BMRB Entry 31101

Name: Solution NMR structure of designed peptide BH26 (RGVTVPHNGESKDYSV)
Published: 2023-09-23

Click here to enlarge.

PDB ID: 8txs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31101
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 designed peptide BH26 (RGVTVPHNGESKDYSV)

Deposition date: 2023-08-24 Original release date: 2023-09-23

Authors: McShan, A.; Torres, M.

Citation: McShan, A.; Torres, M.. "Solution NMR structure of designed peptide BH26 (RGVTVPHNGESKDYSV)" .

Assembly members:
entity_1, polymer, 16 residues, 1747.884 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: RGVTVPHNGESKDYSV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	30
15N chemical shifts	15
1H chemical shifts	57

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 16 residues - 1747.884 Da.

1

ARG

GLY

VAL

THR

VAL

PRO

HIS

ASN

GLY

GLU

2

SER

LYS

ASP

TYR

SER

VAL

Samples:

sample_1: BH26 peptide 3.8 mM; NaCl 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.0; pressure: 1 atm; temperature: 277.15 K

Experiments:

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

Software:

Sparky, Goddard - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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