Header list of 1q38.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 28-JUL-03 1Q38
TITLE ANASTELLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYPE 3 (FN3) DOMAIN;
COMPND 5 SYNONYM: FN, COLD-INSOLUBLE GLOBULIN, CIG, ANASTELLIN;
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 GENE: FN1 OR FN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMYLOID FIBRIL, ANASTELLIN, EXTRACELLULAR MATRIX, FIBRONECTIN TYPE 3
KEYWDS 2 (FN3) DOMAIN, DYNAMIC FLUCTUATIONS, CONFORMATIONAL EXCHANGE, CHAPS,
KEYWDS 3 CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR K.BRIKNAROVA,M.E.AKERMAN,D.W.HOYT,E.RUOSLAHTI,K.R.ELY
REVDAT 3 02-MAR-22 1Q38 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q38 1 VERSN
REVDAT 1 04-NOV-03 1Q38 0
JRNL AUTH K.BRIKNAROVA,M.E.AKERMAN,D.W.HOYT,E.RUOSLAHTI,K.R.ELY
JRNL TITL ANASTELLIN, AN FN3 FRAGMENT WITH FIBRONECTIN POLYMERIZATION
JRNL TITL 2 ACTIVITY, RESEMBLES AMYLOID FIBRIL PRECURSORS
JRNL REF J.MOL.BIOL. V. 332 205 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12946358
JRNL DOI 10.1016/S0022-2836(03)00890-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MORLA,Z.ZHANG,E.RUOSLAHTI
REMARK 1 TITL SUPERFIBRONECTIN IS A FUNCTIONALLY DISTINCT FORM OF
REMARK 1 TITL 2 FIBRONECTIN
REMARK 1 REF NATURE V. 367 193 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/367193A0
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.PASQUALINI,S.BOURDOULOUS,E.KOIVUNEN,V.L.WOODS JR.,
REMARK 1 AUTH 2 E.RUOSLAHTI
REMARK 1 TITL A POLYMERIC FORM OF FIBRONECTIN HAS ANTIMETASTATIC EFFECTS
REMARK 1 TITL 2 AGAINST MULTIPLE TUMOR TYPES
REMARK 1 REF NAT.MED. (N.Y.) V. 2 1197 1996
REMARK 1 REFN ISSN 1078-8956
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.YI,E.RUOSLAHTI
REMARK 1 TITL A FIBRONECTIN FRAGMENT INHIBITS TUMOR GROWTH, ANGIOGENESIS,
REMARK 1 TITL 2 AND METASTASIS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 98 620 2001
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.98.2.620
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, ARIA 1.0
REMARK 3 AUTHORS : BRUNGER (CNS), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MULTIPLE ARIA RUNS
REMARK 4
REMARK 4 1Q38 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019859.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM ANASTELLIN U-15N, 10 MM
REMARK 210 NA2HPO4, 1.8 MM KH2PO4, 140 MM
REMARK 210 NACL, 2.7 MM KCL, 2 MM CHAPS;
REMARK 210 1.5 MM ANASTELLIN U-15N,13C, 10
REMARK 210 MM NA2HPO4, 1.8 MM KH2PO4, 140
REMARK 210 MM NACL, 2.7 MM KCL, 2 MM CHAPS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.0, FELIX 2000
REMARK 210 METHOD USED : ARIA PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
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: 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: 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 ARG A 2 -78.20 -88.20
REMARK 500 1 PRO A 9 -158.92 -85.92
REMARK 500 1 HIS A 11 -157.89 -94.52
REMARK 500 1 LYS A 14 143.84 -171.62
REMARK 500 1 PRO A 21 109.94 -57.60
REMARK 500 1 VAL A 25 85.16 33.77
REMARK 500 1 PRO A 34 91.90 -64.77
REMARK 500 1 HIS A 36 71.18 -107.45
REMARK 500 1 LYS A 43 -156.49 -123.16
REMARK 500 1 LEU A 45 -166.19 -101.63
REMARK 500 1 HIS A 63 96.91 62.77
REMARK 500 1 GLN A 64 -89.93 -124.05
REMARK 500 1 THR A 73 -110.39 -112.76
REMARK 500 1 SER A 77 -102.56 -148.61
REMARK 500 1 SER A 83 85.98 -165.79
REMARK 500 1 HIS A 84 27.57 -166.10
REMARK 500 1 HIS A 87 153.99 64.91
REMARK 500 2 SER A 4 -24.68 -152.80
REMARK 500 2 LYS A 14 143.95 -171.48
REMARK 500 2 PRO A 34 78.35 -56.53
REMARK 500 2 HIS A 36 104.19 74.68
REMARK 500 2 ASN A 38 -63.36 167.22
REMARK 500 2 GLN A 64 0.13 -170.24
REMARK 500 2 THR A 73 91.58 76.81
REMARK 500 2 THR A 74 -153.36 -172.07
REMARK 500 2 ARG A 82 -98.57 56.53
REMARK 500 2 SER A 83 13.31 58.61
REMARK 500 2 HIS A 85 86.66 58.53
REMARK 500 3 LYS A 14 144.58 -171.55
REMARK 500 3 PRO A 34 90.89 -59.63
REMARK 500 3 HIS A 36 93.72 -160.15
REMARK 500 3 ASN A 38 -85.81 169.02
REMARK 500 3 GLN A 64 6.87 -153.81
REMARK 500 3 THR A 73 78.94 76.52
REMARK 500 3 THR A 74 136.68 170.51
REMARK 500 3 PRO A 79 -136.29 -79.91
REMARK 500 3 HIS A 87 -151.57 56.06
REMARK 500 4 ARG A 2 48.04 -162.59
REMARK 500 4 SER A 10 71.87 -165.79
REMARK 500 4 HIS A 11 -86.42 61.13
REMARK 500 4 LYS A 14 143.97 -175.45
REMARK 500 4 VAL A 25 41.86 35.44
REMARK 500 4 PRO A 34 87.09 -60.26
REMARK 500 4 HIS A 36 99.00 58.62
REMARK 500 4 ASN A 38 -105.06 -176.82
REMARK 500 4 LEU A 45 -167.97 57.32
REMARK 500 4 PRO A 47 45.04 -85.49
REMARK 500 4 GLN A 64 6.70 -166.44
REMARK 500 4 THR A 73 65.32 87.20
REMARK 500 4 THR A 74 146.99 174.24
REMARK 500
REMARK 500 THIS ENTRY HAS 531 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FNA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF
REMARK 900 HUMAN FIBRONECTIN
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, 20 STRUCTURES
REMARK 900 RELATED ID: 2FNB RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE FIBRONECTIN ED-B DOMAIN, NMR, 20 STRUCTURES
DBREF 1Q38 A 5 79 UNP P02751 FINC_HUMAN 631 705
SEQADV 1Q38 MET A 1 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 ARG A 2 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 GLY A 3 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 SER A 4 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 GLY A 80 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 SER A 81 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 ARG A 82 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 SER A 83 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 84 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 85 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 86 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 87 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 88 UNP P02751 CLONING ARTIFACT
SEQADV 1Q38 HIS A 89 UNP P02751 CLONING ARTIFACT
SEQRES 1 A 89 MET ARG GLY SER ASN ALA PRO GLN PRO SER HIS ILE SER
SEQRES 2 A 89 LYS TYR ILE LEU ARG TRP ARG PRO LYS ASN SER VAL GLY
SEQRES 3 A 89 ARG TRP LYS GLU ALA THR ILE PRO GLY HIS LEU ASN SER
SEQRES 4 A 89 TYR THR ILE LYS GLY LEU LYS PRO GLY VAL VAL TYR GLU
SEQRES 5 A 89 GLY GLN LEU ILE SER ILE GLN GLN TYR GLY HIS GLN GLU
SEQRES 6 A 89 VAL THR ARG PHE ASP PHE THR THR THR SER THR SER THR
SEQRES 7 A 89 PRO GLY SER ARG SER HIS HIS HIS HIS HIS HIS
SHEET 1 A 4 LYS A 29 ILE A 33 0
SHEET 2 A 4 LYS A 14 PRO A 21 -1 N TYR A 15 O ILE A 33
SHEET 3 A 4 TYR A 51 ILE A 58 -1 O ILE A 58 N LYS A 14
SHEET 4 A 4 VAL A 66 PHE A 71 -1 O PHE A 69 N GLY A 53
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 - r 2 2 Bytes