BMRB Entry 15045

Name: NMR SOLUTION STRUCTURE OF A MINIMAL TRANSMEMBRANE BETA-BARREL PLATFORM PROTEIN
Published: 2007-05-21

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PDB ID: 2jmm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15045
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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:

NMR SOLUTION STRUCTURE OF A MINIMAL TRANSMEMBRANE BETA-BARREL PLATFORM PROTEIN

Deposition date:

2006-11-20

Original release date:

2007-05-21

Authors:

Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin

Citation:

Citation: Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin. "A Minimal Transmembrane Beta-Barrel Platform Protein Studied by NMR" Biochemistry 46, 1128-1140 (2007).
PubMed: 17260943

Assembly members:

Assembly members:
BBP+EF, polymer, 156 residues, 17206.318 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-3b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BBP+EF: MPKDNTWYTGAKLGWSQYSR ENQLGAGAFGGYQVNPYVGF EMGYDWLGRMPRKAQGVQLT AKLGYPKLGTDDLDIYTRLG GMVWRADTSDKDGNGYISAA EASVSPVFAGGVEYVIRRRI TPEIATRLEYQWTNNASDNG MLSLGVSYRFGQGEAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	308
15N chemical shifts	110
1H chemical shifts	110

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BBP+EF in DHPC micelles	1

Entities:

Entity 1, BBP+EF in DHPC micelles 156 residues - 17206.318 Da.

1

MET

PRO

LYS

ASP

ASN

THR

TRP

TYR

THR

GLY

2

ALA

LYS

LEU

GLY

TRP

SER

GLN

TYR

SER

ARG

3

GLU

ASN

GLN

LEU

GLY

ALA

GLY

ALA

PHE

GLY

4

GLY

TYR

GLN

VAL

ASN

PRO

TYR

VAL

GLY

PHE

5

GLU

MET

GLY

TYR

ASP

TRP

LEU

GLY

ARG

MET

6

PRO

ARG

LYS

ALA

GLN

GLY

VAL

GLN

LEU

THR

7

ALA

LYS

LEU

GLY

TYR

PRO

LYS

LEU

GLY

THR

8

ASP

LEU

ASP

ILE

TYR

THR

ARG

LEU

GLY

9

GLY

MET

VAL

TRP

ARG

ALA

ASP

THR

SER

ASP

10

LYS

ASP

GLY

ASN

GLY

TYR

ILE

SER

ALA

11

GLU

ALA

SER

VAL

SER

PRO

VAL

PHE

ALA

GLY

12

GLY

VAL

GLU

TYR

VAL

ILE

ARG

ILE

13

THR

PRO

GLU

ILE

ALA

THR

ARG

LEU

GLU

TYR

14

GLN

TRP

THR

ASN

ALA

SER

ASP

ASN

GLY

15

MET

LEU

SER

LEU

GLY

VAL

SER

TYR

ARG

PHE

16

GLY

GLN

GLY

GLU

ALA

Samples:

sample_1: BBP+EF, [U-100% 13C; U-100% 15N; 80% 2H], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

GROMACS, Lindahl, Hess and van der Spoel - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz