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PDB ID: 9sgw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR35014
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

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:

Rn2, ancient tentative ribonuclease fold

Deposition date:

2025-08-22

Original release date:

2026-06-25

Authors:

Srb, P.; Veverka, V.

Citation:

Citation: Giacobelli, V.; Andresson, S.; Srb, P.; Neuwirthova, T.; Ruszova, Z.; Marhoul, J.; Psenicka, S.; Knetl, A.; Bednarova, L.; Veverka, V.; Andre, I.; Hlouchova, Z.. "Ancient amino acid sets enable stable protein folds " .

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 10390.374 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32644 Superkingdom: not available Kingdom: not available Genus/species: not available not available

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: MTVVTITDTTPTTATVTVSD AETGATLATADVSTADPAEA AEEILELVLAVGATEVTVTI TLATAAEAAEAATELAAALT ELAAEAGITVTVTATTAAPH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	93
1H chemical shifts	623

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_1 105 residues - 10390.374 Da.

1

MET

THR

VAL

THR

ILE

THR

ASP

THR

2

PRO

THR

ALA

THR

VAL

THR

VAL

SER

ASP

3

ALA

GLU

THR

GLY

ALA

THR

LEU

ALA

THR

ALA

4

ASP

VAL

SER

THR

ALA

ASP

PRO

ALA

GLU

ALA

5

ALA

GLU

ILE

LEU

GLU

LEU

VAL

LEU

ALA

6

VAL

GLY

ALA

THR

GLU

VAL

THR

VAL

THR

ILE

7

THR

LEU

ALA

THR

ALA

GLU

ALA

GLU

8

ALA

THR

GLU

LEU

ALA

LEU

THR

9

GLU

LEU

ALA

GLU

ALA

GLY

ILE

THR

VAL

10

THR

VAL

THR

ALA

THR

ALA

PRO

HIS

11

HIS

Samples:

sample_1: Rn2, [U-100% 13C; U-100% 15N], 940 uM; sodium phosphate 50 mM; sodium chloride 280 mM

sample_conditions_1: ionic strength: 330 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

YASARA, YASARA Biosciences GmbH - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III HD 850 MHz

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

BMRB Entry 35014