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 30570

Title: NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae

Deposition date: 2019-02-12 Original release date: 2020-08-14

Authors: Bragantini, B.; Quinternet, M.; Charpentier, B.; Manival, X.

Citation: Bragantini, B.; Terral, G.; Tiotiu, D.; Charron, C.; Bourguet, M.; Rothe, B.; Paul, A.; Marty, H.; Labialle, S.; Quinternet, M.; Cianferani, S.; Manival, X.; Charpentier, B.. "Box C/D protein 1 and the histone chaperone Rtt106 are components of pre-snoRNPs through direct interaction"  . ., .-..

Assembly members:
entity_1, polymer, 188 residues, 21864.262 Da.

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
entity_1: GPHMRDSTECQRIIRRGVNC LMLPKGMQRSSQNRSKWDKT MDLFVWSVEWILCPMQEKGE KKELFKHVSHRIKETDFLVQ GMGKNVFQKCCEFYRLAGTS SCIEGEDGSETKEERTQILQ KSGLKFYTKTFPYNTTHIMD SKKLVELAIHEKCIGELLKN TTVIEFPTIFVAMTEADLPE GYEVLHQE

Data sets:
Data typeCount
13C chemical shifts824
15N chemical shifts202
1H chemical shifts1355

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 188 residues - 21864.262 Da.

1   GLYPROHISMETARGASPSERTHRGLUCYS
2   GLNARGILEILEARGARGGLYVALASNCYS
3   LEUMETLEUPROLYSGLYMETGLNARGSER
4   SERGLNASNARGSERLYSTRPASPLYSTHR
5   METASPLEUPHEVALTRPSERVALGLUTRP
6   ILELEUCYSPROMETGLNGLULYSGLYGLU
7   LYSLYSGLULEUPHELYSHISVALSERHIS
8   ARGILELYSGLUTHRASPPHELEUVALGLN
9   GLYMETGLYLYSASNVALPHEGLNLYSCYS
10   CYSGLUPHETYRARGLEUALAGLYTHRSER
11   SERCYSILEGLUGLYGLUASPGLYSERGLU
12   THRLYSGLUGLUARGTHRGLNILELEUGLN
13   LYSSERGLYLEULYSPHETYRTHRLYSTHR
14   PHEPROTYRASNTHRTHRHISILEMETASP
15   SERLYSLYSLEUVALGLULEUALAILEHIS
16   GLULYSCYSILEGLYGLULEULEULYSASN
17   THRTHRVALILEGLUPHEPROTHRILEPHE
18   VALALAMETTHRGLUALAASPLEUPROGLU
19   GLYTYRGLUVALLEUHISGLNGLU

Samples:

sample_1: Box C/D snoRNA protein 1, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_2: Box C/D snoRNA protein 1, [U-13C; U-15N; U-2H], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_3: Box C/D snoRNA protein 1, [U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM; Pf1 phage 12 mg/mL

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 HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D CCCONHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 950 MHz

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