BMRB Entry 16117

Name: NMR structures of GA95 and GB95, two designed proteins with 95% sequence identity but different folds and functions
Published: 2010-01-12

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PDB ID: 2kdm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16117
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structures of GA95 and GB95, two designed proteins with 95% sequence identity but different folds and functions

Deposition date:

2009-01-12

Original release date:

2010-01-12

Authors:

He, Yanan; Alexander, Patrick; Chen, Yihong; Bryan, Philip; Orban, John

Citation:

Citation: Shen, Yang; Bryan, Philip; He, Yanan; Orban, John; Baker, David; Bax, Ad. "De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds." Protein Sci. 19, 349-356 (2009).
PubMed: 19998407

Assembly members:

Assembly members:
entity, polymer, 56 residues, 6317.434 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: over expression in E. Coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: TTYKLILNLKQAKEEAIKEA VDAGTAEKYFKLIANAKTVE GVWTYKDEIKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	242
15N chemical shifts	59
1H chemical shifts	354

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 56 residues - 6317.434 Da.

1

THR

TYR

LYS

LEU

ILE

LEU

ASN

LEU

LYS

2

GLN

ALA

LYS

GLU

ALA

ILE

LYS

GLU

ALA

3

VAL

ASP

ALA

GLY

THR

ALA

GLU

LYS

TYR

PHE

4

LYS

LEU

ILE

ALA

ASN

ALA

LYS

THR

VAL

GLU

5

GLY

VAL

TRP

THR

TYR

LYS

ASP

GLU

ILE

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

Gb95: Gb95, [U-100% 13C; U-100% 15N], 0.15-0.3 mM; potassium phosphate pH 7.2 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Gb95	isotropic	sample_conditions_1
3D HNCACB	Gb95	isotropic	sample_conditions_1
3D CBCA(CO)NH	Gb95	isotropic	sample_conditions_1
3D HBHA(CO)NH	Gb95	isotropic	sample_conditions_1
3D H(CCO)NH	Gb95	isotropic	sample_conditions_1
3D C(CO)NH	Gb95	isotropic	sample_conditions_1
3D HNCO	Gb95	isotropic	sample_conditions_1
3D 1H-15N NOESY	Gb95	isotropic	sample_conditions_1
3D 1H-13C NOESY(aliphatic)	Gb95	isotropic	sample_conditions_1
3D 1H-13C NOESY(aromatic)	Gb95	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

xwinnmr v2.5, Bruker Biospin - collection

NMRPipe vn/a, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3, Goddard - data analysis

NMR spectrometers:

Bruker DRX 600 MHz