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 18108

Title: 13C, 15N solid-state MAS NMR chemical shift assignment for YadA membrane anchor domain.   PubMed: 23150774

Authors: Shahid, Shakeel; Markovic, Stefan; Bardiaux, Benjamin; Habeck, Michael; Linke, Dirk; van Rossum, Barth-Jan

Citation: Shahid, Shakeel; Markovic, Stefan; Linke, Dirk; van Rossum, Barth-Jan. "Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR."  Sci. Rep. 2, 803-803 (2012).

Assembly members:
YadA_membrane_anchor_domain, polymer, 105 residues, 11200 Da.

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

Entity Sequences (FASTA):
YadA_membrane_anchor_domain: GDQASWSHPQFEKGAHKFRQ LDNRLDKLDTRVDKGLASSA ALNSLFQPYGVGKVNFTAGV GGYRSSQALAIGSGYRVNES VALKAGVAYAGSSDVMYNAS FNIEW

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YadA_membrane_anchor_domain_11
2YadA_membrane_anchor_domain_21
3YadA_membrane_anchor_domain_31

Entities:

Entity 1, YadA_membrane_anchor_domain_1 105 residues - 11200 Da.

Residues 1-15 belong non native strep tag which was introduced.

1   GLYASPGLNALASERTRPSERHISPROGLN
2   PHEGLULYSGLYALAHISLYSPHEARGGLN
3   LEUASPASNARGLEUASPLYSLEUASPTHR
4   ARGVALASPLYSGLYLEUALASERSERALA
5   ALALEUASNSERLEUPHEGLNPROTYRGLY
6   VALGLYLYSVALASNPHETHRALAGLYVAL
7   GLYGLYTYRARGSERSERGLNALALEUALA
8   ILEGLYSERGLYTYRARGVALASNGLUSER
9   VALALALEULYSALAGLYVALALATYRALA
10   GLYSERSERASPVALMETTYRASNALASER
11   PHEASNILEGLUTRP

Samples:

sample_1: YadA membrane anchor domain, [U-13C; U-15N], 11.5 M

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 275 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARR 25 mssample_1solidsample_conditions_1
2D 13C-13C DARR 50 mssample_1solidsample_conditions_1
2D 13C-13C DARR 100 mssample_1solidsample_conditions_1
2D 13C-13C DARR-CP- 15 mssample_1solidsample_conditions_1
2D 13C-13C DARR-CP- 40 mssample_1solidsample_conditions_1
2D 13C-13C DARR-CP- 70 mssample_1solidsample_conditions_1
2D 13C-13C PDSD 15 mssample_1solidsample_conditions_1
2D 13C-13C PDSD 100 mssample_1solidsample_conditions_1
2D 1H-13C INEPTsample_1solidsample_conditions_1
2D 13C-13C DREAM 1.5 mssample_1solidsample_conditions_1
2D 13C-13C DREAM ABsample_1solidsample_conditions_1
2D 13C-13C DREAM BGsample_1solidsample_conditions_1
2D 13C-13C Me-only 70 mssample_1solidsample_conditions_1
2D 13C-13C REDOR 1 mssample_1solidsample_conditions_1
2D 15N-13C NCAsample_1solidsample_conditions_1
2D 15N-13C NCOsample_1solidsample_conditions_1
2D NCACXsample_1solidsample_conditions_1
2D NCOCXsample_1solidsample_conditions_1
3D NCACX 25 mssample_1solidsample_conditions_1
3D NCOCX 25 mssample_1solidsample_conditions_1
3D NCACX 100 mssample_1solidsample_conditions_1
3D NCACX 200 mssample_1solidsample_conditions_1
3D NCOCX 200 mssample_1solidsample_conditions_1
3D NCACX 500 mssample_1solidsample_conditions_1
3D NCACB 3 mssample_1solidsample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
EMBL CAA32085 CAA32086 CAL10087 CBW54734 CBY78119
GB AAK69254 AAN37524 ADZ44497 AJI81101 AJJ21461
REF NP_783714 NP_863557 WP_005176545 WP_011100755 WP_011117647
SP A1JUB7 P0C2W0 P31489