BMRB Entry 10102

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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/BMR10102
MolProbity Validation Chart

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Title:
Solution structure of the second fibronectin Type III domain of human KIAA1568 protein
Deposition date:
2007-02-13
Original release date:
2008-08-15
Authors:
Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the second fibronectin Type III domain of human KIAA1568 protein"  .

Assembly members:

Assembly members:
FN3 domain, polymer, 120 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: P021007-59

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FN3 domain: GSSGSSGRQVQKELGDVLVR LHNPVVLTPTTVQVTWTVDR QPQFIQGYRVMYRQTSGLQA TSSWQNLDAKVPTERSAVLV NLKKGVTYEIKVRPYFNEFQ GMDSESKTVRTTEESGPSSG

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts126
1H chemical shifts805

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1KIAA1568 protein1

Entities:

Entity 1, KIAA1568 protein 120 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGGLNVAL
2   GLNLYSGLULEUGLYASPVALLEUVALARG
3   LEUHISASNPROVALVALLEUTHRPROTHR
4   THRVALGLNVALTHRTRPTHRVALASPARG
5   GLNPROGLNPHEILEGLNGLYTYRARGVAL
6   METTYRARGGLNTHRSERGLYLEUGLNALA
7   THRSERSERTRPGLNASNLEUASPALALYS
8   VALPROTHRGLUARGSERALAVALLEUVAL
9   ASNLEULYSLYSGLYVALTHRTYRGLUILE
10   LYSVALARGPROTYRPHEASNGLUPHEGLN
11   GLYMETASPSERGLUSERLYSTHRVALARG
12   THRTHRGLUGLUSERGLYPROSERSERGLY

Samples:

sample_1: FN3 domain, [U-13C; U-15N], 1.0 mM; phosphate 20 mM; NaCl 100 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1
2D TROSY HNCOsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

xwinnmr v3.1, Bruker - collection

NMRPipe v200204025, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.816, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 600 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