BMRB Entry 34912

Name: NMR structure of the Staphylococcus aureus bacteriophage phi812 hub protein - lytic cleaver (CHAP) domain
Published: 2025-04-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34912

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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:

NMR structure of the Staphylococcus aureus bacteriophage phi812 hub protein - lytic cleaver (CHAP) domain

Deposition date:

2024-03-27

Original release date:

2025-04-07

Authors:

Binovsky, J.; Tripsianes, K.; Novacek, J.; Benesik, M.; Plevka, P.

Citation:

Citation: Binovsky, J.; Tripsianes, K.; Novacek, J.; Benesik, M.; Plevka, P.. "Cell attachment and tail contraction of S. aureus phage phi812" .

Assembly members:

Assembly members:
entity_1, polymer, 176 residues, 18927.041 Da.

Natural source:

Natural source: Common Name: Staphylococcus phage 812 Taxonomy ID: 307898 Superkingdom: Viruses Kingdom: not available Genus/species: Kayvirus Staphylococcus phage 812

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEQSSGDKDGGSDSGGAQDG GSLDSLKKYNGKLPKHDPSF VQPGNRHYKYQCTWYAYNRR GQLGIPVPLWGDAADWIGGA KGAGYGVGRTPKQGACVIWQ RGVQGGSPQYGHVAFVEKVL DGGKKIFISEHNYATPNGYG TRTIDMSSAIGKNAQFIYDK KKNSSSVDKLAAALEH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	516
15N chemical shifts	170
1H chemical shifts	1062

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 176 residues - 18927.041 Da.

1

MET

GLU

GLN

SER

GLY

ASP

LYS

ASP

GLY

2

GLY

SER

ASP

SER

GLY

ALA

GLN

ASP

GLY

3

GLY

SER

LEU

ASP

SER

LEU

LYS

TYR

ASN

4

GLY

LYS

LEU

PRO

LYS

HIS

ASP

PRO

SER

PHE

5

VAL

GLN

PRO

GLY

ASN

ARG

HIS

TYR

LYS

TYR

6

GLN

CYS

THR

TRP

TYR

ALA

TYR

ASN

ARG

7

GLY

GLN

LEU

GLY

ILE

PRO

VAL

PRO

LEU

TRP

8

GLY

ASP

ALA

ASP

TRP

ILE

GLY

ALA

9

LYS

GLY

ALA

GLY

TYR

GLY

VAL

GLY

ARG

THR

10

PRO

LYS

GLN

GLY

ALA

CYS

VAL

ILE

TRP

GLN

11

ARG

GLY

VAL

GLN

GLY

SER

PRO

GLN

TYR

12

GLY

HIS

VAL

ALA

PHE

VAL

GLU

LYS

VAL

LEU

13

ASP

GLY

LYS

ILE

PHE

ILE

SER

GLU

14

HIS

ASN

TYR

ALA

THR

PRO

ASN

GLY

TYR

GLY

15

THR

ARG

THR

ILE

ASP

MET

SER

ALA

ILE

16

GLY

LYS

ASN

ALA

GLN

PHE

ILE

TYR

ASP

LYS

17

LYS

ASN

SER

VAL

ASP

LYS

LEU

18

ALA

LEU

GLU

HIS

Samples:

sample_1: CHAP domain, [U-99% 13C; U-99% 15N], 1.8 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
4D HC(CC TOCSY(CO))NH	sample_1	isotropic	sample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE NEO 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks