BMRB Entry 28106

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

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28106

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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 HNH domain of SpCas9

Deposition date:

2020-03-23

Original release date:

2020-12-02

Authors:

McShan, Andrew; De Paula, Viviane; Moschidi, Danai; 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:
HNH_domain, polymer, 133 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):
HNH_domain: NSRERMKRIEEGIKELGSQI LKEHPVENTQLQNEKLYLYY LQNGRDMYVDQELDINRLSD YDVDHIVPQSFLKDDSIDNK VLTRSDKNRGKSDNVPSEEV VKKMKNYWRQLLNAKLITQR KFDNLTKAERGGL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	329
15N chemical shifts	92
1H chemical shifts	251

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HNH domain	1

Entities:

Entity 1, HNH domain 133 residues - Formula weight is not available

1

ASN

SER

ARG

GLU

ARG

MET

LYS

ARG

ILE

GLU

2

GLU

GLY

ILE

LYS

GLU

LEU

GLY

SER

GLN

ILE

3

LEU

LYS

GLU

HIS

PRO

VAL

GLU

ASN

THR

GLN

4

LEU

GLN

ASN

GLU

LYS

LEU

TYR

LEU

TYR

5

LEU

GLN

ASN

GLY

ARG

ASP

MET

TYR

VAL

ASP

6

GLN

GLU

LEU

ASP

ILE

ASN

ARG

LEU

SER

ASP

7

TYR

ASP

VAL

ASP

HIS

ILE

VAL

PRO

GLN

SER

8

PHE

LEU

LYS

ASP

SER

ILE

ASP

ASN

LYS

9

VAL

LEU

THR

ARG

SER

ASP

LYS

ASN

ARG

GLY

10

LYS

SER

ASP

ASN

VAL

PRO

SER

GLU

VAL

11

VAL

LYS

MET

LYS

ASN

TYR

TRP

ARG

GLN

12

LEU

ASN

ALA

LYS

LEU

ILE

THR

GLN

ARG

13

LYS

PHE

ASP

ASN

LEU

THR

LYS

ALA

GLU

ARG

14

GLY

LEU

Samples:

sample_1: HNH domain, [U-15N; U-13C; ILV], 1 mM; Hepes 20 mM; NaCl 200 mM

sample_2: HNH domain, [U-15N; U-2H; U-13C-all methyl carbons], 0.3 mM; Hepes 20 mM; NaCl 200 mM

sample_3: HNH domain, [U-15N; U-2H; U-13C; IL(CD2)V(CG2)], 0.2 mM; Hepes 20 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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
3D Hm-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
3D Cm-CmHm SOFAST NOESY HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N SOFAST HMQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C SOFAST HMQC	sample_3	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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