BMRB Entry 25339

Name: Backbone amide assignments for human Cyclophilin C with saturating concentrations of the model peptide GSFGPDLRAGD
Published: 2014-12-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25339

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone amide assignments for human Cyclophilin C 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:
CypC, polymer, 190 residues, 20515.3 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-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CypC: GSGAEGFRKRGPSVTAKVFF DVRIGDKDVGRIVIGLFGKV VPKTVENFVALATGEKGYGY KGSKFHRVIKDFMIQGGDIT TGDGTGGVSIYGETFPDENF KLKHYGIGWVSMANAGPDTN GSQFFITLTKPTWLDGKHVV FGKVIDGMTVVHSIELQATD GHDRPLTNCSIINSGKIDVK TPFVVEIADW
GSFGPDLRAGD: GSFGPDLRAGD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
spectral_peak_list
- peak_list_1
- peak_list_1_2

Data type	Count
15N chemical shifts	175
1H chemical shifts	175

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CypC	1
2	GSFGPDLRAGD	2

Entities:

Entity 1, CypC 190 residues - 20515.3 Da.

Residues 25-212 of human Cyclophilin C with two additional N-terminal residues, Gly-Ser-, remaining after removal of affinity tag

1	GLY	SER	GLY	ALA	GLU	GLY	PHE	ARG	LYS	ARG
2	GLY	PRO	SER	VAL	THR	ALA	LYS	VAL	PHE	PHE
3	ASP	VAL	ARG	ILE	GLY	ASP	LYS	ASP	VAL	GLY
4	ARG	ILE	VAL	ILE	GLY	LEU	PHE	GLY	LYS	VAL
5	VAL	PRO	LYS	THR	VAL	GLU	ASN	PHE	VAL	ALA
6	LEU	ALA	THR	GLY	GLU	LYS	GLY	TYR	GLY	TYR
7	LYS	GLY	SER	LYS	PHE	HIS	ARG	VAL	ILE	LYS
8	ASP	PHE	MET	ILE	GLN	GLY	GLY	ASP	ILE	THR
9	THR	GLY	ASP	GLY	THR	GLY	GLY	VAL	SER	ILE
10	TYR	GLY	GLU	THR	PHE	PRO	ASP	GLU	ASN	PHE
11	LYS	LEU	LYS	HIS	TYR	GLY	ILE	GLY	TRP	VAL
12	SER	MET	ALA	ASN	ALA	GLY	PRO	ASP	THR	ASN
13	GLY	SER	GLN	PHE	PHE	ILE	THR	LEU	THR	LYS
14	PRO	THR	TRP	LEU	ASP	GLY	LYS	HIS	VAL	VAL
15	PHE	GLY	LYS	VAL	ILE	ASP	GLY	MET	THR	VAL
16	VAL	HIS	SER	ILE	GLU	LEU	GLN	ALA	THR	ASP
17	GLY	HIS	ASP	ARG	PRO	LEU	THR	ASN	CYS	SER
18	ILE	ILE	ASN	SER	GLY	LYS	ILE	ASP	VAL	LYS
19	THR	PRO	PHE	VAL	VAL	GLU	ILE	ALA	ASP	TRP

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

1

GLY

SER

PHE

GLY

PRO

ASP

LEU

ARG

ALA

GLY

2

ASP

Samples:

CypC-GSFGPDLRAGD: CypC, [U-13C; U-15N; U-2H], 1 mM; GSFGPDLRAGD 6 mM; sodium phosphate 50 mM; EDTA 1 mM; DTT 1 mM; H2O 93%; D2O 7%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	CypC-GSFGPDLRAGD	isotropic	sample_conditions
3D 1H-15N NOESY	CypC-GSFGPDLRAGD	isotropic	sample_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 UnityInova 900 MHz

BMRB	25341
PDB	2ESL
DBJ	BAF83010
GB	AAB31350 AAH02678 ABO43038 ADQ32383 EAW48878
REF	NP_000934 NP_001180902 XP_002815869 XP_003310839 XP_003826742
SP	P45877
AlphaFold	P45877

1	GLY	SER	GLY	ALA	GLU	GLY	PHE	ARG	LYS	ARG
2	GLY	PRO	SER	VAL	THR	ALA	LYS	VAL	PHE	PHE
3	ASP	VAL	ARG	ILE	GLY	ASP	LYS	ASP	VAL	GLY
4	ARG	ILE	VAL	ILE	GLY	LEU	PHE	GLY	LYS	VAL
5	VAL	PRO	LYS	THR	VAL	GLU	ASN	PHE	VAL	ALA
6	LEU	ALA	THR	GLY	GLU	LYS	GLY	TYR	GLY	TYR
7	LYS	GLY	SER	LYS	PHE	HIS	ARG	VAL	ILE	LYS
8	ASP	PHE	MET	ILE	GLN	GLY	GLY	ASP	ILE	THR
9	THR	GLY	ASP	GLY	THR	GLY	GLY	VAL	SER	ILE
10	TYR	GLY	GLU	THR	PHE	PRO	ASP	GLU	ASN	PHE
11	LYS	LEU	LYS	HIS	TYR	GLY	ILE	GLY	TRP	VAL
12	SER	MET	ALA	ASN	ALA	GLY	PRO	ASP	THR	ASN
13	GLY	SER	GLN	PHE	PHE	ILE	THR	LEU	THR	LYS
14	PRO	THR	TRP	LEU	ASP	GLY	LYS	HIS	VAL	VAL
15	PHE	GLY	LYS	VAL	ILE	ASP	GLY	MET	THR	VAL
16	VAL	HIS	SER	ILE	GLU	LEU	GLN	ALA	THR	ASP
17	GLY	HIS	ASP	ARG	PRO	LEU	THR	ASN	CYS	SER
18	ILE	ILE	ASN	SER	GLY	LYS	ILE	ASP	VAL	LYS
19	THR	PRO	PHE	VAL	VAL	GLU	ILE	ALA	ASP	TRP

1	GLY	SER	GLY	ALA	GLU	GLY	PHE	ARG	LYS	ARG
2	GLY	PRO	SER	VAL	THR	ALA	LYS	VAL	PHE	PHE
3	ASP	VAL	ARG	ILE	GLY	ASP	LYS	ASP	VAL	GLY
4	ARG	ILE	VAL	ILE	GLY	LEU	PHE	GLY	LYS	VAL
5	VAL	PRO	LYS	THR	VAL	GLU	ASN	PHE	VAL	ALA
6	LEU	ALA	THR	GLY	GLU	LYS	GLY	TYR	GLY	TYR
7	LYS	GLY	SER	LYS	PHE	HIS	ARG	VAL	ILE	LYS
8	ASP	PHE	MET	ILE	GLN	GLY	GLY	ASP	ILE	THR
9	THR	GLY	ASP	GLY	THR	GLY	GLY	VAL	SER	ILE
10	TYR	GLY	GLU	THR	PHE	PRO	ASP	GLU	ASN	PHE
11	LYS	LEU	LYS	HIS	TYR	GLY	ILE	GLY	TRP	VAL
12	SER	MET	ALA	ASN	ALA	GLY	PRO	ASP	THR	ASN
13	GLY	SER	GLN	PHE	PHE	ILE	THR	LEU	THR	LYS
14	PRO	THR	TRP	LEU	ASP	GLY	LYS	HIS	VAL	VAL
15	PHE	GLY	LYS	VAL	ILE	ASP	GLY	MET	THR	VAL
16	VAL	HIS	SER	ILE	GLU	LEU	GLN	ALA	THR	ASP
17	GLY	HIS	ASP	ARG	PRO	LEU	THR	ASN	CYS	SER
18	ILE	ILE	ASN	SER	GLY	LYS	ILE	ASP	VAL	LYS
19	THR	PRO	PHE	VAL	VAL	GLU	ILE	ALA	ASP	TRP