BMRB Entry 17445

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17445

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Title:
1H 15N 13C Backbone Assignment of Akap79 'M' domain, a human A-kinase anchor protein 5
Deposition date:
2011-02-07
Original release date:
2014-03-05
Authors:
Phelan, Marie; Tully, Mark; Lian, Lu-Yun
Citation:

Citation: Phelan, Marie; Tully, Mark; Lian, Lu-Yun; J., Grossman. "Conformational characterization of synapse-associated protein 97 by nuclear magnetic resonance and small-angle X-ray scattering shows compact and elongated forms"  Biochemistry 51, 899-908 (2012).
PubMed: 22242544

Assembly members:

Assembly members:
Akap79M, polymer, 170 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: pOPIN-S

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Akap79M: IKVQEEAEILDIQTQTPLND QATKAKSTQDLSEGISQKDG DEVCESNVSNSITSGEKVIS VELGLDNGHSAIQTGTLILE EIETIKEKQDVQPQQASPLE TSETDHQQPVLSDVPPLPAI PDQQIVEEASNSTLESAPNG KDYESTEIVAEETKPKDTEL SQESDFKENG

Data sets:
Data typeCount
13C chemical shifts491
15N chemical shifts157
1H chemical shifts577

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Akap79M1

Entities:

Entity 1, Akap79M 170 residues - Formula weight is not available

1   ILELYSVALGLNGLUGLUALAGLUILELEU
2   ASPILEGLNTHRGLNTHRPROLEUASNASP
3   GLNALATHRLYSALALYSSERTHRGLNASP
4   LEUSERGLUGLYILESERGLNLYSASPGLY
5   ASPGLUVALCYSGLUSERASNVALSERASN
6   SERILETHRSERGLYGLULYSVALILESER
7   VALGLULEUGLYLEUASPASNGLYHISSER
8   ALAILEGLNTHRGLYTHRLEUILELEUGLU
9   GLUILEGLUTHRILELYSGLULYSGLNASP
10   VALGLNPROGLNGLNALASERPROLEUGLU
11   THRSERGLUTHRASPHISGLNGLNPROVAL
12   LEUSERASPVALPROPROLEUPROALAILE
13   PROASPGLNGLNILEVALGLUGLUALASER
14   ASNSERTHRLEUGLUSERALAPROASNGLY
15   LYSASPTYRGLUSERTHRGLUILEVALALA
16   GLUGLUTHRLYSPROLYSASPTHRGLULEU
17   SERGLNGLUSERASPPHELYSGLUASNGLY

Samples:

sample_1: Akap79M, [U-98% 13C; U-98% 15N], 1 mM; TRIS 50 mM; sodium chloride 50 mM; sodium azide 0.2%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 288 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

Analysis v2.1.3, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

DBJ BAG37736
GB AAA58363 AAH57229 AAI31517 AIC55599 EAW80862
REF NP_004848 XP_002824884 XP_003831662 XP_004055341 XP_004055342
SP P24588
AlphaFold P24588

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