BMRB Entry 10266

Title:
Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F
Deposition date:
2008-12-15
Original release date:
2009-12-14
Authors:
Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F"  .

Assembly members:

Assembly members:
Fibronectin type III domain, polymer, 103 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P060123-21

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts103
1H chemical shifts688

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fibronectin type III domain1

Entities:

Entity 1, Fibronectin type III domain 103 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROSERGLY
2   PHEPROGLNASNLEUHISVALTHRGLYLEU
3   THRTHRSERTHRTHRGLULEUALATRPASP
4   PROPROVALLEUALAGLUARGASNGLYARG
5   ILEILESERTYRTHRVALVALPHEARGASP
6   ILEASNSERGLNGLNGLULEUGLNASNILE
7   THRTHRASPTHRARGPHETHRLEUTHRGLY
8   LEULYSPROASPTHRTHRTYRASPILELYS
9   VALARGALATRPTHRSERLYSGLYSERGLY
10   PROLEUSERPROSERILEGLNSERARGTHR
11   METPROVAL

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v2.0.17, Johnson, B.A. - data analysis

Kujira v0.932, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks