BMRB Entry 36402

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36402
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Solution structure of human Aha1
Deposition date:
2020-12-03
Original release date:
2025-10-25
Authors:
Hu, H.; Zhou, C.; Zhang, N.
Citation:

Citation: Hu, Huifang; Wang, Qing; Du, Jingwen; Liu, Zhijun; Ding, Yiluan; Xue, Hongjuan; Zhou, Chen; Feng, Linyin; Zhang, Naixia. "Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity."  Molecules 26, 1943-1943 (2021).
PubMed: 33808352

Assembly members:

Assembly members:
Activator of 90 kDa heat shock protein ATPase homolog 1, polymer, 308 residues, 34650.168 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Activator of 90 kDa heat shock protein ATPase homolog 1: TERDASNWSTDKLKTLFLAV QVQNEEGKCEVTEVSKLDGE ASINNRKGKLIFFYEWSVKL NWTGTSKSGVQYKGHVEIPN LSDENSVDEVEISVSLAKDE PDTNLVALMKEEGVKLLREA MGIYISTLKTEFTQGMILPT MNGESVDPVGQPALKTEERK AKPAPSKTQARPVGVKIPTC KITLKETFLTSPEELYRVFT TQELVQAFTHAPATLEADRG GKFHMVDGNVSGEFTDLVPE KHIVMKWRFKSWPEGHFATI TLTFIDKNGETELCMEGRGI PAPEEERTRQGWQRYYFEGI KQTFGYGA

Data sets:
Data typeCount
13C chemical shifts797
15N chemical shifts277
1H chemical shifts709

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 308 residues - 34650.168 Da.

1   THRGLUARGASPALASERASNTRPSERTHR
2   ASPLYSLEULYSTHRLEUPHELEUALAVAL
3   GLNVALGLNASNGLUGLUGLYLYSCYSGLU
4   VALTHRGLUVALSERLYSLEUASPGLYGLU
5   ALASERILEASNASNARGLYSGLYLYSLEU
6   ILEPHEPHETYRGLUTRPSERVALLYSLEU
7   ASNTRPTHRGLYTHRSERLYSSERGLYVAL
8   GLNTYRLYSGLYHISVALGLUILEPROASN
9   LEUSERASPGLUASNSERVALASPGLUVAL
10   GLUILESERVALSERLEUALALYSASPGLU
11   PROASPTHRASNLEUVALALALEUMETLYS
12   GLUGLUGLYVALLYSLEULEUARGGLUALA
13   METGLYILETYRILESERTHRLEULYSTHR
14   GLUPHETHRGLNGLYMETILELEUPROTHR
15   METASNGLYGLUSERVALASPPROVALGLY
16   GLNPROALALEULYSTHRGLUGLUARGLYS
17   ALALYSPROALAPROSERLYSTHRGLNALA
18   ARGPROVALGLYVALLYSILEPROTHRCYS
19   LYSILETHRLEULYSGLUTHRPHELEUTHR
20   SERPROGLUGLULEUTYRARGVALPHETHR
21   THRGLNGLULEUVALGLNALAPHETHRHIS
22   ALAPROALATHRLEUGLUALAASPARGGLY
23   GLYLYSPHEHISMETVALASPGLYASNVAL
24   SERGLYGLUPHETHRASPLEUVALPROGLU
25   LYSHISILEVALMETLYSTRPARGPHELYS
26   SERTRPPROGLUGLYHISPHEALATHRILE
27   THRLEUTHRPHEILEASPLYSASNGLYGLU
28   THRGLULEUCYSMETGLUGLYARGGLYILE
29   PROALAPROGLUGLUGLUARGTHRARGGLN
30   GLYTRPGLNARGTYRTYRPHEGLUGLYILE
31   LYSGLNTHRPHEGLYTYRGLYALA

Samples:

15N_Aha1: Aha1, [U-15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

15N;13C_Aha1: Aha1, [U-15N;U-13C], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: Aha1, [U-15N], 0.5 mM; virus 28%; H2O 62%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCnot availableanisotropicsample_conditions_1
3D HNCOnot availableisotropicsample_conditions_1
3D HN(CA)COnot availableisotropicsample_conditions_1
3D HNCAnot availableisotropicsample_conditions_1
3D CBCA(CO)NHnot availableisotropicsample_conditions_1
3D HNCACBnot availableisotropicsample_conditions_1
3D HBHA(CO)NHnot availableisotropicsample_conditions_1
3D H(CCO)NHnot availableisotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

CARA, Keller and Wuthrich - peak picking

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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