BMRB Entry 19757

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19757

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

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).
PubMed: 24668569

Assembly members:

Assembly members:
rpap3(281-396), polymer, 120 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: pnEA-3CH

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rpap3(281-396): GPHMQAISEKDRGNGFFKEG KYERAIECYTRGIAADGANA LLPANRAMAYLKIQKYEEAE KDCTQAILLDGSYSKAFARR GTARTFLGKLNEAKQDFETV LLLEPGNKQAVTELSKIKKK

Data sets:
Data typeCount
13C chemical shifts501
15N chemical shifts126
1H chemical shifts835

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TPR21

Entities:

Entity 1, TPR2 120 residues - Formula weight is not available

1   GLYPROHISMETGLNALAILESERGLULYS
2   ASPARGGLYASNGLYPHEPHELYSGLUGLY
3   LYSTYRGLUARGALAILEGLUCYSTYRTHR
4   ARGGLYILEALAALAASPGLYALAASNALA
5   LEULEUPROALAASNARGALAMETALATYR
6   LEULYSILEGLNLYSTYRGLUGLUALAGLU
7   LYSASPCYSTHRGLNALAILELEULEUASP
8   GLYSERTYRSERLYSALAPHEALAARGARG
9   GLYTHRALAARGTHRPHELEUGLYLYSLEU
10   ASNGLUALALYSGLNASPPHEGLUTHRVAL
11   LEULEULEUGLUPROGLYASNLYSGLNALA
12   VALTHRGLULEUSERLYSILELYSLYSLYS

Samples:

sample_1: rpap3(281-396), [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride 150 mM; DTT, [U-99% 2H], 10 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N 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
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks