BMRB Entry 17110

Name: chicken IGF2R domain 11
Published: 2012-08-30

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PDB ID: 2l21
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17110
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

chicken IGF2R domain 11

Deposition date:

2010-08-10

Original release date:

2012-08-30

Authors:

Williams, Christopher; Hoppe, Hans; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, Yvonne; Rezgui, Dellel; Crump, Matthew; Hassan, Bassim

Citation:

Citation: Williams, Christopher; Hoppe, Hans; Rezgui, Dellel; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E.; Crump, Matthew; Hassan, A.; Grutzner, Frank; Nolan, Catherine; Mungall, Andrew. "An exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution" Science 338, 1209-1213 (2012).
PubMed: 23197533

Assembly members:

Assembly members:
IGF2R, polymer, 154 residues, 16408.426 Da.

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET26a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IGF2R: MKSNVQNDCRVTNPATGHLF DLTSLKRESGYTITDSHNRK IELNVCAEAKSSCANGAAVC ITDGPKTLNAGKLSKTLTYE DQVLKLVYEDGDPCPTDLKM KHKSYFSFVCKSDAGDDSQP VFLSFDEQTCTSYFSWHTSL ACEEEVPRHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	592
15N chemical shifts	154
1H chemical shifts	959

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IGF2R	1

Entities:

Entity 1, IGF2R 154 residues - 16408.426 Da.

Domain 11 of the IGF2R from Gallus gallus (chicken). The C-terminal residues EEVPRHHHHHH are a non-native affinity tag

1

MET

LYS

SER

ASN

VAL

GLN

ASN

ASP

CYS

ARG

2

VAL

THR

ASN

PRO

ALA

THR

GLY

HIS

LEU

PHE

3

ASP

LEU

THR

SER

LEU

LYS

ARG

GLU

SER

GLY

4

TYR

THR

ILE

THR

ASP

SER

HIS

ASN

ARG

LYS

5

ILE

GLU

LEU

ASN

VAL

CYS

ALA

GLU

ALA

LYS

6

SER

CYS

ALA

ASN

GLY

ALA

VAL

CYS

7

ILE

THR

ASP

GLY

PRO

LYS

THR

LEU

ASN

ALA

8

GLY

LYS

LEU

SER

LYS

THR

LEU

THR

TYR

GLU

9

ASP

GLN

VAL

LEU

LYS

LEU

VAL

TYR

GLU

ASP

10

GLY

ASP

PRO

CYS

PRO

THR

ASP

LEU

LYS

MET

11

LYS

HIS

LYS

SER

TYR

PHE

SER

PHE

VAL

CYS

12

LYS

SER

ASP

ALA

GLY

ASP

SER

GLN

PRO

13

VAL

PHE

LEU

SER

PHE

ASP

GLU

GLN

THR

CYS

14

THR

SER

TYR

PHE

SER

TRP

HIS

THR

SER

LEU

15

ALA

CYS

GLU

VAL

PRO

ARG

HIS

16

HIS

Samples:

sample_1: D2O 5 ± 0.1 %; sodium acetate 20 ± 0.1 mM; EDTA 0.1 ± 0.01 mM; sodium azide 100 ± 0.1 uM; IGF2R, [U-98% 15N], 0.5 – 1 mM; H2O 95%

sample_2: D2O 5 ± 0.1 %; sodium phosphate 20 ± 0.1 mM; EDTA 0.1 ± 0.01 mM; sodium azide 100 ± 0.1 uM; IGF2R, [U-98% 13C; U-98% 15N], 0.5 – 1 mM; H2O 95%

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

iCing vr765, Vuister, Doreleijers, Sousa da Silva - refinement

ANALYSIS v2.13, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides, Laue - chemical shift assignment, data analysis

NMR spectrometers:

Varian VNMRS 600 MHz
Varian INOVA 600 MHz