BMRB Entry 19332

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for p15(PAF)
Published: 2013-07-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19332

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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 p15(PAF)

Deposition date:

2013-07-01

Original release date:

2013-07-11

Authors:

De Biasio, Alfredo; Ibanez de Opakua, Alain

Citation:

Citation: De Biasio, Alfredo; Ibanez de Opakua, Alain; Cordeiro, Tiago; Villate, Maider; Merino, Nekane; Sibille, Nathalie; Lelli, Moreno; Diercks, Tammo; Bernado, Pau; Blanco, Francisco. "p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins." Biophys. J. 106, 865-874 (2014).
PubMed: 24559989

Assembly members:

Assembly members:
p15(PAF), polymer, 111 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p15(PAF): MVRTKADSVPGTYRKVVAAR APRKVLGSSTSATNSTSVSS RKAENKYAGGNPVCVRPTPK WQKGIGEFFRLSPKDSEKEN QIPEEAGSSGLGKAKRKACP LQPDHTNDEKE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	422
15N chemical shifts	107
1H chemical shifts	225

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p15(PAF)	1

Entities:

Entity 1, p15(PAF) 111 residues - Formula weight is not available

1

MET

VAL

ARG

THR

LYS

ALA

ASP

SER

VAL

PRO

2

GLY

THR

TYR

ARG

LYS

VAL

ALA

ARG

3

ALA

PRO

ARG

LYS

VAL

LEU

GLY

SER

THR

4

SER

ALA

THR

ASN

SER

THR

SER

VAL

SER

5

ARG

LYS

ALA

GLU

ASN

LYS

TYR

ALA

GLY

6

ASN

PRO

VAL

CYS

VAL

ARG

PRO

THR

PRO

LYS

7

TRP

GLN

LYS

GLY

ILE

GLY

GLU

PHE

ARG

8

LEU

SER

PRO

LYS

ASP

SER

GLU

LYS

GLU

ASN

9

GLN

ILE

PRO

GLU

ALA

GLY

SER

GLY

10

LEU

GLY

LYS

ALA

LYS

ARG

LYS

ALA

CYS

PRO

11

LEU

GLN

PRO

ASP

HIS

THR

ASN

ASP

GLU

LYS

12

GLU

Samples:

sample_1: p15(PAF), [U-100% 13C; U-100% 15N], 0.9 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D HN(CACO)HA	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz

DBJ	BAA03491 BAF83437 BAG72594
GB	AAH05832 AAH07101 AAH16782 AAQ09604 AAT06735
REF	NP_001177672 NP_055551 XP_003778522 XP_003828000 XP_003952718
SP	Q15004
AlphaFold	Q15004