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 11143

Title: Solution structure of the CH domain from human MICAL-3 protein

Deposition date: 2010-03-31 Original release date: 2011-04-01

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

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain from human MICAL-3 protein"  . ., .-..

Assembly members:
CH domain, polymer, 121 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

Entity Sequences (FASTA):
CH domain: GSSGSSGVARSSKLLGWCQR QTDGYAGVNVTDLTMSWKSG LALCAIIHRYRPDLIDFDSL DEQNVEKNNQLAFDIAEKEL GISPIMTGKEMASVGEPDKL SMVMYLTQFYEMFKDSGPSS G

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts119
1H chemical shifts806

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CH domain1

Entities:

Entity 1, CH domain 121 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALALAARG
2   SERSERLYSLEULEUGLYTRPCYSGLNARG
3   GLNTHRASPGLYTYRALAGLYVALASNVAL
4   THRASPLEUTHRMETSERTRPLYSSERGLY
5   LEUALALEUCYSALAILEILEHISARGTYR
6   ARGPROASPLEUILEASPPHEASPSERLEU
7   ASPGLUGLNASNVALGLULYSASNASNGLN
8   LEUALAPHEASPILEALAGLULYSGLULEU
9   GLYILESERPROILEMETTHRGLYLYSGLU
10   METALASERVALGLYGLUPROASPLYSLEU
11   SERMETVALMETTYRLEUTHRGLNPHETYR
12   GLUMETPHELYSASPSERGLYPROSERSER
13   GLY

Samples:

sample_1: CH domain, [U-13C; U-15N], 1.12 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 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-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 v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA92602 BAG10388
GB AAI57877 AAI71887 EFB16615 EGW04922 EHB13700
REF NP_001129476 NP_056056 XP_002722588 XP_002926775 XP_003278377
SP Q7RTP6

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