BMRB Entry 18761

Title:
1H, 13C, and 15N chemical shift assignments for the phosphotyrosine binding domain 2 (PTB2) of human FE65
Deposition date:
2012-10-04
Original release date:
2013-02-07
Authors:
Dietl, Andreas; Wild, Klemens; Simon, Bernd
Citation:

Citation: Dietl, Andreas; Wild, Klemens; Simon, Bernd. "(1)H, (13)C, and (15)N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23315337

Assembly members:

Assembly members:
FE65_PTB2, polymer, 140 residues, Formula weight is not available

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: pET21d

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts131
1H chemical shifts758

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FE65 PTB21

Entities:

Entity 1, FE65 PTB2 140 residues - Formula weight is not available

1   ALAPROLYSASNGLULEUVALGLNLYSPHE
2   GLNVALTYRTYRLEUGLYASNVALPROVAL
3   ALALYSPROVALGLYVALASPVALILEASN
4   GLYALALEUGLUSERVALLEUSERSERSER
5   SERARGGLUGLNTRPTHRPROSERHISVAL
6   SERVALALAPROALATHRLEUTHRILELEU
7   HISGLNGLNTHRGLUALAVALLEUGLYGLU
8   CYSARGVALARGPHELEUSERPHELEUALA
9   VALGLYARGASPVALHISTHRPHEALAPHE
10   ILEMETALAALAGLYPROALASERPHECYS
11   CYSHISMETPHETRPCYSGLUPROASNALA
12   ALASERLEUSERGLUALAVALGLNALAALA
13   CYSMETLEUARGTYRGLNLYSCYSLEUASP
14   ALAARGSERGLNHISHISHISHISHISHIS

Samples:

sample_1: FE65 PTB2, [U-100% 13C; U-100% 15N], 0.2 – 0.7 mM

sample_2: FE65 PTB2 0.7 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
DBJ BAC27116 BAC39033 BAE37645 BAE73097 BAH11511
EMBL CAA42999 CAD98057
GB AAB51603 AAB93631 AAC79942 AAF20141 AAH10854
REF NP_001068654 NP_001155 NP_001240814 NP_001240815 NP_001240816
SP O00213 P46933 Q9QXJ1
TPG DAA22130
AlphaFold O00213 P46933 Q9QXJ1

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