BMRB Entry 27286

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for VSV8 peptide bound to a truncated MHC H-2Kb (VSV8/Kb-t)
Published: 2017-12-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27286

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for VSV8 peptide bound to a truncated MHC H-2Kb (VSV8/Kb-t)

Deposition date:

2017-10-18

Original release date:

2017-12-14

Authors:

Mallis, Robert; Arthanari, Haribabu; Lang, Matt; Reinherz, Ellis; Wagner, Gerhard

Citation:

Citation: Mallis, Robert; Arthanari, Haribabu; Lang, Matt; Reinherz, Ellis; Wagner, Gerhard. "NMR-Directed Design of PreTCRbeta and pMHC Molecules Implies a Distinct Geometry for preTCR Relative to alphabetaTCR Recognition of pMHC" J. Biol. Chem. 293, 754-766 (2018).
PubMed: 29101227

Assembly members:

Assembly members:
H-2Kb-t, polymer, 186 residues, 21452.86 Da.
VSV8, polymer, 8 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H-2Kb-t: MGPHSLRYFVTAVSRPGLGE PRYMEVGYVDDTEFVRFDSD AENPRYEPRARWMEQEGPEY WERETQKAKGNEQSFRVDLR TLLGYYNQSKGGSHTIQVIS GCEVGSDGRLLRGYQQYAYD GCDYIALNEDLKTWTAADMA ALITKHKWEQAGEAERLRAY LEGTCVEWLRRYLKNGNATL LRTDSP
VSV8: RGYVYQGL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	140
1H chemical shifts	140

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H-2Kb-t	1
2	VSV8	2

Entities:

Entity 1, H-2Kb-t 186 residues - 21452.86 Da.

1

MET

GLY

PRO

HIS

SER

LEU

ARG

TYR

PHE

VAL

2

THR

ALA

VAL

SER

ARG

PRO

GLY

LEU

GLY

GLU

3

PRO

ARG

TYR

MET

GLU

VAL

GLY

TYR

VAL

ASP

4

ASP

THR

GLU

PHE

VAL

ARG

PHE

ASP

SER

ASP

5

ALA

GLU

ASN

PRO

ARG

TYR

GLU

PRO

ARG

ALA

6

ARG

TRP

MET

GLU

GLN

GLU

GLY

PRO

GLU

TYR

7

TRP

GLU

ARG

GLU

THR

GLN

LYS

ALA

LYS

GLY

8

ASN

GLU

GLN

SER

PHE

ARG

VAL

ASP

LEU

ARG

9

THR

LEU

GLY

TYR

ASN

GLN

SER

LYS

10

GLY

SER

HIS

THR

ILE

GLN

VAL

ILE

SER

11

GLY

CYS

GLU

VAL

GLY

SER

ASP

GLY

ARG

LEU

12

LEU

ARG

GLY

TYR

GLN

TYR

ALA

TYR

ASP

13

GLY

CYS

ASP

TYR

ILE

ALA

LEU

ASN

GLU

ASP

14

LEU

LYS

THR

TRP

THR

ALA

ASP

MET

ALA

15

ALA

LEU

ILE

THR

LYS

HIS

LYS

TRP

GLU

GLN

16

ALA

GLY

GLU

ALA

GLU

ARG

LEU

ARG

ALA

TYR

17

LEU

GLU

GLY

THR

CYS

VAL

GLU

TRP

LEU

ARG

18

ARG

TYR

LEU

LYS

ASN

GLY

ASN

ALA

THR

LEU

19

LEU

ARG

THR

ASP

SER

PRO

Entity 2, VSV8 8 residues - Formula weight is not available

1

ARG

GLY

TYR

VAL

TYR

GLN

GLY

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 27286

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: