BMRB Entry 10120

Name: Solution structure of immunoglobulin like domain of mouse nuclear lamin
Published: 2008-09-02

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PDB ID: 1ufg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10120
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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:

Solution structure of immunoglobulin like domain of mouse nuclear lamin

Deposition date:

2007-04-02

Original release date:

2008-09-02

Authors:

Kobayashi, N.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Kobayashi, N.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of immunoglobulin like domain of mouse nuclear lamin" .

Assembly members:

Assembly members:
C-terminal immunoglobulin like domain, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P011206-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C-terminal immunoglobulin like domain: GSSGSSGQSQGGGSVTKKRK LESSESRSSFSQHARTSGRV AVEEVDEEGKFVRLRNKSNE DQSMGNWQIRRQNGDDPLMT YRFPPKFTLKAGQVVTIWAS GAGATHSPPTDLVWKAQNTW GCGSSLRTALINSTGEEVAM RKLVRSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	568
15N chemical shifts	158
1H chemical shifts	922

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lamin A	1

Entities:

Entity 1, Lamin A 151 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

SER

GLN

2

GLY

SER

VAL

THR

LYS

ARG

LYS

3

LEU

GLU

SER

GLU

SER

ARG

SER

PHE

4

SER

GLN

HIS

ALA

ARG

THR

SER

GLY

ARG

VAL

5

ALA

VAL

GLU

VAL

ASP

GLU

GLY

LYS

6

PHE

VAL

ARG

LEU

ARG

ASN

LYS

SER

ASN

GLU

7

ASP

GLN

SER

MET

GLY

ASN

TRP

GLN

ILE

ARG

8

ARG

GLN

ASN

GLY

ASP

PRO

LEU

MET

THR

9

TYR

ARG

PHE

PRO

LYS

PHE

THR

LEU

LYS

10

ALA

GLY

GLN

VAL

THR

ILE

TRP

ALA

SER

11

GLY

ALA

GLY

ALA

THR

HIS

SER

PRO

THR

12

ASP

LEU

VAL

TRP

LYS

ALA

GLN

ASN

THR

TRP

13

GLY

CYS

GLY

SER

LEU

ARG

THR

ALA

LEU

14

ILE

ASN

SER

THR

GLY

GLU

VAL

ALA

MET

15

ARG

LYS

LEU

VAL

ARG

SER

GLY

PRO

SER

16

GLY

Samples:

sample_1: lamin, [U-13C; U-15N], 0.88 mM; phosphate 20 mM; NaCl 100 mM; d10-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

sample_2: lamin, [U-13C; U-15N], 0.70 mM; phosphate 20 mM; NaCl 100 mM; d10-DTT 1 mM; NaN3 0.02%; D2O 100%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY 1	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY 2	sample_2	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v2002045, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.816, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1UFG
DBJ	BAA02476 BAA03578 BAA08569 BAA08570 BAA08571
GB	AAH15302 AAH94020 ABI16251 ABI16252 EDL15275
REF	NP_001002011 NP_001104572 NP_062263 XP_003502967 XP_005080182
SP	P48678
AlphaFold	P48678