BMRB Entry 34188

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PDB ID: 6es6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34188
MolProbity Validation Chart

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Title:
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Deposition date:
2017-10-19
Original release date:
2019-03-21
Authors:
Chi, N.
Citation:

Citation: Jemth, Per; Karlsson, Elin; Vogeli, Beat; Guzovsky, Brenda; Andersson, Eva; Hultqvist, Greta; Dogan, Jakob; Guntert, Peter; Riek, Roland; Chi, Celestine. "Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins"  Sci. Adv. 4, eaau4130-eaau4130 (2018).
PubMed: 30397651

Assembly members:

Assembly members:
entity_1, polymer, 45 residues, 4823.197 Da.
entity_2, polymer, 50 residues, 5594.450 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):
entity_1: GSESQNDEKALLDQLDSLLS STDEMELAEIDRALGIDKLV SQQGG
entity_2: GSIPPNALQDLLRTLRSPSS PQQQQQVLNILKSNPQLMAA FIKQRAAKYQ

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts87
1H chemical shifts588

Additional metadata:

  • Assembly
  • Samples and Experiments
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 45 residues - 4823.197 Da.

1   GLYSERGLUSERGLNASNASPGLULYSALA
2   LEULEUASPGLNLEUASPSERLEULEUSER
3   SERTHRASPGLUMETGLULEUALAGLUILE
4   ASPARGALALEUGLYILEASPLYSLEUVAL
5   SERGLNGLNGLYGLY

Entity 2, entity_2 50 residues - 5594.450 Da.

1   GLYSERILEPROPROASNALALEUGLNASP
2   LEULEUARGTHRLEUARGSERPROSERSER
3   PROGLNGLNGLNGLNGLNVALLEUASNILE
4   LEULYSSERASNPROGLNLEUMETALAALA
5   PHEILELYSGLNARGALAALALYSTYRGLN

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