BMRB Entry 26646

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26646

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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:

A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR

Deposition date:

2015-09-02

Original release date:

2016-07-15

Authors:

Sgourakis, Nikolaos; May, Nathan; Boyd, Lisa; Ying, Jinfa; Bax, Ad; Margulies, David

Citation:

Citation: Sgourakis, Nikolaos; May, Nathan; Boyd, Lisa; Ying, Jinfa; Bax, Ad; Margulies, David. "A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR" J. Biol. Chem. 290, 28857-28868 (2015).
PubMed: 26463211

Assembly members:

Assembly members:
mini_H2-Ld, polymer, 180 residues, Formula weight is not available

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mini_H2-Ld: MGPHSMRYYETATSRRGLGE PRYTSVGYVDDKEFVRFDSD AENPRYEPQVPWMEQEGPEY WERITQVAKGQEQWFRVNLR TLLGYYNQSAGGTHTLQRMY GCDVGSDGRLLRGYEQFAYD GCDYIALNEDLRTWTAADMA AQITRRKWEQAGAAEYYRAY LEGECVEWLHRYLKNGNATL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	506
15N chemical shifts	170
1H chemical shifts	170

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mini H2-Ld	1

Entities:

Entity 1, mini H2-Ld 180 residues - Formula weight is not available

1	MET	GLY	PRO	HIS	SER	MET	ARG	TYR	TYR	GLU
2	THR	ALA	THR	SER	ARG	ARG	GLY	LEU	GLY	GLU
3	PRO	ARG	TYR	THR	SER	VAL	GLY	TYR	VAL	ASP
4	ASP	LYS	GLU	PHE	VAL	ARG	PHE	ASP	SER	ASP
5	ALA	GLU	ASN	PRO	ARG	TYR	GLU	PRO	GLN	VAL
6	PRO	TRP	MET	GLU	GLN	GLU	GLY	PRO	GLU	TYR
7	TRP	GLU	ARG	ILE	THR	GLN	VAL	ALA	LYS	GLY
8	GLN	GLU	GLN	TRP	PHE	ARG	VAL	ASN	LEU	ARG
9	THR	LEU	LEU	GLY	TYR	TYR	ASN	GLN	SER	ALA
10	GLY	GLY	THR	HIS	THR	LEU	GLN	ARG	MET	TYR
11	GLY	CYS	ASP	VAL	GLY	SER	ASP	GLY	ARG	LEU
12	LEU	ARG	GLY	TYR	GLU	GLN	PHE	ALA	TYR	ASP
13	GLY	CYS	ASP	TYR	ILE	ALA	LEU	ASN	GLU	ASP
14	LEU	ARG	THR	TRP	THR	ALA	ALA	ASP	MET	ALA
15	ALA	GLN	ILE	THR	ARG	ARG	LYS	TRP	GLU	GLN
16	ALA	GLY	ALA	ALA	GLU	TYR	TYR	ARG	ALA	TYR
17	LEU	GLU	GLY	GLU	CYS	VAL	GLU	TRP	LEU	HIS
18	ARG	TYR	LEU	LYS	ASN	GLY	ASN	ALA	THR	LEU

Samples:

sample_1: mini H2-Ld, [U-100% 13C; U-100% 15N; U-80% 2H], 0.9 mM; H2O 90%; D2O 10%; PIPES 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.0257 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz

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

1	MET	GLY	PRO	HIS	SER	MET	ARG	TYR	TYR	GLU
2	THR	ALA	THR	SER	ARG	ARG	GLY	LEU	GLY	GLU
3	PRO	ARG	TYR	THR	SER	VAL	GLY	TYR	VAL	ASP
4	ASP	LYS	GLU	PHE	VAL	ARG	PHE	ASP	SER	ASP
5	ALA	GLU	ASN	PRO	ARG	TYR	GLU	PRO	GLN	VAL
6	PRO	TRP	MET	GLU	GLN	GLU	GLY	PRO	GLU	TYR
7	TRP	GLU	ARG	ILE	THR	GLN	VAL	ALA	LYS	GLY
8	GLN	GLU	GLN	TRP	PHE	ARG	VAL	ASN	LEU	ARG
9	THR	LEU	LEU	GLY	TYR	TYR	ASN	GLN	SER	ALA
10	GLY	GLY	THR	HIS	THR	LEU	GLN	ARG	MET	TYR
11	GLY	CYS	ASP	VAL	GLY	SER	ASP	GLY	ARG	LEU
12	LEU	ARG	GLY	TYR	GLU	GLN	PHE	ALA	TYR	ASP
13	GLY	CYS	ASP	TYR	ILE	ALA	LEU	ASN	GLU	ASP
14	LEU	ARG	THR	TRP	THR	ALA	ALA	ASP	MET	ALA
15	ALA	GLN	ILE	THR	ARG	ARG	LYS	TRP	GLU	GLN
16	ALA	GLY	ALA	ALA	GLU	TYR	TYR	ARG	ALA	TYR
17	LEU	GLU	GLY	GLU	CYS	VAL	GLU	TRP	LEU	HIS
18	ARG	TYR	LEU	LYS	ASN	GLY	ASN	ALA	THR	LEU

1	MET	GLY	PRO	HIS	SER	MET	ARG	TYR	TYR	GLU
2	THR	ALA	THR	SER	ARG	ARG	GLY	LEU	GLY	GLU
3	PRO	ARG	TYR	THR	SER	VAL	GLY	TYR	VAL	ASP
4	ASP	LYS	GLU	PHE	VAL	ARG	PHE	ASP	SER	ASP
5	ALA	GLU	ASN	PRO	ARG	TYR	GLU	PRO	GLN	VAL
6	PRO	TRP	MET	GLU	GLN	GLU	GLY	PRO	GLU	TYR
7	TRP	GLU	ARG	ILE	THR	GLN	VAL	ALA	LYS	GLY
8	GLN	GLU	GLN	TRP	PHE	ARG	VAL	ASN	LEU	ARG
9	THR	LEU	LEU	GLY	TYR	TYR	ASN	GLN	SER	ALA
10	GLY	GLY	THR	HIS	THR	LEU	GLN	ARG	MET	TYR
11	GLY	CYS	ASP	VAL	GLY	SER	ASP	GLY	ARG	LEU
12	LEU	ARG	GLY	TYR	GLU	GLN	PHE	ALA	TYR	ASP
13	GLY	CYS	ASP	TYR	ILE	ALA	LEU	ASN	GLU	ASP
14	LEU	ARG	THR	TRP	THR	ALA	ALA	ASP	MET	ALA
15	ALA	GLN	ILE	THR	ARG	ARG	LYS	TRP	GLU	GLN
16	ALA	GLY	ALA	ALA	GLU	TYR	TYR	ARG	ALA	TYR
17	LEU	GLU	GLY	GLU	CYS	VAL	GLU	TRP	LEU	HIS
18	ARG	TYR	LEU	LYS	ASN	GLY	ASN	ALA	THR	LEU

1	MET	GLY	PRO	HIS	SER	MET	ARG	TYR	TYR	GLU
2	THR	ALA	THR	SER	ARG	ARG	GLY	LEU	GLY	GLU
3	PRO	ARG	TYR	THR	SER	VAL	GLY	TYR	VAL	ASP
4	ASP	LYS	GLU	PHE	VAL	ARG	PHE	ASP	SER	ASP
5	ALA	GLU	ASN	PRO	ARG	TYR	GLU	PRO	GLN	VAL
6	PRO	TRP	MET	GLU	GLN	GLU	GLY	PRO	GLU	TYR
7	TRP	GLU	ARG	ILE	THR	GLN	VAL	ALA	LYS	GLY
8	GLN	GLU	GLN	TRP	PHE	ARG	VAL	ASN	LEU	ARG
9	THR	LEU	LEU	GLY	TYR	TYR	ASN	GLN	SER	ALA
10	GLY	GLY	THR	HIS	THR	LEU	GLN	ARG	MET	TYR
11	GLY	CYS	ASP	VAL	GLY	SER	ASP	GLY	ARG	LEU
12	LEU	ARG	GLY	TYR	GLU	GLN	PHE	ALA	TYR	ASP
13	GLY	CYS	ASP	TYR	ILE	ALA	LEU	ASN	GLU	ASP
14	LEU	ARG	THR	TRP	THR	ALA	ALA	ASP	MET	ALA
15	ALA	GLN	ILE	THR	ARG	ARG	LYS	TRP	GLU	GLN
16	ALA	GLY	ALA	ALA	GLU	TYR	TYR	ARG	ALA	TYR
17	LEU	GLU	GLY	GLU	CYS	VAL	GLU	TRP	LEU	HIS
18	ARG	TYR	LEU	LYS	ASN	GLY	ASN	ALA	THR	LEU