BMRB Entry 27265

Name: Backbone and sidechain assignments of human Cyclophilin A
Published: 2017-10-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27265

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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 and sidechain assignments of human Cyclophilin A

Deposition date:

2017-09-26

Original release date:

2017-10-25

Authors:

Aggarwal, Priyanka

Citation:

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:

Assembly members:
cyclophilinA, polymer, 165 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: pETM11

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	677
15N chemical shifts	167
1H chemical shifts	1039

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human Cyclophilin A	1

Entities:

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

1

MET

VAL

ASN

PRO

THR

VAL

PHE

ASP

ILE

2

ALA

VAL

ASP

GLY

GLU

PRO

LEU

GLY

ARG

VAL

3

SER

PHE

GLU

LEU

PHE

ALA

ASP

LYS

VAL

PRO

4

LYS

THR

ALA

GLU

ASN

PHE

ARG

ALA

LEU

SER

5

THR

GLY

GLU

LYS

GLY

PHE

GLY

TYR

LYS

GLY

6

SER

CYS

PHE

HIS

ARG

ILE

PRO

GLY

PHE

7

MET

CYS

GLN

GLY

ASP

PHE

THR

ARG

HIS

8

ASN

GLY

THR

GLY

LYS

SER

ILE

TYR

GLY

9

GLU

LYS

PHE

GLU

ASP

GLU

ASN

PHE

ILE

LEU

10

LYS

HIS

THR

GLY

PRO

GLY

ILE

LEU

SER

MET

11

ALA

ASN

ALA

GLY

PRO

ASN

THR

ASN

GLY

SER

12

GLN

PHE

ILE

CYS

THR

ALA

LYS

THR

GLU

13

TRP

LEU

ASP

GLY

LYS

HIS

VAL

PHE

GLY

14

LYS

VAL

LYS

GLU

GLY

MET

ASN

ILE

VAL

GLU

15

ALA

MET

GLU

ARG

PHE

GLY

SER

ARG

ASN

GLY

16

LYS

THR

SER

LYS

ILE

THR

ILE

ALA

ASP

17

CYS

GLY

GLN

LEU

GLU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks