BMRB Entry 18613

Title:
NMR solution structure of Eph receptor
Deposition date:
2012-07-24
Original release date:
2013-07-22
Authors:
Qin, Haina; Song, Jianxing
Citation:

Citation: Qin, Haina; Lim, Liangzhong; Song, Jianxing. "Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations."  BMC Biophys. 5, 2-2 (2012).
PubMed: 22277260

Assembly members:

Assembly members:
entity, polymer, 183 residues, 20989.896 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   Vector: PET32a

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts163
1H chemical shifts948

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Eph receptor1

Entities:

Entity 1, Eph receptor 183 residues - 20989.896 Da.

1   GLYSERASNGLUVALTHRLEULEUASPSER
2   ARGSERVALGLNGLYGLULEUGLYTRPILE
3   ALASERPROLEUGLUGLYGLYTRPGLUGLU
4   VALSERILEMETASPGLULYSASNTHRPRO
5   ILEARGTHRTYRGLNVALCYSASNVALMET
6   GLUPROSERGLNASNASNTRPLEUARGTHR
7   ASPTRPILETHRARGGLUGLYALAGLNARG
8   VALTYRILEGLUILELYSPHETHRLEUARG
9   ASPCYSASNSERLEUPROGLYVALMETGLY
10   THRCYSLYSGLUTHRPHEASNLEUTYRTYR
11   TYRGLUSERASPASNASPLYSGLUARGPHE
12   ILEARGGLUASNGLNPHEVALLYSILEASP
13   THRILEALAALAASPGLUSERPHETHRGLN
14   VALASPILEGLYASPARGILEMETLYSLEU
15   ASNTHRGLUILEARGASPVALGLYPROLEU
16   SERLYSLYSGLYPHETYRLEUALAPHEGLN
17   ASPVALGLYALACYSILEALALEUVALSER
18   VALARGVALPHETYRLYSLYSALAPROLEU
19   THRVALARG

Samples:

sample_1: protein, [U-99% 15N], 0.5 mM; potassium phosphate 10 mM; sodium azide 0.00002 mM; D2O 10 % v/v; H2O 100 % v/v; DTT 0 w/v

sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 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 HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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