIMULATED
COMPND 6 GENE 6 PROTEIN;
COMPND 7 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRK172;
SOURCE 10 OTHER_DETAILS: EXTRACELLULAR, INFLAMMATION-ASSOCIATED
KEYWDS HYALURONAN-BINDING DOMAIN, CARBOHYDRATE-BINDING DOMAIN, LINK MODULE,
KEYWDS 2 CELL ADHESION, GLYCOPROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.D.BLUNDELL,P.TERIETE,J.D.KAHMANN,A.R.PICKFORD,I.D.CAMPBELL,A.J.DAY
REVDAT 6 24-JAN-18 1O7B 1 JRNL REMARK
REVDAT 5 14-JUN-17 1O7B 1 REMARK
REVDAT 4 24-FEB-09 1O7B 1 VERSN
REVDAT 3 04-DEC-03 1O7B 1 JRNL
REVDAT 2 07-NOV-03 1O7B 1 SPRSDE
REVDAT 1 23-OCT-03 1O7B 0
SPRSDE 07-NOV-03 1O7B 1TSG
JRNL AUTH C.D.BLUNDELL,D.J.MAHONEY,A.ALMOND,P.L.DEANGELIS,J.D.KAHMANN,
JRNL AUTH 2 P.TERIETE,A.R.PICKFORD,I.D.CAMPBELL,A.J.DAY
JRNL TITL THE LINK MODULE FROM OVULATION- AND INFLAMMATION-ASSOCIATED
JRNL TITL 2 PROTEIN TSG-6 CHANGES CONFORMATION ON HYALURONAN BINDING.
JRNL REF J. BIOL. CHEM. V. 278 49261 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12972412
JRNL DOI 10.1074/JBC.M309623200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.GETTING,D.J.MAHONEY,T.CAO,M.S.RUGG,E.FRIES,C.M.MILNER,
REMARK 1 AUTH 2 M.PERRETTI,A.J.DAY
REMARK 1 TITL THE LINK MODULE FROM HUMAN TSG-6 INHIBITS NEUTROPHIL
REMARK 1 TITL 2 MIGRATION IN A HYALURONAN- AND INTER-ALPHA
REMARK 1 TITL 3 -INHIBITOR-INDEPENDENT MANNER
REMARK 1 REF J.BIOL.CHEM. V. 277 51068 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12401803
REMARK 1 DOI 10.1074/JBC.M205121200
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.LESLEY,N.M.ENGLISH,I.GAL,K.MIKECZ,A.J.DAY,R.HYMAN
REMARK 1 TITL HYALURONAN BINDING PROPERTIES OF A CD44 CHIMERA CONTAINING
REMARK 1 TITL 2 THE LINK MODULE OF TSG-6
REMARK 1 REF J.BIOL.CHEM. V. 277 26600 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12011075
REMARK 1 DOI 10.1074/JBC.M201068200
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.J.MAHONEY,C.D.BLUNDELL,A.J.DAY
REMARK 1 TITL MAPPING THE HYALURONAN-BINDING SITE ON THE LINK MODULE FROM
REMARK 1 TITL 2 HUMAN TUMOR NECROSIS FACTOR-STIMULATED GENE-6 BY
REMARK 1 TITL 3 SITE-DIRECTED MUTAGENESIS
REMARK 1 REF J.BIOL.CHEM. V. 276 22764 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11287417
REMARK 1 DOI 10.1074/JBC.M100666200
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.D.KAHMANN,R.O'BRIEN,J.M.WERNER,D.HEINEGARD,J.E.LADBURY,
REMARK 1 AUTH 2 I.D.CAMPBELL,A.J.DAY
REMARK 1 TITL LOCALIZATION AND CHARACTERIZATION OF THE HYALURONAN-BINDING
REMARK 1 TITL 2 SITE ON THE LINK MODULE FROM HUMAN TSG-6
REMARK 1 REF STRUCTURE V. 8 763 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10903951
REMARK 1 DOI 10.1016/S0969-2126(00)00163-5
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.D.KAHMANN,R.KORUTH,A.J.DAY
REMARK 1 TITL METHOD FOR QUANTITATIVE REFOLDING OF THE LINK MODULE FROM
REMARK 1 TITL 2 HUMAN TSG-6
REMARK 1 REF PROTEIN EXPR.PURIF. V. 9 315 1997
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 9126602
REMARK 1 DOI 10.1006/PREP.1996.0694
REMARK 1 REFERENCE 6
REMARK 1 AUTH A.J.DAY,R.T.APLIN,A.C.WILLIS
REMARK 1 TITL OVEREXPRESSION, PURIFICATION, AND REFOLDING OF LINK MODULE
REMARK 1 TITL 2 FROM HUMAN TSG-6 IN ESCHERICHIA COLI: EFFECT OF TEMPERATURE,
REMARK 1 TITL 3 MEDIA, AND MUTAGENESIS ON LYSINE MISINCORPORATION AT
REMARK 1 TITL 4 ARGININE AGA CODONS
REMARK 1 REF PROTEIN EXPR.PURIF. V. 8 1 1996
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 8812829
REMARK 1 DOI 10.1006/PREP.1996.0068
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.KOHDA,C.J.MORTON,A.A.PARKAR,H.HATANAKA,F.M.INAGAKI,
REMARK 1 AUTH 2 I.D.CAMPBELL,A.J.DAY
REMARK 1 TITL SOLUTION STRUCTURE OF THE LINK MODULE: A HYALURONAN-BINDING
REMARK 1 TITL 2 DOMAIN INVOLVED IN EXTRACELLULAR MATRIX STABILITY AND CELL
REMARK 1 TITL 3 MIGRATION
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 86 767 1996
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 8797823
REMARK 1 DOI 10.1016/S0092-8674(00)80151-8
REMARK 1 REFERENCE 8
REMARK 1 AUTH T.H.LEE,H.G.WISNIEWSKI,J.VILCEK
REMARK 1 TITL A NOVEL SECRETORY TUMOUR NECROSIS FACTOR-INDUCIBLE PROTEIN
REMARK 1 TITL 2 (TSG-6) IS A MEMBER OF THE FAMILY OF HYALURONATE BINDING
REMARK 1 TITL 3 PROTEINS, CLOSELY RELATED TO THE ADHESION RECEPTOR CD44
REMARK 1 REF J.CELL BIOL. V. 116 545 1992
REMARK 1 REFN ISSN 0021-9525
REMARK 1 PMID 1730767
REMARK 1 DOI 10.1083/JCB.116.2.545
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1O7B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1290011608.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : ~2MM NA IONS
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O, 1-3MM LINK_TSG6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY-HSQC; 15N-HSQC-NOESY
REMARK 210 -HSQC; 13C-NOESY-HSQC; 2D-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : HOMEBUILT
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.3, XEASY, CNS
REMARK 210 METHOD USED : AB INITIO SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 250
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE DETERMINED BY NMR SPECTROSCOPY ON UNIFORMLY 15N-
REMARK 210 AND 13C,15N-LABELLED LINK_TSG6
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: T
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 400
REMARK 400 COMPOUND
REMARK 400 POSSIBLE ROLE IN CELL-MATRIX INTERACTIONS DURING INFLAMMATION
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 GLU T 6 -169.07 -103.73
REMARK 500 1 ALA T 7 -170.87 -64.23
REMARK 500 1 SER T 9 -19.02 -164.37
REMARK 500 1 LYS T 13 33.33 -174.07
REMARK 500 1 THR T 15 -159.06 -105.75
REMARK 500 1 ALA T 31 -165.74 -60.02
REMARK 500 1 ALA T 49 129.23 -38.94
REMARK 500 1 ALA T 53 -164.27 46.51
REMARK 500 1 LYS T 54 -17.10 -47.69
REMARK 500 1 CYS T 68 -77.22 -155.91
REMARK 500 1 LEU T 82 17.83 54.18
REMARK 500 1 ASN T 83 108.73 -165.89
REMARK 500 1 TRP T 88 -158.98 -137.30
REMARK 500 1 ASP T 89 -141.65 -107.92
REMARK 500 1 CYS T 92 172.08 -56.51
REMARK 500 1 ASN T 94 119.94 -170.17
REMARK 500 1 HIS T 96 -45.84 -131.43
REMARK 500 1 ALA T 97 53.04 33.26
REMARK 500 2 GLU T 6 -168.35 -102.50
REMARK 500 2 ALA T 7 -174.67 -61.45
REMARK 500 2 SER T 9 -16.27 -168.72
REMARK 500 2 LYS T 13 23.00 -167.89
REMARK 500 2 THR T 15 -161.86 -104.78
REMARK 500 2 ALA T 31 -166.57 -60.16
REMARK 500 2 LYS T 54 -8.95 67.83
REMARK 500 2 CYS T 68 -75.68 -170.81
REMARK 500 2 LEU T 82 -18.40 69.46
REMARK 500 2 TRP T 88 -145.19 -126.54
REMARK 500 2 ASP T 89 -138.49 -122.54
REMARK 500 2 ALA T 90 113.87 -166.34
REMARK 500 2 CYS T 92 163.08 -49.72
REMARK 500 3 GLU T 6 -167.39 -129.19
REMARK 500 3 SER T 9 23.85 -169.30
REMARK 500 3 TYR T 12 59.43 38.88
REMARK 500 3 LYS T 13 18.97 -153.38
REMARK 500 3 THR T 15 -161.34 -102.34
REMARK 500 3 ALA T 31 -167.06 -56.05
REMARK 500 3 PRO T 60 91.58 -66.58
REMARK 500 3 VAL T 62 -27.10 -141.80
REMARK 500 3 PRO T 64 159.42 -49.62
REMARK 500 3 PRO T 66 6.22 -65.75
REMARK 500 3 ASN T 67 60.52 178.51
REMARK 500 3 CYS T 68 -69.50 -165.23
REMARK 500 3 LEU T 82 15.37 56.16
REMARK 500 3 ARG T 84 34.71 -79.26
REMARK 500 3 CYS T 92 172.83 -57.13
REMARK 500 3 ASN T 94 119.98 -166.34
REMARK 500 3 ALA T 97 44.85 -85.83
REMARK 500 4 ALA T 7 -170.67 -60.26
REMARK 500 4 SER T 9 1.57 -163.63
REMARK 500
REMARK 500 THIS ENTRY HAS 311 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TSG RELATED DB: PDB
REMARK 900 NMR STUDY OF THE LINK MODULE FROM TSG-6 MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1O7C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE IN THE PRESENCE
REMARK 900 OF A HYALURONAN OCTASACCHARIDE
REMARK 900 RELATED ID: 6392 RELATED DB: BMRB
DBREF 1O7B T 1 98 UNP P98066 TSG6_HUMAN 36 133
SEQRES 1 T 98 GLY VAL TYR HIS ARG GLU ALA ARG SER GLY LYS TYR LYS
SEQRES 2 T 98 LEU THR TYR ALA GLU ALA LYS ALA VAL CYS GLU PHE GLU
SEQRES 3 T 98 GLY GLY HIS LEU ALA THR TYR LYS GLN LEU GLU ALA ALA
SEQRES 4 T 98 ARG LYS ILE GLY PHE HIS VAL CYS ALA ALA GLY TRP MET
SEQRES 5 T 98 ALA LYS GLY ARG VAL GLY TYR PRO ILE VAL LYS PRO GLY
SEQRES 6 T 98 PRO ASN CYS GLY PHE GLY LYS THR GLY ILE ILE ASP TYR
SEQRES 7 T 98 GLY ILE ARG LEU ASN ARG SER GLU ARG TRP ASP ALA TYR
SEQRES 8 T 98 CYS TYR ASN PRO HIS ALA LYS
HELIX 1 1 TYR T 16 PHE T 25 1 10
HELIX 2 2 TYR T 33 ILE T 42 1 10
SHEET 1 TA 3 VAL T 2 ARG T 5 0
SHEET 2 TA 3 ASP T 89 TYR T 93 -1 O ALA T 90 N ARG T 5
SHEET 3 TA 3 HIS T 29 ALA T 31 -1 O HIS T 29 N TYR T 93
SHEET 1 TB 3 VAL T 2 ARG T 5 0
SHEET 2 TB 3 ASP T 89 TYR T 93 -1 O ALA T 90 N ARG T 5
SHEET 3 TB 3 ALA T 49 MET T 52 1 O TRP T 51 N TYR T 91
SHEET 1 TC 2 ARG T 56 ILE T 61 0
SHEET 2 TC 2 GLY T 74 ASP T 77 -1 O GLY T 74 N ILE T 61
SSBOND 1 CYS T 23 CYS T 92 1555 1555 2.03
SSBOND 2 CYS T 47 CYS T 68 1555 1555 2.03
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 - n 24 2 Bytes