BMRB Entry 19879

Name: NMR solution structure of a computational designed protein based on structure template 1cy5
Published: 2014-10-27

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PDB ID: 2mn4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19879
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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:

NMR solution structure of a computational designed protein based on structure template 1cy5

Deposition date:

2014-03-28

Original release date:

2014-10-27

Authors:

Xiong, Peng; Wang, Meng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan

Citation:

Citation: Xiong, Peng; Wang, Meng; Zhou, Xiaoqun; Zhang, Tongchuan; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Boost computational protein design with a comprehensive statistical energy function and an in vivo experimental approach" Nat. Struct. Biol. ., .-..

Assembly members:

Assembly members:
entity, polymer, 94 residues, 10745.617 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: PET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MTPEQREFLPEILAEIIANL DPTKILEELLRRGLLTPAEL QEVLDLKTPEEQAKKLIDFI LKLSPADVQARINVLRAHGY QALADKLNKYLTLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	57
1H chemical shifts	442

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 94 residues - 10745.617 Da.

1

MET

THR

PRO

GLU

GLN

ARG

GLU

PHE

LEU

PRO

2

GLU

ILE

LEU

ALA

GLU

ILE

ALA

ASN

LEU

3

ASP

PRO

THR

LYS

ILE

LEU

GLU

LEU

4

ARG

GLY

LEU

THR

PRO

ALA

GLU

LEU

5

GLN

GLU

VAL

LEU

ASP

LEU

LYS

THR

PRO

GLU

6

GLU

GLN

ALA

LYS

LEU

ILE

ASP

PHE

ILE

7

LEU

LYS

LEU

SER

PRO

ALA

ASP

VAL

GLN

ALA

8

ARG

ILE

ASN

VAL

LEU

ARG

ALA

HIS

GLY

TYR

9

GLN

ALA

LEU

ALA

ASP

LYS

LEU

ASN

LYS

TYR

10

LEU

THR

LEU

GLU

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM

sample_2: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker DMX 600 MHz