BMRB Entry 30708

Name: De novo designed Rossmann fold protein ROS2_36830
Published: 2020-08-14

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PDB ID: 6vgb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30708
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_36830

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, 121 residues, 13953.312 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 MGLLVLIWSNDKKLIEEARK MAEKANLYLLTLETDDKKIE DILKSLGPPVKILVLLEDTK DADKVKKEIEKKARKKNLPV RIRKVTSPDEAKRWIKEFSE E

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	370
15N chemical shifts	101
1H chemical shifts	746

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_1 121 residues - 13953.312 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLY

LEU

VAL

LEU

ILE

TRP

SER

ASN

4

ASP

LYS

LEU

ILE

GLU

ALA

ARG

LYS

5

MET

ALA

GLU

LYS

ALA

ASN

LEU

TYR

LEU

6

THR

LEU

GLU

THR

ASP

LYS

ILE

GLU

7

ASP

ILE

LEU

LYS

SER

LEU

GLY

PRO

VAL

8

LYS

ILE

LEU

VAL

LEU

GLU

ASP

THR

LYS

9

ASP

ALA

ASP

LYS

VAL

LYS

GLU

ILE

GLU

10

LYS

ALA

ARG

LYS

ASN

LEU

PRO

VAL

11

ARG

ILE

ARG

LYS

VAL

THR

SER

PRO

ASP

GLU

12

ALA

LYS

ARG

TRP

ILE

LYS

GLU

PHE

SER

GLU

13

GLU

Samples:

sample_1: de novo protein RO2_20, [U-99% 13C; U-99% 15N], 0.8 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

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