BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11140

Title: Solution structure of the 4th KH type I domain from human Vigilin

Deposition date: 2010-03-31 Original release date: 2011-04-01

Authors: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the 4th KH type I domain from human Vigilin"  . ., .-..

Assembly members:
KH domain, polymer, 102 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
KH domain: GSSGSSGEPEKLGQALTEVY AKANSFTVSSVAAPSWLHRF IIGKKGQNLAKITQQMPKVH IEFTEGEDKITLEGPTEDVS VAQEQIEGMVKDLINRSGPS SG

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts98
1H chemical shifts681

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KH domain1

Entities:

Entity 1, KH domain 102 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUPROGLU
2   LYSLEUGLYGLNALALEUTHRGLUVALTYR
3   ALALYSALAASNSERPHETHRVALSERSER
4   VALALAALAPROSERTRPLEUHISARGPHE
5   ILEILEGLYLYSLYSGLYGLNASNLEUALA
6   LYSILETHRGLNGLNMETPROLYSVALHIS
7   ILEGLUPHETHRGLUGLYGLUASPLYSILE
8   THRLEUGLUGLYPROTHRGLUASPVALSER
9   VALALAGLNGLUGLNILEGLUGLYMETVAL
10   LYSASPLEUILEASNARGSERGLYPROSER
11   SERGLY

Samples:

sample_1: KH domain, [U-13C; U-15N], 1.16 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 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC33456
EMBL CAI46262
GB EDL39954 EDL91932 EDL91937 EDL91944

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts