BMRB Entry 16509

Name: Complement Repeats 16 17 and 18 from LRP-1
Published: 2010-02-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16509

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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:

Complement Repeats 16 17 and 18 from LRP-1

Deposition date:

2009-09-22

Original release date:

2010-02-02

Authors:

Guttman, Miklos; Komives, Elizabeth

Citation:

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).
PubMed: 20030366

Assembly members:

Assembly members:
CR1618, polymer, 129 residues, Formula weight is not available
CA, non-polymer, 40.078 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: pMMHB

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CR1618: GSNKFCSEAQFECQNHRCIS KQWLCDGSDDCGDGSDEAAH CEGKTCGPSSFSCPGTHVCV PERWLCDGDKDCADGADESI AAGCLYNSTCDDREFMCQNR QCIPKHFVCDHDRDCADGSD ESPECEYPT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	193
15N chemical shifts	101
1H chemical shifts	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CR1618	1
2	Calcium ion	2

Entities:

Entity 1, CR1618 129 residues - Formula weight is not available

There's an extra GS at the N terminus, from the expression vector.

1

GLY

SER

ASN

LYS

PHE

CYS

SER

GLU

ALA

GLN

2

PHE

GLU

CYS

GLN

ASN

HIS

ARG

CYS

ILE

SER

3

LYS

GLN

TRP

LEU

CYS

ASP

GLY

SER

ASP

4

CYS

GLY

ASP

GLY

SER

ASP

GLU

ALA

HIS

5

CYS

GLU

GLY

LYS

THR

CYS

GLY

PRO

SER

6

PHE

SER

CYS

PRO

GLY

THR

HIS

VAL

CYS

VAL

7

PRO

GLU

ARG

TRP

LEU

CYS

ASP

GLY

ASP

LYS

8

ASP

CYS

ALA

ASP

GLY

ALA

ASP

GLU

SER

ILE

9

ALA

GLY

CYS

LEU

TYR

ASN

SER

THR

CYS

10

ASP

ARG

GLU

PHE

MET

CYS

GLN

ASN

ARG

11

GLN

CYS

ILE

PRO

LYS

HIS

PHE

VAL

CYS

ASP

12

HIS

ASP

ARG

ASP

CYS

ALA

ASP

GLY

SER

ASP

13

GLU

SER

PRO

GLU

CYS

GLU

TYR

PRO

THR

Entity 2, Calcium ion - Ca - 40.078 Da.

1

CA

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.7 mM; sodium chloride 150 mM; sodium azide 3 mM; CA 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.6; pressure: 1 atm; temperature: 307 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

AZARA v2.7, Boucher - processing

FELIX v2000, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

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

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks