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 10333

Title: Solution structure of the filamin domain from human BK158_1 protein

Deposition date: 2009-04-14 Original release date: 2010-04-14

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

Citation: Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the filamin domain from human BK158_1 protein"  .

Assembly members:
Filamin-type immunoglobulin domains, polymer, 124 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   Vector: P050905-05

Entity Sequences (FASTA):
Filamin-type immunoglobulin domains: GSSGSSGETGGERQLSPEKS EIWGPGLKADVVLPARYFYI QAVDTSGNKFTSSPGEKVFQ VKVSAPEEQFTRVGVQVLDR KDGSFIVRYRMYASYKNLKV EIKFQGQHVAKSPYILKGSG PSSG

Data sets:
Data typeCount
13C chemical shifts529
15N chemical shifts109
1H chemical shifts827

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Filamin-type immunoglobulin domains1

Entities:

Entity 1, Filamin-type immunoglobulin domains 124 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUTHRGLY
2   GLYGLUARGGLNLEUSERPROGLULYSSER
3   GLUILETRPGLYPROGLYLEULYSALAASP
4   VALVALLEUPROALAARGTYRPHETYRILE
5   GLNALAVALASPTHRSERGLYASNLYSPHE
6   THRSERSERPROGLYGLULYSVALPHEGLN
7   VALLYSVALSERALAPROGLUGLUGLNPHE
8   THRARGVALGLYVALGLNVALLEUASPARG
9   LYSASPGLYSERPHEILEVALARGTYRARG
10   METTYRALASERTYRLYSASNLEULYSVAL
11   GLUILELYSPHEGLNGLYGLNHISVALALA
12   LYSSERPROTYRILELEULYSGLYSERGLY
13   PROSERSERGLY

Samples:

sample_1: Filamin domain, [U-13C; U-15N], 1.11 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 v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9742, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAD96287
GB AAH01297 AAQ89318 ABM82133 ABM85316 AIC57069
REF NP_076994 XP_001094880 XP_002824457 XP_003832113 XP_003919616
SP Q6UW63
AlphaFold Q6UW63

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