BMRB Entry 18337

Name: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR136
Published: 2012-04-16

Click here to enlarge.

PDB ID: 2lr0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18337
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR136

Deposition date:

2012-03-19

Original release date:

2012-04-16

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. "SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR136" To be published ., .-..

Assembly members:

Assembly members:
OR136, polymer, 134 residues, 15990.547 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):
OR136: MKILILINTNNDELIKKIKK EVENQGYQVRDVNDSDELKK EMKKLAEEKNFEKILIKSND KQLLKEMLELISKLGYKVFL LLADQDENELEEFKRKIESQ GYEVRKVTDDEEALKIVREF MQKAGSLEHHHHHH

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	609
15N chemical shifts	140
1H chemical shifts	1015
residual dipolar couplings	91

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR136	1

Entities:

Entity 1, OR136 134 residues - 15990.547 Da.

1

MET

LYS

ILE

LEU

ILE

LEU

ILE

ASN

THR

ASN

2

ASN

ASP

GLU

LEU

ILE

LYS

ILE

LYS

3

GLU

VAL

GLU

ASN

GLN

GLY

TYR

GLN

VAL

ARG

4

ASP

VAL

ASN

ASP

SER

ASP

GLU

LEU

LYS

5

GLU

MET

LYS

LEU

ALA

GLU

LYS

ASN

6

PHE

GLU

LYS

ILE

LEU

ILE

LYS

SER

ASN

ASP

7

LYS

GLN

LEU

LYS

GLU

MET

LEU

GLU

LEU

8

ILE

SER

LYS

LEU

GLY

TYR

LYS

VAL

PHE

LEU

9

LEU

ALA

ASP

GLN

ASP

GLU

ASN

GLU

LEU

10

GLU

PHE

LYS

ARG

LYS

ILE

GLU

SER

GLN

11

GLY

TYR

GLU

VAL

ARG

LYS

VAL

THR

ASP

12

GLU

ALA

LEU

LYS

ILE

VAL

ARG

GLU

PHE

13

MET

GLN

LYS

ALA

GLY

SER

LEU

GLU

HIS

14

HIS

Samples:

sample_NC: OR136.001, [U-100% 13C; U-100% 15N], 1.16309 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

sample_NC5_RDC: OR136.007, [U-100% 13C; U-100% 15N], 0.72 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

sample_NC5: OR136.006, [U-100% 13C; U-100% 15N], 0.72 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

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_RDC	isotropic	sample_conditions_1
3D HCCH-TOCSY	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

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

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