BMRB Entry 34000

Name: D11 bound IGF-II
Published: 2016-08-01

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PDB ID: 5l3l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34000
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:

D11 bound IGF-II

Deposition date:

2016-05-23

Original release date:

2016-08-01

Authors:

Hexnerova, R.

Citation:

Citation: Hexnerova, Rozalie; Krizkova, Kvetoslava; Fabry, Milan; Sieglova, Irena; Kedrova, Katerina; Collinsova, Michaela; Ullrichova, Pavlina; Srb, Pavel; Williams, Christopher; Crump, Matthew; Tosner, Zdenek; Jiracek, Jiri; Veverka, Vaclav; Zakova, Lenka. "Probing Receptor Specificity by Sampling the Conformational Space of the Insulin-like Growth Factor II C-domain" J. Biol. Chem. 291, 21234-21245 (2016).
PubMed: 27510031

Assembly members:

Assembly members:
Insulin-like growth factor II, polymer, 67 residues, 7484.472 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):
Insulin-like growth factor II: AYRPSETLCGGELVDTLQFV CGDRGFYFSRPASRVSRRSR GIVEECCFRSCDLALLETYC ATPAKSE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	174
15N chemical shifts	72
1H chemical shifts	448

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 67 residues - 7484.472 Da.

1

ALA

TYR

ARG

PRO

SER

GLU

THR

LEU

CYS

GLY

2

GLY

GLU

LEU

VAL

ASP

THR

LEU

GLN

PHE

VAL

3

CYS

GLY

ASP

ARG

GLY

PHE

TYR

PHE

SER

ARG

4

PRO

ALA

SER

ARG

VAL

SER

ARG

SER

ARG

5

GLY

ILE

VAL

GLU

CYS

PHE

ARG

SER

6

CYS

ASP

LEU

ALA

LEU

GLU

THR

TYR

CYS

7

ALA

THR

PRO

ALA

LYS

SER

GLU

Samples:

sample_1: acetic acid, d4, 20 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

YASARA, Hoegenauer, Koraimann, Kungl, Vriend - refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker AvanceIII 850 MHz

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