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 10141

Title: Solution structure of the alpha adaptinC2 domain from human Adapter-related protein complex 1 gamma 2 subunit

Deposition date: 2007-12-04 Original release date: 2008-12-10

Authors: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the alpha adaptinC2 domain from human Adapter-related protein complex 1 gamma 2 subunit"  .

Assembly members:
alpha adaptinC2 domain, polymer, 131 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Vector: P060123-24

Entity Sequences (FASTA):
alpha adaptinC2 domain: GSSGSSGPPPAPIPDLKVFE REGVQLNLSFIRPPENPALL LITITATNFSEGDVTHFICQ AAVPKSLQLQLQAPSGNTVP ARGGLPITQLFRILNPNKAP LRLKLRLTYDHFHQSVQEIF EVNNLPVESWQ

Data sets:
Data typeCount
13C chemical shifts583
15N chemical shifts127
1H chemical shifts929

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AP-1 complex subunit gamma-21

Entities:

Entity 1, AP-1 complex subunit gamma-2 131 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROPROPRO
2   ALAPROILEPROASPLEULYSVALPHEGLU
3   ARGGLUGLYVALGLNLEUASNLEUSERPHE
4   ILEARGPROPROGLUASNPROALALEULEU
5   LEUILETHRILETHRALATHRASNPHESER
6   GLUGLYASPVALTHRHISPHEILECYSGLN
7   ALAALAVALPROLYSSERLEUGLNLEUGLN
8   LEUGLNALAPROSERGLYASNTHRVALPRO
9   ALAARGGLYGLYLEUPROILETHRGLNLEU
10   PHEARGILELEUASNPROASNLYSALAPRO
11   LEUARGLEULYSLEUARGLEUTHRTYRASP
12   HISPHEHISGLNSERVALGLNGLUILEPHE
13   GLUVALASNASNLEUPROVALGLUSERTRP
14   GLN

Samples:

sample_1: alpha adaptinC2 domain, [U-13C; U-15N], 0.54 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

TOPSPIN v1.3, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9747, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE II 900 MHz

Related Database Links:

PDB
DBJ BAA33390 BAG65453
EMBL CAD61898
GB AAH51833 AIC59448 EAW66132 EAW66134 EAW66138
REF NP_001269403 NP_001269404 NP_003908 XP_001163757 XP_002833830
SP O75843
AlphaFold O75843

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