BMRB Entry 16195

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16195
MolProbity Validation Chart

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Title:
Resonance assignments of the human AKAP13 PH domain and stabilizing DH helix
Deposition date:
2009-03-05
Original release date:
2009-08-10
Authors:
Sugawara, Masae; Whittaker, Sara; Bishop, Shurene; Ball, Linda; Overduin, Michael
Citation:

Citation: Sugawara, Masae; Whittaker, Sara; Bishop, Shurene; Ball, Linda; Overduin, Michael. "Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix"  Biomol. NMR Assignments 3, 215-218 (2009).
PubMed: 19888694

Assembly members:

Assembly members:
AKAP13-PH, polymer, 185 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: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AKAP13-PH: SMTKDNEVEQEDLAQSLSLV KDVIGAVDSKVASYEKKVRL NEIYTKTDSKSIMRMKSGQM FAKEDLKRKKLVRDGSVFLK NAAGRLKEVQAVLLTDILVF LQEKDQKYIFASLDQKSTVI SLKKLIVREVAHEEKGLFLI SMGMTDPEMVEVHASSKEER NSWIQIIQDTINTLNRDEDE GIPSE

Data sets:
Data typeCount
13C chemical shifts818
15N chemical shifts189
1H chemical shifts1274

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AKAP13-PH1

Entities:

Entity 1, AKAP13-PH 185 residues - Formula weight is not available

1   SERMETTHRLYSASPASNGLUVALGLUGLN
2   GLUASPLEUALAGLNSERLEUSERLEUVAL
3   LYSASPVALILEGLYALAVALASPSERLYS
4   VALALASERTYRGLULYSLYSVALARGLEU
5   ASNGLUILETYRTHRLYSTHRASPSERLYS
6   SERILEMETARGMETLYSSERGLYGLNMET
7   PHEALALYSGLUASPLEULYSARGLYSLYS
8   LEUVALARGASPGLYSERVALPHELEULYS
9   ASNALAALAGLYARGLEULYSGLUVALGLN
10   ALAVALLEULEUTHRASPILELEUVALPHE
11   LEUGLNGLULYSASPGLNLYSTYRILEPHE
12   ALASERLEUASPGLNLYSSERTHRVALILE
13   SERLEULYSLYSLEUILEVALARGGLUVAL
14   ALAHISGLUGLULYSGLYLEUPHELEUILE
15   SERMETGLYMETTHRASPPROGLUMETVAL
16   GLUVALHISALASERSERLYSGLUGLUARG
17   ASNSERTRPILEGLNILEILEGLNASPTHR
18   ILEASNTHRLEUASNARGASPGLUASPGLU
19   GLYILEPROSERGLU

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 150 mM; Sodium azide 0.02%; D2O, [U-99% 2H], 10%; AKAP13-PH, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis v2, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAB62913 BAD92651 BAE01465
GB AAC50065 AAD21311 AAD40799 AAI40863 AAI71798
REF NP_001257475 NP_006729 NP_009131 XP_001086697 XP_001163473
SP Q12802
AlphaFold Q12802

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