BMRB Entry 16562

Name: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16
Published: 2009-11-02

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PDB ID: 2kpo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16562
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16

Deposition date: 2009-10-17 Original release date: 2009-11-02

Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; CICCOSANTI, C.; Acton, Thomas; Baker, David; Montelione, Gaetano

Citation: Liu, Gaohua; Koga, Nobuyasu; Baker, David; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF DENOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16" Not known ., .-..

Assembly members:
2x2, polymer, 110 residues, 13078.123 Da.

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

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

Entity Sequences (FASTA):
2x2: MLLYVLIISNDKKLIEEARK MAEKANLELRTVKTEDELKK YLEEFRKESQNIKVLILVSN DEELDKAKELAQKMEIDVRT RKVTSPDEAKRWIKEFSEEG GSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	497
15N chemical shifts	115
1H chemical shifts	818

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR16	1

Entities:

Entity 1, OR16 110 residues - 13078.123 Da.

1	MET	LEU	LEU	TYR	VAL	LEU	ILE	ILE	SER	ASN
2	ASP	LYS	LYS	LEU	ILE	GLU	GLU	ALA	ARG	LYS
3	MET	ALA	GLU	LYS	ALA	ASN	LEU	GLU	LEU	ARG
4	THR	VAL	LYS	THR	GLU	ASP	GLU	LEU	LYS	LYS
5	TYR	LEU	GLU	GLU	PHE	ARG	LYS	GLU	SER	GLN
6	ASN	ILE	LYS	VAL	LEU	ILE	LEU	VAL	SER	ASN
7	ASP	GLU	GLU	LEU	ASP	LYS	ALA	LYS	GLU	LEU
8	ALA	GLN	LYS	MET	GLU	ILE	ASP	VAL	ARG	THR
9	ARG	LYS	VAL	THR	SER	PRO	ASP	GLU	ALA	LYS
10	ARG	TRP	ILE	LYS	GLU	PHE	SER	GLU	GLU	GLY
11	GLY	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.859 mM; H2O 93%; D2O 7%; NaCl 200 mM

sample_2: entity, [U-10% 13C; U-100% 15N], 0.867 mM; H2O 93%; D2O 7%; NaCl 200 mM

sample_conditions_1: ionic strength: 200 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
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
GFT (4,3)D HABCABcoNHN	sample_1	isotropic	sample_conditions_1
SIMUTANEOUS 1H, 15N, 13C NOESY	sample_1	isotropic	sample_conditions_1
3D CCHTOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
AROMATIC 1H, 15N, 13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, geometry optimization, refinement

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

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

VNMRJ, Varian - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

Biological Magnetic Resonance Data Bank