BMRB Entry 34718

Name: Solution NMR structure of the HTH_8cm consensus miniprotein in 30% TFE at 278K
Published: 2022-04-01

Click here to enlarge.

PDB ID: 7zbs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34718
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Solution NMR structure of the HTH_8cm consensus miniprotein in 30% TFE at 278K

Deposition date: 2022-03-24 Original release date: 2022-04-01

Authors: Socha, O.; Jakubec, D.

Citation: Jakubec, D.; Bednarova, L.; Postova, L.; Socha, O.; Budesinsky, M.; Vondrasek, J.. "Consensus design of structured miniproteins using spectral analysis of domain residue interaction networks" .

Assembly members:
entity_1, polymer, 25 residues, 2795.275 Da.

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

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: ALERTGGNKSKAARLLGISR RTLYR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	93
15N chemical shifts	24
1H chemical shifts	180

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 25 residues - 2795.275 Da.

1

ALA

LEU

GLU

ARG

THR

GLY

ASN

LYS

SER

2

LYS

ALA

ARG

LEU

GLY

ILE

SER

ARG

3

ARG

THR

LEU

TYR

ARG

Samples:

sample_1: D2O, [U-2H], 5 % v/v; TFE, [U-2H], 30 % v/v; HTH_8cm 8.6 mg/uL

sample_conditions_1: ionic strength: 0 Not defined; pH: 2.7; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
1H	sample_1	isotropic	sample_conditions_1
13C	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMBC	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.44, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

CcpNmr Analysis v2.4., CCPN - chemical shift assignment, peak picking

TALOS-N, Yang Shen, Ad Bax - structure calculation

NMR spectrometers:

Bruker AVANCE III HD 600 MHz

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