BMRB Entry 19892

Name: REFINED STRUCTURE OF OUTER MEMBRANE PROTEIN X IN NANODISC BY MEASURING RESIDUAL DIPOLAR COUPLINGS
Published: 2015-03-16

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PDB ID: 2mnh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19892
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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.; Sabo, T.; Schwiegk, C.; Becker, S.; Riek, R.; Lee, D.

Citation: Bibow, S.; Carneiro, M.; Sabo, T.; Schwiegk, C.; Becker, S.; Riek, R.; Lee, D.. "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: 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):
OUTER_MEMBRANE_PROTEIN_X: ATSTVTGGYAQSDAQGQMNK MGGFNLKYRYEEDNSPLGVI GSFTYTEKSRTASSGDYNKN QYYGITAGPAYRINDWASIY GVVGVGYGKFQTTEYPTYKN DTSDYGFSYGAGLQFNPMEN VALDFSYEQSRIRSVDVGTW IAGVGYRF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	117
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OUTER MEMBRANE PROTEIN X	1

Entities:

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

1

ALA

THR

SER

THR

VAL

THR

GLY

TYR

ALA

2

GLN

SER

ASP

ALA

GLN

GLY

GLN

MET

ASN

LYS

3

MET

GLY

PHE

ASN

LEU

LYS

TYR

ARG

TYR

4

GLU

ASP

ASN

SER

PRO

LEU

GLY

VAL

ILE

5

GLY

SER

PHE

THR

TYR

THR

GLU

LYS

SER

ARG

6

THR

ALA

SER

GLY

ASP

TYR

ASN

LYS

ASN

7

GLN

TYR

GLY

ILE

THR

ALA

GLY

PRO

ALA

8

TYR

ARG

ILE

ASN

ASP

TRP

ALA

SER

ILE

TYR

9

GLY

VAL

GLY

VAL

GLY

TYR

GLY

LYS

PHE

10

GLN

THR

GLU

TYR

PRO

THR

TYR

LYS

ASN

11

ASP

THR

SER

ASP

TYR

GLY

PHE

SER

TYR

GLY

12

ALA

GLY

LEU

GLN

PHE

ASN

PRO

MET

GLU

ASN

13

VAL

ALA

LEU

ASP

PHE

SER

TYR

GLU

GLN

SER

14

ARG

ILE

ARG

SER

VAL

ASP

VAL

GLY

THR

TRP

15

ILE

ALA

GLY

VAL

GLY

TYR

ARG

PHE

Samples:

sample_1: OUTER MEMBRANE PROTEIN X, [U-100% 13C; U-100% 15N], 0.5 mM; Tris-HCl 10 mM; sodium azide 0.05%; NaCl 100 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N COCAINE	sample_1	isotropic	sample_conditions_1

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