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Biological Magnetic Resonance Data Bank


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BMRB Entry 19989

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PDB ID:
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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Title: Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1   PubMed: 25450766

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: 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).

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

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

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

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

Data sets:
Data typeCount
1H chemical shifts576
13C chemical shifts225
15N chemical shifts74

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 74 residues - 8381.003 Da.

1   GLYPROALASERVALPROTHRTHRCYSCYS
2   PHEASNLEUALAASNARGLYSILEPROLEU
3   GLNARGLEUGLUSERTYRARGARGILETHR
4   SERGLYLYSCYSPROGLNLYSALAVALILE
5   PHELYSTHRLYSLEUALALYSASPILECYS
6   ALAASPPROLYSLYSLYSTRPVALGLNASP
7   SERMETLYSTYRLEUASPGLNLYSSERPRO
8   THRPROLYSPRO

Entity 2, entity_2 16 residues - 1940.029 Da.

1   VALGLUTHRPHEGLYTHRTHRSERTYSTYS
2   ASPASPVALGLYLEULEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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

Related Database Links:

BMRB 4155 4390
PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts