BMRB Entry 34200

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34200
MolProbity Validation Chart

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Title:
NMR structure of the C-terminal domain of the human RPAP3 protein
Deposition date:
2017-11-14
Original release date:
2018-04-13
Authors:
Fabre, P.; Chagot, M.; Bragantini, B.; Manival, X.; Quinternet, M.
Citation:

Citation: Maurizy, Chloe; Quinternet, Marc; Abel, Yoann; Verheggen, Celine; Santo, Paulo; Bourguet, Maxime; C F Paiva, Ana; Bragantini, Benoit; Chagot, Marie-Eve; Robert, Marie-Cecile; Abeza, Claire; Fabre, Philippe; Fort, Philippe; Vandermoere, Franck; M F Sousa, Pedro; Rain, Jean-Christophe; Charpentier, Bruno; Cianferani, Sarah; Bandeiras, Tiago; Pradet-Balade, Berengere; Manival, Xavier; Bertrand, Edouard. "The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones"  Nat. Commun. 9, 2093-2093 (2018).
PubMed: 29844425

Assembly members:

Assembly members:
entity_1, polymer, 135 residues, 15804.365 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMAQFATTVLPPIPANSF QLESDFRQLKSSPDMLYQYL KQIEPSLYPKLFQKNLDPDV FNQIVKILHDFYIEKEKPLL IFEILQRLSELKRFDMAVMF MSETEKKIARALFNHIDKSG LKDSSVEELKKRYGG

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts142
1H chemical shifts1041

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 135 residues - 15804.365 Da.

1   GLYPROHISMETALAGLNPHEALATHRTHR
2   VALLEUPROPROILEPROALAASNSERPHE
3   GLNLEUGLUSERASPPHEARGGLNLEULYS
4   SERSERPROASPMETLEUTYRGLNTYRLEU
5   LYSGLNILEGLUPROSERLEUTYRPROLYS
6   LEUPHEGLNLYSASNLEUASPPROASPVAL
7   PHEASNGLNILEVALLYSILELEUHISASP
8   PHETYRILEGLULYSGLULYSPROLEULEU
9   ILEPHEGLUILELEUGLNARGLEUSERGLU
10   LEULYSARGPHEASPMETALAVALMETPHE
11   METSERGLUTHRGLULYSLYSILEALAARG
12   ALALEUPHEASNHISILEASPLYSSERGLY
13   LEULYSASPSERSERVALGLUGLULEULYS
14   LYSARGTYRGLYGLY

Samples:

sample_1: RPAP3 C-terminal domain, [U-13C; U-15N], 1 mM; TCEP 0.5 mM; sodium chloride 150 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availablesample_conditions_1
2D 1H-13C HSQC aliphaticsample_1not availablesample_conditions_1
2D 1H-13C HSQC aromaticsample_1not availablesample_conditions_1
3D HNCAsample_1not availablesample_conditions_1
3D HNCACBsample_1not availablesample_conditions_1
2D 1H-1H NOESYsample_1not availablesample_conditions_1
3D HBHA(CO)NHsample_1not availablesample_conditions_1
3D HCCH-COSYsample_1not availablesample_conditions_1
3D HCCH-TOCSYsample_1not availablesample_conditions_1
3D (H)CCCONHsample_1not availablesample_conditions_1
3D H(CCO)NHsample_1not availablesample_conditions_1
3D HNHAsample_1not availablesample_conditions_1
3D HNCO E.cosysample_1not availablesample_conditions_1
3D HNCACOsample_1not availablesample_conditions_1
3D HNCOsample_1not availablesample_conditions_1
3D CBCA(CO)NHsample_1not availablesample_conditions_1
3D 1H-13C NOESYsample_1not availablesample_conditions_1
3D 1H-15N NOESYsample_1not availablesample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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