BMRB Entry 18794

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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/BMR18794
MolProbity Validation Chart

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Title:
Structure of module 2 from the E1 domain of C. elegans APL-1
Deposition date:
2012-10-20
Original release date:
2013-10-21
Authors:
Hinds, Mark; Leong, Su Ling
Citation:

Citation: Leong, Su Ling; Young, Tessa; Barnham, Kevin; Wedd, Anthony; Hinds, Mark; Xiao, Zhiguang; Cappai, Roberto. "Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function."  Metallomics 6, 105-116 (2014).
PubMed: 24276282

Assembly members:

Assembly members:
entity, polymer, 65 residues, 7428.485 Da.

Natural source:

Natural source:   Common Name: Caenorhabditis elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: EACQFSHVNSRDQCNDYQHW KDEAGKQCKTKKSKGNKDMI VRSFAVLEPCALDMFTGVEF VCCPN

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts68
1H chemical shifts439

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1module 2 from the E1 domain of C. elegans APL-11

Entities:

Entity 1, module 2 from the E1 domain of C. elegans APL-1 65 residues - 7428.485 Da.

residues 133-197 of C. elegans APL-1

1   GLUALACYSGLNPHESERHISVALASNSER
2   ARGASPGLNCYSASNASPTYRGLNHISTRP
3   LYSASPGLUALAGLYLYSGLNCYSLYSTHR
4   LYSLYSSERLYSGLYASNLYSASPMETILE
5   VALARGSERPHEALAVALLEUGLUPROCYS
6   ALALEUASPMETPHETHRGLYVALGLUPHE
7   VALCYSCYSPROASN

Samples:

sample_1: APL-1 0.5 mM; APL-1, [U-100% 15N], 0.5 mM; APL-1, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker AG - collection

XEASY, Bartels et al. - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q10651
PDB
EMBL CCD65568 CCD65569
GB AAC46470
REF NP_508870 NP_508871
SP Q10651
AlphaFold Q95ZX1 Q10651

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