BMRB Entry 36353

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36353
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Complex structure of tyrosinated alpha-tubulin carboxy-terminal peptide and A1aY1 binder
Deposition date:
2020-05-05
Original release date:
2025-10-13
Authors:
Kesarwani, S.; Reddy, P.; Sirajuddin, M.; Das, R.
Citation:

Citation: Kesarwani, Shubham; Lama, Prakash; Chandra, Anchal; Reddy, P; Jijumon, A; Bodakuntla, Satish; Rao, Balaji; Janke, Carsten; Das, Ranabir; Sirajuddin, Minhajuddin. "Genetically encoded live-cell sensor for tyrosinated microtubules."  J. Cell Biol. 219, .-. (2020).
PubMed: 32886100

Assembly members:

Assembly members:
Nanobody binder from SSO7d library, polymer, 67 residues, 7486.859 Da.
Carboxy-terminal peptide from tyrosinated alpha-tubulin, polymer, 12 residues, 1355.272 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 555311   Superkingdom: not available   Kingdom: Thermoproteati   Genus/species: Saccharolobus solfataricus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nanobody binder from SSO7d library: GSHMATVKFKYKGEEKQVDI SKILSVGRYGKLIHFLYDLG GGKAGMGMVSEKDAPKELLQ MLEKQKK
Carboxy-terminal peptide from tyrosinated alpha-tubulin: VEGEGEEEGEEY

Data sets:
Data typeCount
13C chemical shifts179
15N chemical shifts57
1H chemical shifts284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 67 residues - 7486.859 Da.

1   GLYSERHISMETALATHRVALLYSPHELYS
2   TYRLYSGLYGLUGLULYSGLNVALASPILE
3   SERLYSILELEUSERVALGLYARGTYRGLY
4   LYSLEUILEHISPHELEUTYRASPLEUGLY
5   GLYGLYLYSALAGLYMETGLYMETVALSER
6   GLULYSASPALAPROLYSGLULEULEUGLN
7   METLEUGLULYSGLNLYSLYS

Entity 2, entity_2 12 residues - 1355.272 Da.

1   VALGLUGLYGLUGLYGLUGLUGLUGLYGLU
2   GLUTYR

Samples:

sample_1: Nanobody binder mM; Nanobody binder mM; sodium chloride 200 mM; sodium phosphate 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D Filtered NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D Filtered TOCSYsample_1isotropicsample_conditions_1
3D 13C-filtered, 13C-edited NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

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

Sparky, Goddard - data analysis

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

HADDOCK, Bonvin - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks