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 19892

Title: REFINED STRUCTURE OF OUTER MEMBRANE PROTEIN X IN NANODISC BY MEASURING RESIDUAL DIPOLAR COUPLINGS   PubMed: 24752984

Deposition date: 2014-04-05 Original release date: 2015-03-16

Authors: Bibow, S.; ., Carneiro; M., .; ., .; ., .; 7, .; ,

Citation: Bibow, S.; ., Carneiro; M., .; ., .; ., .; 19892, .; , 19892. "Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings"  Protein Sci. 23, .-851 (856).

Assembly members:
OUTER_MEMBRANE_PROTEIN_X, polymer, 148 residues, 16371.898 Da.

Natural source:   Common Name: not available   Taxonomy ID: 562   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology' 'ESCHERICHIA COLI' . . . ESCHERICHIA COLI 'BL21 (DE3)

Entity Sequences (FASTA):
OUTER_MEMBRANE_PROTEIN_X: ATSTVTGGYAQSDAQGQMNK MGGFNLKYRYEEDNSPLGVI GSFTYTEKSRTASSGDYNKN QYYGITAGPAYRINDWASIY GVVGVGYGKFQTTEYPTYKN DTSDYGFSYGAGLQFNPMEN VALDFSYEQSRIRSVDVGTW IAGVGYRF

Data sets:
Data typeCount
15N chemical shifts117
118

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OUTER MEMBRANE PROTEIN X1

Entities:

Entity 1, OUTER MEMBRANE PROTEIN X 148 residues - 16371.898 Da.

1   ALA.198925.GLY.1989211.
2   ASP.1989217.ASN.1989223.
3   ASN.1989229.GLU.1989235.
4   LEU.1989241.PHE.1989247.
5   SER.1989253.GLY.1989259.
6   GLN.1989265.ALA.1989271.
7   ILE.1989277.ILE.1989283.
8   VAL.1989289.GLN.1989295.
9   THR.19892101.SER.19892107.
10   TYR.19892113.PHE.19892119.
11   VAL.19892125.TYR.19892131.
12   ARG.19892137.THR.19892143.
13   GLY.19892

Samples:

sample_1: OUTER MEMBRANE PROTEIN X' '[U-100% 13C; U-100% 15N]; .; .; . 19892; . 6; ., 90, 19892 – 7 D2O; 10 19892

sample_conditions_1: ionic strength: 100 mM; 7.4: . 19892; .: atm temperature; K: 19892

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available

Software:

X-_PLOR_NIH, SCHWIETERS, KUSZEWSKI, TJ - refinement

NMRPIPE, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - structure solution

TOPSPIN, Bruker Biospin - structure solution

SPARKY, Goddard - structure solution

NMR spectrometers:

  • BRUKER AVANCE I and AVANCE III 700. 800, 900 MHz

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