BMRB Entry 30706

Name: De novo designed Rossmann fold protein ROS2_49223
Published: 2020-08-14

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PDB ID: 6vg7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30706
MolProbity Validation Chart

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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:

De novo designed Rossmann fold protein ROS2_49223

Deposition date:

2020-01-07

Original release date:

2020-08-14

Authors:

Pan, X.; Zhang, Y.; Kelly, M.; Kortemme, T.

Citation:

Citation: Pan, Xingjie; Thompson, Michael; Zhang, Yang; Liu, Lin; Fraser, James; Kelly, Mark; Kortemme, Tanja. "Expanding the space of protein geometries by computational design of de novo fold families" Science 369, 1132-1136 (2020).
PubMed: 32855341

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 14153.302 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MTLFVLILSNDKKLIEEARK MAEKANLILITVGDEEELKK AIKKADDIAKKQNSSEAKIL ILLEKPVSPEYEKKLQKYAD AEVRVRTVTSPDEAKRWIKE FSEE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	106
1H chemical shifts	737

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_1 124 residues - 14153.302 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

THR

LEU

PHE

VAL

LEU

ILE

LEU

SER

ASN

4

ASP

LYS

LEU

ILE

GLU

ALA

ARG

LYS

5

MET

ALA

GLU

LYS

ALA

ASN

LEU

ILE

LEU

ILE

6

THR

VAL

GLY

ASP

GLU

LEU

LYS

7

ALA

ILE

LYS

ALA

ASP

ILE

ALA

LYS

8

LYS

GLN

ASN

SER

GLU

ALA

LYS

ILE

LEU

9

ILE

LEU

GLU

LYS

PRO

VAL

SER

PRO

GLU

10

TYR

GLU

LYS

LEU

GLN

LYS

TYR

ALA

ASP

11

ALA

GLU

VAL

ARG

VAL

ARG

THR

VAL

THR

SER

12

PRO

ASP

GLU

ALA

LYS

ARG

TRP

ILE

LYS

GLU

13

PHE

SER

GLU

Samples:

sample_1: de novo protein RO2_25, [U-99% 13C; U-99% 15N], 0.76 mM; potassium phosphate monobasic 21.1 mM; sodium phosphate dibasic 28.9 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 300 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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:

TopSpin v4.0.6, Bruker Biospin - collection

NMRPipe v9.8, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE 800 MHz
Bruker DRX 500 MHz

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