BMRB Entry 25868

Name: Solution NMR Structure of Designed Protein DA05R1, Northeast Structural Genomics Consortium (NESG) Target OR690
Published: 2015-11-23

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PDB ID: 2n8w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25868
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of Designed Protein DA05R1, Northeast Structural Genomics Consortium (NESG) Target OR690

Deposition date:

2015-10-27

Original release date:

2015-11-23

Authors:

Eletsky, Alexander; Federizon, Jasmin; Xu, Xianzhong; Pulavarti, S.V.S.R. Krishna; Jacobs, Tim; Kuhlman, Brian; Szyperski, Thomas

Citation:

Citation: Jacobs, Tim; Xu, Xianzhong; Eletsky, Alexander; Federizon, Jasmin; Szyperski, Thomas; Kuhlman, Brian. "Design of Structurally Unique Proteins Using Strategies Inspired by Evolution" .

Assembly members:

Assembly members:
DA05R1, polymer, 208 residues, 23847.180 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: pCDB24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DA05R1: ADENIAKFEKAYKKAEELNQ GELMGRALYNIGLEKNKMGK AREAAEYFFRAAIVFYKEHD TDGLRRAAKSLKEAITAIPE EEGRKEAKEMAKKAEEWLQA EQNNADENIAKFEKAYKKAE ELNQGELMGRALYNIGLEKN KMGKAREAAEYFFRAAIVFY KEHDTDGLRRAAKSLKEAIT AIPEEEGRKEAKEMAKKAEE WLQAEQNN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	425
15N chemical shifts	94
1H chemical shifts	689

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DA05R1	1

Entities:

Entity 1, DA05R1 208 residues - 23847.180 Da.

1

ALA

ASP

GLU

ASN

ILE

ALA

LYS

PHE

GLU

LYS

2

ALA

TYR

LYS

ALA

GLU

LEU

ASN

GLN

3

GLY

GLU

LEU

MET

GLY

ARG

ALA

LEU

TYR

ASN

4

ILE

GLY

LEU

GLU

LYS

ASN

LYS

MET

GLY

LYS

5

ALA

ARG

GLU

ALA

GLU

TYR

PHE

ARG

6

ALA

ILE

VAL

PHE

TYR

LYS

GLU

HIS

ASP

7

THR

ASP

GLY

LEU

ARG

ALA

LYS

SER

8

LEU

LYS

GLU

ALA

ILE

THR

ALA

ILE

PRO

GLU

9

GLU

GLY

ARG

LYS

GLU

ALA

LYS

GLU

MET

10

ALA

LYS

ALA

GLU

TRP

LEU

GLN

ALA

11

GLU

GLN

ASN

ALA

ASP

GLU

ASN

ILE

ALA

12

LYS

PHE

GLU

LYS

ALA

TYR

LYS

ALA

GLU

13

GLU

LEU

ASN

GLN

GLY

GLU

LEU

MET

GLY

ARG

14

ALA

LEU

TYR

ASN

ILE

GLY

LEU

GLU

LYS

ASN

15

LYS

MET

GLY

LYS

ALA

ARG

GLU

ALA

GLU

16

TYR

PHE

ARG

ALA

ILE

VAL

PHE

TYR

17

LYS

GLU

HIS

ASP

THR

ASP

GLY

LEU

ARG

18

ALA

LYS

SER

LEU

LYS

GLU

ALA

ILE

THR

19

ALA

ILE

PRO

GLU

GLY

ARG

LYS

GLU

20

ALA

LYS

GLU

MET

ALA

LYS

ALA

GLU

21

TRP

LEU

GLN

ALA

GLU

GLN

ASN

Samples:

NC5: DA05R1, [U-5% 13C; U-15N], 660 uM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM

NC: DA05R1, [U-13C; U-15N], 1 mM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D CT 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
2D CT 1H-13C HSQC aromatic	NC	isotropic	sample_conditions_1
3D 15N/13C-edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
2D CT 1H-13C HSQC aliphatic 28 ms	NC5	isotropic	sample_conditions_1
3D 1H-15N TOCSY	NC5	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5	isotropic	sample_conditions_1

Software:

PROSA v6.4, Guntert - processing

AS-DP v1.0, Huang, Tejero, Powers and Montelione - structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

XEASY v1.3.13, Bartels et al. - data analysis

VNMRJ v4.0, Varian - collection

TALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.5, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz

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