Header list of 1o9a.pdb file
Complete list - n 24 2 Bytes
HEADER CELL ADHESION 11-DEC-02 1O9A
TITLE SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3
TITLE 2 FROM FNBB FROM S. DYSGALACTIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL F1 MODULE PAIR, RESIDUES 48-140;
COMPND 5 SYNONYM: COLD-INSOLUBLE GLOBULIN, FN, CIG;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FIBRONECTIN BINDING PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: B3 FIBRONECTIN-BINDING REPEAT, RESIDUES 1031-1066;
COMPND 11 SYNONYM: FNBB;
COMPND 12 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 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: STREPTOCOCCUS DYSGALACTIAE;
SOURCE 10 ORGANISM_TAXID: 1334
KEYWDS CELL ADHESION-COMPLEX, HOST-PATHOGEN PROTEIN COMPLEX, CELL ADHESION,
KEYWDS 2 FIBRONECTIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR U.SCHWARZ-LINEK,J.M.WERNER,A.R.PICKFORD,E.S.PILKA,S.GURUSIDDAPPA,
AUTHOR 2 J.A.G.BRIGGS,M.HOOK,I.D.CAMPBELL,J.R.POTTS
REVDAT 4 24-JAN-18 1O9A 1 JRNL REMARK
REVDAT 3 15-APR-15 1O9A 1 JRNL REMARK VERSN
REVDAT 2 24-FEB-09 1O9A 1 VERSN
REVDAT 1 08-MAY-03 1O9A 0
JRNL AUTH U.SCHWARZ-LINEK,J.M.WERNER,A.R.PICKFORD,S.GURUSIDDAPPA,
JRNL AUTH 2 J.H.KIM,E.S.PILKA,J.A.BRIGGS,T.S.GOUGH,M.HOOK,I.D.CAMPBELL,
JRNL AUTH 3 J.R.POTTS
JRNL TITL PATHOGENIC BACTERIA ATTACH TO HUMAN FIBRONECTIN THROUGH A
JRNL TITL 2 TANDEM BETA-ZIPPER.
JRNL REF NATURE V. 423 177 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12736686
JRNL DOI 10.1038/NATURE01589
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FURTHER REFINEMENT DETAILS CAN BE FOUND
REMARK 3 IN THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 1O9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1290011850.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; 15N-NOESY
REMARK 210 -HSQC; 15N-TOCSY-HSQC; HNCO;
REMARK 210 CCCONH; 13C-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING NMR SPECTROSCOPY ON
REMARK 210 UNLABELLED, 15N-, 2H,15N- AND 15N,13C-LABELLED 1F12F1 IN COMPLEX
REMARK 210 WITH UNLABELLED B3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 FIBRONECTINS BIND CELL SURFACES AND VARIOUS COMPOUNDS
REMARK 400 INCLUDING COLLAGEN, FIBRIN, HEPARIN, DNA, AND ACTIN.
REMARK 400 THEY ARE ALSO INVOLVED IN CELL ADHESION, CELL MOTILITY,
REMARK 400 OPSONIZATION, WOUND HEALING, AND MAINTENANCE OF CELL SHAPE
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 GLU B 1
REMARK 465 GLU B 2
REMARK 465 SER B 3
REMARK 465 LEU B 4
REMARK 465 PRO B 5
REMARK 465 THR B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 GLY B 9
REMARK 465 GLN B 10
REMARK 465 SER B 11
REMARK 465 GLY B 12
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 PRO A 19 102.28 -57.07
REMARK 500 1 ASN A 24 -1.81 -59.07
REMARK 500 1 LEU A 39 -36.95 72.02
REMARK 500 1 GLU A 61 -168.40 -75.35
REMARK 500 1 GLU A 63 64.40 -102.11
REMARK 500 1 LYS A 85 133.87 -174.21
REMARK 500 1 SER A 87 9.68 55.44
REMARK 500 1 MET A 88 -165.51 -124.34
REMARK 500 1 ARG A 99 -83.15 -145.24
REMARK 500 1 ALA A 107 68.44 -167.15
REMARK 500 1 GLU B 16 -62.13 -141.27
REMARK 500 1 VAL B 17 109.71 62.03
REMARK 500 1 ASP B 19 -163.28 55.99
REMARK 500 1 SER B 20 -72.81 -146.36
REMARK 500 1 LYS B 21 70.29 -150.26
REMARK 500 1 PRO B 22 93.08 -58.53
REMARK 500 1 LYS B 23 -174.91 58.32
REMARK 500 1 LEU B 24 120.48 -174.15
REMARK 500 1 ILE B 26 -168.69 -104.84
REMARK 500 1 HIS B 27 51.34 -164.12
REMARK 500 1 GLU B 35 84.18 56.69
REMARK 500 2 ASN A 24 86.04 -45.68
REMARK 500 2 LEU A 39 -4.91 60.17
REMARK 500 2 TYR A 48 -76.20 -105.14
REMARK 500 2 PRO A 60 -169.13 -72.00
REMARK 500 2 ALA A 62 -38.64 -175.44
REMARK 500 2 GLU A 64 -167.89 51.91
REMARK 500 2 THR A 65 167.84 53.19
REMARK 500 2 THR A 71 -9.75 -143.20
REMARK 500 2 VAL A 77 109.53 -58.86
REMARK 500 2 ASP A 86 -62.39 74.66
REMARK 500 2 SER A 87 4.42 -172.83
REMARK 500 2 MET A 88 -163.11 -125.48
REMARK 500 2 ARG A 99 49.91 -160.48
REMARK 500 2 ALA A 107 69.43 -169.12
REMARK 500 2 GLU B 16 63.28 -155.31
REMARK 500 2 ASP B 19 79.46 54.74
REMARK 500 2 PRO B 22 173.27 -59.25
REMARK 500 2 SER B 25 112.75 -162.23
REMARK 500 2 HIS B 27 51.36 -110.04
REMARK 500 2 ASN B 30 -49.75 -143.63
REMARK 500 2 TRP B 32 96.08 57.41
REMARK 500 2 GLU B 35 -165.50 57.41
REMARK 500 3 ASN A 24 86.29 -46.41
REMARK 500 3 LEU A 39 -33.71 72.40
REMARK 500 3 THR A 46 -164.46 -106.92
REMARK 500 3 TYR A 48 -31.49 -131.22
REMARK 500 3 GLU A 61 -174.05 -67.64
REMARK 500 3 ALA A 62 -47.96 -133.59
REMARK 500 3 GLU A 63 60.42 -104.29
REMARK 500
REMARK 500 THIS ENTRY HAS 312 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E88 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF 6F11F22F2, A COMPACT THREE-MODULE FRAGMENT OF
REMARK 900 THE GELATIN-BINDING DOMAIN OF HUMAN FIBRONECTIN
REMARK 900 RELATED ID: 1E8B RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF 6F11F22F2, A COMPACT THREE-MODULE FRAGMENT OF
REMARK 900 THE GELATIN-BINDING DOMAIN OF HUMAN FIBRONECTIN
REMARK 900 RELATED ID: 1FBR RELATED DB: PDB
REMARK 900 FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR
REMARK 900 RELATED ID: 1FNA RELATED DB: PDB
REMARK 900 FIBRONECTIN CELL-ADHESION MODULE TYPE III-10
REMARK 900 RELATED ID: 1FNF RELATED DB: PDB
REMARK 900 FRAGMENT OF HUMAN FIBRONECTIN ENCOMPASSING TYPE-III REPEATS 7
REMARK 900 THROUGH 10
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: 1J8K RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE FIBRONECTIN EDA DOMAIN , NMR, 20STRUCTURES
REMARK 900 RELATED ID: 1QGB RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN
REMARK 900 FIBRONECTIN
REMARK 900 RELATED ID: 1QO6 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING
REMARK 900 DOMAIN OF FIBRONECTIN
REMARK 900 RELATED ID: 1TTF RELATED DB: PDB
REMARK 900 FIBRONECTIN (TENTH TYPE III MODULE) (NMR, 36 STRUCTURES)
REMARK 900 RELATED ID: 1TTG RELATED DB: PDB
REMARK 900 FIBRONECTIN (TENTH TYPE III MODULE) (NMR, RESTRAINED MINIMIZED
REMARK 900 AVERAGE STRUCTURE)
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 1O9A A 17 109 UNP P02751 FINC_HUMAN 48 140
DBREF 1O9A B 1 36 UNP Q53971 Q53971 1031 1066
SEQRES 1 A 93 SER LYS PRO GLY CYS TYR ASP ASN GLY LYS HIS TYR GLN
SEQRES 2 A 93 ILE ASN GLN GLN TRP GLU ARG THR TYR LEU GLY ASN ALA
SEQRES 3 A 93 LEU VAL CYS THR CYS TYR GLY GLY SER ARG GLY PHE ASN
SEQRES 4 A 93 CYS GLU SER LYS PRO GLU ALA GLU GLU THR CYS PHE ASP
SEQRES 5 A 93 LYS TYR THR GLY ASN THR TYR ARG VAL GLY ASP THR TYR
SEQRES 6 A 93 GLU ARG PRO LYS ASP SER MET ILE TRP ASP CYS THR CYS
SEQRES 7 A 93 ILE GLY ALA GLY ARG GLY ARG ILE SER CYS THR ILE ALA
SEQRES 8 A 93 ASN ARG
SEQRES 1 B 36 GLU GLU SER LEU PRO THR GLU GLN GLY GLN SER GLY SER
SEQRES 2 B 36 THR THR GLU VAL GLU ASP SER LYS PRO LYS LEU SER ILE
SEQRES 3 B 36 HIS PHE ASP ASN GLU TRP PRO LYS GLU ASP
SHEET 1 AA 2 CYS A 21 ASP A 23 0
SHEET 2 AA 2 LYS A 26 TYR A 28 -1 O LYS A 26 N ASP A 23
SHEET 1 AB 4 GLN A 33 THR A 37 0
SHEET 2 AB 4 ALA A 42 CYS A 47 -1 O LEU A 43 N ARG A 36
SHEET 3 AB 4 PHE A 54 SER A 58 -1 O ASN A 55 N THR A 46
SHEET 4 AB 4 LEU B 24 HIS B 27 -1 O LEU B 24 N SER A 58
SHEET 1 AC 2 CYS A 66 ASP A 68 0
SHEET 2 AC 2 ASN A 73 TYR A 75 -1 O ASN A 73 N ASP A 68
SHEET 1 AD 4 THR A 80 PRO A 84 0
SHEET 2 AD 4 TRP A 90 ILE A 95 -1 O TRP A 90 N ARG A 83
SHEET 3 AD 4 ILE A 102 ILE A 106 -1 O SER A 103 N THR A 93
SHEET 4 AD 4 THR B 14 VAL B 17 -1 O THR B 14 N ILE A 106
SSBOND 1 CYS A 21 CYS A 47 1555 1555 2.03
SSBOND 2 CYS A 45 CYS A 56 1555 1555 2.03
SSBOND 3 CYS A 66 CYS A 94 1555 1555 2.03
SSBOND 4 CYS A 92 CYS A 104 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