BMRB Entry 30753

Name: Solution NMR structure of de novo designed TMB2.3
Published: 2021-02-15

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PDB ID: 6x1k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30753
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of de novo designed TMB2.3 PubMed: 33602829

Deposition date: 2020-05-19 Original release date: 2021-02-15

Authors: Liang, B.; Vorobieva, A.; Chow, C.; Baker, D.; Tamm, L.

Citation: Vorobieva, Anastassia; White, Paul; Liang, Binyong; Horne, Jim; Bera, Asim; Chow, Cameron; Gerben, Stacey; Marx, Sinduja; Kang, Alex; Stiving, Alyssa; Harvey, Sophie; Marx, Dagan; Khan, G Nasir; Fleming, Karen; Wysocki, Vicki; Brockwell, David; Tamm, Lukas; Radford, Sheena; Baker, David. "De novo design of transmembrane beta-barrels" Science 371, eabc8182-eabc8182 (2021).

Assembly members:
entity_1, polymer, 124 residues, 13547.988 Da.

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: MQDGPGTLDVFVAAGWNTDN TIEITGGATYQLSPYIMVKA GYGWNNSSLNRFEFGGGLQY KVTPDLEPYAWAGATYNTDN TLVPAAGAGFRYKVSPEVKL VVEYGWNNSSLQFLQAGLSY RIQP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	333
15N chemical shifts	108
1H chemical shifts	108

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 124 residues - 13547.988 Da.

1

MET

GLN

ASP

GLY

PRO

GLY

THR

LEU

ASP

VAL

2

PHE

VAL

ALA

GLY

TRP

ASN

THR

ASP

ASN

3

THR

ILE

GLU

ILE

THR

GLY

ALA

THR

TYR

4

GLN

LEU

SER

PRO

TYR

ILE

MET

VAL

LYS

ALA

5

GLY

TYR

GLY

TRP

ASN

SER

LEU

ASN

6

ARG

PHE

GLU

PHE

GLY

LEU

GLN

TYR

7

LYS

VAL

THR

PRO

ASP

LEU

GLU

PRO

TYR

ALA

8

TRP

ALA

GLY

ALA

THR

TYR

ASN

THR

ASP

ASN

9

THR

LEU

VAL

PRO

ALA

GLY

ALA

GLY

PHE

10

ARG

TYR

LYS

VAL

SER

PRO

GLU

VAL

LYS

LEU

11

VAL

GLU

TYR

GLY

TRP

ASN

SER

12

LEU

GLN

PHE

LEU

GLN

ALA

GLY

LEU

SER

TYR

13

ARG

ILE

GLN

PRO

Samples:

sample_1: TMB2.3, [U-98% 13C; U-98% 15N, U-98% 2H], 1.8 ± 0.1 mM; DPC 200 ± 10 mM; HEPES 10 ± 0.1 mM; MES 10 ± 0.1 mM; sodium acetate 10 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; sodium azide 0.05 ± 0.001 % w/v

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 313 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 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 NOESY-TROSY	sample_1	isotropic	sample_conditions_1
3D HSQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
1H-15N hetNOE	sample_1	isotropic	sample_conditions_1
1D proton	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard, TD, and Kneller, DG - data analysis

hmsIST, S. G. Hyberts, A. G. Milbradt, A. B. Wagner, H. Arthanari, G. Wagner, - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE III 800 MHz

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