BMRB Entry 51211

Name: 13C/15N/1H chemical shift assignments for Human Cytomegalovirus Protease delta221
Published: 2022-04-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51211

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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:

13C/15N/1H chemical shift assignments for Human Cytomegalovirus Protease delta221

Deposition date:

2021-12-03

Original release date:

2022-04-07

Authors:

Lee, Gregory; Craik, Charles

Citation:

Citation: Hulce, Kaitlin; Jaishankar, Priyadarshini; Lee, Gregory; Bohn, Markus-Frederik; Connelly, Emily; Wucherer, Kristin; Volk, Regan; Chuo, Shih-Wei; Arkin, Michelle; Renslo, Adam; Craik, Charles. "Inhibiting a dynamic viral protease by targeting a non-catalytic cysteine" Cell Chem. Biol. 29, 785-798 (2022).
PubMed: 35364007

Assembly members:

Assembly members:
entity_1, polymer, 228 residues, 24033.9 Da.

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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHMTMDEQQSQAVAP VYVGGFLARYDQSPDEAELL LPRDVVEHWLHAQGQGQPSL SVALPLNINHDDTAVVGHVA AMQSVRDGLFCLGCVTSPRF LEIVRRASEKSELVSRGPVS PLQPDKVVEFLSGSYAGLSL SSRRCDDVEVATSLSGSETT PFKHVALCSVGRRRGTLAVY GRDPEWVTQRFPDLTAADRD GLRAQWQRCGSTAVDVSGDP FRSDSYGL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	695
15N chemical shifts	203
1H chemical shifts	592

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HCMV Pr delta221	1

Entities:

Entity 1, HCMV Pr delta221 228 residues - 24033.9 Da.

Contains a non-native N-terminal Met+His6-tag (residues -7 to -1). Residue numbering begins at Met1. This is a C-terminal truncated construct that ends with L221.

1

MET

HIS

MET

THR

MET

2

ASP

GLU

GLN

SER

GLN

ALA

VAL

ALA

PRO

3

VAL

TYR

VAL

GLY

PHE

LEU

ALA

ARG

TYR

4

ASP

GLN

SER

PRO

ASP

GLU

ALA

GLU

LEU

5

LEU

PRO

ARG

ASP

VAL

GLU

HIS

TRP

LEU

6

HIS

ALA

GLN

GLY

GLN

GLY

GLN

PRO

SER

LEU

7

SER

VAL

ALA

LEU

PRO

LEU

ASN

ILE

ASN

HIS

8

ASP

THR

ALA

VAL

GLY

HIS

VAL

ALA

9

ALA

MET

GLN

SER

VAL

ARG

ASP

GLY

LEU

PHE

10

CYS

LEU

GLY

CYS

VAL

THR

SER

PRO

ARG

PHE

11

LEU

GLU

ILE

VAL

ARG

ALA

SER

GLU

LYS

12

SER

GLU

LEU

VAL

SER

ARG

GLY

PRO

VAL

SER

13

PRO

LEU

GLN

PRO

ASP

LYS

VAL

GLU

PHE

14

LEU

SER

GLY

SER

TYR

ALA

GLY

LEU

SER

LEU

15

SER

ARG

CYS

ASP

VAL

GLU

VAL

16

ALA

THR

SER

LEU

SER

GLY

SER

GLU

THR

17

PRO

PHE

LYS

HIS

VAL

ALA

LEU

CYS

SER

VAL

18

GLY

ARG

GLY

THR

LEU

ALA

VAL

TYR

19

GLY

ARG

ASP

PRO

GLU

TRP

VAL

THR

GLN

ARG

20

PHE

PRO

ASP

LEU

THR

ALA

ASP

ARG

ASP

21

GLY

LEU

ARG

ALA

GLN

TRP

GLN

ARG

CYS

GLY

22

SER

THR

ALA

VAL

ASP

VAL

SER

GLY

ASP

PRO

23

PHE

ARG

SER

ASP

SER

TYR

GLY

LEU

Samples:

sample_1: HCMV Protease delta 221, [U-13C; U-15N; U-2H], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM

sample_2: HCMV Protease delta 221, [U-100% 13C; U-100% 15N], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM

sample_3: HCMV Protease delta 221, [U-100% 15N], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3pl10 v1.3pl10 - collection

TOPSPIN v2.1pl8 v2.1pl8 - collection

NMRPipe v8.7 v8.7 - processing

SPARKY v.3.114 v3.114 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance/DRX 500 MHz
Bruker Avance 800 MHz