BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19758

Title: 1H, 15N and 13C resonance assignments of the two TPR domains of the human RPAP3 protein   PubMed: 24668569

Deposition date: 2014-01-30 Original release date: 2019-08-13

Authors: Chagot, Marie-Eve; Jacquemin, Cl mence; Charpentier, Bruno; Manival, Xavier; Quinternet, Marc

Citation: Chagot, Marie-Eve; Jacquemin, Clemence; Branlant, Christiane; Charpentier, Bruno; Manival, Xavier; Quinternet, Marc. "(1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein."  Biomol. NMR Assignments 9, 99-102 (2014).

Assembly members:
rpap3(133-255), polymer, 127 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' 'Escherichia coli

Entity Sequences (FASTA):
rpap3(133-255): GPHMALVLKEKGNKYFKQGK YDEAIDCYTKGMDADPYNPV LPTNRASAYFRLKKFAVAES DCNLAVALNRSYTKAYSRRG AARFALQKLEEAKKDYERVL ELEPNNFEATNELRKISQAL ASKENSY

Data sets:
Data typeCount
13C chemical shifts537
15N chemical shifts132
1H chemical shifts880

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TPR11

Entities:

Entity 1, TPR1 127 residues - Formula weight is not available

1   GLYPROHISMETALALEUVALLEULYSGLU
2   LYSGLYASNLYSTYRPHELYSGLNGLYLYS
3   TYRASPGLUALAILEASPCYSTYRTHRLYS
4   GLYMETASPALAASPPROTYRASNPROVAL
5   LEUPROTHRASNARGALASERALATYRPHE
6   ARGLEULYSLYSPHEALAVALALAGLUSER
7   ASPCYSASNLEUALAVALALALEUASNARG
8   SERTYRTHRLYSALATYRSERARGARGGLY
9   ALAALAARGPHEALALEUGLNLYSLEUGLU
10   GLUALALYSLYSASPTYRGLUARGVALLEU
11   GLULEUGLUPROASNASNPHEGLUALATHR
12   ASNGLULEUARGLYSILESERGLNALALEU
13   ALASERLYSGLUASNSERTYR

Samples:

sample_1: rpap3(133-255), [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride' 'natural abundance; [U-99% 2H]; natural abundance; [U-100% 2H]

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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