BMRB Entry 19989

Name: Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1
Published: 2014-12-08

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PDB ID: 2mpm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19989
MolProbity Validation Chart

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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:

Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1

Deposition date:

2014-05-26

Original release date:

2014-12-08

Authors:

Millard, Christopher; Ludeman, Justin; Canals, Meritxell; Bridgford, Jessica; Hinds, Mark; Clayton, Daniel; Christopoulos, Arthur; Payne, Richard; Stone, Martin

Citation:

Citation: Millard, Christopher; Ludeman, Justin; Canals, Meritxell; Bridgford, Jessica; Hinds, Mark; Clayton, Daniel; Christopoulos, Arthur; Payne, Richard; Stone, Martin. "Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: The N-Terminal Region of CCR3 Bound to CCL11/Eotaxin-1" Structure 22, 1571-1581 (2014).
PubMed: 25450766

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, 8381.003 Da.
entity_2, polymer, 16 residues, 1940.029 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPASVPTTCCFNLANRKIPL QRLESYRRITSGKCPQKAVI FKTKLAKDICADPKKKWVQD SMKYLDQKSPTPKP
entity_2: VETFGTTSXXDDVGLL

Data sets:

assigned_chemical_shifts
- Chemical_Shifts

Data type	Count
1H chemical shifts	576
13C chemical shifts	225
15N chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 74 residues - 8381.003 Da.

1

GLY

PRO

ALA

SER

VAL

PRO

THR

CYS

2

PHE

ASN

LEU

ALA

ASN

ARG

LYS

ILE

PRO

LEU

3

GLN

ARG

LEU

GLU

SER

TYR

ARG

ILE

THR

4

SER

GLY

LYS

CYS

PRO

GLN

LYS

ALA

VAL

ILE

5

PHE

LYS

THR

LYS

LEU

ALA

LYS

ASP

ILE

CYS

6

ALA

ASP

PRO

LYS

TRP

VAL

GLN

ASP

7

SER

MET

LYS

TYR

LEU

ASP

GLN

LYS

SER

PRO

8

THR

PRO

LYS

PRO

Entity 2, entity_2 16 residues - 1940.029 Da.

1

VAL

GLU

THR

PHE

GLY

THR

SER

TYS

2

ASP

VAL

GLY

LEU

Samples:

sample_1: CCL11/Eotaxin-1, [U-100% 13C; U-100% 15N], 0.2 – 0.4 mM; CCR3 Su1617 sulfopeptide0.2 – 0.4 mM; H2O 95%; D2O, [U-100% 2H], 5%; sodium acetate-d6, [U-100% 2H], 20 mM; sodium azide 0.02%; DSS 20 uM

sample_conditions_1: temperature: 313 K; pH: 7.0; pressure: 1 atm; ionic strength: 20 mM

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

SPARKY v3.92, Goddard - peak picking, chemical shift assignment, chemical shift calculation

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

CANDID v2.1, Herrmann, Guntert and Wuthrich - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization, structure solution

X-PLOR_NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

AQUA, Rullmann, Doreleijers and Kaptein - refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - refinement, structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 600 MHz

BMRB	4155 4390
PDB	1EOT 2EOT 2MPM
DBJ	BAA08370 BAG72995
EMBL	CAA99997 CAA99998 CAB07027 CAG33702
GB	AAA98957 AAC50369 AAC51297 AAH17850 ABK41951
PRF	2208449A
REF	NP_002977 XP_002827294 XP_003818054 XP_004041989 XP_004041990
SP	P51671
AlphaFold	P51671