Header list of 1oww.pdb file
Complete list - l 7 2 Bytes
HEADER STRUCTURAL PROTEIN 31-MAR-03 1OWW
TITLE SOLUTION STRUCTURE OF THE FIRST TYPE III MODULE OF HUMAN FIBRONECTIN
TITLE 2 DETERMINED BY 1H, 15N NMR SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN FIRST TYPE III MODULE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 608-701 OF SWS P02751;
COMPND 5 SYNONYM: FN; COLD-INSOLUBLE GLOBULIN; CIG;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2
KEYWDS FIBRONECTIN TYPE III MODULE, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR M.GAO,D.CRAIG,O.LEQUIN,I.D.CAMPBELL,V.VOGEL,K.SCHULTEN
REVDAT 4 07-JUL-21 1OWW 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1OWW 1 VERSN
REVDAT 2 30-DEC-03 1OWW 1 JRNL
REVDAT 1 07-OCT-03 1OWW 0
JRNL AUTH M.GAO,D.CRAIG,O.LEQUIN,I.D.CAMPBELL,V.VOGEL,K.SCHULTEN
JRNL TITL STRUCTURE AND FUNCTIONAL SIGNIFICANCE OF MECHANICALLY
JRNL TITL 2 UNFOLDED FIBRONECTIN TYPE III1 INTERMEDIATES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 14784 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14657397
JRNL DOI 10.1073/PNAS.2334390100
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH O.LEQUIN,D.SACHCHIDANAND,D.STAUNTON,J.POTTS,J.M.WERNER,
REMARK 1 AUTH 2 I.D.CAMPBELL
REMARK 1 TITL SOLUTION STRUCTURE OF THE FIRST TYPE III MODULE OF HUMAN
REMARK 1 TITL 2 FIBRONECTIN DETERMINED BY 1H, 15N NMR SPECTROSCOPY
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES REFINED BY MOLECULAR
REMARK 3 DYNAMICS USING RESIDUAL DIPOLAR COUPLINGS. STRUCTURES BASED ON A
REMARK 3 TOTAL OF 1113 DISTANCE RESTRAINTS, 81 DIHEDRAL ANGLE RESTRAINTS
REMARK 3 AND 57 RESIDUAL DIPOLAR COUPLINGS.
REMARK 4
REMARK 4 1OWW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018753.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : UNBUFFERED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2 MM [U-15N] PROTEIN, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; HNHA; 2D NOESY;
REMARK 210 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA; DMX
REMARK 210 SPECTROMETER MANUFACTURER : OXFORD; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.3, XWINNMR 2.6, XEASY
REMARK 210 1.3, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 24
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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 1-24
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 A 10 82.66 -169.15
REMARK 500 1 SER A 28 58.52 -98.99
REMARK 500 1 SER A 31 -84.24 -104.01
REMARK 500 1 LYS A 40 85.02 -69.86
REMARK 500 1 ASN A 41 -67.78 -147.52
REMARK 500 1 VAL A 43 53.42 -119.82
REMARK 500 2 THR A 9 -152.43 -132.58
REMARK 500 2 GLU A 10 -18.89 79.51
REMARK 500 2 SER A 13 119.47 -169.02
REMARK 500 2 HIS A 29 -49.89 -162.37
REMARK 500 2 SER A 31 -87.50 -110.53
REMARK 500 2 LYS A 40 83.07 -69.75
REMARK 500 2 ASN A 41 -89.81 -145.90
REMARK 500 3 GLU A 10 40.73 -107.08
REMARK 500 3 SER A 28 64.66 71.89
REMARK 500 3 SER A 31 -83.90 -99.35
REMARK 500 3 ASN A 41 -58.55 -154.32
REMARK 500 3 SER A 42 -167.53 -107.32
REMARK 500 3 LEU A 63 -160.83 -117.08
REMARK 500 3 THR A 92 -37.37 -157.57
REMARK 500 4 SER A 13 32.29 -157.54
REMARK 500 4 ASN A 16 -39.22 -165.80
REMARK 500 4 HIS A 29 -50.78 -160.85
REMARK 500 4 SER A 31 -87.55 -106.06
REMARK 500 4 LYS A 40 88.02 -63.66
REMARK 500 4 ASN A 41 -132.09 -130.39
REMARK 500 4 VAL A 43 41.63 -100.60
REMARK 500 4 GLN A 78 34.00 -76.29
REMARK 500 4 TYR A 79 14.13 -148.67
REMARK 500 5 GLU A 10 -64.91 149.21
REMARK 500 5 THR A 11 87.45 -155.08
REMARK 500 5 PRO A 12 34.87 -86.32
REMARK 500 5 SER A 28 78.73 64.95
REMARK 500 5 SER A 31 -87.49 -103.95
REMARK 500 5 ASN A 41 -56.93 -154.57
REMARK 500 5 THR A 92 21.47 -157.71
REMARK 500 6 THR A 9 10.92 -143.63
REMARK 500 6 SER A 28 78.08 71.33
REMARK 500 6 SER A 31 -87.77 -102.69
REMARK 500 6 ASN A 41 -81.62 -152.01
REMARK 500 7 PRO A 25 -179.29 -67.23
REMARK 500 7 SER A 28 58.59 -99.00
REMARK 500 7 SER A 31 -84.65 -110.52
REMARK 500 7 ASN A 41 -69.18 -150.58
REMARK 500 7 VAL A 43 51.36 -115.69
REMARK 500 8 GLU A 10 50.28 -117.93
REMARK 500 8 HIS A 29 -44.84 -169.73
REMARK 500 8 SER A 31 -87.29 -113.06
REMARK 500 8 ASN A 41 -50.06 -164.65
REMARK 500 9 SER A 13 82.11 -159.73
REMARK 500
REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 6 PHE A 7 10 -148.20
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 9 TYR A 69 0.07 SIDE CHAIN
REMARK 500 10 TYR A 33 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OWW A 0 93 UNP P02751 FINC_HUMAN 608 701
SEQADV 1OWW GLY A -4 UNP P02751 CLONING ARTIFACT
SEQADV 1OWW PRO A -3 UNP P02751 CLONING ARTIFACT
SEQADV 1OWW LEU A -2 UNP P02751 CLONING ARTIFACT
SEQADV 1OWW GLY A -1 UNP P02751 CLONING ARTIFACT
SEQRES 1 A 98 GLY PRO LEU GLY SER SER GLY PRO VAL GLU VAL PHE ILE
SEQRES 2 A 98 THR GLU THR PRO SER GLN PRO ASN SER HIS PRO ILE GLN
SEQRES 3 A 98 TRP ASN ALA PRO GLN PRO SER HIS ILE SER LYS TYR ILE
SEQRES 4 A 98 LEU ARG TRP ARG PRO LYS ASN SER VAL GLY ARG TRP LYS
SEQRES 5 A 98 GLU ALA THR ILE PRO GLY HIS LEU ASN SER TYR THR ILE
SEQRES 6 A 98 LYS GLY LEU LYS PRO GLY VAL VAL TYR GLU GLY GLN LEU
SEQRES 7 A 98 ILE SER ILE GLN GLN TYR GLY HIS GLN GLU VAL THR ARG
SEQRES 8 A 98 PHE ASP PHE THR THR THR SER
SHEET 1 A 3 GLU A 5 PHE A 7 0
SHEET 2 A 3 HIS A 18 ASN A 23 -1 O ASN A 23 N GLU A 5
SHEET 3 A 3 SER A 57 ILE A 60 -1 O ILE A 60 N HIS A 18
SHEET 1 B 4 LYS A 47 ILE A 51 0
SHEET 2 B 4 ILE A 30 PRO A 39 -1 N LEU A 35 O ALA A 49
SHEET 3 B 4 VAL A 67 GLN A 77 -1 O ILE A 74 N ILE A 34
SHEET 4 B 4 GLN A 82 THR A 91 -1 O GLU A 83 N SER A 75
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 - l 7 2 Bytes