BMRB Entry 30707

Name: De novo designed Rossmann fold protein ROS2_835
Published: 2020-08-14

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PDB ID: 6vga
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30707
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_835

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, 125 residues, 13925.990 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MRLVVLIVSNDKKLIEEARK MAEKANLELITVPGSPEEAI RLAQEIAEKAPGPVKVLVLI TGSADPDEKTKAKKAAEEAR KWNVRVRTVTSPDEAKRWIK EFSEE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	335
15N chemical shifts	104
1H chemical shifts	652

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 - 13925.990 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ARG

LEU

VAL

LEU

ILE

VAL

SER

ASN

4

ASP

LYS

LEU

ILE

GLU

ALA

ARG

LYS

5

MET

ALA

GLU

LYS

ALA

ASN

LEU

GLU

LEU

ILE

6

THR

VAL

PRO

GLY

SER

PRO

GLU

ALA

ILE

7

ARG

LEU

ALA

GLN

GLU

ILE

ALA

GLU

LYS

ALA

8

PRO

GLY

PRO

VAL

LYS

VAL

LEU

VAL

LEU

ILE

9

THR

GLY

SER

ALA

ASP

PRO

ASP

GLU

LYS

THR

10

LYS

ALA

LYS

ALA

GLU

ALA

ARG

11

LYS

TRP

ASN

VAL

ARG

VAL

ARG

THR

VAL

THR

12

SER

PRO

ASP

GLU

ALA

LYS

ARG

TRP

ILE

LYS

13

GLU

PHE

SER

GLU

Samples:

sample_1: de novo protein RO2_1, [U-99% 13C; U-99% 15N], 0.74 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-13C 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

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

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

CcpNmr Analysis, CCPN - peak picking

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