BMRB Entry 19442

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for E7 protein from human Papillomavirus 16
Published: 2013-09-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19442

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for E7 protein from human Papillomavirus 16

Deposition date:

2013-08-20

Original release date:

2013-09-19

Authors:

Calcada, Eduardo; Felli, Isabella; Hosek, Tomas; Pierattelli, Roberta

Citation:

Citation: Calcada, Eduardo; Felli, Isabella; Hoek, Toma; Pierattelli, Roberta. "The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy." Chembiochem 14, 1876-1882 (2013).
PubMed: 23940009

Assembly members:

Assembly members:
HPV16_E7, polymer, 106 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: HPV Taxonomy ID: 10566 Superkingdom: Virus Kingdom: not available Genus/species: Alphapapillomavirus Human Papillomavirus-16

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET20-E7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HPV16_E7: MHGDTPTLHEYMLDLQPETT DLYCYEQLNDSSEEEDEIDG PAGQAEPDRAHYNIVTFCCK CDSTLRLCVQSTHVDIRTLE DLLMGTLGIVCPICSQKPLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	126
15N chemical shifts	42
1H chemical shifts	39

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E7_1	1
2	E7_2	1
3	Zinc Ion 1	2
4	Zinc Ion 2	2

Entities:

Entity 1, E7_1 106 residues - Formula weight is not available

1

MET

HIS

GLY

ASP

THR

PRO

THR

LEU

HIS

GLU

2

TYR

MET

LEU

ASP

LEU

GLN

PRO

GLU

THR

3

ASP

LEU

TYR

CYS

TYR

GLU

GLN

LEU

ASN

ASP

4

SER

GLU

ASP

GLU

ILE

ASP

GLY

5

PRO

ALA

GLY

GLN

ALA

GLU

PRO

ASP

ARG

ALA

6

HIS

TYR

ASN

ILE

VAL

THR

PHE

CYS

LYS

7

CYS

ASP

SER

THR

LEU

ARG

LEU

CYS

VAL

GLN

8

SER

THR

HIS

VAL

ASP

ILE

ARG

THR

LEU

GLU

9

ASP

LEU

MET

GLY

THR

LEU

GLY

ILE

VAL

10

CYS

PRO

ILE

CYS

SER

GLN

LYS

PRO

LEU

GLU

11

HIS

Entity 2, Zinc Ion 1 - 65.409 Da.

1

ZN

Samples:

sample_1: HEPES 10 mM; potassium chloride 150 mM; DTT 10 mM; zinc chloride 10 uM; HPV16 E7, [U-13C; U-15N], 760 ± 76 mM; H2O 90%; D2O 10%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N SOFAST HMQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCANNH	sample_1	isotropic	sample_conditions_1
2D 13C-15N CON-IPAP	sample_1	isotropic	sample_conditions_1
2D 13C-13C HCACO-IPAP	sample_1	isotropic	sample_conditions_1
3D HCBCACON-IPAP	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.0, Bruker - processing

SPARKY v3.115, T. D. Goddard and D. G. Kneller - chemical shift assignment

CARA v2.1, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz
Bruker DRX 500 MHz

DBJ	BAA00633 BAN15982 BAN15983 BAN15984 BAN15985
EMBL	CAB45105 CAB45107 CAB45109 CAB45111 CAB45113
GB	AAA46940 AAB18962 AAB18963 AAB18964 AAB70737
PRF	2002324A
REF	NP_041326 WP_053289714
SP	P03129
AlphaFold	P03129