BMRB Entry 25067

Name: Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459
Published: 2014-09-15

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PDB ID: 2mra
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25067
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:

Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459

Deposition date:

2014-07-02

Original release date:

2014-09-15

Authors:

Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459" To be published ., .-..

Assembly members:

Assembly members:
OR459, polymer, 117 residues, 13406.451 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: pET21_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR459: MAGKELRVEIKIDCGNDDKE TTYDLYFSKAEEAKELLKKV AEKAADKIKKQGCKRVKIRF EKKGLDDDARKKAKKWALEV ANKIANELGAKQSTTTTDGD TFEVEVILELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	782
13C chemical shifts	486
15N chemical shifts	104

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR459	1

Entities:

Entity 1, OR459 117 residues - 13406.451 Da.

1

MET

ALA

GLY

LYS

GLU

LEU

ARG

VAL

GLU

ILE

2

LYS

ILE

ASP

CYS

GLY

ASN

ASP

LYS

GLU

3

THR

TYR

ASP

LEU

TYR

PHE

SER

LYS

ALA

4

GLU

ALA

LYS

GLU

LEU

LYS

VAL

5

ALA

GLU

LYS

ALA

ASP

LYS

ILE

LYS

6

GLN

GLY

CYS

LYS

ARG

VAL

LYS

ILE

ARG

PHE

7

GLU

LYS

GLY

LEU

ASP

ALA

ARG

8

LYS

ALA

LYS

TRP

ALA

LEU

GLU

VAL

9

ALA

ASN

LYS

ILE

ALA

ASN

GLU

LEU

GLY

ALA

10

LYS

GLN

SER

THR

ASP

GLY

ASP

11

THR

PHE

GLU

VAL

GLU

VAL

ILE

LEU

GLU

LEU

12

GLU

HIS

Samples:

sample_1: H2O 90 ± 0.005 %; D2O 10%; OR459.005, [U-13C,15N], 1.17 mM

sample_2: H2O 90%; D2O 10%; OR459.005, [5% 13C; U-15N], 1.17 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
GFT-4,3d-hcch-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	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

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

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

CARA, Rochus Keller - Analysis

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

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

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz