BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34430

Title: NMR solution structure of staphylococcal protein A, C domain

Deposition date: 2019-08-30 Original release date: 2020-09-07

Authors: Backlund, S.; Iwai, H.

Citation: Backlund, S.; Iwai, H.. "NMR solution structure of staphylococcal protein A, C domain"  . ., .-..

Assembly members:
entity_1, polymer, 58 residues, 6653.353 Da.

Natural source:   Common Name: Staphylococcus aureus   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_1: SDNKFNKEQQNAFYEILHLP NLTEEQRNGFIQSLKDDPSV SKEILAEAKKLNDAQAPK

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts68
1H chemical shifts418

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 58 residues - 6653.353 Da.

1   SERASPASNLYSPHEASNLYSGLUGLNGLN
2   ASNALAPHETYRGLUILELEUHISLEUPRO
3   ASNLEUTHRGLUGLUGLNARGASNGLYPHE
4   ILEGLNSERLEULYSASPASPPROSERVAL
5   SERLYSGLUILELEUALAGLUALALYSLYS
6   LEUASNASPALAGLNALAPROLYS

Samples:

sample_1: Protein A C domain, [U-20% 13C; U-100% 15N], 5.6 mM

sample_2: Protein A C domain, [U-20% 13C; U-100% 15N], 2.8 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
3D HNCAsample_1isotropicsample_conditions_1
2D CACOsample_2isotropicsample_conditions_2
2D CONsample_2isotropicsample_conditions_2
3D HCCH-COSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCACBisample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOisample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

PSVS v1.5, Bhattacharya and Montelione - data analysis

TALOS vN, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE 850 MHz

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