BMRB Entry 30074

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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/BMR30074
MolProbity Validation Chart

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Title:
Molecular basis for protein recognition specificity of the DYNLT1/Tctex1 canonical binding groove. Characterization of the interaction with activin receptor IIB
Deposition date:
2016-05-04
Original release date:
2016-08-11
Authors:
Rodriguez-Crespo, I.; Merino-Gracia, J.; Bruix, M.; Zamora-Carreras, H.
Citation:

Citation: Rodriguez-Crespo, I.; Merino-Gracia, J.; Bruix, M.; Zamora-Carreras, H.. "Molecular basis for protein recognition specificity of the DYNLT1/Tctex1 canonical binding groove. Characterization of the interaction with activin receptor IIB"  J. Biol. Chem. 291, 20962-20975 (2016).
PubMed: 27502274

Assembly members:

Assembly members:
Dynein light chain Tctex-type 1,Cytoplasmic dynein 1 intermediate chain 2, polymer, 143 residues, 15431.400 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dynein light chain Tctex-type 1,Cytoplasmic dynein 1 intermediate chain 2: GSMEDYQAAEETAFVVDEVS NIVKEAIESAIGGNAYQHSK VNQWTTNVVEQTLSQLTKLG KPFKYIVTCVIMQKNGAGLH TASSCFWDSSTDGSCTVRWE NKTMYCIVSAFGLSIGGGSG QSGPIKLGMAKITQVDFPPR EIV

Data sets:
Data typeCount
13C chemical shifts808
15N chemical shifts268
1H chemical shifts1672

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

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

Entities:

Entity 1, entity_1, chain 1 143 residues - 15431.400 Da.

1   GLYSERMETGLUASPTYRGLNALAALAGLU
2   GLUTHRALAPHEVALVALASPGLUVALSER
3   ASNILEVALLYSGLUALAILEGLUSERALA
4   ILEGLYGLYASNALATYRGLNHISSERLYS
5   VALASNGLNTRPTHRTHRASNVALVALGLU
6   GLNTHRLEUSERGLNLEUTHRLYSLEUGLY
7   LYSPROPHELYSTYRILEVALTHRCYSVAL
8   ILEMETGLNLYSASNGLYALAGLYLEUHIS
9   THRALASERSERCYSPHETRPASPSERSER
10   THRASPGLYSERCYSTHRVALARGTRPGLU
11   ASNLYSTHRMETTYRCYSILEVALSERALA
12   PHEGLYLEUSERILEGLYGLYGLYSERGLY
13   GLNSERGLYPROILELYSLEUGLYMETALA
14   LYSILETHRGLNVALASPPHEPROPROARG
15   GLUILEVAL

Samples:

sample_1: DSS 50 uM; DTT 1 mM; DYNLT1/Tctex1-DIC chimera 100 uM; potassium phosphate 100 mM; H2O 90%; D2O 10%

sample_2: DSS 50 uM; DTT 1 mM; DYNLT1/Tctex1-DIC chimera, [U-99% 15N], 100 uM; potassium phosphate 100 mM; H2O 90%; D2O 10%

sample_3: DSS 50 uM; DTT 1 mM; DYNLT1/Tctex1-DIC chimera, [U-99% 13C; U-99% 15N], 100 uM; potassium phosphate 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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