BMRB Entry 50408

Name: V98A EcRNHI 15N-1H Backbone Chemical Shifts
Published: 2020-07-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50408

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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:

V98A EcRNHI 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, 155 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLKQVEIFTDGSCLGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQ WIHNWKKRGWKTADKKPAKN VDLWQRLDAALGQHQIKWEW VKGHAGHPENERCDELARAA AMNPTLEDTGYQVEV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	V98A EcRNHI	1

Entities:

Entity 1, V98A EcRNHI 155 residues - Formula weight is not available

1

MET

LEU

LYS

GLN

VAL

GLU

ILE

PHE

THR

ASP

2

GLY

SER

CYS

LEU

GLY

ASN

PRO

GLY

PRO

GLY

3

GLY

TYR

GLY

ALA

ILE

LEU

ARG

TYR

ARG

GLY

4

ARG

GLU

LYS

THR

PHE

SER

ALA

GLY

TYR

THR

5

ARG

THR

ASN

ARG

MET

GLU

LEU

MET

6

ALA

ILE

VAL

ALA

LEU

GLU

ALA

LEU

LYS

7

GLU

HIS

CYS

GLU

VAL

ILE

LEU

SER

THR

ASP

8

SER

GLN

TYR

VAL

ARG

GLN

GLY

ILE

THR

GLN

9

TRP

ILE

HIS

ASN

TRP

LYS

ARG

GLY

TRP

10

LYS

THR

ALA

ASP

LYS

PRO

ALA

LYS

ASN

11

VAL

ASP

LEU

TRP

GLN

ARG

LEU

ASP

ALA

12

LEU

GLY

GLN

HIS

GLN

ILE

LYS

TRP

GLU

TRP

13

VAL

LYS

GLY

HIS

ALA

GLY

HIS

PRO

GLU

ASN

14

GLU

ARG

CYS

ASP

GLU

LEU

ALA

ARG

ALA

15

ALA

MET

ASN

PRO

THR

LEU

GLU

ASP

THR

GLY

16

TYR

GLN

VAL

GLU

VAL

Samples:

sample_1: V98A E. coli 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	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

Software:

NMRPipe - processing

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

NMR spectrometers:

Bruker DRX 600 MHz

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