BMRB Entry 30925

Name: NMR Solution structure of Se0862
Published: 2021-07-12

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PDB ID: 7n82
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30925
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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:

NMR Solution structure of Se0862

Deposition date:

2021-06-11

Original release date:

2021-07-12

Authors:

Zhang, N.; LiWang, A.

Citation:

Citation: Huang, Yuanpeng Janet; Zhang, Ning; Bersch, Beate; Fidelis, Krzysztof; Inouye, Masayori; Ishida, Yojiro; Kryshtafovych, Andriy; Kobayashi, Naohiro; Kuroda, Yutaka; Liu, Gaohua; LiWang, Andy; Swapna, G; Wu, Nan; Yamazaki, Toshio; Montelione, Gaetano. "Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2" Proteins 89, 1959-1976 (2021).
PubMed: 34559429

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14425.336 Da.

Natural source:

Natural source: Common Name: Synechococcus elongatus Taxonomy ID: 32046 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechococcus elongatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MRIDELVPADPRAVSLYTPY YSQANRRRYLPYALSLYQGS SIEGSRAVEGGAPISFVATW TVTPLPADMTRCHLQFNNDA ELTYEILLPNHEFLEYLIDM LMGYQRMQKTDFPGAFYRRL LGYDS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	461
15N chemical shifts	121
1H chemical shifts	791

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 125 residues - 14425.336 Da.

1

MET

ARG

ILE

ASP

GLU

LEU

VAL

PRO

ALA

ASP

2

PRO

ARG

ALA

VAL

SER

LEU

TYR

THR

PRO

TYR

3

TYR

SER

GLN

ALA

ASN

ARG

TYR

LEU

4

PRO

TYR

ALA

LEU

SER

LEU

TYR

GLN

GLY

SER

5

SER

ILE

GLU

GLY

SER

ARG

ALA

VAL

GLU

GLY

6

GLY

ALA

PRO

ILE

SER

PHE

VAL

ALA

THR

TRP

7

THR

VAL

THR

PRO

LEU

PRO

ALA

ASP

MET

THR

8

ARG

CYS

HIS

LEU

GLN

PHE

ASN

ASP

ALA

9

GLU

LEU

THR

TYR

GLU

ILE

LEU

PRO

ASN

10

HIS

GLU

PHE

LEU

GLU

TYR

LEU

ILE

ASP

MET

11

LEU

MET

GLY

TYR

GLN

ARG

MET

GLN

LYS

THR

12

ASP

PHE

PRO

GLY

ALA

PHE

TYR

ARG

LEU

13

LEU

GLY

TYR

ASP

SER

Samples:

sample_1: Se0862, [U-100% 13C; U-100% 15N], 0.6 mM; TRIS 20 mM; sodium chloride 100 mM; TCEP 5 mM; DSS 10 uM; sodium azide 0.02 % v/v

sample_conditions_1: ionic strength: 125 mM; pH: 7; pressure: 1013.25 mbar; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
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 HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE DMX 600 MHz

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