BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19025

Title: Solid-state Chemical Shift Assignments for CAP-Gly Domain of Mammalian at 19.9 T   PubMed: 23648839

Authors: Yan, Si; Hou, Guangjin; Schwieters, Charles; Ahmed, Shubbir; Williams, John; Polenova, Tatyana

Citation: Yan, Si; Hou, Guangjin; Schwieters, Charles; Ahmed, Shubbir; Williams, John; Polenova, Tatyana. "Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1."  J. Mol. Biol. 425, 4249-4266 (2013).

Assembly members:
CAP-Gly, polymer, 89 residues, 9530 Da.

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
CAP-Gly: STEASARPLRVGSRVEVIGK GHRGTVAYVGATLFATGKWV GVILDEAKGKNDGTVQGRKY FTCDEGHGIFVRQSQIQVFE DGADTTSPE

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAP-Gly1

Entities:

Entity 1, CAP-Gly 89 residues - 9530 Da.

The sequence starts from S19, and ends at E107. Residues S19-P26 and E98-E107 are not assigned due to the dynamics of the termini.

1   SERTHRGLUALASERALAARGPROLEUARG
2   VALGLYSERARGVALGLUVALILEGLYLYS
3   GLYHISARGGLYTHRVALALATYRVALGLY
4   ALATHRLEUPHEALATHRGLYLYSTRPVAL
5   GLYVALILELEUASPGLUALALYSGLYLYS
6   ASNASPGLYTHRVALGLNGLYARGLYSTYR
7   PHETHRCYSASPGLUGLYHISGLYILEPHE
8   VALARGGLNSERGLNILEGLNVALPHEGLU
9   ASPGLYALAASPTHRTHRSERPROGLU

Samples:

sample_1: CAP-Gly, [U-13C; U-15N], 24.4 mg; H2O 100%

sample_conditions_1: ionic strength: 30 mM; pH: 6.0; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D DARRsample_1solidsample_conditions_1
2D NCAsample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1
3D CANCXsample_1solidsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Ascend 850 MHz

Related Database Links:

BMRB 17937 17938 19031 25005
PDB
DBJ BAE34241 BAE37079 BAE42418 BAE42912 BAE87998
EMBL CAA44091 CAA67333 CAE45882 CAH10572 CAH10575
GB AAB57773 AAD03694 AAD55811 AAH66061 AAI42510
REF NP_001092404 NP_001127253 NP_001128512 NP_001177765 NP_001177766
SP O08788 P28023 Q14203
TPG DAA24857