BMRB Entry 25338

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25338

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Title:
Backbone assignments for human Cyclophilin B with saturating concentrations of the model peptide GSFGPDLRAGD
Deposition date:
2014-11-13
Original release date:
2014-12-16
Authors:
Holliday, Michael; Camilloni, Carlo; Armstrong, Geoffrey; Isern, Nancy; Zhang, Fengli; Vendruscolo, Michele; Eisenmesser, Elan
Citation:

Citation: Holliday, Michael; Camilloni, Carlo; Armstrong, Geoffrey; Isern, Nancy; Zhang, Fengli; Vendruscolo, Michele; Eisenmesser, Elan. "Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures"  Biochemistry 54, 3207-3217 (2015).
PubMed: 25923019

Assembly members:

Assembly members:
CypB, polymer, 208 residues, 22752.3662 Da.
GSFGPDLRAGD, polymer, 11 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: pET-17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CypB: MKVLLAAALIAGSVFFLLLP GPSAADEKKKGPKVTVKVYF DLRIGDEDVGRVIFGLFGKT VPKTVDNFVALATGEKGFGY KNSKFHRVIKDFMIQGGDFT RGDGTGGKSIYGERFPDENF KLKHYGPGWVSMANAGKDTN GSQFFITTVKTAWLDGKHVV FGKVLEGMEVVRKVESTKTD SRDKPLKDVIIADCGKIEVE KPFAIAKE
GSFGPDLRAGD: GSFGPDLRAGD

Data sets:
Data typeCount
13C chemical shifts310
15N chemical shifts164
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CypB1
2GSFGPDLRAGD2

Entities:

Entity 1, CypB 208 residues - 22752.3662 Da.

Full length human Cyclophilin B

1   METLYSVALLEULEUALAALAALALEUILE
2   ALAGLYSERVALPHEPHELEULEULEUPRO
3   GLYPROSERALAALAASPGLULYSLYSLYS
4   GLYPROLYSVALTHRVALLYSVALTYRPHE
5   ASPLEUARGILEGLYASPGLUASPVALGLY
6   ARGVALILEPHEGLYLEUPHEGLYLYSTHR
7   VALPROLYSTHRVALASPASNPHEVALALA
8   LEUALATHRGLYGLULYSGLYPHEGLYTYR
9   LYSASNSERLYSPHEHISARGVALILELYS
10   ASPPHEMETILEGLNGLYGLYASPPHETHR
11   ARGGLYASPGLYTHRGLYGLYLYSSERILE
12   TYRGLYGLUARGPHEPROASPGLUASNPHE
13   LYSLEULYSHISTYRGLYPROGLYTRPVAL
14   SERMETALAASNALAGLYLYSASPTHRASN
15   GLYSERGLNPHEPHEILETHRTHRVALLYS
16   THRALATRPLEUASPGLYLYSHISVALVAL
17   PHEGLYLYSVALLEUGLUGLYMETGLUVAL
18   VALARGLYSVALGLUSERTHRLYSTHRASP
19   SERARGASPLYSPROLEULYSASPVALILE
20   ILEALAASPCYSGLYLYSILEGLUVALGLU
21   LYSPROPHEALAILEALALYSGLU

Entity 2, GSFGPDLRAGD 11 residues - Formula weight is not available

1   GLYSERPHEGLYPROASPLEUARGALAGLY
2   ASP

Samples:

CypB-GSFGPDLRAGD: CypB, [U-100% 13C; U-100% 15N], 1 mM; GSFGPDLRAGD 6 mM; sodium phosphate 50 mM; EDTA 1 mM; DTT 1 mM; H20 93%; D2O 7%

sample_conditions: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBCypB-GSFGPDLRAGDisotropicsample_conditions
3D CBCA(CO)NHCypB-GSFGPDLRAGDisotropicsample_conditions
2D 1H-15N HSQC/HMQCCypB-GSFGPDLRAGDisotropicsample_conditions

Software:

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, peak picking

nmrPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Varian - Spectrum processing, collection

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

BMRB 15505
PDB
DBJ BAF83838 BAI46658
EMBL CAG33110
GB AAA35733 AAA36601 AAA52150 AAH01125 AAH08848
REF NP_000933 NP_001253241 XP_002753266 XP_002825583 XP_003480239
SP P23284
AlphaFold P23284

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