BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17934

Title: AIDA1 PTB domain   PubMed: 23799029

Deposition date: 2011-09-12 Original release date: 2012-09-17

Authors: Donaldson, Logan

Citation: Smirnova, Ekaterina; Shanbhag, Riya; Kurabi, Arwa; Mobli, Mehdi; Kwan, Jamie; Donaldson, Logan. "Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein."  PLoS ONE 8, e65605-e65605 (2013).

Assembly members:
AIDA1 PTB domain, polymer, 153 residues, 15011.303 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):
AIDA1 PTB domain: STPVQAWQHHPEKLIAQSCD YKAAYLGSMLIKELRGTEST QDACAKMRANCQKSTEQMKK VPTIILSVSAKGVKFIDATN KNIIAEHEIRNISCAAQDPE DLSTFAYITKDLKSNHHYCH VFTAFDVNLAAEIILTLGQA FEVAYQLALQARK

Data sets:
Data typeCount
13C chemical shifts561
15N chemical shifts134
1H chemical shifts858

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AIDA1 PTB domain1

Entities:

Entity 1, AIDA1 PTB domain 153 residues - 15011.303 Da.

1   SERTHRPROVALGLNALATRPGLNHISHIS
2   PROGLULYSLEUILEALAGLNSERCYSASP
3   TYRLYSALAALATYRLEUGLYSERMETLEU
4   ILELYSGLULEUARGGLYTHRGLUSERTHR
5   GLNASPALACYSALALYSMETARGALAASN
6   CYSGLNLYSSERTHRGLUGLNMETLYSLYS
7   VALPROTHRILEILELEUSERVALSERALA
8   LYSGLYVALLYSPHEILEASPALATHRASN
9   LYSASNILEILEALAGLUHISGLUILEARG
10   ASNILESERCYSALAALAGLNASPPROGLU
11   ASPLEUSERTHRPHEALATYRILETHRLYS
12   ASPLEULYSSERASNHISHISTYRCYSHIS
13   VALPHETHRALAPHEASPVALASNLEUALA
14   ALAGLUILEILELEUTHRLEUGLYGLNALA
15   PHEGLUVALALATYRGLNLEUALALEUGLN
16   ALAARGLYS

Samples:

sample_1: AIDA1 PTB domain 0.8 mM; sodium azide 0.05%; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Uniform NMR System 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 17428
PDB
DBJ BAE87950
GB EDL21516 EDL21517 EDL21518 EDM16964 EDM16965
REF XP_003126745 XP_005658157 XP_006077488 XP_013846696

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