BMRB Entry 18565

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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/BMR18565
MolProbity Validation Chart

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Title:
Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin
Deposition date:
2012-07-01
Original release date:
2014-02-11
Authors:
Brothers, Michael; Geissler, Brett; Hisao, Grant; Satchell, Karla; Wilson, Brenda; Rienstra, Chad
Citation:

Citation: Brothers, Michael; Geissler, Brett; Hisao, Grant; Satchell, Karla; Wilson, Brenda; Rienstra, Chad. "Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin."  Biomol. NMR Assignments 8, 221-224 (2014).
PubMed: 23765284

Assembly members:

Assembly members:
MLD_PMT, polymer, 90 residues, 10.5 Da.

Natural source:

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 747   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pasteurella multocida

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MLD_PMT: MGVWTPEVLKARASVIGKPI GESYKRILAKLQRIHNSNIL DERQGLMHELMELIDLYEES QPSSERLNAFRELRTQLEKA LGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts81
1H chemical shifts568

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1MLD PMT1

Entities:

Entity 1, MLD PMT 90 residues - 10.5 Da.

1   METGLYVALTRPTHRPROGLUVALLEULYS
2   ALAARGALASERVALILEGLYLYSPROILE
3   GLYGLUSERTYRLYSARGILELEUALALYS
4   LEUGLNARGILEHISASNSERASNILELEU
5   ASPGLUARGGLNGLYLEUMETHISGLULEU
6   METGLULEUILEASPLEUTYRGLUGLUSER
7   GLNPROSERSERGLUARGLEUASNALAPHE
8   ARGGLULEUARGTHRGLNLEUGLULYSALA
9   LEUGLYLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: MLD PMT, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tris 20 mM; sodium chloride 100 mM; EDTA 1 mM; sodium azide 0.01 mM; DSS 0.01 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAA35885 CAA36717 CAA40921 CAA82233 CAD92744
GB AAL55665 AAW57319 AAX76908 ABR23002 ACG56672
PRF 1703272A
REF WP_015691094
SP P17452
AlphaFold P17452

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