BMRB Entry 17287

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17287
MolProbity Validation Chart

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Title:
NMR solution structure ensemble of domain 11 of the echidna M6P/IGF2R receptor
Deposition date:
2010-11-09
Original release date:
2012-11-05
Authors:
Strickland, Madeleine; Crump, Matthew; Williams, Christopher; Rezgui, Dellel; Ellis, Rosamund; Hoppe, Hans; Frago, Susana; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E Yvonne; Hassan, A Bassim; Wattana-Amorn, Pakorn
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:
entity, polymer, 140 residues, 15298.419 Da.

Natural source:

Natural source:   Common Name: Australian echidna   Taxonomy ID: 9261   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Tachyglossus aculeatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MVQDNCQVTNPATGYVFDLN SLKRESGYTISDIRKGSIRL GVCGEVKDCGPGIGACFEGT GIKAGKWNQKLSYVDQVLQL VYEDGDPCPANLHLKYKSVI SFVCKSDAGPTSQPLLLSVD EHTCTLFFSWHTSLACEQEV

Data sets:
Data typeCount
13C chemical shifts585
15N chemical shifts146
1H chemical shifts949

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1M6P/IGF2_receptor1

Entities:

Entity 1, M6P/IGF2_receptor 140 residues - 15298.419 Da.

1   METVALGLNASPASNCYSGLNVALTHRASN
2   PROALATHRGLYTYRVALPHEASPLEUASN
3   SERLEULYSARGGLUSERGLYTYRTHRILE
4   SERASPILEARGLYSGLYSERILEARGLEU
5   GLYVALCYSGLYGLUVALLYSASPCYSGLY
6   PROGLYILEGLYALACYSPHEGLUGLYTHR
7   GLYILELYSALAGLYLYSTRPASNGLNLYS
8   LEUSERTYRVALASPGLNVALLEUGLNLEU
9   VALTYRGLUASPGLYASPPROCYSPROALA
10   ASNLEUHISLEULYSTYRLYSSERVALILE
11   SERPHEVALCYSLYSSERASPALAGLYPRO
12   THRSERGLNPROLEULEULEUSERVALASP
13   GLUHISTHRCYSTHRLEUPHEPHESERTRP
14   HISTHRSERLEUALACYSGLUGLNGLUVAL

Samples:

sample_1: sodium azide 100 uM; sodium phosphate 10 mM; EDTA 1 mM; D2O 7%; H2O 93%; M6P/IGF2_receptor, [U-95% 13C; U-95% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 5.50; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

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

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

ProcheckNMR, Laskowski and MacArthur - refinement

VNMRJ v2.2c, Varian - collection

Analysis v2.1, CCPN - chemical shift assignment, peak picking, refinement

CS23D v1.0, Wishart DS, Arndt D, Berjanskii M, Tang P, Zhou J, Lin G. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian VNMRS600 600 MHz

Related Database Links:

PDB

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