BMRB Entry 11283

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11283
MolProbity Validation Chart

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Title:
Solution Structure of the Ubiquitin-like Domain in Human FAS-associated factor 1 (hFAF1)
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Zhao, C.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Zhao, C.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the Ubiquitin-like Domain in Human FAS-associated factor 1 (hFAF1)"  .

Assembly members:

Assembly members:
ubiquitin-like domain, residues 8-100, polymer, 100 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   Host organism: E. coli - cell free   Vector: P060327-21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like domain, residues 8-100: GSSGSSGRMLDFRVEYRDRN VDVVLEDTCTVGEIKQILEN ELQIPVSKMLLKGWKTGDVE DSTVLKSLHLPKNNSLYVLT PDLPPPSSSSHAGALQESLN

Data sets:
Data typeCount
13C chemical shifts400
15N chemical shifts91
1H chemical shifts645

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ubiquitin-like domain, residues 8-1001

Entities:

Entity 1, ubiquitin-like domain, residues 8-100 100 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGMETLEU
2   ASPPHEARGVALGLUTYRARGASPARGASN
3   VALASPVALVALLEUGLUASPTHRCYSTHR
4   VALGLYGLUILELYSGLNILELEUGLUASN
5   GLULEUGLNILEPROVALSERLYSMETLEU
6   LEULYSGLYTRPLYSTHRGLYASPVALGLU
7   ASPSERTHRVALLEULYSSERLEUHISLEU
8   PROLYSASNASNSERLEUTYRVALLEUTHR
9   PROASPLEUPROPROPROSERSERSERSER
10   HISALAGLYALALEUGLNGLUSERLEUASN

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.17 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: 296.0 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 v0.9748, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAF85529 BAG11065
EMBL CAB63755 CAB67705
GB AAA92091 AAD27713 AAD51876 AAD51886 AAH04970
REF NP_001252796 NP_008982 NP_032009 NP_569090 XP_001137725
SP P54731 Q924K2 Q9UNN5
AlphaFold P54731 Q924K2 Q9UNN5

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