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 19031

Title: Solid-state Chemical Shift Assignments for p150Glued CAP-Gly Domain in complex with EB1 at 19.9 T   PubMed: 23648839

Deposition date: 2013-02-12 Original release date: 2013-06-04

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, 9513 Da.
EB1, polymer, 75 residues, 8747 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b-His6-SMT3

Entity Sequences (FASTA):
CAP-Gly: STEASARPLRVGSRVEVIGK GHRGTVAYVGATLFATGKWV GVILDEAKGKNDGTVQGRKY FTCDEGHGIFVRQSQIQVFE DGADTTSPE
EB1: AELMQQVNVLKLTVEDLEKE RDFYFGKLRNIELICQENEG ENDPVLQRIVDILYATDEGF VIPDEGGPQEEQEEY

Data sets:
Data typeCount
13C chemical shifts258
15N chemical shifts65

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAP-Gly, 11
2CAP-Gly, 21
3EB1, 12
4EB1, 22

Entities:

Entity 1, CAP-Gly, 1 89 residues - 9513 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

Entity 2, EB1, 1 75 residues - 8747 Da.

This sequence starts from residue A193, and ends at residue Y268.

1   ALAGLULEUMETGLNGLNVALASNVALLEU
2   LYSLEUTHRVALGLUASPLEUGLULYSGLU
3   ARGASPPHETYRPHEGLYLYSLEUARGASN
4   ILEGLULEUILECYSGLNGLUASNGLUGLY
5   GLUASNASPPROVALLEUGLNARGILEVAL
6   ASPILELEUTYRALATHRASPGLUGLYPHE
7   VALILEPROASPGLUGLYGLYPROGLNGLU
8   GLUGLNGLUGLUTYR

Samples:

sample_1: CAP-Gly, [U-13C; U-15N], 11.8 mg; EB1 10.2 mg; H2O 100%

sample_conditions_1: ionic strength: 90 mM; pH: 7.0; 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 19025 25005 18371
PDB
DBJ BAE34241 BAE37079 BAE42418 BAE42912 BAE87998 BAE32461 BAE89438 BAG35484 BAG59745 BAG73401
EMBL CAA44091 CAA67333 CAE45882 CAH10572 CAH10575 CAH92115
GB AAB57773 AAD03694 AAD55811 AAH66061 AAI42510 AAA96320 AAC09471 AAH52405 AAH64444 AAH81726
REF NP_001092404 NP_001127253 NP_001128512 NP_001177765 NP_001177766 NP_001038078 NP_001068802 NP_001126236 NP_001238875 NP_001253729
SP O08788 P28023 Q14203 Q15691 Q3ZBD9 Q5R7Z5 Q61166 Q66HR2
TPG DAA24857 DAA23186
AlphaFold O08788 P28023 Q14203 Q3ZBD9 Q5R7Z5 Q61166 Q15691 Q66HR2