BMRB Entry 34408

Name: STRUCTURE OF [ASP58]-IGF-I ANALOGUE
Published: 2019-10-17

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PDB ID: 6rva
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34408
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:

STRUCTURE OF [ASP58]-IGF-I ANALOGUE

Deposition date:

2019-05-31

Original release date:

2019-10-17

Authors:

Jiracek, J.; Zakova, L.; Socha, O.

Citation:

Citation: Machackova, K.; Mlcochova, K.; Potalitsyn, P.; Hankova, K.; Socha, O.; Budesinsky, M.; Muzdalo, A.; Lepsik, M.; Cernekova, M.; Radosavljevic, J.; Fabry, M.; Mitrova, K.; Chrudinova, M.; Lin, J.; Yurenko, Y.; Hobza, P.; Selicharova, I.; Akova, L.; Jiracek, J.. "Mutations at hypothetical binding site 2 in insulin and insulin-like growth factors 1 and 2 result in receptor- and hormone-specific responses." J. Biol. Chem. 294, 17371-17382 (2019).
PubMed: 31558604

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, 7706.778 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGPETLCGAELVDALQFVCG DRGFYFNKPTGYGSSSRRAP QTGIVDECCFRSCDLRRLDM YCAPLKPAKSA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	189
15N chemical shifts	74
1H chemical shifts	461

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 71 residues - 7706.778 Da.

1

GLY

PRO

GLU

THR

LEU

CYS

GLY

ALA

GLU

2

LEU

VAL

ASP

ALA

LEU

GLN

PHE

VAL

CYS

GLY

3

ASP

ARG

GLY

PHE

TYR

PHE

ASN

LYS

PRO

THR

4

GLY

TYR

GLY

SER

ARG

ALA

PRO

5

GLN

THR

GLY

ILE

VAL

ASP

GLU

CYS

PHE

6

ARG

SER

CYS

ASP

LEU

ARG

LEU

ASP

MET

7

TYR

CYS

ALA

PRO

LEU

LYS

PRO

ALA

LYS

SER

8

ALA

Samples:

sample_1: [L-Asp58]-IGF-1 analogue 0.18 mM; sodium azide 0.01%; acetic acid, [U-2H], 50 mM

sample_2: [L-Asp58]-IGF-1 analogue, [U-13C; U-15N], 0.05 mM; sodium azide 0.01%; acetic acid, [U-2H], 50 mM

sample_3: [L-Asp58]-IGF-1 analogue, [U-13C; U-15N], 0.05 mM; sodium azide 0.01%; acetic acid, [U-2H], 50 mM

sample_conditions_1: ionic strength: 0 Not defined; pH: 3.0; pressure: 1 atm; temperature: 313.15 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_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1

Software:

Xplor-NIH v2.44, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

CcpNmr Analysis v2.4.2, Wim F. Vranken, Wayne Boucher, and etc. - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

TopSpin v3.5, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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