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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

Polymer type: polypeptide(L)

Total1H13C15N
All93.5 % (1293 of 1383)92.5 % (667 of 721)93.3 % (502 of 538)100.0 % (124 of 124)
Backbone99.9 % (715 of 716)99.6 % (247 of 248)100.0 % (350 of 350)100.0 % (118 of 118)
Sidechain88.5 % (688 of 777)88.8 % (420 of 473)87.9 % (262 of 298)100.0 % (6 of 6)
Aromatic69.8 % (60 of 86)88.4 % (38 of 43)50.0 % (21 of 42)100.0 % (1 of 1)
Methyl94.1 % (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

Sample

Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1Ubiquitin-like domain of tubulin-folding cofactor B[U-13C; U-15N]1 mM
2NaCl50 mM
3sodium phosphate buffer20 mM
4H2090 %
5D2010 %

LACS Plot; CA
Referencing offset: -0.24 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.24 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.03 ppm, Outliers: 2 Detail
LACS Plot; CO
Referencing offset: 0.04 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 1T0Y, Strand ID: A Detail


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 ,
Citation 2
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , DOI 10.1007/bf00197809 ,
Citation 3
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
J. Biomol. NMR (1995), 6, 1-10, PubMed 22911575 , DOI 10.1007/BF00417486 ,
Citation 4
Automated sequence-specific NMR assignment of homologous proteins using the program GARANT
J. Biomol. NMR (1996), 7, 207-213, PubMed 22911044 , DOI 10.1007/BF00202037 ,
Citation 5
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 ,
Citation 6
Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
Herrmann, T., Guntert, P., Wuthrich, K.
J. Mol. Biol. (2002), 319, 209-227, PubMed 12051947 , DOI 10.1016/s0022-2836(02)00241-3 ,
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 ,
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    Title TBCB_CAEEL Entity Tubulin-specific chaperone B
Related entities 1. Ubiquitin-like domain of tubulin-folding cofactor B, : 1 : 2 : 20 entities Detail
Experiments performed 11 experiments Detail
nullKeywords ubiquitin-like, tubulin, microtubule, cytoskeleton, chaperone, Center for Eukaryotic Structural Genomics