BMRB Entry 4765

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4765

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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 1H,13C, and 15N resonance assignments of an 18.2kDa protein, E.Coli peptidyl-prolyl cis-trans isomerase b (EPPIb)

Deposition date:

2000-06-19

Original release date:

2000-09-27

Authors:

Kainosho, Masatsune

Citation:

Citation: Kariya, Eri; Ohki, Shin-ya; Hayano, Toshiya; Kainosho, Masatsune. "Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of an 18.2 kDa protein, E. coli peptidyl-prolyl cis-trans isomerase b (EPPIb)" J. Biomol. NMR 18, 75-76 (2000).

Assembly members:

Assembly members:
E.Coli peptidyl-prolyl cis-trans isomerase b, polymer, 164 residues, Formula weight is not available

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: cell free synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E.Coli peptidyl-prolyl cis-trans isomerase b: MVTFHTNHGDIVIKTFDDKA PETVKNFLDYCREGFYNNTI FHRVINGFMIQGGGFEPGMK QKATKEPIKNEANNGLKNTR GTLAMARTQAPHSATAQFFI NVVDNDFLNFSGESLQGWGY CVFAEVVDGMDVVDKIKGVA TGRSGMHQDVPKEDVIIESV TVSE

Data sets:

assigned_chemical_shifts
- shift_set_1
- shift_set_2

Data type	Count
1H chemical shifts	160
13C chemical shifts	474
15N chemical shifts	159

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EPPIb	1

Entities:

Entity 1, EPPIb 164 residues - Formula weight is not available

1

MET

VAL

THR

PHE

HIS

THR

ASN

HIS

GLY

ASP

2

ILE

VAL

ILE

LYS

THR

PHE

ASP

LYS

ALA

3

PRO

GLU

THR

VAL

LYS

ASN

PHE

LEU

ASP

TYR

4

CYS

ARG

GLU

GLY

PHE

TYR

ASN

THR

ILE

5

PHE

HIS

ARG

VAL

ILE

ASN

GLY

PHE

MET

ILE

6

GLN

GLY

PHE

GLU

PRO

GLY

MET

LYS

7

GLN

LYS

ALA

THR

LYS

GLU

PRO

ILE

LYS

ASN

8

GLU

ALA

ASN

GLY

LEU

LYS

ASN

THR

ARG

9

GLY

THR

LEU

ALA

MET

ALA

ARG

THR

GLN

ALA

10

PRO

HIS

SER

ALA

THR

ALA

GLN

PHE

ILE

11

ASN

VAL

ASP

ASN

ASP

PHE

LEU

ASN

PHE

12

SER

GLY

GLU

SER

LEU

GLN

GLY

TRP

GLY

TYR

13

CYS

VAL

PHE

ALA

GLU

VAL

ASP

GLY

MET

14

ASP

VAL

ASP

LYS

ILE

LYS

GLY

VAL

ALA

15

THR

GLY

ARG

SER

GLY

MET

HIS

GLN

ASP

VAL

16

PRO

LYS

GLU

ASP

VAL

ILE

GLU

SER

VAL

17

THR

VAL

SER

GLU

Samples:

sample_1: E.Coli peptidyl-prolyl cis-trans isomerase b 1.6 mM

sample_2: E.Coli peptidyl-prolyl cis-trans isomerase b, [U-15N], 1.6 mM

sample_3: E.Coli peptidyl-prolyl cis-trans isomerase b, [U-13C; U-15N], 1.6 mM

sample_4: E.Coli peptidyl-prolyl cis-trans isomerase b 1.6 mM

Ex-cond_1: pH: 6.2; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

Bruker DMX 500.13 MHz
Bruker DRX 600.13 MHz
Bruker DRX 800.13 MHz

PDB	1LOP 2NUL 2RS4
DBJ	BAB34010 BAE76302 BAG76074 BAI23892 BAI29364
EMBL	CAD05020 CAP75055 CAQ30997 CAQ88114 CAQ97399
GB	AAA23453 AAC73627 AAG54882 AAL19490 AAN42110
PIR	AB0569
REF	NP_286274 NP_308614 NP_415058 NP_455128 NP_459531
SP	P23869
AlphaFold	P23869