BMRB Entry 50409

Name: SoRNHI 15N-1H Backbone Chemical Shifts
Published: 2020-07-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50409

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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:

SoRNHI 15N-1H Backbone Chemical Shifts

Deposition date:

2020-07-24

Original release date:

2020-07-30

Authors:

Martin, James; Robustelli, Paul; Palmer, Arthur

Citation:

Citation: Martin, James; Robustelli, Paul; Palmer, Arthur. "Quantifying the Relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues" Biochemistry 59, 3201-3205 (2020).
PubMed: 32813972

Assembly members:

Assembly members:
entity_1, polymer, 158 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Shewanella oneidensis Taxonomy ID: 70863 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella oneidensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-25b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTELKLIHIFTDGSCLGNPG PGGYGIVMNYKGHTKEMSDG FSLTTNNRMELLAPIVALEA LKEPCKIILTSDSQYMRQGI MTWIHGWKKKGWMTSNRTPV KNVDLWKRLDKAAQLHQIDW RWVKGHAGHAENERCDQLAR AAAEANPTQIDTGYQAES

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SoRNHI	1

Entities:

Entity 1, SoRNHI 158 residues - Formula weight is not available

1

MET

THR

GLU

LEU

LYS

LEU

ILE

HIS

ILE

PHE

2

THR

ASP

GLY

SER

CYS

LEU

GLY

ASN

PRO

GLY

3

PRO

GLY

TYR

GLY

ILE

VAL

MET

ASN

TYR

4

LYS

GLY

HIS

THR

LYS

GLU

MET

SER

ASP

GLY

5

PHE

SER

LEU

THR

ASN

ARG

MET

GLU

6

LEU

ALA

PRO

ILE

VAL

ALA

LEU

GLU

ALA

7

LEU

LYS

GLU

PRO

CYS

LYS

ILE

LEU

THR

8

SER

ASP

SER

GLN

TYR

MET

ARG

GLN

GLY

ILE

9

MET

THR

TRP

ILE

HIS

GLY

TRP

LYS

10

GLY

TRP

MET

THR

SER

ASN

ARG

THR

PRO

VAL

11

LYS

ASN

VAL

ASP

LEU

TRP

LYS

ARG

LEU

ASP

12

LYS

ALA

GLN

LEU

HIS

GLN

ILE

ASP

TRP

13

ARG

TRP

VAL

LYS

GLY

HIS

ALA

GLY

HIS

ALA

14

GLU

ASN

GLU

ARG

CYS

ASP

GLN

LEU

ALA

ARG

15

ALA

GLU

ALA

ASN

PRO

THR

GLN

ILE

16

ASP

THR

GLY

TYR

GLN

ALA

GLU

SER

Samples:

sample_1: S. oneidensis Ribonuclease HI, [U-100% 13C; U-100% 15N], 325 uM; deuterated sodium acetate 50 mM; sodium chloride 50 mM; sodium azide 0.02 % (w/v); DTT 1 mM; DSS 3 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 5.5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

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