BMRB Entry 19282

Name: NMR structure of the lymphocyte receptor NKR-P1A
Published: 2014-06-09

Click here to enlarge.

PDB ID: 2mti
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19282
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure of the lymphocyte receptor NKR-P1A

Deposition date:

2013-05-31

Original release date:

2014-06-09

Authors:

Chmelik, Josef; Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr

Citation:

Citation: Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr; Chmelik, Josef. "NMR structure of the lymphocyte receptor NKR-P1A reveals a different conformation of the conserved loop compared to crystal structure" .

Assembly members:

Assembly members:
NKR-P1A, polymer, 139 residues, 16008.889 Da.

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: pET-30a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NKR-P1A: SAKLECPQDWLSHRDKCFHV SQVSNTWEEGLVDCDGKGAT LMLIQDQEELRFLLDSIKEK YNSFWIGLRYTLPDMNWKWI NGSTLNSDVLKITGDTENDS CAAISGDKVTFESCNSDNRW ICQKELYHETLSNYVGYGH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	622
15N chemical shifts	157
1H chemical shifts	967

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	lymphocyte receptor NKR-P1A	1

Entities:

Entity 1, lymphocyte receptor NKR-P1A 139 residues - 16008.889 Da.

1

SER

ALA

LYS

LEU

GLU

CYS

PRO

GLN

ASP

TRP

2

LEU

SER

HIS

ARG

ASP

LYS

CYS

PHE

HIS

VAL

3

SER

GLN

VAL

SER

ASN

THR

TRP

GLU

GLY

4

LEU

VAL

ASP

CYS

ASP

GLY

LYS

GLY

ALA

THR

5

LEU

MET

LEU

ILE

GLN

ASP

GLN

GLU

LEU

6

ARG

PHE

LEU

ASP

SER

ILE

LYS

GLU

LYS

7

TYR

ASN

SER

PHE

TRP

ILE

GLY

LEU

ARG

TYR

8

THR

LEU

PRO

ASP

MET

ASN

TRP

LYS

TRP

ILE

9

ASN

GLY

SER

THR

LEU

ASN

SER

ASP

VAL

LEU

10

LYS

ILE

THR

GLY

ASP

THR

GLU

ASN

ASP

SER

11

CYS

ALA

ILE

SER

GLY

ASP

LYS

VAL

THR

12

PHE

GLU

SER

CYS

ASN

SER

ASP

ASN

ARG

TRP

13

ILE

CYS

GLN

LYS

GLU

LEU

TYR

HIS

GLU

THR

14

LEU

SER

ASN

TYR

VAL

GLY

TYR

GLY

HIS

Samples:

sample: NKR-P1A, [U-100% 13C; U-100% 15N], 0.5 mM; PIPES 15 mM; sodium chloride 50 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_conditions: pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample	isotropic	sample_conditions
2D 1H-13C HSQC aliphatic	sample	isotropic	sample_conditions
3D CBCA(CO)NH	sample	isotropic	sample_conditions
3D HNCACB	sample	isotropic	sample_conditions
3D HNCA	sample	isotropic	sample_conditions
3D HN(CO)CA	sample	isotropic	sample_conditions
3D HNCO	sample	isotropic	sample_conditions
3D HN(CA)CO	sample	isotropic	sample_conditions
3D H(CCO)NH	sample	isotropic	sample_conditions
3D (H)C(CO)NH	sample	isotropic	sample_conditions
3D HCCH-TOCSY aliphatic	sample	isotropic	sample_conditions
3D 1H-15N NOESY	sample	isotropic	sample_conditions
2D 1H-13C HSQC aromatic	sample	isotropic	sample_conditions
3D HCCH-TOCSY aromatic	sample	isotropic	sample_conditions
2D (HB)CB(CGCD)HD	sample	isotropic	sample_conditions
3D 1H-13C NOESY aliphatic	sample	isotropic	sample_conditions
3D 1H-13C NOESY aromatic	sample	isotropic	sample_conditions

Software:

TOPSPIN v2.3.6, Bruker Biospin - collection

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

SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

RECOORD, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CING, (CING) Vuister, Doreleijer, da Silva - validation

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2M94 2MTI 3M9Z 3T3A
EMBL	CAA45971 CAA45976
GB	AAA39366 AAA39822 AAI20708 AAI45046 AAK39101
REF	NP_001153374 NP_034867
SP	P27811
AlphaFold	P27811