BMRB Entry 30681

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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/BMR30681
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
3D structure of the leiomodin/tropomyosin binding interface
Deposition date:
2019-10-29
Original release date:
2020-09-28
Authors:
Tolkatchev, D.; Smith, G.; Helms, G.; Cort, J.; Kostyukova, A.
Citation:

Citation: Tolkatchev, Dmitri; Smith, Garry; Schultz, Lauren; Colpan, Mert; Helms, Gregory; Cort, John; Gregorio, Carol; Kostyukova, Alla. "Leiomodin creates a leaky cap at the pointed end of actin-thin filaments"  PLoS Biol. 18, e3000848-e3000848 (2020).
PubMed: 32898131

Assembly members:

Assembly members:
entity_1, polymer, 40 residues, 4669.050 Da.
entity_2, polymer, 33 residues, 3909.709 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STFGYRRGLSKYESIDEDEL LASLSAEELKELERELEDIE
entity_2: GMDAIKKKMQMLKLDNYHLE NEVARLKKLVGER

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts70
1H chemical shifts337

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 40 residues - 4669.050 Da.

1   SERTHRPHEGLYTYRARGARGGLYLEUSER
2   LYSTYRGLUSERILEASPGLUASPGLULEU
3   LEUALASERLEUSERALAGLUGLULEULYS
4   GLULEUGLUARGGLULEUGLUASPILEGLU

Entity 2, entity_2, 1 33 residues - 3909.709 Da.

1   GLYMETASPALAILELYSLYSLYSMETGLN
2   METLEULYSLEUASPASNTYRHISLEUGLU
3   ASNGLUVALALAARGLEULYSLYSLEUVAL
4   GLYGLUARG

Samples:

sample_1: leiomodin peptide, [U-13C; U-15N], 0.5 ± 0.1 mM; tropomyosin peptide 1 ± 0.2 mM

sample_2: leiomodin peptide 1 ± 0.2 mM; tropomyosin peptide, [U-13C; U-15N], 0.5 ± 0.1 mM

sample_3: leiomodin peptide, [U-15N], 0.3 ± 0.05 mM; tropomyosin peptide 0.6 ± 0.1 mM

sample_4: leiomodin peptide 0.6 ± 0.1 mM; tropomyosin peptide, [U-15N], 0.3 ± 0.05 mM

sample_conditions_1: ionic strength: 0.081 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

TALOS vTALOS+, Cornilescu, Delaglio and Bax - structure calculation

NMRView v9.2.0-b4, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian INOVA 500 MHz

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