BMRB Entry 16870

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16870

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Title:
1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Cofactor C
Deposition date:
2010-04-15
Original release date:
2011-09-28
Authors:
Garcia Mayoral, Maria Flor
Citation:

Citation: Garcia Mayoral, Maria Flor; Castano, Raquel; Zabala, Juan Carlos; Santoro, Jorge; Rico, Manuel; Bruix, Marta. "1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C"  Biomol. NMR Assignments 4, 219-221 (2010).
PubMed: 20617401

Assembly members:

Assembly members:
Human Tubulin Cofactor C, polymer, 111 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: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human Tubulin Cofactor C: MPERLQRREQERQLEVERRK QKRQNQEVEKENSHFFVATF ARERAAVEELLERAESVERL EEAASRLQGLQKLINDSVFF LAAYDLRQGQEALARLQAAL AERRRGLQPKK

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts108
1H chemical shifts797

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human Tubulin Cofactor C1

Entities:

Entity 1, Human Tubulin Cofactor C 111 residues - Formula weight is not available

1   METPROGLUARGLEUGLNARGARGGLUGLN
2   GLUARGGLNLEUGLUVALGLUARGARGLYS
3   GLNLYSARGGLNASNGLNGLUVALGLULYS
4   GLUASNSERHISPHEPHEVALALATHRPHE
5   ALAARGGLUARGALAALAVALGLUGLULEU
6   LEUGLUARGALAGLUSERVALGLUARGLEU
7   GLUGLUALAALASERARGLEUGLNGLYLEU
8   GLNLYSLEUILEASNASPSERVALPHEPHE
9   LEUALAALATYRASPLEUARGGLNGLYGLN
10   GLUALALEUALAARGLEUGLNALAALALEU
11   ALAGLUARGARGARGGLYLEUGLNPROLYS
12   LYS

Samples:

sample_1: TBCC_Nterm, [U-13C; U-15N], 0.5 – 1.0 mM; potassium phosphate 20 mM; potassium chloride 20 mM; TCEP 1.0 mM; EDTA 1.0 mM; DSS 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAG35561
EMBL CAH92969
GB AAB17539 AAH17479 AAH20170 AAP35648 AAP36382
REF NP_001126753 NP_003183 XP_003833336 XP_004044073 XP_518477
SP Q15814 Q5R5J7
AlphaFold Q15814 Q5R5J7

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