BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25910

Title: 1H, 13C, and 15N Chemical Shift Assignments for in-cell GB1   PubMed: 27910948

Deposition date: 2015-11-30 Original release date: 2016-12-21

Authors: Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka

Citation: Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka. "Improved in-cell structure determination of proteins at near-physiological concentration"  Sci. Rep. 6, 38312-38312 (2016).

Assembly members:
entity, polymer, 57 residues, 6258.896 Da.

Natural source:   Common Name: firmicutes   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

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

Entity Sequences (FASTA):
entity: MGTYKLILNGKTLKGETTTE AVDAATAEKVFKQYANDNGV DGEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts217
15N chemical shifts57
1H chemical shifts322

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 57 residues - 6258.896 Da.

1   METGLYTHRTYRLYSLEUILELEUASNGLY
2   LYSTHRLEULYSGLYGLUTHRTHRTHRGLU
3   ALAVALASPALAALATHRALAGLULYSVAL
4   PHELYSGLNTYRALAASNASPASNGLYVAL
5   ASPGLYGLUTRPTHRTYRASPASPALATHR
6   LYSTHRPHETHRVALTHRGLU

Samples:

sample_1: Protein G B1, [U-100% 13C; U-100% 15N], 250 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.31 M; pH: 7.0; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

AZARA v2.8.1, Boucher - processing

ANSIG v3.3, Kraulis - chemical shift assignment

Molmol v2.6, Koradi, Billeter and Wuthrich - structure solution

TALOS v1, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts