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 11305

Title: Solution Structure of the LIM Domain of the Human Actin Binding LIM Protein 2

Deposition date: 2010-08-10 Original release date: 2011-08-19

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

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the LIM Domain of the Human Actin Binding LIM Protein 2"  . ., .-..

Assembly members:
LIM Domain, polymer, 81 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

Entity Sequences (FASTA):
LIM Domain: GSSGSSGLDYQRLYGTRCFS CDQFIEGEVVSALGKTYHPD CFVCAVCRLPFPPGDRVTFN GKECMCQKCSLPVSVSGPSS G

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts65
1H chemical shifts463

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LIM Domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, LIM Domain 81 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUASPTYR
2   GLNARGLEUTYRGLYTHRARGCYSPHESER
3   CYSASPGLNPHEILEGLUGLYGLUVALVAL
4   SERALALEUGLYLYSTHRTYRHISPROASP
5   CYSPHEVALCYSALAVALCYSARGLEUPRO
6   PHEPROPROGLYASPARGVALTHRPHEASN
7   GLYLYSGLUCYSMETCYSGLNLYSCYSSER
8   LEUPROVALSERVALSERGLYPROSERSER
9   GLY

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

1   ZN

Samples:

sample_1: LIM Domain, [U-13C; U-15N], 1.22 mM; d-Tris-HCl 20 mM; NaCl 100 mM; NaN3 0.02%; ZnCl2 0.1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, 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
REF XP_004038463 XP_008577003 XP_009204733 XP_009204734 XP_009204735

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