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 19332

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for p15(PAF)   PubMed: 24559989

Deposition date: 2013-07-01 Original release date: 2013-07-11

Authors: De Biasio, Alfredo; Ibanez de Opakua, Alain

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts107
1H chemical shifts225

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1p15(PAF)1

Entities:

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

1   METVALARGTHRLYSALAASPSERVALPRO
2   GLYTHRTYRARGLYSVALVALALAALAARG
3   ALAPROARGLYSVALLEUGLYSERSERTHR
4   SERALATHRASNSERTHRSERVALSERSER
5   ARGLYSALAGLUASNLYSTYRALAGLYGLY
6   ASNPROVALCYSVALARGPROTHRPROLYS
7   TRPGLNLYSGLYILEGLYGLUPHEPHEARG
8   LEUSERPROLYSASPSERGLULYSGLUASN
9   GLNILEPROGLUGLUALAGLYSERSERGLY
10   LEUGLYLYSALALYSARGLYSALACYSPRO
11   LEUGLNPROASPHISTHRASNASPGLULYS
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1
3D HN(CACO)HAsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts