BMRB Entry 31084

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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/BMR31084
MolProbity Validation Chart

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Title:
Solution structure of the model miniprotein HHH_rd4_0518
Deposition date:
2023-04-20
Original release date:
2024-04-16
Authors:
Houliston, S.; Carter, L.; Baker, D.; Arrowsmith, C.; Rocklin, G.
Citation:

Citation: Houliston, S.; Carter, L.; Baker, D.; Arrowsmith, C.; Rocklin, G.. "Solution structure of the model miniprotein HHH_rd4_0518"  .

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7489.482 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MNEKVEKIVEELLRRGYSEE DIRRYLKKQGIDDREVDRAI KKVG

Data sets:
Data typeCount
13C chemical shifts191
15N chemical shifts41
1H chemical shifts313

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 64 residues - 7489.482 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METASNGLULYSVALGLULYSILEVALGLU
4   GLULEULEUARGARGGLYTYRSERGLUGLU
5   ASPILEARGARGTYRLEULYSLYSGLNGLY
6   ILEASPASPARGGLUVALASPARGALAILE
7   LYSLYSVALGLY

Samples:

sample_1: miniprotein, [U-100% 13C; U-100% 15N], 200 uM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE II 800 MHz

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