BMRB Entry 6176

Name: Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B
Published: 2004-06-25

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PDB ID: 1t0y
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
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B PubMed: 15364906

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: 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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	772
13C chemical shifts	502
15N chemical shifts	124

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin-like domain	1

Entities:

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

1	MET	THR	GLU	VAL	TYR	ASP	LEU	GLU	ILE	THR
2	THR	ASN	ALA	THR	ASP	PHE	PRO	MET	GLU	LYS
3	LYS	TYR	PRO	ALA	GLY	MET	SER	LEU	ASN	ASP
4	LEU	LYS	LYS	LYS	LEU	GLU	LEU	VAL	VAL	GLY
5	THR	THR	VAL	ASP	SER	MET	ARG	ILE	GLN	LEU
6	PHE	ASP	GLY	ASP	ASP	GLN	LEU	LYS	GLY	GLU
7	LEU	THR	ASP	GLY	ALA	LYS	SER	LEU	LYS	ASP
8	LEU	GLY	VAL	ARG	ASP	GLY	TYR	ARG	ILE	HIS
9	ALA	VAL	ASP	VAL	THR	GLY	GLY	ASN	GLU	ASP
10	PHE	LYS	ASP	GLU	SER	MET	VAL	GLU	LYS	TYR
11	GLU	MET	SER	ASP	ASP	THR	TYR	GLY	LYS	ARG
12	THR	ASP	SER	VAL	ARG	ALA	TRP	LYS	LYS	LYS

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:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	sample_1	not available	sample_cond_1
HNCA	sample_1	not available	sample_cond_1
HNCO	sample_1	not available	sample_cond_1
HN(CO)CA	sample_1	not available	sample_cond_1
HNCACB	sample_1	not available	sample_cond_1
HN(CA)CO	sample_1	not available	sample_cond_1
C(CO)NH	sample_1	not available	sample_cond_1
HCCH-TOCSY	sample_1	not available	sample_cond_1
3D 15N-NOESY	sample_1	not available	sample_cond_1
3D 13C-NOESY-aliphatic	sample_1	not available	sample_cond_1
3D 13C-NOESY-aromatic	sample_1	not available	sample_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

PDB	1T0Y
EMBL	CAB01212
REF	NP_506367
SP	Q20728
AlphaFold	Q20728

Biological Magnetic Resonance Data Bank