BMRB Entry 17390

Name: Solution NMR Structure of de novo designed protein, P-loop NTPase fold, Northeast Structural Genomics Consortium Target OR32
Published: 2011-01-24

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PDB ID: 2l82
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17390
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of de novo designed protein, P-loop NTPase fold, Northeast Structural Genomics Consortium Target OR32

Deposition date:

2010-12-31

Original release date:

2011-01-24

Authors:

Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Tong, Saichu; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures" Nat. Commun. 12, 3921-3921 (2021).
PubMed: 34168113

Assembly members:

Assembly members:
OR32, polymer, 162 residues, 19701.238 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR32: MSQIFVVFSSDPEILKEIVR EIKRQGVRVVLLYSDQDEKR RRERLEEFEKQGVDVRTVED KEDFRENIREIWERYPQLDV VVIVTTDDKEWIKDFIEEAK ERGVEVFVVYNNKDDDRRKE AQQEFRSDGVDVRTVSDKEE LIEQVRRFVRKVGSLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	584
15N chemical shifts	173
1H chemical shifts	1181

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR32	1

Entities:

Entity 1, OR32 162 residues - 19701.238 Da.

1

MET

SER

GLN

ILE

PHE

VAL

PHE

SER

2

ASP

PRO

GLU

ILE

LEU

LYS

GLU

ILE

VAL

ARG

3

GLU

ILE

LYS

ARG

GLN

GLY

VAL

ARG

VAL

4

LEU

TYR

SER

ASP

GLN

ASP

GLU

LYS

ARG

5

ARG

GLU

ARG

LEU

GLU

PHE

GLU

LYS

6

GLN

GLY

VAL

ASP

VAL

ARG

THR

VAL

GLU

ASP

7

LYS

GLU

ASP

PHE

ARG

GLU

ASN

ILE

ARG

GLU

8

ILE

TRP

GLU

ARG

TYR

PRO

GLN

LEU

ASP

VAL

9

VAL

ILE

VAL

THR

ASP

LYS

GLU

10

TRP

ILE

LYS

ASP

PHE

ILE

GLU

ALA

LYS

11

GLU

ARG

GLY

VAL

GLU

VAL

PHE

VAL

TYR

12

ASN

LYS

ASP

ARG

LYS

GLU

13

ALA

GLN

GLU

PHE

ARG

SER

ASP

GLY

VAL

14

ASP

VAL

ARG

THR

VAL

SER

ASP

LYS

GLU

15

LEU

ILE

GLU

GLN

VAL

ARG

PHE

VAL

ARG

16

LYS

VAL

GLY

SER

LEU

GLU

HIS

17

HIS

Samples:

sample_NC: OR32, [U-100% 13C; U-100% 15N], 1.06 mM; H2O 90%; D2O 10%

sample_NC5: OR32, [U-5% 13C; U-100% 15N], 0.85 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC5	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D C(CO)NH	sample_NC	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

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