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 50310

Title: Backbone 1H, and 15N chemical shift Assignments for the ligand-free GlnBP   PubMed: 35446849

Deposition date: 2020-06-08 Original release date: 2022-05-09

Authors: Qin, Peiwu; Yu, Dongmei; Chen, Qun

Citation: Chen, Qun; Li, Fang; Zuo, Xiaobing; Chen, Jin; Qin, Peiwu; Wang, Chuhui; Xu, Jin; Yang, Danyu; Xing, Baogang; Liu, Ying; Jia, Peng; Li, Linling; Yang, Chengming; Yu, Dongmei. "Reversible domain closure modulates GlnBP ligand binding affinity"  PLoS One 17, e0263102-e0263102 (2022).

Assembly members:
entity_1, polymer, 248 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: pET11a

Entity Sequences (FASTA):
entity_1: MKSVLKVSLAALTLAFAVSS HAADKKLVVATDTAFVPFEF KQGDKYVGFDVDLWAAIAKE LKLDYELKPMDFSGIIPALQ TKNVDLALAGITITDERKKA IDFSDGYYKSGLLVMVKANN NDVKSVKDLDGKVVAVKSGT GSVDYAKANIKTKDKRQFPN IDNAYMELGTNRADAVLHDT PNILYFIKTAGNGQFKAVGD SLEAQQYGIAFPKGSDEQRD KVNGALKTLRENGTYNEIYK KWFGTEPK

Data sets:
Data typeCount
15N chemical shifts151
1H chemical shifts151

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GlnBP1

Entities:

Entity 1, GlnBP 248 residues - Formula weight is not available

1   METLYSSERVALLEULYSVALSERLEUALA
2   ALALEUTHRLEUALAPHEALAVALSERSER
3   HISALAALAASPLYSLYSLEUVALVALALA
4   THRASPTHRALAPHEVALPROPHEGLUPHE
5   LYSGLNGLYASPLYSTYRVALGLYPHEASP
6   VALASPLEUTRPALAALAILEALALYSGLU
7   LEULYSLEUASPTYRGLULEULYSPROMET
8   ASPPHESERGLYILEILEPROALALEUGLN
9   THRLYSASNVALASPLEUALALEUALAGLY
10   ILETHRILETHRASPGLUARGLYSLYSALA
11   ILEASPPHESERASPGLYTYRTYRLYSSER
12   GLYLEULEUVALMETVALLYSALAASNASN
13   ASNASPVALLYSSERVALLYSASPLEUASP
14   GLYLYSVALVALALAVALLYSSERGLYTHR
15   GLYSERVALASPTYRALALYSALAASNILE
16   LYSTHRLYSASPLYSARGGLNPHEPROASN
17   ILEASPASNALATYRMETGLULEUGLYTHR
18   ASNARGALAASPALAVALLEUHISASPTHR
19   PROASNILELEUTYRPHEILELYSTHRALA
20   GLYASNGLYGLNPHELYSALAVALGLYASP
21   SERLEUGLUALAGLNGLNTYRGLYILEALA
22   PHEPROLYSGLYSERASPGLUGLNARGASP
23   LYSVALASNGLYALALEULYSTHRLEUARG
24   GLUASNGLYTHRTYRASNGLUILETYRLYS
25   LYSTRPPHEGLYTHRGLUPROLYS

Samples:

sample_1: Glutamine binding protein (GlnBP), [U-100% 15N], 500 uM

sample_conditions_1: ionic strength: 0.003 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

MARS - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHZ MHz

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