BMRB: 6176

Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B

Authors

Lytle, B.L., Peterson, F.C., Qui, S.H., Luo, M., Volkman, B.F., Markley, J.L.

Assembly

Ubiquitin-like domain of tubulin-folding cofactor B

Entity

1. Ubiquitin-like domain of tubulin-folding cofactor B (polymer, Thiol state: not present), 120 monomers, 13580.12 Da Detail

MTEVYDLEIT TNATDFPMEK KYPAGMSLND LKKKLELVVG TTVDSMRIQL FDGDDQLKGE LTDGAKSLKD LGVRDGYRIH AVDVTGGNED FKDESMVEKY EMSDDTYGKR TDSVRAWKKK

Formula weight

13580.12 Da

Source organism

Caenorhabditis elegans

Exptl. method

NMR

Refine. method

TORSION ANGLE DYNAMICS FOLLOWED BY CARTESIAN MOLECULAR DYNAMICS IN EXPLICIT SOLVENT

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 93.5 %, Completeness (bb): 99.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	93.5 % (1293 of 1383)	92.5 % (667 of 721)	93.3 % (502 of 538)	100.0 % (124 of 124)
Backbone	99.9 % (715 of 716)	99.6 % (247 of 248)	100.0 % (350 of 350)	100.0 % (118 of 118)
Sidechain	88.5 % (688 of 777)	88.8 % (420 of 473)	87.9 % (262 of 298)	100.0 % (6 of 6)
Aromatic	69.8 % (60 of 86)	88.4 % (38 of 43)	50.0 % (21 of 42)	100.0 % (1 of 1)
Methyl	94.1 % (111 of 118)	94.9 % (56 of 59)	93.2 % (55 of 59)

1. Ubiquitin-like domain of tubulin-folding cofactor B

MTEVYDLEIT TNATDFPMEK KYPAGMSLND LKKKLELVVG TTVDSMRIQL FDGDDQLKGE LTDGAKSLKD LGVRDGYRIH AVDVTGGNED FKDESMVEKY EMSDDTYGKR TDSVRAWKKK

Show sample condition

Sample

Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	Ubiquitin-like domain of tubulin-folding cofactor B	[U-13C; U-15N]		1 mM
2	NaCl			50 mM
3	sodium phosphate buffer			20 mM
4	H20			90 %
5	D20			10 %

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LACS Plot; CA

Referencing offset: -0.24 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; CB

Referencing offset: -0.24 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; HA

Referencing offset: 0.03 ppm, Outliers: 2 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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LACS Plot; CO

Referencing offset: 0.04 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

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Protein Blocks Logo

Calculated from 20 models in PDB: 1T0Y, Strand ID: A Detail

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Release date

2004-06-24

Citation 1

Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B
Lytle, B.L., Peterson, F.C., Qui, S.H., Luo, M., Zhao, Q., Markley, J.L., Volkman, B.F.
J. Biol. Chem. (2004), 279, 46787-46793, PubMed 15364906 , DOI 10.1074/jbc.M409422200 , Abstract

Show more 6 citaions

Citation 2

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Citation 3

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Citation 4

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Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 , Abstract

Citation 6

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J. Mol. Biol. (2002), 319, 209-227, PubMed 12051947 , DOI 10.1016/s0022-2836(02)00241-3 , Abstract

Citation 7

The Xplor-NIH NMR molecular structure determination package
Schwieters, C.D., Kuszewski, J.J., Tjandra, N., Clore, G.M.
J. Magn. Reson. (2003), 160, 65-73, PubMed 12565051 , DOI 10.1016/s1090-7807(02)00014-9 , Abstract

Hide non-primary 6 citaions

Related entities 1. Ubiquitin-like domain of tubulin-folding cofactor B, : 1 : 2 : 20 entities Detail

Experiments performed 11 experiments Detail