BMRB Entry 6877

Name: NMR assignments of the Human Papillomavirus type 16 E2C DNA-bound form
Published: 2007-01-29

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6877

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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:

NMR assignments of the Human Papillomavirus type 16 E2C DNA-bound form

Deposition date:

2005-10-26

Original release date:

2007-01-29

Authors:

Eliseo, Tommaso; Nadra, Alejandro; Paci, Maurizio; de Prat-Gay, Gonzalo; Cicero, Daniel

Citation:

Citation: Cicero, Daniel; Nadra, Alejandro; Eliseo, Tommaso; Dellarole, Mariano; Paci, Maurizio; de Prat-Gay, Gonzalo. "Structural and Thermodynamic Basis for the Enhanced Transcriptional Control by the Human Papillomavirus Strain-16 E2 Protein" Biochemistry 45, 6551-6560 (2006).
PubMed: 16716065

Assembly members:

Assembly members:
HPV E2C, polymer, 81 residues, 9366 Da.
site35 DNA, polymer, 18 residues, 5500 Da.

Natural source:

Natural source: Common Name: Human Papillomavirus type 16 Taxonomy ID: 10566 Superkingdom: Viruses Kingdom: not available Genus/species: Papillomavirus Human Papillomavirus

Experimental source:

Experimental source: Production method: recombinant technology Vector: ptz18

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HPV E2C: MTPIVHLKGDANTLKCLRYR FKKHCTLYTAVSSTWHWTGH NVKHKSAIVTLTYDSEWQRD QFLSQVKIPKTITVSTGFMS I
site35 DNA: GTAACCGAAATCGGTTGA

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	245
15N chemical shifts	76
1H chemical shifts	343

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HPV E2C chain A	1
2	HPV E2C chain B	1
3	site 35 strand A	2
4	site 35 strand B	2

Entities:

Entity 1, HPV E2C chain A 81 residues - 9366 Da.

1

MET

THR

PRO

ILE

VAL

HIS

LEU

LYS

GLY

ASP

2

ALA

ASN

THR

LEU

LYS

CYS

LEU

ARG

TYR

ARG

3

PHE

LYS

HIS

CYS

THR

LEU

TYR

THR

ALA

4

VAL

SER

THR

TRP

HIS

TRP

THR

GLY

HIS

5

ASN

VAL

LYS

HIS

LYS

SER

ALA

ILE

VAL

THR

6

LEU

THR

TYR

ASP

SER

GLU

TRP

GLN

ARG

ASP

7

GLN

PHE

LEU

SER

GLN

VAL

LYS

ILE

PRO

LYS

8

THR

ILE

THR

VAL

SER

THR

GLY

PHE

MET

SER

9

ILE

Entity 2, site 35 strand A 18 residues - 5500 Da.

1

DG

DT

DA

DC

DG

DA

2

DT

DC

DG

DT

DG

DA

Samples:

sample_1: HPV E2C, [U-15N], 0.6 mM; site35, none, 0.7 mM; NaCl 250 mM; MgCl2 5 mM; Sodium Phosphate 10 mM; Sodium Acetate 50 mM; DTT 5 mM

sample_2: HPV E2C, [U-15N; U-13C], 0.6 mM; site35, none, 0.7 mM; Sodium Chloride 250 mM; Magnesium Chloride 5 mM; Sodium Phosphate 10 mM; Sodium Acetate 50 mM; DTT 5 mM

conditions_1: pH: 5.6; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N HSQC	sample_2	not available	conditions_1
HNCO	sample_2	not available	conditions_1
HNCA	sample_2	not available	conditions_1
HN(CO)CA	sample_2	not available	conditions_1
CBCA(CO)NH	sample_2	not available	conditions_1
15N NOESY	sample_2	not available	conditions_1
13C NOESY	sample_1	not available	conditions_1

Software:

NMRPipe - Data processing

NMRView v5.0.4 - Data analysis

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	5952
PDB	1BY9 1R8P 1ZZF 2Q79 3MI7
DBJ	BAN63221 BAN63229 BAN63253 BAN63261 BAN63269
GB	AAA46941 AAD03824 AAD03825 AAD03826 AAD03827
REF	NP_041328
SP	P03120
AlphaFold	P03120