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 11223

Title: Solution structure of the Ig-like domain of human Leucine-rich repeat-containing protein 4

Deposition date: 2010-07-23 Original release date: 2011-08-03

Authors: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the Ig-like domain of human Leucine-rich repeat-containing protein 4"  .

Assembly members:
IG-like domain, polymer, 103 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   Vector: P050719-19

Entity Sequences (FASTA):
IG-like domain: GSSGSSGPFIMDAPRDLNIS EGRMAELKCRTPPMSSVKWL LPNGTVLSHASRHPRISVLN DGTLNFSHVLLSDTGVYTCM VTNVAGNSNASAYLNVSSGP SSG

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts96
1H chemical shifts654

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1IG-like domain1

Entities:

Entity 1, IG-like domain 103 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROPHEILE
2   METASPALAPROARGASPLEUASNILESER
3   GLUGLYARGMETALAGLULEULYSCYSARG
4   THRPROPROMETSERSERVALLYSTRPLEU
5   LEUPROASNGLYTHRVALLEUSERHISALA
6   SERARGHISPROARGILESERVALLEUASN
7   ASPGLYTHRLEUASNPHESERHISVALLEU
8   LEUSERASPTHRGLYVALTYRTHRCYSMET
9   VALTHRASNVALALAGLYASNSERASNALA
10   SERALATYRLEUASNVALSERSERGLYPRO
11   SERSERGLY

Samples:

sample_1: IG-like domain, [U-13C; U-15N], 1.26 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 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9296, Kobayashi N. - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB

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