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 18348

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain   PubMed: 23128140

Deposition date: 2012-03-26 Original release date: 2012-11-15

Authors: Kanaba, Teppei; Mishima, Masaki

Citation: Kanaba, Teppei; Maesaki, Ryoko; Mori, Tomoyuki; Ito, Yutaka; Hakoshima, Toshio; Mishima, Masaki. "Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR."  Biochim. Biophys. Acta 1834, 499-507 (2013).

Assembly members:
EB1_CH_domain, polymer, 133 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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
EB1_CH_domain: GPGMAVNVYSTSVTSDNLSR HDMLAWINESLQLNLTKIEQ LCSGAAYCQFMDMLFPGSIA LKKVKFQAKLEHEYIQNFKI LQAGFKRMGVDKIIPVDKLV KGKFQDNFEFVQWFKKFFDA NYDGKDYDPVAAR

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EB1 CH domain1

Entities:

Entity 1, EB1 CH domain 133 residues - Formula weight is not available

1   GLYPROGLYMETALAVALASNVALTYRSER
2   THRSERVALTHRSERASPASNLEUSERARG
3   HISASPMETLEUALATRPILEASNGLUSER
4   LEUGLNLEUASNLEUTHRLYSILEGLUGLN
5   LEUCYSSERGLYALAALATYRCYSGLNPHE
6   METASPMETLEUPHEPROGLYSERILEALA
7   LEULYSLYSVALLYSPHEGLNALALYSLEU
8   GLUHISGLUTYRILEGLNASNPHELYSILE
9   LEUGLNALAGLYPHELYSARGMETGLYVAL
10   ASPLYSILEILEPROVALASPLYSLEUVAL
11   LYSGLYLYSPHEGLNASPASNPHEGLUPHE
12   VALGLNTRPPHELYSLYSPHEPHEASPALA
13   ASNTYRASPGLYLYSASPTYRASPPROVAL
14   ALAALAARG

Samples:

sample_1: EB1 CH domain, [U-13C; U-15N], 1.0 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.4 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAE32461 BAE89438 BAG35484 BAG73401
EMBL CAG31466 CAH92115
GB AAA96320 AAC09471 AAH52405 AAH64444 AAH81726
REF NP_001026031 NP_001038078 NP_001068802 NP_001126236 NP_001238875
SP Q15691 Q3ZBD9 Q5R7Z5 Q5ZLC7 Q61166
TPG DAA23186

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