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 34223

Title: NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP90 peptide DTSRMEEVD   PubMed: 30033218

Deposition date: 2017-12-26 Original release date: 2018-07-26

Authors: Quinternet, M.; Chagot, M.; Manival, X.

Citation: Henri, Julien; Chagot, Marie-Eve; Bourguet, Maxime; Abel, Yoann; Terral, Guillaume; Maurizy, Chloe; Aigueperse, Christelle; Georgescauld, Florian; Vandermoere, Franck; Saint-Fort, Renette; Behm-Ansmant, Isabelle; Charpentier, Bruno; Pradet-Balade, Berengere; Verheggen, Celine; Bertrand, Edouard; Meyer, Philippe; Cianferani, Sarah; Manival, Xavier; Quinternet, Marc. "Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex"  Structure 26, 1196-1209 (2018).

Assembly members:
entity_1, polymer, 120 residues, 13368.283 Da.
entity_2, polymer, 9 residues, 1082.120 Da.

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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GPHMQAISEKDRGNGFFKEG KYERAIECYTRGIAADGANA LLPANRAMAYLKIQKYEEAE KDCTQAILLDGSYSKAFARR GTARTFLGKLNEAKQDFETV LLLEPGNKQAVTELSKIKKK
entity_2: DTSRMEEVD

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts141
1H chemical shifts920

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 120 residues - 13368.283 Da.

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

Entity 2, entity_2 9 residues - 1082.120 Da.

1   ASPTHRSERARGMETGLUGLUVALASP

Samples:

sample_1: RPAP3-TPR2, [U-13C; U-15N], 1 mM; HSP90-pep 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_2: RPAP3-TPR2, [U-13C; U-15N], 1 mM; HSP90-pep 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

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

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D X-halffiltered 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D X-half filtered 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D double X-half filtered 1H-1H NOESYsample_2isotropicsample_conditions_1
2D double X-half filtered 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS, Cornilescu, Delaglio and Bax - structure calculation

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

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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