BMRB Entry 10299

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10299
MolProbity Validation Chart

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Title:
Solution structures of the fn3 domain of human Tripartite motif protein 9
Deposition date:
2008-12-24
Original release date:
2010-01-11
Authors:
Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the fn3 domain of human Tripartite motif protein 9"  .

Assembly members:

Assembly members:
Fibronectin type III domain, polymer, 110 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: P040921-16

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fibronectin type III domain: GSSGSSGPVPATPILQLEEC CTHNNSATLSWKQPPLSTVP ADGYILELDDGNGGQFREVY VGKETMCTVDGLHFNSTYNA RVKAFNKTGVSPYSKTLVLQ TSEGSGPSSG

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts101
1H chemical shifts678

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Fibronectin type III domain1

Entities:

Entity 1, Fibronectin type III domain 110 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROVALPRO
2   ALATHRPROILELEUGLNLEUGLUGLUCYS
3   CYSTHRHISASNASNSERALATHRLEUSER
4   TRPLYSGLNPROPROLEUSERTHRVALPRO
5   ALAASPGLYTYRILELEUGLULEUASPASP
6   GLYASNGLYGLYGLNPHEARGGLUVALTYR
7   VALGLYLYSGLUTHRMETCYSTHRVALASP
8   GLYLEUHISPHEASNSERTHRTYRASNALA
9   ARGVALLYSALAPHEASNLYSTHRGLYVAL
10   SERPROTYRSERLYSTHRLEUVALLEUGLN
11   THRSERGLUGLYSERGLYPROSERSERGLY

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: 296 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, 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 800 MHz

Related Database Links:

PDB
DBJ BAA13398 BAB70913 BAG09692
GB AAG53490 AAG53491 AAG53492 AAH63872 EAW65681
REF NP_055978 XP_001102351 XP_001156684 XP_002824781 XP_003267727
SP Q9C026
AlphaFold Q9C026

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