BMRB Entry 18497

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18497
MolProbity Validation Chart

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Title:
Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit
Deposition date:
2012-06-01
Original release date:
2013-06-10
Authors:
Xia, Bin; Hu, Jicheng
Citation:

Citation: Xia, Bin; Hu, Jicheng. "Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit"  .

Assembly members:

Assembly members:
entity, polymer, 62 residues, 7026.763 Da.

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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPHMSYDANVIDDEAVKEVC EKFECTESEVMNSLYSGDPQ DQLAVAYHLIIDNRRIMNQA SE

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts62
1H chemical shifts361

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1autoinhibitory domain of human AMP-activated protein kinase catalytic subunit1

Entities:

Entity 1, autoinhibitory domain of human AMP-activated protein kinase catalytic subunit 62 residues - 7026.763 Da.

1   GLYPROHISMETSERTYRASPALAASNVAL
2   ILEASPASPGLUALAVALLYSGLUVALCYS
3   GLULYSPHEGLUCYSTHRGLUSERGLUVAL
4   METASNSERLEUTYRSERGLYASPPROGLN
5   ASPGLNLEUALAVALALATYRHISLEUILE
6   ILEASPASNARGARGILEMETASNGLNALA
7   SERGLU

Samples:

sample_1: AID protein, [U-100% 13C; U-100% 15N], 0.2 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 10%; H2O 90%; EDTA 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 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 HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - peak picking

TOPSPIN, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

DYANA, Guntert, Braun and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

ProcheckNMR, Laskowski and MacArthur - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC31746 BAE22188 BAG36722
EMBL CAA82620 CAH90357
GB AAA64745 AAA85033 AAB32732 AAH69680 AAH69740
REF NP_001075410 NP_001106287 NP_001125173 NP_001135554 NP_001192534
SP P54646 Q09137 Q28948 Q5RD00 Q8BRK8
TPG DAA31222
AlphaFold P54646 Q09137 Q28948 Q5RD00 Q8BRK8

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