BMRB Entry 25442

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25442
MolProbity Validation Chart

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Title:
Snu17p-Bud13p structure intermediate during RES complex assembly
Deposition date:
2015-01-19
Original release date:
2015-08-10
Authors:
Wysoczanski, Piotr; Becker, Stefan; Zweckstetter, Markus
Citation:

Citation: Wysoczanski, Piotr; Becker, Stefan; Zweckstetter, Markus. "Structures of intermediates during RES complex assembly"  Sci. Rep. 5, 12545-12545 (2015).
PubMed: 26212312

Assembly members:

Assembly members:
Snu17p, polymer, 118 residues, 13496.103 Da.
Bud13p, polymer, 41 residues, 4888.440 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Snu17p: GAMGNEYKDNAYIYIGNLNR ELTEGDILTVFSEYGVPVDV ILSRDENTGESQGFAYLKYE DQRSTILAVDNLNGFKIGGR ALKIDHTFYRPKRSLQKYYE AVKEELDRDIVSKNNAEK
Bud13p: YDKPAPENRFAIMPGSRWDG VHRSNGFEEKWFAKQNEINE K

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts148
1H chemical shifts1013

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 118 residues - 13496.103 Da.

as above

1   GLYALAMETGLYASNGLUTYRLYSASPASN
2   ALATYRILETYRILEGLYASNLEUASNARG
3   GLULEUTHRGLUGLYASPILELEUTHRVAL
4   PHESERGLUTYRGLYVALPROVALASPVAL
5   ILELEUSERARGASPGLUASNTHRGLYGLU
6   SERGLNGLYPHEALATYRLEULYSTYRGLU
7   ASPGLNARGSERTHRILELEUALAVALASP
8   ASNLEUASNGLYPHELYSILEGLYGLYARG
9   ALALEULYSILEASPHISTHRPHETYRARG
10   PROLYSARGSERLEUGLNLYSTYRTYRGLU
11   ALAVALLYSGLUGLULEUASPARGASPILE
12   VALSERLYSASNASNALAGLULYS

Entity 2, entity_2 41 residues - 4888.440 Da.

as above

1   TYRASPLYSPROALAPROGLUASNARGPHE
2   ALAILEMETPROGLYSERARGTRPASPGLY
3   VALHISARGSERASNGLYPHEGLUGLULYS
4   TRPPHEALALYSGLNASNGLUILEASNGLU
5   LYS

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_1, [U-13C; U-15N], 0.8 – 1 mM; entity_21.0 – 1.2 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_11 – 1.2 mM; entity_2, [U-13C; U-15N], 0.8 – 1 mM; Snu17p 90%; Snu17p 10%

sample_3: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_1, [U-13C; U-15N], 1 mM; entity_2, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions: pH: 6.8; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
3D HNCAsample_2isotropicsample_conditions
3D HN(CO)CAsample_1isotropicsample_conditions
3D HN(CO)CAsample_2isotropicsample_conditions
3D HNCOsample_1isotropicsample_conditions
3D HNCOsample_2isotropicsample_conditions
HCCH-TOCSYsample_1isotropicsample_conditions
HCCH-TOCSYsample_2isotropicsample_conditions
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis_CCPN, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP P40565 P46947
BMRB 19766 25047 25443
PDB
DBJ GAA24120
EMBL CAA86207 CAY80517
GB AAS56407 AEO21093 AHY76002 AJP39470 AJR36763
REF NP_012270
SP P40565
TPG DAA08551
AlphaFold D6VVT5 P40565 D6VTX8

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