BMRB Entry 16482

Name: Solution Structure of complement repeat CR17 from LRP-1
Published: 2010-02-03

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PDB ID: 2knx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16482
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of complement repeat CR17 from LRP-1 PubMed: 20030366

Deposition date: 2009-09-07 Original release date: 2010-02-03

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, 50 residues, 5102.559 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: GSEGKTCGPSSFSCPGTHVC VPERWLCDGDKDCADGADES IAAGCLYNST

Data sets:

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

Data type	Count
13C chemical shifts	169
15N chemical shifts	40
1H chemical shifts	275
heteronuclear NOE values	28
T1 relaxation values	28
T2 relaxation values	28

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, CR17 50 residues - 5102.559 Da.

Extra GS at N terminus, so residue 3 is 2751 of LRP1

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

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1

CA

Samples:

sample_1: sodium chloride 150 mM; HEPES, [U-99% 2H], 20 mM; entity_1, [U-99% 13C; U-99% 15N], 0.7 mM; CALCIUM ION 5 mM; sodium azide 3 mM; H2O 90%; D2O 10%

sample_2: sodium chloride 150 mM; HEPES, [U-99% 2H], 20 mM; entity_1, [U-99% 15N], 0.6 mM; CALCIUM ION 5 mM; sodium azide 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.45; pressure: 1 atm; temperature: 307 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_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

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

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

AZARA v2.7, Boucher - processing

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

NMR spectrometers:

Bruker Avance 600 MHz

Biological Magnetic Resonance Data Bank