BMRB Entry 30647

Name: Dg12a
Published: 2020-01-17

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PDB ID: 6px7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30647
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:

Dg12a

Deposition date:

2019-07-25

Original release date:

2020-01-17

Authors:

Agwa, A.; Schroeder, C.

Citation:

Citation: Jin, Jiayi; Agwa, Akello; Szanto, Tibor; Csoti, Agota; Panyi, Gyorgy; Schroeder, Christina; Walker, Andrew; King, Glenn. "Weaponisation 'on the fly': Convergent recruitment of knottin and defensin peptide scaffolds into the venom of predatory assassin flies" Insect Biochem. Mol. Biol. 118, 103310-103310 (2020).
PubMed: 31870846

Assembly members:

Assembly members:
entity_1, polymer, 34 residues, 3922.558 Da.

Natural source:

Natural source: Common Name: Dolopus genitalis Taxonomy ID: 2488630 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Dolopus genitalis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SQEQRQCKKIGEHCYVADEC CSKRCLFYAAKCVS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	99
15N chemical shifts	33
1H chemical shifts	233

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 34 residues - 3922.558 Da.

1

SER

GLN

GLU

GLN

ARG

GLN

CYS

LYS

ILE

2

GLY

GLU

HIS

CYS

TYR

VAL

ALA

ASP

GLU

CYS

3

CYS

SER

LYS

ARG

CYS

LEU

PHE

TYR

ALA

4

LYS

CYS

VAL

SER

Samples:

sample_1: Dg12a 1 mg/mL

sample_conditions_1: ionic strength: 1 M; pH: 4; pressure: 1 Pa; temperature: 298 K

Experiments:

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

Software:

TopSpin v3.5, Bruker Biospin - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis v2.4.1, CCPN - chemical shift assignment

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