BMRB Entry 50787

Name: Backbone chemical shift assignments of saccharomyces cerevisiae Ess1 Prolyl-isomerase C120S
Published: 2021-03-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50787

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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 chemical shift assignments of saccharomyces cerevisiae Ess1 Prolyl-isomerase C120S

Deposition date:

2021-02-23

Original release date:

2021-03-23

Authors:

Zheng, Tongyin; Castaneda, Carlos

Citation:

Citation: Namitz, Kevin; Zheng, Tongyin; Canning, Ashley; Alicea-Velazquez, Nilda; Castaneda, Carlos; Cosgrove, Michael; Hanes, Steven. "Structural basis for Ess1-dependent isomerization of the RNAPII CTD via a bivalent anchoring mechanism" Commun. Biol. 4, 398-398 (2021).
PubMed: 33767358

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMDMPSDVASSTGLPTPWT VRYSKSKKREYFFNPETKHS QWEEPEGTNKDQLHKHLRDH PVRVRCLHILIKHKDSRRPA SHRSENITISKQDATDELKT LITRLDDDSKTNSFEALAKE RSDSSSYKRGGDLGWFGRGE MQPSFEDAAFQLKVGEVSDI VESGSGVHVIKRVG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	453
15N chemical shifts	152
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ess1	1

Entities:

Entity 1, Ess1 174 residues - Formula weight is not available

1

GLY

ALA

MET

ASP

MET

PRO

SER

ASP

VAL

ALA

2

SER

THR

GLY

LEU

PRO

THR

PRO

TRP

THR

3

VAL

ARG

TYR

SER

LYS

SER

LYS

ARG

GLU

4

TYR

PHE

ASN

PRO

GLU

THR

LYS

HIS

SER

5

GLN

TRP

GLU

PRO

GLU

GLY

THR

ASN

LYS

6

ASP

GLN

LEU

HIS

LYS

HIS

LEU

ARG

ASP

HIS

7

PRO

VAL

ARG

VAL

ARG

CYS

LEU

HIS

ILE

LEU

8

ILE

LYS

HIS

LYS

ASP

SER

ARG

PRO

ALA

9

SER

HIS

ARG

SER

GLU

ASN

ILE

THR

ILE

SER

10

LYS

GLN

ASP

ALA

THR

ASP

GLU

LEU

LYS

THR

11

LEU

ILE

THR

ARG

LEU

ASP

SER

LYS

12

THR

ASN

SER

PHE

GLU

ALA

LEU

ALA

LYS

GLU

13

ARG

SER

ASP

SER

TYR

LYS

ARG

GLY

14

GLY

ASP

LEU

GLY

TRP

PHE

GLY

ARG

GLY

GLU

15

MET

GLN

PRO

SER

PHE

GLU

ASP

ALA

PHE

16

GLN

LEU

LYS

VAL

GLY

GLU

VAL

SER

ASP

ILE

17

VAL

GLU

SER

GLY

SER

GLY

VAL

HIS

VAL

ILE

18

LYS

ARG

VAL

GLY

Samples:

sample_1: Peptidyl-prolyl cis-trans isomerase Ess1 C120S, [U-95% 13C; U-95% 15N], 500 uM; Na Phosphate 20 mM; NaCl 150 mM; TCEP 3 mM; NaN3 0.02%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS v2.4.2 - chemical shift assignment, peak picking

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

UNP	P22696
AlphaFold	D6VWJ3