BMRB Entry 53269

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53269

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Title:
NP artificial IDP, backbone chemical shifts
Deposition date:
2025-07-10
Original release date:
2026-06-11
Authors:
Kobayashi, Ryoga
Citation:

Citation: Kobayashi, Ryoga. "Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins "  PNAS Nexus ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 91 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHHHHHHHSENL YFQGGNMAQLPGQVQMGGQS VPGSPSYQVNQPSYGRYASN WGQPQPAGTYPQQPVGNQFV EPGTYSYPAWW

Data sets:
Data typeCount
13C chemical shifts172
15N chemical shifts62
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1His-TEV-NP1

Entities:

Entity 1, His-TEV-NP 91 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   HISHISHISHISHISHISSERGLUASNLEU
3   TYRPHEGLNGLYGLYASNMETALAGLNLEU
4   PROGLYGLNVALGLNMETGLYGLYGLNSER
5   VALPROGLYSERPROSERTYRGLNVALASN
6   GLNPROSERTYRGLYARGTYRALASERASN
7   TRPGLYGLNPROGLNPROALAGLYTHRTYR
8   PROGLNGLNPROVALGLYASNGLNPHEVAL
9   GLUPROGLYTHRTYRSERTYRPROALATRP
10   TRP

Samples:

sample_1: His-TEV-NP, [U-13C; U-15N], 500 uM; D2O 5%; DTT 1 mM; sodium chloride 150 mM; MES 50 mM; 1,6-hexanediol 12%

sample_conditions_1: pH: 6.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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