BMRB Entry 50389

Name: Backbone Assignments of the Rec3 domain of CRISPR-Cas9 for S. pyogenes
Published: 2020-09-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50389

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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 Assignments of the Rec3 domain of CRISPR-Cas9 for S. pyogenes

Deposition date:

2020-07-13

Original release date:

2020-09-17

Authors:

Skeens, Erin; East, Kyle; Lisi, George

Citation:

Citation: Skeens, Erin; East, Kyle; Lisi, George. "1H, 13C, 15N backbone resonance assignment of the recognition lobe subdomain 3 (Rec3) from Streptococcus pyogenes CRISPR-Cas9" Biomol. NMR Assignments 15, 25-28 (2021).
PubMed: 32935194

Assembly members:

Assembly members:
entity_1, polymer, 218 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNFDKNLPNEKVLPKHSLLY EYFTVYNELTKVKYVTEGMR KPAFLSGEQKKAIVDLLFKT NRKVTVKQLKEDYFKKIECF DSVEISGVEDRFNASLGTYH DLLKIIKDKDFLDNEENEDI LEDIVLTLTLFEDREMIEER LKTYAHLFDDKVMKQLKRRR YTGWGRLSRKLINGIRDKQS GKTILDFLKSDGFANRNFMQ LIHDDSLTFKEDIQKAQV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	583
15N chemical shifts	200
1H chemical shifts	200

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spyRec3	1

Entities:

Entity 1, spyRec3 218 residues - Formula weight is not available

1

SER

ASN

PHE

ASP

LYS

ASN

LEU

PRO

ASN

GLU

2

LYS

VAL

LEU

PRO

LYS

HIS

SER

LEU

TYR

3

GLU

TYR

PHE

THR

VAL

TYR

ASN

GLU

LEU

THR

4

LYS

VAL

LYS

TYR

VAL

THR

GLU

GLY

MET

ARG

5

LYS

PRO

ALA

PHE

LEU

SER

GLY

GLU

GLN

LYS

6

LYS

ALA

ILE

VAL

ASP

LEU

PHE

LYS

THR

7

ASN

ARG

LYS

VAL

THR

VAL

LYS

GLN

LEU

LYS

8

GLU

ASP

TYR

PHE

LYS

ILE

GLU

CYS

PHE

9

ASP

SER

VAL

GLU

ILE

SER

GLY

VAL

GLU

ASP

10

ARG

PHE

ASN

ALA

SER

LEU

GLY

THR

TYR

HIS

11

ASP

LEU

LYS

ILE

LYS

ASP

LYS

ASP

12

PHE

LEU

ASP

ASN

GLU

ASN

GLU

ASP

ILE

13

LEU

GLU

ASP

ILE

VAL

LEU

THR

LEU

THR

LEU

14

PHE

GLU

ASP

ARG

GLU

MET

ILE

GLU

ARG

15

LEU

LYS

THR

TYR

ALA

HIS

LEU

PHE

ASP

16

LYS

VAL

MET

LYS

GLN

LEU

LYS

ARG

17

TYR

THR

GLY

TRP

GLY

ARG

LEU

SER

ARG

LYS

18

LEU

ILE

ASN

GLY

ILE

ARG

ASP

LYS

GLN

SER

19

GLY

LYS

THR

ILE

LEU

ASP

PHE

LEU

LYS

SER

20

ASP

GLY

PHE

ALA

ASN

ARG

ASN

PHE

MET

GLN

21

LEU

ILE

HIS

ASP

SER

LEU

THR

PHE

LYS

22

GLU

ASP

ILE

GLN

LYS

ALA

GLN

VAL

Samples:

sample_1: spyRec3, [U-13C; U-15N; U-2H], 1.2 mM; potassium chloride 80 mM; HEPES 20 mM

sample_conditions_1: ionic strength: 80 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
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
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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