BMRB Entry 30145

Name: NMR Solution Structure of Designed Peptide NC_cHHH_D1
Published: 2016-09-16

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PDB ID: 5kx1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30145
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:

NMR Solution Structure of Designed Peptide NC_cHHH_D1

Deposition date:

2016-07-19

Original release date:

2016-09-16

Authors:

Harvey, P.; Craik, D.

Citation:

Citation: Bhardwaj, G.; Mulligan, V.; Bahl, C.; Gilmore, J.; Harvey, P.; Cheneval, O.; Buchko, G.; Pulavarti, S.; Kaas, Q.; Eletsky, A.; Huang, P.; Johnsen, W.; Greisen, P.; Rocklin, G.; Song, Y.; Linsky, T.; Watkins, A.; Rettie, S.; Xu, X.; Carter, L.; Bonneau, R.; Olson, J.; Coutsias, E.; Correnti, C.; Szyperski, T.; Craik, D.; Baker, D.. "Accurate de novo design of hyperstable constrained peptides." Nature 538, 329-335 (2016).
PubMed: 27626386

Assembly members:

Assembly members:
entity_1, polymer, 22 residues, 2563.837 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NPEDCRQDPEANKSPEECKK LK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	22
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 22 residues - 2563.837 Da.

1

ASN

PRO

GLU

ASP

CYS

ARG

GLN

ASP

PRO

GLU

2

ALA

ASN

LYS

SER

PRO

GLU

CYS

LYS

3

LEU

LYS

Samples:

sample_1: design peptide NC_cHHH_D1 1.0 mg/mL

sample_2: design peptide NC_cHHH_D1 1.0 mg/mL

sample_conditions_1: pH: 3.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D ECOSY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - processing

NMR spectrometers:

Bruker Avance 600 MHz

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