BMRB Entry 19623

Name: GA-79-MBP cs-rosetta structures
Published: 2015-04-07

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PDB ID: 2mh8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19623
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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:

GA-79-MBP cs-rosetta structures

Deposition date:

2013-11-19

Original release date:

2015-04-07

Authors:

He, Yanan; Chen, Yihong; Porter, Lauren; Bryan, Philip; Orban, John

Citation:

Citation: Porter, Lauren; He, Yanan; Chen, Yihong; Orban, John; Bryan, Philip. "Subdomain interactions foster the design of two protein pairs with ~80% sequence identity but different folds" Biophys J. 108, 154-162 (2015).
PubMed: 25564862

Assembly members:

Assembly members:
entity, polymer, 56 residues, 6312.319 Da.

Natural source:

Natural source: Common Name: Streptococcus canis Taxonomy ID: 1329 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus canis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: hisPPAL8

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: NGDKGYNGLAEAKEKAIKDL KIYGIGEHYIKLIEKAKQVA AVEDLKDEILKAHDRF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	55
1H chemical shifts	112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GA-79-MBP	1

Entities:

Entity 1, GA-79-MBP 56 residues - 6312.319 Da.

1

ASN

GLY

ASP

LYS

GLY

TYR

ASN

GLY

LEU

ALA

2

GLU

ALA

LYS

GLU

LYS

ALA

ILE

LYS

ASP

LEU

3

LYS

ILE

TYR

GLY

ILE

GLY

GLU

HIS

TYR

ILE

4

LYS

LEU

ILE

GLU

LYS

ALA

LYS

GLN

VAL

ALA

5

ALA

VAL

GLU

ASP

LEU

LYS

ASP

GLU

ILE

LEU

6

LYS

ALA

HIS

ASP

ARG

PHE

Samples:

sample_1: GA-79-MBP, [U-100% 13C; U-100% 15N], 0.27 mM; potassium phosphate 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 283 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - structure display

TOPSPIN, Bruker Biospin - Data collection

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - structure quality analysis

CSI, David Wishart, Brian Sykes - Secondary structure prediction

NMR spectrometers:

Bruker DMX 600 MHz
Bruker Avance III 600 MHz