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 11350

Title: Solution structure of LIM domain in Four and a half LIM domains protein 2

Deposition date: 2010-09-07 Original release date: 2011-09-07

Authors: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.

Citation: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.. "Solution structure of LIM domain in Four and a half LIM domains protein 2"  .

Assembly members:
LIM domain, polymer, 72 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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: P040921-14

Entity Sequences (FASTA):
LIM domain: GSSGSSGCAGCTNPISGLGG TKYISFEERQWHNDCFNCKK CSLSLVGRGFLTERDDILCP DCGKDISGPSSG

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts67
1H chemical shifts417

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1LIM domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, LIM domain 72 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYCYSALAGLY
2   CYSTHRASNPROILESERGLYLEUGLYGLY
3   THRLYSTYRILESERPHEGLUGLUARGGLN
4   TRPHISASNASPCYSPHEASNCYSLYSLYS
5   CYSSERLEUSERLEUVALGLYARGGLYPHE
6   LEUTHRGLUARGASPASPILELEUCYSPRO
7   ASPCYSGLYLYSASPILESERGLYPROSER
8   SERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: LIM domain, [U-13C; U-15N], 0.8 mM; d-Tris-HCl 20 mM; NaCl 100 mM; ZnCl2 100 uM; 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:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio F. - processing

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

Kujira v0.863, 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