BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27265

Title: Backbone and sidechain assignments of human Cyclophilin A

Deposition date: 2017-09-26 Original release date: 2017-10-25

Authors: Aggarwal, Priyanka

Citation: Aggarwal, Priyanka; Bhavesh, Neel Sarovar. "1H, 13C, 15N chemical shift assignments for human Cyclophilin A"  The BMRB entry is the only known published source for the data..

Assembly members:
cyclophilinA, polymer, 165 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
cyclophilinA: MVNPTVFFDIAVDGEPLGRV SFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGF MCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSM ANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVE AMERFGSRNGKTSKKITIAD CGQLE

Data sets:
Data typeCount
13C chemical shifts677
15N chemical shifts167
1H chemical shifts1039

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human Cyclophilin A1

Entities:

Entity 1, human Cyclophilin A 165 residues - Formula weight is not available

1   METVALASNPROTHRVALPHEPHEASPILE
2   ALAVALASPGLYGLUPROLEUGLYARGVAL
3   SERPHEGLULEUPHEALAASPLYSVALPRO
4   LYSTHRALAGLUASNPHEARGALALEUSER
5   THRGLYGLULYSGLYPHEGLYTYRLYSGLY
6   SERCYSPHEHISARGILEILEPROGLYPHE
7   METCYSGLNGLYGLYASPPHETHRARGHIS
8   ASNGLYTHRGLYGLYLYSSERILETYRGLY
9   GLULYSPHEGLUASPGLUASNPHEILELEU
10   LYSHISTHRGLYPROGLYILELEUSERMET
11   ALAASNALAGLYPROASNTHRASNGLYSER
12   GLNPHEPHEILECYSTHRALALYSTHRGLU
13   TRPLEUASPGLYLYSHISVALVALPHEGLY
14   LYSVALLYSGLUGLYMETASNILEVALGLU
15   ALAMETGLUARGPHEGLYSERARGASNGLY
16   LYSTHRSERLYSLYSILETHRILEALAASP
17   CYSGLYGLNLEUGLU

Samples:

sample_1: cyclophilinA, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate buffer 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; 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 H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts