BMRB Entry 6176

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6176
MolProbity Validation Chart

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Title:
Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B
Deposition date:
2004-04-13
Original release date:
2004-06-25
Authors:
Lytle, B.; Peterson, F.; Qui, S.; Luo, M.; Volkman, B.; Markley, J.
Citation:

Citation: Lytle, B.; Peterson, F.; Qui, S.; Luo, M.; Zhao, Q.; Markley, J.; Volkman, B.. "Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B"  J. Biol. Chem. 279, 46787-46793 (2004).
PubMed: 15364906

Assembly members:

Assembly members:
Ubiquitin-like domain of tubulin-folding cofactor B, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: C. elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubiquitin-like domain of tubulin-folding cofactor B: MTEVYDLEITTNATDFPMEK KYPAGMSLNDLKKKLELVVG TTVDSMRIQLFDGDDQLKGE LTDGAKSLKDLGVRDGYRIH AVDVTGGNEDFKDESMVEKY EMSDDTYGKRTDSVRAWKKK

Data sets:
Data typeCount
1H chemical shifts772
13C chemical shifts502
15N chemical shifts124

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin-like domain1

Entities:

Entity 1, ubiquitin-like domain 120 residues - Formula weight is not available

1   METTHRGLUVALTYRASPLEUGLUILETHR
2   THRASNALATHRASPPHEPROMETGLULYS
3   LYSTYRPROALAGLYMETSERLEUASNASP
4   LEULYSLYSLYSLEUGLULEUVALVALGLY
5   THRTHRVALASPSERMETARGILEGLNLEU
6   PHEASPGLYASPASPGLNLEULYSGLYGLU
7   LEUTHRASPGLYALALYSSERLEULYSASP
8   LEUGLYVALARGASPGLYTYRARGILEHIS
9   ALAVALASPVALTHRGLYGLYASNGLUASP
10   PHELYSASPGLUSERMETVALGLULYSTYR
11   GLUMETSERASPASPTHRTYRGLYLYSARG
12   THRASPSERVALARGALATRPLYSLYSLYS

Samples:

sample_1: Ubiquitin-like domain of tubulin-folding cofactor B, [U-13C; U-15N], 1 mM; NaCl 50 mM; sodium phosphate buffer 20 mM; H20 90%; D20 10%

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 70 mM

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablesample_cond_1
HNCAsample_1not availablesample_cond_1
HNCOsample_1not availablesample_cond_1
HN(CO)CAsample_1not availablesample_cond_1
HNCACBsample_1not availablesample_cond_1
HN(CA)COsample_1not availablesample_cond_1
C(CO)NHsample_1not availablesample_cond_1
HCCH-TOCSYsample_1not availablesample_cond_1
3D 15N-NOESYsample_1not availablesample_cond_1
3D 13C-NOESY-aliphaticsample_1not availablesample_cond_1
3D 13C-NOESY-aromaticsample_1not availablesample_cond_1

Software:

XWINNMR v3.1 - collection

NMRPipe v2.1 - processing

XEASY v1.3.1 - analysis

SPSCAN v1.1.0 - peak picking

GARANT v2.1 - automated backbone assignments

TALOS - generation of torsion angle restraints

CYANA v1.0.6 - refinement (torsion angle dynamics)

XPLOR-NIH v2.0.6 - refinement (cartesian MD in explicit solvent)

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAB01212
REF NP_506367
SP Q20728
AlphaFold Q20728

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