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 50157

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50157

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Title: BR-PsrP   PubMed: 32314099

Deposition date: 2020-01-14 Original release date: 2021-08-12

Authors: Agback, Peter

Citation: Schulte, Tim; Sala, Benedetta; Nilvebrant, Johan; Nygren, Per-Ake; Achour, Adnane; Shernyukov, Andrey; Agback, Tatiana; Agback, Peter. "Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution"  Biomol. NMR Assignments 14, 195-200 (2020).

Assembly members:
BR-PsrP, polymer, 200 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21d

Entity Sequences (FASTA):
BR-PsrP: GSGNTIVNGAPAINASLNIA KSETKVYTGEGVDSVYRVPI YYKLKVTNDGSKLTFTYTVT YVNPKTNDLGNISSMRPGYS IYNSGTSTQTMLTLGSDLGK PSGVKNYITDKNGRQVLSYN TSTMTTQGSGYTWGNGAQMN GFFAKKGYGLTSSWTVPITG TDTSFTFTPYAARTDRIGIN YFNGGGKVVESSTTSQSLSQ

Data sets:
Data typeCount
13C chemical shifts554
15N chemical shifts181
1H chemical shifts350

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BR-PsrP1

Entities:

Entity 1, BR-PsrP 200 residues - Formula weight is not available

1   GLYSERGLYASNTHRILEVALASNGLYALA
2   PROALAILEASNALASERLEUASNILEALA
3   LYSSERGLUTHRLYSVALTYRTHRGLYGLU
4   GLYVALASPSERVALTYRARGVALPROILE
5   TYRTYRLYSLEULYSVALTHRASNASPGLY
6   SERLYSLEUTHRPHETHRTYRTHRVALTHR
7   TYRVALASNPROLYSTHRASNASPLEUGLY
8   ASNILESERSERMETARGPROGLYTYRSER
9   ILETYRASNSERGLYTHRSERTHRGLNTHR
10   METLEUTHRLEUGLYSERASPLEUGLYLYS
11   PROSERGLYVALLYSASNTYRILETHRASP
12   LYSASNGLYARGGLNVALLEUSERTYRASN
13   THRSERTHRMETTHRTHRGLNGLYSERGLY
14   TYRTHRTRPGLYASNGLYALAGLNMETASN
15   GLYPHEPHEALALYSLYSGLYTYRGLYLEU
16   THRSERSERTRPTHRVALPROILETHRGLY
17   THRASPTHRSERPHETHRPHETHRPROTYR
18   ALAALAARGTHRASPARGILEGLYILEASN
19   TYRPHEASNGLYGLYGLYLYSVALVALGLU
20   SERSERTHRTHRSERGLNSERLEUSERGLN

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 0.7 mM; sodium phosphate 50 mM; sodium chloride 100 mM; NaN3 1 mM

sample_conditions_1: ionic strength: 0.151 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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