BMRB Entry 18161

Name: Solution NMR Structure of DE NOVO DESIGNED PROTEIN, PFK fold, Northeast Structural Genomics Consortium Target OR134
Published: 2012-02-06

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PDB ID: 2lnd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18161
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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, PFK fold, Northeast Structural Genomics Consortium Target OR134

Deposition date:

2011-12-23

Original release date:

2012-02-06

Authors:

Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target OR134" To be published ., .-..

Assembly members:

Assembly members:
OR134, polymer, 112 residues, 12705.332 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):
OR134: MGKVLLVISTDTNIISSVQE RAKHNYPGRYIRTATSSQDI RDIIKSMKDNGKPLVVFVNG ASQNDVNEFQNEAKKEGVSY DVLKSTDPEELTQRVREFLK TAGSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
- RDC_list_2

Data type	Count
13C chemical shifts	458
15N chemical shifts	108
1H chemical shifts	748
residual dipolar couplings	123

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR134	1

Entities:

Entity 1, OR134 112 residues - 12705.332 Da.

1

MET

GLY

LYS

VAL

LEU

VAL

ILE

SER

THR

2

ASP

THR

ASN

ILE

SER

VAL

GLN

GLU

3

ARG

ALA

LYS

HIS

ASN

TYR

PRO

GLY

ARG

TYR

4

ILE

ARG

THR

ALA

THR

SER

GLN

ASP

ILE

5

ARG

ASP

ILE

LYS

SER

MET

LYS

ASP

ASN

6

GLY

LYS

PRO

LEU

VAL

PHE

VAL

ASN

GLY

7

ALA

SER

GLN

ASN

ASP

VAL

ASN

GLU

PHE

GLN

8

ASN

GLU

ALA

LYS

GLU

GLY

VAL

SER

TYR

9

ASP

VAL

LEU

LYS

SER

THR

ASP

PRO

GLU

10

LEU

THR

GLN

ARG

VAL

ARG

GLU

PHE

LEU

LYS

11

THR

ALA

GLY

SER

LEU

GLU

HIS

12

HIS

Samples:

sample_NC: OR134, [U-100% 13C; U-100% 15N], 1.3 mM; H2O 95%; D2O 5%

sample_NC5: OR134, [U-5% 13C; U-100% 15N], 1.15 mM; H2O 95%; D2O 5%

sample_NC5_RDC: OR134, [U-5% 13C; U-100% 15N], 1.15 mM; H2O 95%; D2O 5%

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_NC	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-13C HSQC	sample_NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5_RDC	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

SPARKY, Goddard - data analysis

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

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz
Varian INOVA 600 MHz