BMRB Entry 17713

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17713
MolProbity Validation Chart

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Title:
Fpr4p PPIase domain
Deposition date:
2011-06-16
Original release date:
2011-09-13
Authors:
Monneau, Yoan; Mackereth, Cameron
Citation:

Citation: Monneau, Yoan; Nelson, Christopher; Mackereth, Cameron. "Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p."  Biomol. NMR Assignments 6, 123-126 (2012).
PubMed: 21898050

Assembly members:

Assembly members:
Fpr4p, polymer, 117 residues, Formula weight is not available

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: pET-His1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fpr4p: GAMAKPKTKLLEGGIIIEDR VTGKGPHAKKGTRVGMRYVG KLKNGKVFDKNTKGKPFVFK LGQGEVIKGWDIGVAGMAVG GERRIVIPAPYAYGKQALPG IPANSELTFDVKLVSMK

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts120
1H chemical shifts859

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fpr4p(280-392)1

Entities:

Entity 1, Fpr4p(280-392) 117 residues - Formula weight is not available

Contains N-terminal Gly-Ala-Met-Ala- residues following cleavage of the His6-tag by TEV protease

1   GLYALAMETALALYSPROLYSTHRLYSLEU
2   LEUGLUGLYGLYILEILEILEGLUASPARG
3   VALTHRGLYLYSGLYPROHISALALYSLYS
4   GLYTHRARGVALGLYMETARGTYRVALGLY
5   LYSLEULYSASNGLYLYSVALPHEASPLYS
6   ASNTHRLYSGLYLYSPROPHEVALPHELYS
7   LEUGLYGLNGLYGLUVALILELYSGLYTRP
8   ASPILEGLYVALALAGLYMETALAVALGLY
9   GLYGLUARGARGILEVALILEPROALAPRO
10   TYRALATYRGLYLYSGLNALALEUPROGLY
11   ILEPROALAASNSERGLULEUTHRPHEASP
12   VALLYSLEUVALSERMETLYS

Samples:

sample_1: Fpr4p, [U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_2: Fpr4p, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_3: Fpr4p, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_4: Fpr4p, [U-10% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 292 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_3isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D HBHDsample_3isotropicsample_conditions_1
2D HBHEsample_3isotropicsample_conditions_1
2D 1H-13C HSQCCTsample_4isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ GAA25303
EMBL CAY81672
GB AAB67528 AHY78796 AJP40573 AJV46477 AJV46929
REF NP_013554
SP Q06205
TPG DAA09749
AlphaFold Q06205

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