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 50123

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50123

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Title: Backbone 13C, and 15N Chemical Shift Assignments for KirBac1.1   PubMed: 31980523

Deposition date: 2019-12-11 Original release date: 2019-12-19

Authors: Amani, Reza

Citation: Amani, Reza; Borcik, Collin; Khan, Nazmul; Versteeg, Derek; Yekefallah, Maryam; Do, Hoa; Coats, Heather; Wylie, Benjamin. "Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays"  Proc. Natl. Acad. Sci. U.S.A. 117, 2938-2947 (2020).

Assembly members:
entity_1, polymer, 345 residues, Formula weight is not available

Natural source:   Common Name: Burkholderia Pseudomallei   Taxonomy ID: 28450   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia Pseudomallei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE60

Entity Sequences (FASTA):
entity_1: MNVDPFSPHSSDSFAQAASP ARKPPRGGRRIWSGTREVIA YGMPASVWRDLYYWALKVSW PVFFASLAALFVVNNTLFAL LYQLGDAPIANQSPPGFVGA FFFSVETLATVGYGDMHPQT VYAHAIATLECFVGMSGIAL STGLVFARFARPRAKIMFAR HAIVRPFNGRMTLMVRAANA RQNVIAEARAKMRLMRREHS SEGYSLMKIHDLKLVRNEHP IFLLGWNMMHVIDESSPLFG ETPESLAEGRAMLLVMIEGS DETTAQVMQARHAWEHDDIR WHHRYVDLMSDVDGMTHIDY TRFNDTEPVEPPGAAPDAQA FAAKPGEGDARPVPRGSRSH HHHHH

Data sets:
Data typeCount
13C chemical shifts1311
15N chemical shifts316

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Kirbac1.1, chain 11
2Kirbac1.1, chain 21
3Kirbac1.1, chain 31
4Kirbac1.1, chain 41

Entities:

Entity 1, Kirbac1.1, chain 1 345 residues - Formula weight is not available

1   METASNVALASPPROPHESERPROHISSER
2   SERASPSERPHEALAGLNALAALASERPRO
3   ALAARGLYSPROPROARGGLYGLYARGARG
4   ILETRPSERGLYTHRARGGLUVALILEALA
5   TYRGLYMETPROALASERVALTRPARGASP
6   LEUTYRTYRTRPALALEULYSVALSERTRP
7   PROVALPHEPHEALASERLEUALAALALEU
8   PHEVALVALASNASNTHRLEUPHEALALEU
9   LEUTYRGLNLEUGLYASPALAPROILEALA
10   ASNGLNSERPROPROGLYPHEVALGLYALA
11   PHEPHEPHESERVALGLUTHRLEUALATHR
12   VALGLYTYRGLYASPMETHISPROGLNTHR
13   VALTYRALAHISALAILEALATHRLEUGLU
14   CYSPHEVALGLYMETSERGLYILEALALEU
15   SERTHRGLYLEUVALPHEALAARGPHEALA
16   ARGPROARGALALYSILEMETPHEALAARG
17   HISALAILEVALARGPROPHEASNGLYARG
18   METTHRLEUMETVALARGALAALAASNALA
19   ARGGLNASNVALILEALAGLUALAARGALA
20   LYSMETARGLEUMETARGARGGLUHISSER
21   SERGLUGLYTYRSERLEUMETLYSILEHIS
22   ASPLEULYSLEUVALARGASNGLUHISPRO
23   ILEPHELEULEUGLYTRPASNMETMETHIS
24   VALILEASPGLUSERSERPROLEUPHEGLY
25   GLUTHRPROGLUSERLEUALAGLUGLYARG
26   ALAMETLEULEUVALMETILEGLUGLYSER
27   ASPGLUTHRTHRALAGLNVALMETGLNALA
28   ARGHISALATRPGLUHISASPASPILEARG
29   TRPHISHISARGTYRVALASPLEUMETSER
30   ASPVALASPGLYMETTHRHISILEASPTYR
31   THRARGPHEASNASPTHRGLUPROVALGLU
32   PROPROGLYALAALAPROASPALAGLNALA
33   PHEALAALALYSPROGLYGLUGLYASPALA
34   ARGPROVALPROARGGLYSERARGSERHIS
35   HISHISHISHISHIS

Samples:

sample_1: entity_1, [U-13C; U-15N], 25%; H2O 55.55 M; POPC 66%; POPG 33%; KCl 50 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D NCACXsample_1isotropicsample_conditions_1
3D NCOCXsample_1isotropicsample_conditions_1
3D CANcoCAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • JEOL ASC 600 MHz