HEADER CELL ADHESION PROTEIN 08-AUG-95 1FBR
TITLE FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
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 TISSUE: PLASMA;
SOURCE 6 GENE: HUMAN FIBRONECTIN;
SOURCE 7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMA91;
SOURCE 11 EXPRESSION_SYSTEM_GENE: HUMAN FIBRONECTIN;
SOURCE 12 OTHER_DETAILS: EXTRACELLULAR
KEYWDS CELL ADHESION PROTEIN
EXPDTA SOLUTION NMR
AUTHOR I.Q.H.PHAN,M.J.WILLIAMS,I.D.CAMPBELL
REVDAT 4 23-FEB-22 1FBR 1 REMARK
REVDAT 3 24-FEB-09 1FBR 1 VERSN
REVDAT 2 01-APR-03 1FBR 1 JRNL
REVDAT 1 15-OCT-95 1FBR 0
JRNL AUTH M.J.WILLIAMS,I.PHAN,T.S.HARVEY,A.ROSTAGNO,L.I.GOLD,
JRNL AUTH 2 I.D.CAMPBELL
JRNL TITL SOLUTION STRUCTURE OF A PAIR OF FIBRONECTIN TYPE 1 MODULES
JRNL TITL 2 WITH FIBRIN BINDING ACTIVITY.
JRNL REF J.MOL.BIOL. V. 235 1302 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8308892
JRNL DOI 10.1006/JMBI.1994.1083
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FBR 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_1000173226.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 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 CYS A 4 64.14 -118.60
REMARK 500 HIS A 7 -82.79 54.90
REMARK 500 TYR A 23 -120.07 -69.60
REMARK 500 GLN A 24 -88.04 -43.85
REMARK 500 MET A 27 158.10 -46.75
REMARK 500 ARG A 59 -164.28 -124.89
REMARK 500 LYS A 67 -178.41 -63.39
REMARK 500 ASP A 68 -95.22 -110.05
REMARK 500 ASN A 69 10.22 -143.12
REMARK 500 ASN A 72 -155.80 -66.61
REMARK 500 GLN A 75 87.78 -66.68
REMARK 500 ASN A 81 53.71 -141.45
REMARK 500 ARG A 83 25.42 -151.91
REMARK 500 TRP A 86 101.59 -56.53
REMARK 500 ARG A 90 174.36 -50.19
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 40 0.29 SIDE CHAIN
REMARK 500 ARG A 46 0.26 SIDE CHAIN
REMARK 500 ARG A 48 0.20 SIDE CHAIN
REMARK 500 ARG A 55 0.24 SIDE CHAIN
REMARK 500 ARG A 59 0.32 SIDE CHAIN
REMARK 500 ARG A 70 0.26 SIDE CHAIN
REMARK 500 ARG A 83 0.12 SIDE CHAIN
REMARK 500 ARG A 90 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FBR A 1 93 UNP P02751 FINC_HUMAN 183 275
SEQRES 1 A 93 ALA GLU LYS CYS PHE ASP HIS ALA ALA GLY THR SER TYR
SEQRES 2 A 93 VAL VAL GLY GLU THR TRP GLU LYS PRO TYR GLN GLY TRP
SEQRES 3 A 93 MET MET VAL ASP CYS THR CYS LEU GLY GLU GLY SER GLY
SEQRES 4 A 93 ARG ILE THR CYS THR SER ARG ASN ARG CYS ASN ASP GLN
SEQRES 5 A 93 ASP THR ARG THR SER TYR ARG ILE GLY ASP THR TRP SER
SEQRES 6 A 93 LYS LYS ASP ASN ARG GLY ASN LEU LEU GLN CYS ILE CYS
SEQRES 7 A 93 THR GLY ASN GLY ARG GLY GLU TRP LYS CYS GLU ARG HIS
SEQRES 8 A 93 THR SER
SHEET 1 A 2 LYS A 3 ASP A 6 0
SHEET 2 A 2 THR A 11 VAL A 14 -1
SHEET 1 B 3 THR A 18 PRO A 22 0
SHEET 2 B 3 MET A 28 CYS A 33 -1 O CYS A 31 N TRP A 19
SHEET 3 B 3 ILE A 41 SER A 45 -1 O THR A 44 N ASP A 30
SHEET 1 C 2 ARG A 48 ASP A 51 0
SHEET 2 C 2 THR A 56 ARG A 59 -1
SHEET 1 D 3 THR A 63 LYS A 67 0
SHEET 2 D 3 LEU A 73 CYS A 78 -1 O CYS A 76 N TRP A 64
SHEET 3 D 3 TRP A 86 ARG A 90 -1 O GLU A 89 N GLN A 75
SSBOND 1 CYS A 4 CYS A 33 1555 1555 2.02
SSBOND 2 CYS A 31 CYS A 43 1555 1555 2.02
SSBOND 3 CYS A 49 CYS A 78 1555 1555 2.02
SSBOND 4 CYS A 76 CYS A 88 1555 1555 2.02
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
(ATOM LINES ARE NOT SHOWN.)
END