BMRB Entry 16152

Name: NMR assignment of jerdostatin mutant R24K from Trimeresurus jerdonii, with deletion of two residues (N45 G46) from the end C-terminal
Published: 2012-08-07

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PDB ID: 2w9w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16152
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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 assignment of jerdostatin mutant R24K from Trimeresurus jerdonii, with deletion of two residues (N45 G46) from the end C-terminal

Deposition date:

2009-01-30

Original release date:

2012-08-07

Authors:

Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Calvete, Juan Jose; Pineda-Lucena, Antonio

Citation:

Citation: Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Perez, Alicia; Marcinkiewicz, Cezary; Pineda-Lucena, Antonio; Calvete, Juan. "NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin 11." Proteins 79, 2530-2542 (2011).
PubMed: 21656569

Assembly members:

Assembly members:
jerdostatin_R24K_-N45G46, polymer, 44 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Trimeresurus jerdonii Taxonomy ID: 135726 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Trimeresurus jerdonii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
jerdostatin_R24K_-N45G46: AMDCTTGPCCRQCKLKPAGT TCWKTSVSSHYCTGRSCECP SYPG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	116
15N chemical shifts	43
1H chemical shifts	262

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	jerdostatin R24K -N45G46 polypeptide	1

Entities:

Entity 1, jerdostatin R24K -N45G46 polypeptide 44 residues - Formula weight is not available

Residues 1-3 (AMD) are a cloning artifact

1

ALA

MET

ASP

CYS

THR

GLY

PRO

CYS

2

ARG

GLN

CYS

LYS

LEU

LYS

PRO

ALA

GLY

THR

3

THR

CYS

TRP

LYS

THR

SER

VAL

SER

HIS

4

TYR

CYS

THR

GLY

ARG

SER

CYS

GLU

CYS

PRO

5

SER

TYR

PRO

GLY

Samples:

sample_1: jerdostatin R24K -N45G46, [U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1.0 atm; temperature: 300 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz

BMRB	16136 16150 16151
PDB	2W9O 2W9U 2W9V 2W9W
EMBL	CAJ34936 CAK12627 CAL18287
GB	AAP20878
SP	Q3BK17 Q7ZZM2
AlphaFold	Q7ZZM2 Q3BK17