BMRB Entry 25839

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25839
MolProbity Validation Chart

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Title:
THE STRUCTURE OF KBP.K FROM E. COLI
Deposition date:
2015-10-06
Original release date:
2016-05-23
Authors:
Smith, Brian; Ashraf, Khuram; Walker, Daniel
Citation:

Citation: Ashraf, Khuram; Josts, Inokentijs; Mosbahi, Khedidja; Kelly, Sharon; Byron, Olwyn; Smith, Brian; Walker, Daniel. "The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor"  Structure 24, 741-749 (2016).
PubMed: 27112601

Assembly members:

Assembly members:
YgaU, polymer, 157 residues, 17133.2295 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YgaU: MGLFNFVKDAGEKLWDAVTG QHDKDDQAKKVQEHLNKTGI PDADKVNIQIADGKATVTGD GLSQEAKEKILVAVGNISGI ASVDDQVKTATPATASQFYT VKSGDTLSAISKQVYGNANL YNKIFEANKPMLKSPDKIYP GQVLRIPEELEHHHHHH

Data typeCount
13C chemical shifts658
15N chemical shifts160
1H chemical shifts1061

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YgaU1

Entities:

Entity 1, YgaU 157 residues - 17133.2295 Da.

1   METGLYLEUPHEASNPHEVALLYSASPALA
2   GLYGLULYSLEUTRPASPALAVALTHRGLY
3   GLNHISASPLYSASPASPGLNALALYSLYS
4   VALGLNGLUHISLEUASNLYSTHRGLYILE
5   PROASPALAASPLYSVALASNILEGLNILE
6   ALAASPGLYLYSALATHRVALTHRGLYASP
7   GLYLEUSERGLNGLUALALYSGLULYSILE
8   LEUVALALAVALGLYASNILESERGLYILE
9   ALASERVALASPASPGLNVALLYSTHRALA
10   THRPROALATHRALASERGLNPHETYRTHR
11   VALLYSSERGLYASPTHRLEUSERALAILE
12   SERLYSGLNVALTYRGLYASNALAASNLEU
13   TYRASNLYSILEPHEGLUALAASNLYSPRO
14   METLEULYSSERPROASPLYSILETYRPRO
15   GLYGLNVALLEUARGILEPROGLUGLULEU
16   GLUHISHISHISHISHISHIS

Samples:

CN1: YgaU, [U-99% 13C; U-99% 15N], 1.0 mM; KCl 5.0 mM; NaPi 20.0 mM; NaCl 50.0 mM

298K: ionic strength: 0.070 M; pH: 7.400; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCCN1isotropic298K
2D 1H-15N HSQC/HMQCCN1isotropic298K
HNCACO (H[N[ca[CO]]])CN1isotropic298K
3D CBCA(CO)NHCN1isotropic298K
3D HNCOCN1isotropic298K
3D HNCACBCN1isotropic298K
HCCCONH (hC_cacoNH.relayed)CN1isotropic298K
3D 1H-15N NOESYCN1isotropic298K
3D HBHA(CO)NHCN1isotropic298K
HBHANH (H{ca|cca}NH)CN1isotropic298K
3D HCCH-TOCSYCN1isotropic298K
2D 1H-13C HSQC/HMQCCN1isotropic298K
3D 1H-13C NOESYCN1isotropic298K
3D HCCH-TOCSYCN1isotropic298K
3D HCCH-TOCSYCN1isotropic298K
hCccoNH (hC_cacoNH.relayed)CN1isotropic298K
3D H(CCO)NHCN1isotropic298K
2D 1H-15N HSQC/HMQCCN1isotropic298K
HBCBCGHD (hbCBcgcdHD)CN1isotropic298K
HBCBCGHE (hbCBcgcdceHE)CN1isotropic298K
2D 1H-13C HSQC/HMQCCN1isotropic298K

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

AutoDep v4.3, PDBe - collection

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure Calculation

CcpNmr_Analysis v2.0, CCPN - data analysis

CcpNmr_Entry_Completion_Interface v2.1, PDBe & CCPN - data deposition

DANGLE v1.1, DANGLE - data analysis

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

UNP YGAU_ECOLI
AlphaFold P77023 P77023

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