BMRB Entry 34187

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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/BMR34187
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, 5613.384 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: GSTPPQALQQLLQTLKSPSS PQQQQQVLQILKSNPQLMAA FIKQRSQHQQ

Data typeCount
13C chemical shifts233
15N chemical shifts93
1H chemical shifts604

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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 - 5613.384 Da.

1   GLYSERTHRPROPROGLNALALEUGLNGLN
2   LEULEUGLNTHRLEULYSSERPROSERSER
3   PROGLNGLNGLNGLNGLNVALLEUGLNILE
4   LEULYSSERASNPROGLNLEUMETALAALA
5   PHEILELYSGLNARGSERGLNHISGLNGLN

Samples:

sample_1: entity_1, [U-100% 13C], 100 uM; entity_2, [U-100% 15N], 100 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-1H NOESYsample_1isotropicsample_conditions_1
Filtered NOESYsample_1isotropicsample_conditions_1
3JHNHAsample_1isotropicsample_conditions_1
3JHNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
T1, T2, NOEsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker AvanceII 700 MHz
  • Bruker AvanceII 900 MHz

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