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 10320

Title: Solution structure of the 9th filamin domain from human Filamin-B

Deposition date: 2009-04-02 Original release date: 2010-04-07

Authors: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the 9th filamin domain from human Filamin-B"  .

Assembly members:
Filamin domain, polymer, 131 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: P051205-13

Entity Sequences (FASTA):
Filamin domain: GSSGSSGDVTYDGHPVPGSP YTVEASLPPDPSKVKAHGPG LEGGLVGKPAEFTIDTKGAG TGGLGLTVEGPCEAKIECSD NGDGTCSVSYLPTKPGEYFV NILFEEVHIPGSPFKADIEM PFDPSSGPSSG

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts107
1H chemical shifts782

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Filamin domain1

Entities:

Entity 1, Filamin domain 131 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASPVALTHR
2   TYRASPGLYHISPROVALPROGLYSERPRO
3   TYRTHRVALGLUALASERLEUPROPROASP
4   PROSERLYSVALLYSALAHISGLYPROGLY
5   LEUGLUGLYGLYLEUVALGLYLYSPROALA
6   GLUPHETHRILEASPTHRLYSGLYALAGLY
7   THRGLYGLYLEUGLYLEUTHRVALGLUGLY
8   PROCYSGLUALALYSILEGLUCYSSERASP
9   ASNGLYASPGLYTHRCYSSERVALSERTYR
10   LEUPROTHRLYSPROGLYGLUTYRPHEVAL
11   ASNILELEUPHEGLUGLUVALHISILEPRO
12   GLYSERPROPHELYSALAASPILEGLUMET
13   PROPHEASPPROSERSERGLYPROSERSER
14   GLY

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: 298 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

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