BMRB Entry 18371

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18371

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 C-terminal domain
Deposition date:
2012-03-30
Original release date:
2012-11-15
Authors:
Kanaba, Teppei; Mishima, Masaki
Citation:

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).
PubMed: 23128140

Assembly members:

Assembly members:
EB1_C-terminal_domain, polymer, 85 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6P-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EB1_C-terminal_domain: GPLGSGDDEAAELMQQVNVL KLTVEDLEKERDFYFGKLRN IELICQENEGENDPVLQRIV DILYATDEGFVIPDEGGPQE EQEEY

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts67
1H chemical shifts67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EB1 C-terminal domain1

Entities:

Entity 1, EB1 C-terminal domain 85 residues - Formula weight is not available

1   GLYPROLEUGLYSERGLYASPASPGLUALA
2   ALAGLULEUMETGLNGLNVALASNVALLEU
3   LYSLEUTHRVALGLUASPLEUGLULYSGLU
4   ARGASPPHETYRPHEGLYLYSLEUARGASN
5   ILEGLULEUILECYSGLNGLUASNGLUGLY
6   GLUASNASPPROVALLEUGLNARGILEVAL
7   ASPILELEUTYRALATHRASPGLUGLYPHE
8   VALILEPROASPGLUGLYGLYPROGLNGLU
9   GLUGLNGLUGLUTYR

Samples:

sample_1: EB1 C-terminal domain, [U-100% 13C; U-100% 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 CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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 BAE89438 BAG35484 BAG59745 BAG73401
EMBL CAH92115
GB AAC09471 AAI06069 AAI09282 AAY18920 ACE87787
REF NP_001126236 NP_001253729 NP_001271003 NP_036457 XP_002710850
SP Q15691 Q5R7Z5
AlphaFold Q15691 Q5R7Z5

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