BMRB Entry 11070

Name: DPC micelle bound structure of 1-28 GBP (growth-blocking peptide)
Published: 2009-09-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11070

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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:

DPC micelle bound structure of 1-28 GBP (growth-blocking peptide)

Deposition date:

2009-04-07

Original release date:

2009-09-04

Authors:

Umetsu, Yoshitaka; Aizawa, Tomoyasu; Muto, Kaori; Yamamoto, Hiroko; Kamiya, Masakatsu; Kumaki, Yasuhiro; Mizuguchi, Mineyuki; Demura, Makoto; Hayakawa, Yoichi; Kawano, Keiichi

Citation:

Citation: Umetsu, Yoshitaka; Aizawa, Tomoyasu; Muto, Kaori; Yamamoto, Hiroko; Kamiya, Masakatsu; Kumaki, Yasuhiro; Mizuguchi, Mineyuki; Demura, Makoto; Hayakawa, Yoichi; Kawano, Keiichi. "C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity." J. Biol. Chem. 284, 29625-29634 (2009).
PubMed: 19710009

Assembly members:

Assembly members:
1-28 GBP, polymer, 28 residues, Formula weight is not available

Natural source:

Natural source: Common Name: armyworm Taxonomy ID: not available Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Spodoptera not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
1-28 GBP: ENFSGGCVAGYMRTPDGRCK PTFYQLIT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	24
1H chemical shifts	175

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	1-28 GBP	1

Entities:

Entity 1, 1-28 GBP 28 residues - Formula weight is not available

1

GLU

ASN

PHE

SER

GLY

CYS

VAL

ALA

GLY

2

TYR

MET

ARG

THR

PRO

ASP

GLY

ARG

CYS

LYS

3

PRO

THR

PHE

TYR

GLN

LEU

ILE

THR

Samples:

sample_1: 1-28 GBP 3 mM; DPC, [U-99% 2H], 200 mM; DSS 0.1 mM; H2O 90%; D2O 10%

sample_2: 1-28 GBP, [U-99% 15N], 1 mM; DPC, [U-99% 2H], 100 mM; DSS 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.4; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

JEOL ECA 600 MHz
Bruker DRX 500 MHz

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