BMRB Entry 19868

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for p15(PAF) in complex with PCNA
Deposition date:
2014-03-19
Original release date:
2024-09-18
Authors:
Blanco, Francisco J; Ibanez de Opakua, Alain; De Biasio, Alfredo
Citation:

Citation: De Biasio, Alfredo; Ibanez de Opakua, Alain; Mortuza, Gulnehar B; Molina, Rafael; Cordeiro, Tiago N; Castillo, Francisco; Villate, Maider; Merino, Nekane; Delgado, Sandra; Gil, David; Diercks, Tammo; Luque, Irene; Bernado, Pau; Montoya, Guillermo; Blanco, Francisco J. "Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair"  Nat. Commun. 6, 6439-6439 (2015).
PubMed: 25762514

Assembly members:

Assembly members:
p15(PAF), polymer, 111 residues, Formula weight is not available
PCNA_trimer, polymer, 264 residues, Formula weight is not available

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   Vector: pet11d

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts78
1H chemical shifts78

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p15(PAF)1
2PCNA trimer, 12
3PCNA trimer, 22
4PCNA trimer, 32

Entities:

Entity 1, p15(PAF) 111 residues - Formula weight is not available

1   METVALARGTHRLYSALAASPSERVALPRO
2   GLYTHRTYRARGLYSVALVALALAALAARG
3   ALAPROARGLYSVALLEUGLYSERSERTHR
4   SERALATHRASNSERTHRSERVALSERSER
5   ARGLYSALAGLUASNLYSTYRALAGLYGLY
6   ASNPROVALCYSVALARGPROTHRPROLYS
7   TRPGLNLYSGLYILEGLYGLUPHEPHEARG
8   LEUSERPROLYSASPSERGLULYSGLUASN
9   GLNILEPROGLUGLUALAGLYSERSERGLY
10   LEUGLYLYSALALYSARGLYSALACYSPRO
11   LEUGLNPROASPHISTHRASNASPGLULYS
12   GLU

Entity 2, PCNA trimer, 1 264 residues - Formula weight is not available

1   GLYPROHISMETPHEGLUALAARGLEUVAL
2   GLNGLYSERILELEULYSLYSVALLEUGLU
3   ALALEULYSASPLEUILEASNGLUALACYS
4   TRPASPILESERSERSERGLYVALASNLEU
5   GLNSERMETASPSERSERHISVALSERLEU
6   VALGLNLEUTHRLEUARGSERGLUGLYPHE
7   ASPTHRTYRARGCYSASPARGASNLEUALA
8   METGLYVALASNLEUTHRSERMETSERLYS
9   ILELEULYSCYSALAGLYASNGLUASPILE
10   ILETHRLEUARGALAGLUASPASNALAASP
11   THRLEUALALEUVALPHEGLUALAPROASN
12   GLNGLULYSVALSERASPTYRGLUMETLYS
13   LEUMETASPLEUASPVALGLUGLNLEUGLY
14   ILEPROGLUGLNGLUTYRSERCYSVALVAL
15   LYSMETPROSERGLYGLUPHEALAARGILE
16   CYSARGASPLEUSERHISILEGLYASPALA
17   VALVALILESERCYSALALYSASPGLYVAL
18   LYSPHESERALASERGLYGLULEUGLYASN
19   GLYASNILELYSLEUSERGLNTHRSERASN
20   VALASPLYSGLUGLUGLUALAVALTHRILE
21   GLUMETASNGLUPROVALGLNLEUTHRPHE
22   ALALEUARGTYRLEUASNPHEPHETHRLYS
23   ALATHRPROLEUSERSERTHRVALTHRLEU
24   SERMETSERALAASPVALPROLEUVALVAL
25   GLUTYRLYSILEALAASPMETGLYHISLEU
26   LYSTYRTYRLEUALAPROLYSILEGLUASP
27   GLUGLUGLYSER

Samples:

sample_1: p15(PAF), [U-100% 13C; U-100% 15N], 400 uM; PCNA trimer, [U-100% 2H], 1.1 mM; DTT 2 mM; sodium azide 0.01 % w/v; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM

sample_2: p15(PAF), [U-100% 13C; U-100% 15N], 150 uM; PCNA trimer, [U-100% 2H], 750 mM; DTT 2 mM; sodium azide 0.01 % w/v; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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