BMRB Entry 34629

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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/BMR34629
MolProbity Validation Chart

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Title:
EB1 bound to MACF peptide
Deposition date:
2021-05-20
Original release date:
2022-05-26
Authors:
Almeida, T.; Barsukov, I.
Citation:

Citation: Almeida, T.; Barsukov, I.. "EB1 bound to MACF peptide"  .

Assembly members:

Assembly members:
Microtubule-associated protein RP/EB family member 1, polymer, 70 residues, 8049.979 Da.
11MACF, polymer, 11 residues, 1283.561 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):
Microtubule-associated protein RP/EB family member 1: DEAAELMQQVKVLKLTVEDL EKERDFYFGKLRNIELICQE NEGENDPVLQRIVDILYATD EGFVIPDEGG
11MACF: KPSKIPTPQRK

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts72
1H chemical shifts538

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_32
4unit_42

Entities:

Entity 1, unit_1 70 residues - 8049.979 Da.

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

Entity 2, unit_3 11 residues - 1283.561 Da.

1   LYSPROSERLYSILEPROTHRPROGLNARG
2   LYS

Samples:

sample_1: cEB1, [U-13C; U-15N], 1.15 mM; 11MACF 1.265 mM

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

Experiments:

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

Software:

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

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

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE II 600 MHz
  • Bruker AVANCE II 800 MHz

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