Header list of 2fn2.pdb file
Complete list - l 29 2 Bytes
HEADER GLYCOPROTEIN 06-AUG-97 2FN2
TITLE SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED SECOND TYPE TWO MODULE OF
TITLE 2 FIBRONECTIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 375 - 433;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: GLYCOSYLATED SECOND TYPE II MODULE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115 (HIS4-)
KEYWDS GLYCOPROTEIN, FIBRONECTIN, TYPE TWO MODULE, GLYCOSYLATED PROTEIN,
KEYWDS 2 COLLAGEN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.STICHT,A.R.PICKFORD,J.R.POTTS,I.D.CAMPBELL
REVDAT 4 29-JUL-20 2FN2 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 13-JUL-11 2FN2 1 VERSN
REVDAT 2 24-FEB-09 2FN2 1 VERSN
REVDAT 1 16-SEP-98 2FN2 0
JRNL AUTH H.STICHT,A.R.PICKFORD,J.R.POTTS,I.D.CAMPBELL
JRNL TITL SOLUTION STRUCTURE OF THE GLYCOSYLATED SECOND TYPE 2 MODULE
JRNL TITL 2 OF FIBRONECTIN.
JRNL REF J.MOL.BIOL. V. 276 177 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514732
JRNL DOI 10.1006/JMBI.1997.1528
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.R.PICKFORD,J.R.POTTS,J.R.BRIGHT,I.PHAN,I.D.CAMPBELL
REMARK 1 TITL SOLUTION STRUCTURE OF A TYPE 2 MODULE FROM FIBRONECTIN:
REMARK 1 TITL 2 IMPLICATIONS FOR THE STRUCTURE AND FUNCTION OF THE
REMARK 1 TITL 3 GELATIN-BINDING DOMAIN
REMARK 1 REF STRUCTURE V. 5 359 1997
REMARK 1 REFN ISSN 0969-2126
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 2FN2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178100.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 0 MM
REMARK 210 PRESSURE : 10E+5 PA ATM
REMARK 210 SAMPLE CONTENTS : H2O/D2O(9:1) OR D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TWO-DIMENSIONAL 1H-1H
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA 500
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
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: 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 6 96.26 -165.01
REMARK 500 1 ASN A 11 16.48 56.53
REMARK 500 1 CYS A 15 155.29 -49.70
REMARK 500 1 HIS A 24 79.84 -114.48
REMARK 500 1 ASN A 25 101.69 -52.30
REMARK 500 1 THR A 27 31.67 -88.84
REMARK 500 1 ASP A 28 -167.31 -170.87
REMARK 500 1 ASP A 36 -74.00 -118.27
REMARK 500 1 ASN A 37 -37.77 177.75
REMARK 500 1 MET A 38 176.92 -52.80
REMARK 500 1 GLN A 51 47.91 71.36
REMARK 500 1 PRO A 57 88.43 -59.52
REMARK 500 2 ARG A 6 53.94 -165.14
REMARK 500 2 ASN A 11 28.05 41.48
REMARK 500 2 LEU A 20 106.65 -59.91
REMARK 500 2 HIS A 24 79.44 -114.21
REMARK 500 2 ASN A 25 99.96 -48.49
REMARK 500 2 ASP A 36 -67.65 -129.39
REMARK 500 2 ASN A 37 -27.03 170.98
REMARK 500 2 MET A 38 -171.63 -52.63
REMARK 500 2 GLN A 51 40.80 37.00
REMARK 500 2 PRO A 57 86.05 -59.01
REMARK 500 2 MET A 58 77.30 -173.76
REMARK 500 3 LEU A 2 74.22 -157.46
REMARK 500 3 ARG A 6 76.90 -161.00
REMARK 500 3 ASN A 25 105.62 -55.28
REMARK 500 3 THR A 27 24.93 -152.32
REMARK 500 3 ASP A 36 -70.54 -122.61
REMARK 500 3 ASN A 37 -33.93 174.47
REMARK 500 3 MET A 38 -179.56 -50.44
REMARK 500 3 ASP A 50 -56.24 -123.76
REMARK 500 3 GLN A 51 44.09 72.39
REMARK 500 3 PRO A 57 85.71 -62.29
REMARK 500 3 MET A 58 98.41 -166.64
REMARK 500 4 ASN A 25 102.68 -58.89
REMARK 500 4 ARG A 35 19.23 -146.37
REMARK 500 4 ASP A 36 -79.42 -133.35
REMARK 500 4 ASN A 37 29.14 -179.72
REMARK 500 4 ASN A 46 81.67 -160.39
REMARK 500 4 ASP A 50 -48.41 -130.48
REMARK 500 4 GLN A 51 56.64 71.68
REMARK 500 4 PRO A 57 86.79 -59.42
REMARK 500 5 ARG A 6 92.55 -164.96
REMARK 500 5 ASN A 25 96.50 -55.03
REMARK 500 5 ARG A 35 19.49 56.63
REMARK 500 5 ASN A 37 -53.57 177.43
REMARK 500 5 ASN A 46 79.93 -152.32
REMARK 500 5 ASP A 50 -49.14 -131.82
REMARK 500 5 GLN A 51 81.09 73.27
REMARK 500 5 PRO A 57 88.02 -58.54
REMARK 500
REMARK 500 THIS ENTRY HAS 221 RAMACHANDRAN OUTLIERS.
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 1 ARG A 6 0.21 SIDE CHAIN
REMARK 500 1 ARG A 34 0.24 SIDE CHAIN
REMARK 500 1 ARG A 35 0.11 SIDE CHAIN
REMARK 500 2 ARG A 6 0.30 SIDE CHAIN
REMARK 500 2 ARG A 34 0.31 SIDE CHAIN
REMARK 500 2 ARG A 35 0.31 SIDE CHAIN
REMARK 500 3 ARG A 6 0.14 SIDE CHAIN
REMARK 500 3 ARG A 34 0.21 SIDE CHAIN
REMARK 500 3 ARG A 35 0.21 SIDE CHAIN
REMARK 500 4 ARG A 6 0.28 SIDE CHAIN
REMARK 500 4 ARG A 34 0.20 SIDE CHAIN
REMARK 500 4 ARG A 35 0.30 SIDE CHAIN
REMARK 500 5 ARG A 6 0.28 SIDE CHAIN
REMARK 500 5 ARG A 35 0.31 SIDE CHAIN
REMARK 500 6 ARG A 6 0.30 SIDE CHAIN
REMARK 500 6 ARG A 34 0.32 SIDE CHAIN
REMARK 500 6 ARG A 35 0.24 SIDE CHAIN
REMARK 500 7 ARG A 6 0.32 SIDE CHAIN
REMARK 500 7 ARG A 34 0.26 SIDE CHAIN
REMARK 500 7 ARG A 35 0.30 SIDE CHAIN
REMARK 500 8 ARG A 6 0.25 SIDE CHAIN
REMARK 500 8 ARG A 34 0.29 SIDE CHAIN
REMARK 500 8 ARG A 35 0.32 SIDE CHAIN
REMARK 500 9 ARG A 6 0.29 SIDE CHAIN
REMARK 500 9 ARG A 34 0.27 SIDE CHAIN
REMARK 500 9 ARG A 35 0.25 SIDE CHAIN
REMARK 500 10 ARG A 34 0.15 SIDE CHAIN
REMARK 500 10 ARG A 35 0.16 SIDE CHAIN
REMARK 500 11 ARG A 6 0.29 SIDE CHAIN
REMARK 500 11 ARG A 34 0.28 SIDE CHAIN
REMARK 500 11 ARG A 35 0.30 SIDE CHAIN
REMARK 500 12 ARG A 6 0.08 SIDE CHAIN
REMARK 500 12 ARG A 34 0.25 SIDE CHAIN
REMARK 500 12 ARG A 35 0.25 SIDE CHAIN
REMARK 500 13 ARG A 6 0.32 SIDE CHAIN
REMARK 500 13 ARG A 34 0.26 SIDE CHAIN
REMARK 500 13 ARG A 35 0.21 SIDE CHAIN
REMARK 500 14 ARG A 6 0.17 SIDE CHAIN
REMARK 500 14 ARG A 34 0.28 SIDE CHAIN
REMARK 500 14 ARG A 35 0.30 SIDE CHAIN
REMARK 500 15 ARG A 6 0.31 SIDE CHAIN
REMARK 500 15 ARG A 34 0.24 SIDE CHAIN
REMARK 500 15 ARG A 35 0.25 SIDE CHAIN
REMARK 500 16 ARG A 6 0.25 SIDE CHAIN
REMARK 500 16 ARG A 34 0.29 SIDE CHAIN
REMARK 500 16 ARG A 35 0.26 SIDE CHAIN
REMARK 500 17 ARG A 6 0.19 SIDE CHAIN
REMARK 500 17 ARG A 34 0.30 SIDE CHAIN
REMARK 500 17 ARG A 35 0.31 SIDE CHAIN
REMARK 500 18 ARG A 6 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FN2 A 1 59 UNP P02751 FINC_HUMAN 375 433
SEQRES 1 A 59 VAL LEU VAL GLN THR ARG GLY GLY ASN SER ASN GLY ALA
SEQRES 2 A 59 LEU CYS HIS PHE PRO PHE LEU TYR ASN ASN HIS ASN TYR
SEQRES 3 A 59 THR ASP CYS THR SER GLU GLY ARG ARG ASP ASN MET LYS
SEQRES 4 A 59 TRP CYS GLY THR THR GLN ASN TYR ASP ALA ASP GLN LYS
SEQRES 5 A 59 PHE GLY PHE CYS PRO MET ALA
MODRES 2FN2 ASN A 25 ASN GLYCOSYLATION SITE
HET NAG A 60 28
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 2 NAG C8 H15 N O6
HELIX 1 1 TYR A 47 ASP A 50 1 4
SHEET 1 A 2 TRP A 40 GLY A 42 0
SHEET 2 A 2 PHE A 53 PHE A 55 -1 N GLY A 54 O CYS A 41
SSBOND 1 CYS A 15 CYS A 41 1555 1555 2.02
SSBOND 2 CYS A 29 CYS A 56 1555 1555 2.02
LINK ND2 ASN A 25 C1 NAG A 60 1555 1555 1.46
CISPEP 1 PHE A 17 PRO A 18 1 -1.90
CISPEP 2 PHE A 17 PRO A 18 2 -1.26
CISPEP 3 PHE A 17 PRO A 18 3 -1.01
CISPEP 4 PHE A 17 PRO A 18 4 -1.32
CISPEP 5 PHE A 17 PRO A 18 5 -1.24
CISPEP 6 PHE A 17 PRO A 18 6 -0.90
CISPEP 7 PHE A 17 PRO A 18 7 -1.65
CISPEP 8 PHE A 17 PRO A 18 8 -1.54
CISPEP 9 PHE A 17 PRO A 18 9 -1.19
CISPEP 10 PHE A 17 PRO A 18 10 -1.99
CISPEP 11 PHE A 17 PRO A 18 11 -1.34
CISPEP 12 PHE A 17 PRO A 18 12 -2.18
CISPEP 13 PHE A 17 PRO A 18 13 -2.07
CISPEP 14 PHE A 17 PRO A 18 14 -1.63
CISPEP 15 PHE A 17 PRO A 18 15 -1.85
CISPEP 16 PHE A 17 PRO A 18 16 -1.31
CISPEP 17 PHE A 17 PRO A 18 17 -1.74
CISPEP 18 PHE A 17 PRO A 18 18 -1.67
CISPEP 19 PHE A 17 PRO A 18 19 -2.11
CISPEP 20 PHE A 17 PRO A 18 20 -1.64
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 29 2 Bytes