BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25990

Title: 1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A289 (E1A-13S)   PubMed: 27490777

Authors: Hosek, Tomas; Calcada, Eduardo; Salvi, Michele; Pagani, Talita; Nogueira, Marcela; Felli, Isabella; Pierattelli, Roberta

Citation: Hosek, Tomas; Calcada, Eduardo; Nogueira, Marcela; Salvi, Michele; Pagani, Talita; Felli, Isabella; Pierattelli, Roberta. "Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus"  Chemistry 22, 13010-13013 (2016).

Assembly members:
E1A-13S, polymer, 299 residues, Formula weight is not available

Natural source:   Common Name: Human adenovirus 5   Taxonomy ID: 28285   Superkingdom: Viruses   Kingdom: not available   Genus/species: Mastadenovirus Human mastadenovirus C

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
E1A-13S: MRHIICHGGVITEEMAASLL DQLIEEVLADNLPPPSHFEP PTLHELYDLDVTAPEDPNEE AVSQIFPESVMLAVQEGIDL FTFPPAPGSPEPPHLSRQPE QPEQRALGPVSMPNLVPEVI DLTCHEAGFPPSDDEDEEGE EFVLDYVGHPGHGCRSCHYH RRNTGDPDIMCSLCYMRTCG MFVYSPVSEPEPEPEPEPEP ARPTRRPKLVPAILRRPTSP VSRECNSSTDSCDSGPSNTP PEIHPVVPLCPIKPVAVRVG GRRQAVECIEDLLNEPGQPL DLSCKRPRPLEHHHHHHHH

Data sets:
Data typeCount
13C chemical shifts572
15N chemical shifts167
1H chemical shifts167

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1E1A-13S1

Entities:

Entity 1, E1A-13S 299 residues - Formula weight is not available

1   METARGHISILEILECYSHISGLYGLYVAL
2   ILETHRGLUGLUMETALAALASERLEULEU
3   ASPGLNLEUILEGLUGLUVALLEUALAASP
4   ASNLEUPROPROPROSERHISPHEGLUPRO
5   PROTHRLEUHISGLULEUTYRASPLEUASP
6   VALTHRALAPROGLUASPPROASNGLUGLU
7   ALAVALSERGLNILEPHEPROGLUSERVAL
8   METLEUALAVALGLNGLUGLYILEASPLEU
9   PHETHRPHEPROPROALAPROGLYSERPRO
10   GLUPROPROHISLEUSERARGGLNPROGLU
11   GLNPROGLUGLNARGALALEUGLYPROVAL
12   SERMETPROASNLEUVALPROGLUVALILE
13   ASPLEUTHRCYSHISGLUALAGLYPHEPRO
14   PROSERASPASPGLUASPGLUGLUGLYGLU
15   GLUPHEVALLEUASPTYRVALGLYHISPRO
16   GLYHISGLYCYSARGSERCYSHISTYRHIS
17   ARGARGASNTHRGLYASPPROASPILEMET
18   CYSSERLEUCYSTYRMETARGTHRCYSGLY
19   METPHEVALTYRSERPROVALSERGLUPRO
20   GLUPROGLUPROGLUPROGLUPROGLUPRO
21   ALAARGPROTHRARGARGPROLYSLEUVAL
22   PROALAILELEUARGARGPROTHRSERPRO
23   VALSERARGGLUCYSASNSERSERTHRASP
24   SERCYSASPSERGLYPROSERASNTHRPRO
25   PROGLUILEHISPROVALVALPROLEUCYS
26   PROILELYSPROVALALAVALARGVALGLY
27   GLYARGARGGLNALAVALGLUCYSILEGLU
28   ASPLEULEUASNGLUPROGLYGLNPROLEU
29   ASPLEUSERCYSLYSARGPROARGPROLEU
30   GLUHISHISHISHISHISHISHISHIS

Samples:

sample_1: E1A-13S, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 10 mM; potassium chloride 150 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: E1A-13S, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 10 mM; potassium chloride 150 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D CON-IPAPsample_1isotropicsample_conditions_1
3D HCBCACON-IPAPsample_1isotropicsample_conditions_1
2D 1H-15N BEST-TROSYsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCOsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCACOsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCOCACBsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCACBsample_2isotropicsample_conditions_1
3D BEST-TROSY HN(CA)NNHsample_2isotropicsample_conditions_1
3D TROSY HN(COCA)NNHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

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