BMRB Entry 27949

Name: 1H, 13C, 15N Backbone and Sidechain Assignments of HNH from SpyCas9
Published: 2019-09-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27949

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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:

1H, 13C, 15N Backbone and Sidechain Assignments of HNH from SpyCas9

Deposition date:

2019-06-17

Original release date:

2019-09-25

Authors:

Belato, Helen; East, Kyle; Lisi, George

Citation:

Citation: Belato, Helen; East, Kyle; Lisi, George. "1H, 13C, 15N backbone and side chain resonance assignment of the HNH nuclease from Streptococcus pyogenes CRISPR-Cas9" Biomol. NMR Assignments 13, 367-370 (2019).
PubMed: 31377985

Assembly members:

Assembly members:
HNH, polymer, 135 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: bacteria Kingdom: bacteria Genus/species: Streptococcus pyogenes

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HNH: SKNSRERMKRIEEGIKELGS QILKEHPVENTQLQNEKLYL YYLQNGRDMYVDQELDINRL SDYDVDHIVPQSFLKDDSID NKVLTRSDKNRGKSDNVPSE EVVKKMKNYWRQLLNAKLIT QRKFDNLTKAERGGL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	408
15N chemical shifts	107
1H chemical shifts	544

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HNH	1

Entities:

Entity 1, HNH 135 residues - Formula weight is not available

1

SER

LYS

ASN

SER

ARG

GLU

ARG

MET

LYS

ARG

2

ILE

GLU

GLY

ILE

LYS

GLU

LEU

GLY

SER

3

GLN

ILE

LEU

LYS

GLU

HIS

PRO

VAL

GLU

ASN

4

THR

GLN

LEU

GLN

ASN

GLU

LYS

LEU

TYR

LEU

5

TYR

LEU

GLN

ASN

GLY

ARG

ASP

MET

TYR

6

VAL

ASP

GLN

GLU

LEU

ASP

ILE

ASN

ARG

LEU

7

SER

ASP

TYR

ASP

VAL

ASP

HIS

ILE

VAL

PRO

8

GLN

SER

PHE

LEU

LYS

ASP

SER

ILE

ASP

9

ASN

LYS

VAL

LEU

THR

ARG

SER

ASP

LYS

ASN

10

ARG

GLY

LYS

SER

ASP

ASN

VAL

PRO

SER

GLU

11

GLU

VAL

LYS

MET

LYS

ASN

TYR

TRP

12

ARG

GLN

LEU

ASN

ALA

LYS

LEU

ILE

THR

13

GLN

ARG

LYS

PHE

ASP

ASN

LEU

THR

LYS

ALA

14

GLU

ARG

GLY

LEU

Samples:

sample_1: HNH, [U-100% 13C; U-100% 15N], 800 uM; potassium chloride 80 mM; HEPES 20 mM; DTT 2 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Varian INOVA 600 MHz

UNP	Q99ZW2
AlphaFold	Q99ZW2