BMRB Entry 25443

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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/BMR25443
MolProbity Validation Chart

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Title:
Snu17p-Pml1p 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.
Pml1p, polymer, 23 residues, 2514.800 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   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
Pml1p: GSKSQYIDIMPDFSPSGLLE LES

Data sets:
Data typeCount
13C chemical shifts572
15N chemical shifts135
1H chemical shifts930

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Snu17p1
2Pml1p2

Entities:

Entity 1, Snu17p 118 residues - 13496.103 Da.

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, Pml1p 23 residues - 2514.800 Da.

1   GLYSERLYSSERGLNTYRILEASPILEMET
2   PROASPPHESERPROSERGLYLEULEUGLU
3   LEUGLUSER

Samples:

Snu17p_13C15N: sodium phosphate 25 mM; sodium chloride 250 mM; Snu17p, [U-13C; U-15N], 0.8 – 1 mM; Pml1p_Fmoc1.2 – 1.5 mM; sodium azide 1 mM; D2O 10%; H2O 90%

Pml1p_13C15N: sodium phosphate 25 mM; sodium chloride 250 mM; Snu17p1 – 1.2 mM; Pml1p, [U-13C; U-15N], 0.8 – 1 mM; sodium azide 1 mM; D2O 10%; H2O 90%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSnu17p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCPml1p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCSnu17p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCPml1p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCSnu17p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCPml1p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCSnu17p_13C15NisotropicStandard_conditions
2D 1H-15N HSQCPml1p_13C15NisotropicStandard_conditions
2D 1H-13C HSQC aliphaticSnu17p_13C15NisotropicStandard_conditions
3D 1H-13C NOESY aromaticSnu17p_13C15NisotropicStandard_conditions
3D 1H-13C NOESY aromaticPml1p_13C15NisotropicStandard_conditions
3D 1H-13C NOESY aliphaticPml1p_13C15NisotropicStandard_conditions
3D HNCOSnu17p_13C15NisotropicStandard_conditions
3D HNCASnu17p_13C15NisotropicStandard_conditions
3D HNCAPml1p_13C15NisotropicStandard_conditions
3D HN(CO)CASnu17p_13C15NisotropicStandard_conditions
3D HN(CO)CAPml1p_13C15NisotropicStandard_conditions
3D HCCH-TOCSYSnu17p_13C15NisotropicStandard_conditions
3D 1H-15N NOESYSnu17p_13C15NisotropicStandard_conditions
3D 1H-15N NOESYPml1p_13C15NisotropicStandard_conditions
HBCBCGCDHDSnu17p_13C15NisotropicStandard_conditions

Software:

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

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - H2O 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:

BMRB 19766 25047 25442
PDB
DBJ GAA24120
EMBL CAA86207 CAY80517
GB AAS56407 AEO21093 AHY76002 AJP39470 AJR36763
REF NP_012270
SP P40565
TPG DAA08551
AlphaFold P40565 Q06901

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