BMRB Entry 16483

Name: Fusion construct of CR17 from LRP-1 and ApoE residues 130-149
Published: 2010-02-02

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PDB ID: 2kny
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16483
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Fusion construct of CR17 from LRP-1 and ApoE residues 130-149 PubMed: 20030366

Deposition date: 2009-09-08 Original release date: 2010-02-02

Authors: Guttman, Miklos; Komives, Elizabeth

Citation: Guttman, Miklos; Prieto, J. Helena; Croy, Johnny; Komives, Elizabeth. "Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E." Biochemistry 49, 1207-1216 (2010).

Assembly members:
CR17, polymer, 80 residues, 8399.479 Da.
apoE, polymer, 23 residues, 8399.479 Da.
CA, non-polymer, 40.078 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):
CR17: GSKLEGKTCGPSSFSCPGTH VCVPERWLCDGDKDCADGAD ESIAAGCLYNSTGSGSGSGS TEELRVRLASHLRKLRKRLL
apoE: GSYTEELRVRLASHLRKLRK RLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2
heteronucl_NOEs
- heteronuclear_noe_list_1
- heteronuclear_noe_list_2
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	89
1H chemical shifts	651
heteronuclear NOE values	60
T1 relaxation values	46
T2 relaxation values	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CR17	1
2	ApoE	2
3	CALCIUM ION	3

Entities:

Entity 1, CR17 80 residues - 8399.479 Da.

Residues 3-50 correspond to mature human LRP-1 (2751-2798), followed by an 8 residue linker (GSGSGSGS) and human mature ApoE residues 130-149

1	GLY	SER	LYS	LEU	GLU	GLY	LYS	THR	CYS	GLY
2	PRO	SER	SER	PHE	SER	CYS	PRO	GLY	THR	HIS
3	VAL	CYS	VAL	PRO	GLU	ARG	TRP	LEU	CYS	ASP
4	GLY	ASP	LYS	ASP	CYS	ALA	ASP	GLY	ALA	ASP
5	GLU	SER	ILE	ALA	ALA	GLY	CYS	LEU	TYR	ASN
6	SER	THR	GLY	SER	GLY	SER	GLY	SER	GLY	SER
7	THR	GLU	GLU	LEU	ARG	VAL	ARG	LEU	ALA	SER
8	HIS	LEU	ARG	LYS	LEU	ARG	LYS	ARG	LEU	LEU

Entity 2, ApoE 23 residues - 8399.479 Da.

N terminal GSY overhang from expression vector followed by human mature apoE residues 130-149

1

GLY

SER

TYR

THR

GLU

LEU

ARG

VAL

ARG

2

LEU

ALA

SER

HIS

LEU

ARG

LYS

LEU

ARG

LYS

3

ARG

LEU

Entity 3, CALCIUM ION - Ca - 40.078 Da.

1

CA

Samples:

sample_1: HEPES, [U-99% 2H], 20 mM; sodium chloride 50 mM; sodium azide 3 mM; CALCIUM ION 5 mM; entity_1, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: HEPES, [U-99% 2H], 20 mM; sodium chloride 50 mM; sodium azide 3 mM; CALCIUM ION 5 mM; entity_1, [U-99% 13C; U-99% 15N], 0.8 mM; D2O 100%

sample_3: HEPES, [U-99% 2H], 20 mM; sodium chloride 50 mM; sodium azide 3 mM; CALCIUM ION 5 mM; entity_1, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_4: HEPES, [U-99% 2H], 20 mM; sodium chloride 150 mM; sodium azide 3 mM; EDTA, [U-99% 2H], 2 mM; entity_2, [U-99% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_5: HEPES, [U-99% 2H], 20 mM; sodium chloride 150 mM; sodium azide 3 mM; EDTA, [U-99% 2H], 2 mM; entity_2, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.45; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.15 M; pH: 7.45; pressure: 1 atm; temperature: 298 K

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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_5	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_5	isotropic	sample_conditions_2
3D HNCO	sample_5	isotropic	sample_conditions_2
3D HCCH-COSY	sample_5	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_2

Software:

AZARA v2.7, Boucher - processing

ARIA v2.2, Linge, O, . - chemical shift assignment, refinement

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMRPipe, Goddard - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - refinement

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

NMR spectrometers:

Bruker Avance 600 MHz

Biological Magnetic Resonance Data Bank