BMRB Entry 28110

Name: Backbone and ILV methyl assignments for REC3 domain of SpCas9
Published: 2020-12-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28110

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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 and ILV methyl assignments for REC3 domain of SpCas9

Deposition date:

2020-03-27

Original release date:

2020-12-02

Authors:

De Paula, Viviane; Sgourakis, Nikolaos

Citation:

Citation: Nerli, Santrupti; De Paula, Viviane; McShan, Andrew; Sgourakis, Nikolaos. "Backbone-independent NMR resonance assignments of methyl probes in large proteins" Nat. Commun. 12, 691-691 (2021).
PubMed: 33514730

Assembly members:

Assembly members:
REC3_domain, polymer, 207 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
REC3_domain: KVLPKHSLLYEYFTVYNELT KVKYVTEGMRKPAFLSGEQK KAIVDLLFKTNRKVTVKQLK EDYFKKIECFDSVEISGVED RFNASLGTYHDLLKIIKDKD FLDNEENEDILEDIVLTLTL FEDREMIEERLKTYAHLFDD KVMKQLKRRRYTGWGRLSRK LINGIRDKQSGKTILDFLKS DGFANRNFMQLIHDDSLTFK EDIQKAQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	304
15N chemical shifts	86
1H chemical shifts	341

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	REC3	1

Entities:

Entity 1, REC3 207 residues - Formula weight is not available

1

LYS

VAL

LEU

PRO

LYS

HIS

SER

LEU

TYR

2

GLU

TYR

PHE

THR

VAL

TYR

ASN

GLU

LEU

THR

3

LYS

VAL

LYS

TYR

VAL

THR

GLU

GLY

MET

ARG

4

LYS

PRO

ALA

PHE

LEU

SER

GLY

GLU

GLN

LYS

5

LYS

ALA

ILE

VAL

ASP

LEU

PHE

LYS

THR

6

ASN

ARG

LYS

VAL

THR

VAL

LYS

GLN

LEU

LYS

7

GLU

ASP

TYR

PHE

LYS

ILE

GLU

CYS

PHE

8

ASP

SER

VAL

GLU

ILE

SER

GLY

VAL

GLU

ASP

9

ARG

PHE

ASN

ALA

SER

LEU

GLY

THR

TYR

HIS

10

ASP

LEU

LYS

ILE

LYS

ASP

LYS

ASP

11

PHE

LEU

ASP

ASN

GLU

ASN

GLU

ASP

ILE

12

LEU

GLU

ASP

ILE

VAL

LEU

THR

LEU

THR

LEU

13

PHE

GLU

ASP

ARG

GLU

MET

ILE

GLU

ARG

14

LEU

LYS

THR

TYR

ALA

HIS

LEU

PHE

ASP

15

LYS

VAL

MET

LYS

GLN

LEU

LYS

ARG

16

TYR

THR

GLY

TRP

GLY

ARG

LEU

SER

ARG

LYS

17

LEU

ILE

ASN

GLY

ILE

ARG

ASP

LYS

GLN

SER

18

GLY

LYS

THR

ILE

LEU

ASP

PHE

LEU

LYS

SER

19

ASP

GLY

PHE

ALA

ASN

ARG

ASN

PHE

MET

GLN

20

LEU

ILE

HIS

ASP

SER

LEU

THR

PHE

LYS

21

GLU

ASP

ILE

GLN

LYS

ALA

GLN

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C SOFAST HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N SOFAST HMQC	sample_2	isotropic	sample_conditions_1
3D Hm-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
3D Cm-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
3D Hn-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
3D N-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C SOFAST HMQC	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 28110

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: