Header list of 1qo6.pdb file
Complete list - n 17 2 Bytes
HEADER CELL ADHESION PROTEIN 04-NOV-99 1QO6
TITLE SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING
TITLE 2 DOMAIN OF FIBRONECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIBRONECTIN TYPE-I AND FIBRONECTIN TYPE-II MODULE PAIR FROM
COMPND 5 COLLAGEN-BINDING DOMAIN;
COMPND 6 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: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115
KEYWDS CELL ADHESION PROTEIN, FIBRONECTIN MODULE PAIR, GELATIN-BINDING
EXPDTA SOLUTION NMR
NUMMDL 55
AUTHOR A.A.BOCQUIER,J.R.POTTS,A.R.PICKFORD,I.D.CAMPBELL
REVDAT 3 17-JAN-18 1QO6 1 REMARK
REVDAT 2 24-FEB-09 1QO6 1 VERSN
REVDAT 1 11-JAN-00 1QO6 0
JRNL AUTH A.A.BOCQUIER,J.R.POTTS,A.R.PICKFORD,I.D.CAMPBELL
JRNL TITL SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE
JRNL TITL 2 GELATIN-BINDING DOMAIN OF FIBRONECTIN
JRNL REF STRUCTURE V. 7 1451 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10647176
JRNL DOI 10.1016/S0969-2126(00)88336-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JOURNAL CITATION ABOVE
REMARK 4
REMARK 4 1QO6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1290004354.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; NOESY-HSQC;
REMARK 210 TOCSY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : OXFORD
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 55
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY AND AGREEMENT WITH
REMARK 210 EXPERIMENTAL RESTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE FAMILY OF STRUCTURES HAS BEEN ALIGNED USING THE C, CA,
REMARK 210 N ATOMS OF RESIDUES LEU19, LEU28, PRO59 AND TYR68 OF THE
REMARK 210 INTERMODULE INTERFACE.
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 H THR A 30 O SER A 37 1.57
REMARK 500 H CYS A 82 O SER A 95 1.58
REMARK 500 H VAL A 57 O SER A 83 1.58
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 TYR A 12 -172.17 -64.75
REMARK 500 1 VAL A 14 87.12 -43.18
REMARK 500 1 MET A 16 51.41 -114.88
REMARK 500 1 GLN A 17 128.86 -31.35
REMARK 500 1 ASN A 24 -35.23 179.51
REMARK 500 1 LEU A 32 -96.89 -79.50
REMARK 500 1 THR A 41 -53.57 75.39
REMARK 500 1 ALA A 42 -62.23 71.55
REMARK 500 1 VAL A 43 -178.76 -67.45
REMARK 500 1 PRO A 55 98.83 -62.18
REMARK 500 1 CYS A 56 171.82 -49.02
REMARK 500 1 ARG A 65 -166.61 -103.07
REMARK 500 1 CYS A 70 172.90 -47.68
REMARK 500 1 THR A 71 157.55 179.58
REMARK 500 1 SER A 86 -29.29 -39.88
REMARK 500 1 ASN A 87 79.39 -111.20
REMARK 500 1 THR A 98 -73.42 -94.70
REMARK 500 1 ASP A 99 -59.27 80.49
REMARK 500 1 HIS A 100 -73.94 -119.62
REMARK 500 2 HIS A 3 157.53 -38.39
REMARK 500 2 THR A 6 -38.20 -37.29
REMARK 500 2 ASP A 7 -42.96 -179.51
REMARK 500 2 SER A 8 56.16 176.80
REMARK 500 2 VAL A 14 86.27 -49.14
REMARK 500 2 MET A 16 48.49 -88.80
REMARK 500 2 GLN A 17 151.37 -30.85
REMARK 500 2 ASN A 24 -36.14 -176.11
REMARK 500 2 LYS A 25 -145.52 -120.89
REMARK 500 2 MET A 27 114.63 -176.86
REMARK 500 2 LEU A 32 -86.37 -79.08
REMARK 500 2 GLU A 40 101.43 -55.00
REMARK 500 2 THR A 41 -54.43 74.75
REMARK 500 2 ALA A 42 96.28 80.90
REMARK 500 2 VAL A 43 -157.78 -142.64
REMARK 500 2 THR A 46 133.93 57.33
REMARK 500 2 SER A 51 -80.03 -114.14
REMARK 500 2 ASN A 52 -31.03 174.99
REMARK 500 2 PRO A 55 107.18 -58.27
REMARK 500 2 CYS A 56 159.42 -48.77
REMARK 500 2 VAL A 57 71.48 -118.14
REMARK 500 2 ARG A 65 -165.67 -104.72
REMARK 500 2 SER A 69 -161.59 -179.24
REMARK 500 2 THR A 72 68.71 -117.13
REMARK 500 2 ASP A 99 -56.07 77.75
REMARK 500 3 THR A 6 -44.17 -156.79
REMARK 500 3 ASP A 7 12.58 -141.51
REMARK 500 3 VAL A 11 82.07 -69.33
REMARK 500 3 TYR A 12 -170.83 -63.99
REMARK 500 3 VAL A 14 87.67 -46.11
REMARK 500 3 MET A 16 50.56 -103.16
REMARK 500
REMARK 500 THIS ENTRY HAS 1107 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TTF RELATED DB: PDB
REMARK 900 HUMAN FIBRONECTIN (TENTH TYPE III MODULE) (NMR, 36 STRUCTURES)
REMARK 900 RELATED ID: 1TTG RELATED DB: PDB
REMARK 900 HUMAN FIBRONECTIN (TENTH TYPE III MODULE) (NMR, RESTRAINED
REMARK 900 MINIMIZED AVERAGE STRUCTURE)
REMARK 900 RELATED ID: 1FNA RELATED DB: PDB
REMARK 900 HUMAN FIBRONECTIN CELL-ADHESION MODULE TYPE III-10
REMARK 900 RELATED ID: 1FNF RELATED DB: PDB
REMARK 900 HUMAN FRAGMENT OF HUMAN FIBRONECTIN ENCOMPASSING TYPE-III REPEATS 7
REMARK 900 THROUGH 10
REMARK 900 RELATED ID: 1FBR RELATED DB: PDB
REMARK 900 HUMAN FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR
REMARK 900 RELATED ID: 1FNH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEPARIN AND INTEGRIN BINDING SEGMENT OF HUMAN
REMARK 900 FIBRONECTIN
REMARK 900 RELATED ID: 2FN2 RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED SECOND TYPE TWO MODULE
REMARK 900 OF FIBRONECTIN, 20 STRUCTURES
DBREF 1QO6 A 1 101 UNP P02751 FINC_HUMAN 305 405
SEQRES 1 A 101 TYR GLY HIS CYS VAL THR ASP SER GLY VAL VAL TYR SER
SEQRES 2 A 101 VAL GLY MET GLN TRP LEU LYS THR GLN GLY ASN LYS GLN
SEQRES 3 A 101 MET LEU CYS THR CYS LEU GLY ASN GLY VAL SER CYS GLN
SEQRES 4 A 101 GLU THR ALA VAL THR GLN THR TYR GLY GLY ASN SER ASN
SEQRES 5 A 101 GLY GLU PRO CYS VAL LEU PRO PHE THR TYR ASN GLY ARG
SEQRES 6 A 101 THR PHE TYR SER CYS THR THR GLU GLY ARG GLN ASP GLY
SEQRES 7 A 101 HIS LEU TRP CYS SER THR THR SER ASN TYR GLU GLN ASP
SEQRES 8 A 101 GLN LYS TYR SER PHE CYS THR ASP HIS THR
SHEET 1 A 3 TRP A 18 THR A 21 0
SHEET 2 A 3 GLN A 26 THR A 30 -1 N CYS A 29 O TRP A 18
SHEET 3 A 3 SER A 37 GLU A 40 -1 N GLN A 39 O LEU A 28
SHEET 1 B 2 PHE A 60 TYR A 62 0
SHEET 2 B 2 ARG A 65 PHE A 67 -1 N PHE A 67 O PHE A 60
SHEET 1 C 2 LEU A 80 SER A 83 0
SHEET 2 C 2 TYR A 94 CYS A 97 -1 N CYS A 97 O LEU A 80
SSBOND 1 CYS A 4 CYS A 31 1555 1555 2.03
SSBOND 2 CYS A 29 CYS A 38 1555 1555 2.03
SSBOND 3 CYS A 56 CYS A 82 1555 1555 2.03
SSBOND 4 CYS A 70 CYS A 97 1555 1555 2.03
CISPEP 1 LEU A 58 PRO A 59 1 0.06
CISPEP 2 LEU A 58 PRO A 59 2 -0.07
CISPEP 3 LEU A 58 PRO A 59 3 0.19
CISPEP 4 LEU A 58 PRO A 59 4 0.09
CISPEP 5 LEU A 58 PRO A 59 5 0.00
CISPEP 6 LEU A 58 PRO A 59 6 0.13
CISPEP 7 LEU A 58 PRO A 59 7 0.01
CISPEP 8 LEU A 58 PRO A 59 8 0.24
CISPEP 9 LEU A 58 PRO A 59 9 0.15
CISPEP 10 LEU A 58 PRO A 59 10 0.13
CISPEP 11 LEU A 58 PRO A 59 11 0.09
CISPEP 12 LEU A 58 PRO A 59 12 0.10
CISPEP 13 LEU A 58 PRO A 59 13 0.34
CISPEP 14 LEU A 58 PRO A 59 14 0.13
CISPEP 15 LEU A 58 PRO A 59 15 0.29
CISPEP 16 LEU A 58 PRO A 59 16 0.07
CISPEP 17 LEU A 58 PRO A 59 17 0.04
CISPEP 18 LEU A 58 PRO A 59 18 0.07
CISPEP 19 LEU A 58 PRO A 59 19 0.29
CISPEP 20 LEU A 58 PRO A 59 20 0.09
CISPEP 21 LEU A 58 PRO A 59 21 0.09
CISPEP 22 LEU A 58 PRO A 59 22 0.18
CISPEP 23 LEU A 58 PRO A 59 23 0.00
CISPEP 24 LEU A 58 PRO A 59 24 -0.02
CISPEP 25 LEU A 58 PRO A 59 25 0.16
CISPEP 26 LEU A 58 PRO A 59 26 0.23
CISPEP 27 LEU A 58 PRO A 59 27 0.08
CISPEP 28 LEU A 58 PRO A 59 28 0.00
CISPEP 29 LEU A 58 PRO A 59 29 0.26
CISPEP 30 LEU A 58 PRO A 59 30 0.21
CISPEP 31 LEU A 58 PRO A 59 31 0.08
CISPEP 32 LEU A 58 PRO A 59 32 0.26
CISPEP 33 LEU A 58 PRO A 59 33 -0.05
CISPEP 34 LEU A 58 PRO A 59 34 0.23
CISPEP 35 LEU A 58 PRO A 59 35 0.11
CISPEP 36 LEU A 58 PRO A 59 36 -0.07
CISPEP 37 LEU A 58 PRO A 59 37 0.05
CISPEP 38 LEU A 58 PRO A 59 38 -0.06
CISPEP 39 LEU A 58 PRO A 59 39 0.46
CISPEP 40 LEU A 58 PRO A 59 40 0.20
CISPEP 41 LEU A 58 PRO A 59 41 0.20
CISPEP 42 LEU A 58 PRO A 59 42 0.16
CISPEP 43 LEU A 58 PRO A 59 43 0.24
CISPEP 44 LEU A 58 PRO A 59 44 0.09
CISPEP 45 LEU A 58 PRO A 59 45 0.15
CISPEP 46 LEU A 58 PRO A 59 46 0.23
CISPEP 47 LEU A 58 PRO A 59 47 0.19
CISPEP 48 LEU A 58 PRO A 59 48 0.13
CISPEP 49 LEU A 58 PRO A 59 49 -0.21
CISPEP 50 LEU A 58 PRO A 59 50 0.12
CISPEP 51 LEU A 58 PRO A 59 51 0.25
CISPEP 52 LEU A 58 PRO A 59 52 0.07
CISPEP 53 LEU A 58 PRO A 59 53 0.10
CISPEP 54 LEU A 58 PRO A 59 54 -0.12
CISPEP 55 LEU A 58 PRO A 59 55 -0.03
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 17 2 Bytes