BMRB Entry 19798

Name: Solution Structure of 6aJL2-R24G Amyloidogenic Light Chain Protein
Published: 2014-06-16

Click here to enlarge.

PDB ID: 2mkw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19798
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution Structure of 6aJL2-R24G Amyloidogenic Light Chain Protein

Deposition date:

2014-02-13

Original release date:

2014-06-16

Authors:

Maya, Roberto; Gil, Paloma; Amero, Carlos

Citation:

Citation: Maya, Roberto; Gil, Paloma; Amero, Carlos. "Solution Structure of 6aJL2 and 6aJL2-R24G Amyloidogenic Light Chain Proteins" .

Assembly members:

Assembly members:
entity, polymer, 111 residues, 11861.857 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: pET27

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: NFMLTQPHSVSESPGKTVTI SCTGSSGSIASNYVQWYQQR PGSSPTTVIYEDNQRPSGVP DRFSGSIDSSSNSASLTISG LKTEDEADYYCQSYDSSNHV VFGGGTKLTVL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
1H chemical shifts	677
15N chemical shifts	104
13C chemical shifts	392

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	6aJL2-R24G Amyloidogenic Light Chain Protein	1

Entities:

Entity 1, 6aJL2-R24G Amyloidogenic Light Chain Protein 111 residues - 11861.857 Da.

1

ASN

PHE

MET

LEU

THR

GLN

PRO

HIS

SER

VAL

2

SER

GLU

SER

PRO

GLY

LYS

THR

VAL

THR

ILE

3

SER

CYS

THR

GLY

SER

GLY

SER

ILE

ALA

4

SER

ASN

TYR

VAL

GLN

TRP

TYR

GLN

ARG

5

PRO

GLY

SER

PRO

THR

VAL

ILE

TYR

6

GLU

ASP

ASN

GLN

ARG

PRO

SER

GLY

VAL

PRO

7

ASP

ARG

PHE

SER

GLY

SER

ILE

ASP

SER

8

SER

ASN

SER

ALA

SER

LEU

THR

ILE

SER

GLY

9

LEU

LYS

THR

GLU

ASP

GLU

ALA

ASP

TYR

10

CYS

GLN

SER

TYR

ASP

SER

ASN

HIS

VAL

11

VAL

PHE

GLY

THR

LYS

LEU

THR

VAL

12

LEU

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.8 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 75 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 75 mM; pH: 7.4; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR_NIH v2.33, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

CARA v1.8.4, Keller and Wuthrich - data analysis

NMR spectrometers:

Varian Uniform NMR System 700 MHz

BMRB	15276 19870
PDB	2MKW 2MMX 2W0K 2W0L 3B5G 3BDX 5C9K
DBJ	BAA19991 BAC01822 BAC01823 BAC01824 BAC01857
EMBL	CAD43014 CAJ75494 CAJ75495 CAP74492 CAP74493
GB	AAB33217 AAG24687 AAG24691 AAG47681 AAM46210