BMRB Entry 25609

Name: NMR solution structure of RsAFP2
Published: 2016-05-23

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PDB ID: 2n2r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25609
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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 RsAFP2

Deposition date:

2015-05-12

Original release date:

2016-05-23

Authors:

Harvey, Peta; Craik, David; Vriens, Kim

Citation:

Citation: Vriens, Kim; Cools, Tanne; Harvey, Peta; Craik, David; DeConinck, Barbara; Cammue, Bruno; Thevissen, Karin. "The radish defensins RsAFP1 and RsAFP2 act synergistically with caspofungin against Candida albicans biofilms" peptides 75, 71-79 (2016).
PubMed: 26592804

Assembly members:

Assembly members:
entity, polymer, 51 residues, 5744.706 Da.

Natural source:

Natural source: Common Name: radish Taxonomy ID: 3726 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Raphanus sativus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pPICZaA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QKLCQRPSGTWSGVCGNNNA CKNQCIRLEKARHGSCNYVF PAHKCICYFPC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	142
15N chemical shifts	51
1H chemical shifts	347

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 51 residues - 5744.706 Da.

1

GLN

LYS

LEU

CYS

GLN

ARG

PRO

SER

GLY

THR

2

TRP

SER

GLY

VAL

CYS

GLY

ASN

ALA

3

CYS

LYS

ASN

GLN

CYS

ILE

ARG

LEU

GLU

LYS

4

ALA

ARG

HIS

GLY

SER

CYS

ASN

TYR

VAL

PHE

5

PRO

ALA

HIS

LYS

CYS

ILE

CYS

TYR

PHE

PRO

6

CYS

Samples:

sample_1: entity 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: entity 1 mM; D2O, [U-2H], 100%

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 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-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D E-COSY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment, peak picking

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

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