BMRB Entry 34191

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34191
MolProbity Validation Chart

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Title:
solution NMR structure of EB1 C terminus (191-260)
Deposition date:
2017-11-01
Original release date:
2019-03-28
Authors:
Barsukov, I.; Almeida, T.
Citation:

Citation: Almeida, T.; Carnell, A.; Barsukov, I.; Berry, N.. "Targeting SxIP-EB1 interaction: An integrated approach to the discovery of small molecule modulators of dynamic binding sites."  Sci. Rep. 7, 15533-15533 (2017).
PubMed: 29138501

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 8049.979 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DEAAELMQQVKVLKLTVEDL EKERDFYFGKLRNIELICQE NEGENDPVLQRIVDILYATD EGFVIPDEGG

Data sets:
Data typeCount
13C chemical shifts558
15N chemical shifts146
1H chemical shifts968

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 70 residues - 8049.979 Da.

1   ASPGLUALAALAGLULEUMETGLNGLNVAL
2   LYSVALLEULYSLEUTHRVALGLUASPLEU
3   GLULYSGLUARGASPPHETYRPHEGLYLYS
4   LEUARGASNILEGLULEUILECYSGLNGLU
5   ASNGLUGLYGLUASNASPPROVALLEUGLN
6   ARGILEVALASPILELEUTYRALATHRASP
7   GLUGLYPHEVALILEPROASPGLUGLYGLY

Samples:

sample_1: End binding protein 1 (EB1), [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CcpNMR, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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