BMRB Entry 4037

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4037

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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:

Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli

Deposition date:

1997-06-26

Original release date:

1998-07-05

Authors:

Clubb, Robert; Thanabal, Venkataraman; Fejzo, Jasna; Ferguson, Stephen; Zydowsky, Lynne; Baker, C.; Walsh, Christopher; Wagner, Gerhard

Citation:

Citation: Clubb, Robert; Thanabal, Venkataraman; Fejzo, Jasna; Ferguson, Stephen; Zydowsky, Lynne; Baker, C.; Walsh, Christopher; Wagner, Gerhard. "Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli " Biochemistry 32, 6391-6401 (1993).

Assembly members:

Assembly members:
periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, polymer, 167 residues, 18244 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJLEC-2B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase: AAKGDPHVLLTTSAGNIELE LDKQKAPVSVQNFVDYVNSG FYNNTTFHRVIPGFMIQGGG FTEQMQQKKPNPPIKNEADN GLRNTRGTIAMARTADKDSA TSQFFINVADNAFLDHGQRD FGYAVFGKVVKGMDVADKIS QVPTHDVGPYQNVPSKPVVI LSAKVLP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_one

Data type	Count
1H chemical shifts	323
13C chemical shifts	328
15N chemical shifts	153

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	eCyP	1

Entities:

Entity 1, eCyP 167 residues - 18244 Da.

1

ALA

LYS

GLY

ASP

PRO

HIS

VAL

LEU

2

THR

SER

ALA

GLY

ASN

ILE

GLU

LEU

GLU

3

LEU

ASP

LYS

GLN

LYS

ALA

PRO

VAL

SER

VAL

4

GLN

ASN

PHE

VAL

ASP

TYR

VAL

ASN

SER

GLY

5

PHE

TYR

ASN

THR

PHE

HIS

ARG

VAL

6

ILE

PRO

GLY

PHE

MET

ILE

GLN

GLY

7

PHE

THR

GLU

GLN

MET

GLN

LYS

PRO

8

ASN

PRO

ILE

LYS

ASN

GLU

ALA

ASP

ASN

9

GLY

LEU

ARG

ASN

THR

ARG

GLY

THR

ILE

ALA

10

MET

ALA

ARG

THR

ALA

ASP

LYS

ASP

SER

ALA

11

THR

SER

GLN

PHE

ILE

ASN

VAL

ALA

ASP

12

ASN

ALA

PHE

LEU

ASP

HIS

GLY

GLN

ARG

ASP

13

PHE

GLY

TYR

ALA

VAL

PHE

GLY

LYS

VAL

14

LYS

GLY

MET

ASP

VAL

ALA

ASP

LYS

ILE

SER

15

GLN

VAL

PRO

THR

HIS

ASP

VAL

GLY

PRO

TYR

16

GLN

ASN

VAL

PRO

SER

LYS

PRO

VAL

ILE

17

LEU

SER

ALA

LYS

VAL

LEU

PRO

Samples:

sample_one: periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, [U-15N], 0.2 – 2.0 mM; phosphate_buffer 50 mM

sample_two: periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, [U-13C;U-15N], 0.2 – 2.0 mM; phosphate_buffer 50 mM

sample_conditions_one: pH: 6.2; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

Bruker AMX500 500MHz MHz
Bruker AMX600 600MHz MHz

PDB	1CLH 1J2A 1V9T 1VAI
DBJ	BAB37637 BAE77927 BAG79149 BAI27622 BAI32792
EMBL	CAD08141 CAP77816 CAQ33683 CAQ90814 CAR00303
GB	AAA23451 AAA23772 AAA24261 AAA58160 AAC76388
PIR	AI1001
REF	NP_312241 NP_417822 NP_458430 NP_462375 NP_709138
SP	P0AFL3 P0AFL4 P0AFL5 P20753
AlphaFold	P0AFL3 P0AFL4 P0AFL5 P20753