BMRB Entry 18312

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18312

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Title:
1H, 13C and 15N assignments of Cyclophilin A from Piriformospora indica, a plant root-colonizing basidiomycete fungus
Deposition date:
2012-03-06
Original release date:
2012-06-18
Authors:
Bhatt, Harshesh; Trivedi, Dipesh Kumar; Tuteja, Narendra; Bhavesh, Neel Sarovar
Citation:

Citation: Trivedi, Dipesh Kumar; Bhatt, Harshesh; Pal, Ravi Kant; Tuteja, Renu; Garg, Bharti; Johri, Atul Kumar; Bhavesh, Neel Sarovar; Tuteja, Narendra. "Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants."  Sci. Rep. 3, 3001-3001 (2013).
PubMed: 24141523

Assembly members:

Assembly members:
PiCyp_A, polymer, 167 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Piriformospora indica   Taxonomy ID: 65672   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Piriformospora indica

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PiCyp_A: GSHMSQPNVYFDISIDNQNA GRIVFKLYDDVVPLTAKNFR ELAKNPAGQGYTGSTFHRII PQFMLQGGDFTNHNGTGGRS IYGNKFKDENFQLKHTKPGL LSMANAGPHTNGSQFFITTV VTSWLDGKHVVFGEVVEGMD VVKKVEAVGTQSGKPSKVVK ITASGTV

Data sets:
Data typeCount
13C chemical shifts665
15N chemical shifts171
1H chemical shifts893

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PiCyp_A1

Entities:

Entity 1, PiCyp_A 167 residues - Formula weight is not available

1   GLYSERHISMETSERGLNPROASNVALTYR
2   PHEASPILESERILEASPASNGLNASNALA
3   GLYARGILEVALPHELYSLEUTYRASPASP
4   VALVALPROLEUTHRALALYSASNPHEARG
5   GLULEUALALYSASNPROALAGLYGLNGLY
6   TYRTHRGLYSERTHRPHEHISARGILEILE
7   PROGLNPHEMETLEUGLNGLYGLYASPPHE
8   THRASNHISASNGLYTHRGLYGLYARGSER
9   ILETYRGLYASNLYSPHELYSASPGLUASN
10   PHEGLNLEULYSHISTHRLYSPROGLYLEU
11   LEUSERMETALAASNALAGLYPROHISTHR
12   ASNGLYSERGLNPHEPHEILETHRTHRVAL
13   VALTHRSERTRPLEUASPGLYLYSHISVAL
14   VALPHEGLYGLUVALVALGLUGLYMETASP
15   VALVALLYSLYSVALGLUALAVALGLYTHR
16   GLNSERGLYLYSPROSERLYSVALVALLYS
17   ILETHRALASERGLYTHRVAL

Samples:

sample_1: PiCyp A, [U-99% 13C; U-99% 15N], 1 mM; D2O, [U-2H], 5%; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 75 mM; pH: 6.7; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
EMBL CCA72484
GB ACS71332

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