BMRB Entry 36401

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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/BMR36401
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of human Aha1 N-terminal domain
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, 135 residues, 15135.936 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 MGIYISTLKTEFTQG

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts131
1H chemical shifts757

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 135 residues - 15135.936 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   GLUPHETHRGLNGLY

Samples:

15N_Aha1N: Aha1N, [U-15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

15N;13C_Aha1N: Aha1N, [U-15N;U-13C], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

13C_Aha1N: Aha1N, [U-13C], 0.5 mM; D2O, [U-2H], 100%

sample_4: Aha1N, [U-15N], 0.5 mM; virus 37%; H2O 53%; 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 HSQC15N_Aha1Nisotropicsample_conditions_1
2D 1H-13C HSQC13C_Aha1Nisotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_4anisotropicsample_conditions_1
3D HNCO15N;13C_Aha1Nisotropicsample_conditions_1
3D HN(CA)CO15N;13C_Aha1Nisotropicsample_conditions_1
3D HNCA15N;13C_Aha1Nisotropicsample_conditions_1
3D CBCA(CO)NH15N;13C_Aha1Nisotropicsample_conditions_1
3D HNCACB15N;13C_Aha1Nisotropicsample_conditions_1
3D HBHA(CO)NH15N;13C_Aha1Nisotropicsample_conditions_1
3D H(CCO)NH15N;13C_Aha1Nisotropicsample_conditions_1
3D C(CO)NH15N;13C_Aha1Nisotropicsample_conditions_1
3D HCCH-TOCSY13C_Aha1Nisotropicsample_conditions_1
3D 1H-15N NOESY15N_Aha1Nisotropicsample_conditions_1
3D 1H-13C NOESY13C_Aha1Nisotropicsample_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