BMRB Entry 25991

Name: 1H, 13C, and 15N Chemical Shift Assignments of HAdV E1ACR3 (E1A CR3)
Published: 2017-09-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25991

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments of HAdV E1ACR3 (E1A CR3)

Deposition date:

2016-03-11

Original release date:

2017-09-25

Authors:

Hosek, Tomas; Nogueira, Marcela; Calcada, Eduardo; Pagani, Talita; Salvi, Nicola; Felli, Isabella; Pierattelli, Roberta

Citation:

Citation: Hosek, Tomas; Calcada, Eduardo; Nogueira, Marcela; Salvi, Nicola; 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).
PubMed: 27490777

Assembly members:

Assembly members:
E1A-CR3, polymer, 55 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human adenovirus 2 Taxonomy ID: 10515 Superkingdom: Viruses Kingdom: not available Genus/species: Mastadenovirus Human mastadenovirus C

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E1A-CR3: MDEEGEEFVLDYVEHPGHGC RSCHYHRRNTGDPDIMCSLC YMRTCGMFVYSPVSE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	191
15N chemical shifts	50
1H chemical shifts	287

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E1A-CR3	1

Entities:

Entity 1, E1A-CR3 55 residues - Formula weight is not available

1

MET

ASP

GLU

GLY

GLU

PHE

VAL

LEU

2

ASP

TYR

VAL

GLU

HIS

PRO

GLY

HIS

GLY

CYS

3

ARG

SER

CYS

HIS

TYR

HIS

ARG

ASN

THR

4

GLY

ASP

PRO

ASP

ILE

MET

CYS

SER

LEU

CYS

5

TYR

MET

ARG

THR

CYS

GLY

MET

PHE

VAL

TYR

6

SER

PRO

VAL

SER

GLU

Samples:

sample_1: E1A-CR3, [U-100% 13C; U-100% 15N], 0.07 mM; HEPES 10 mM; potassium chloride 50 mM; DTT 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: E1A-CR3, [U-100% 13C; U-100% 15N], 0.14 mM; HEPES 10 mM; potassium chloride 50 mM; DTT 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N BEST TROSY	sample_1	isotropic	sample_conditions_1
3D BEST TROSY HNCO	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D BEST TROSY HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D BEST TROSY HNCACB	sample_1	isotropic	sample_conditions_1
3D BEST TROSY HNCA	sample_2	isotropic	sample_conditions_1
3D BEST TROSY HN(CO)CA	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.0 and 3.1, Bruker Biospin - collection

CcpNMR vv2.3.1, CCPN - chemical shift assignment, data analysis, peak picking

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 950 MHz
Bruker Avance 900 MHz

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