BMRB Entry 16572

Name: NMR solution structure of Lamin-B1 protein from Home sapiens: Northeast Structural Genomics Consortium target, HR5546A(438-548)
Published: 2009-10-22

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PDB ID: 2kpw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16572
MolProbity Validation Chart

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

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Title:

NMR solution structure of Lamin-B1 protein from Home sapiens: Northeast Structural Genomics Consortium target, HR5546A(438-548)

Deposition date:

2009-10-21

Original release date:

2009-10-22

Authors:

Swapna, G. V. T.; Montelione, Gaetano

Citation:

Citation: Swapna, G. V. T.; Ciccosanti, Colleen; Belote, Rachel; Hamilton, Keith; Acton, Thomas; Huang, Y; Xiao, Rong; Everett, John; Montelione, Gaetano. "NMR solution structure of Lamin-B1 protein from Home sapiens: Northeast Structural Genomics Consortium target, HR5546A(438-548)" To be Published ., .-..

Assembly members:

Assembly members:
Lamin-B1_protein, polymer, 122 residues, 13672.427 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: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lamin-B1_protein: MGHHHHHHSHMTGNVCIEEI DVDGKFIRLKNTSEQDQPMG GWEMIRKIGDTSVSYKYTSR YVLKAGQTVTIWAANAGVTA SPPTDLIWKNQNSWGTGEDV KVILKNSQGEEVAQRSTVFK TT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shift_list_1

Data type	Count
13C chemical shifts	398
15N chemical shifts	134
1H chemical shifts	824

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lamin-B1_protein	1

Entities:

Entity 1, Lamin-B1_protein 122 residues - 13672.427 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

THR

GLY

ASN

VAL

CYS

ILE

GLU

ILE

3

ASP

VAL

ASP

GLY

LYS

PHE

ILE

ARG

LEU

LYS

4

ASN

THR

SER

GLU

GLN

ASP

GLN

PRO

MET

GLY

5

GLY

TRP

GLU

MET

ILE

ARG

LYS

ILE

GLY

ASP

6

THR

SER

VAL

SER

TYR

LYS

TYR

THR

SER

ARG

7

TYR

VAL

LEU

LYS

ALA

GLY

GLN

THR

VAL

THR

8

ILE

TRP

ALA

ASN

ALA

GLY

VAL

THR

ALA

9

SER

PRO

THR

ASP

LEU

ILE

TRP

LYS

ASN

10

GLN

ASN

SER

TRP

GLY

THR

GLY

GLU

ASP

VAL

11

LYS

VAL

ILE

LEU

LYS

ASN

SER

GLN

GLY

GLU

12

GLU

VAL

ALA

GLN

ARG

SER

THR

VAL

PHE

LYS

13

THR

Samples:

HR5546A_sample_1: Lamin-B1 protein, [U-100% 13C; U-100% 15N], 1.219 ± 0.20 mM; NH4OAc 20 mM; DTT 100 mM; NaCl 200 mM; CaCl2 5 mM

HR5546A_sample_2: Lamin-B1 protein, [U-5% 13C; U-100% 15N], 1.219 ± 0.20 mM; NH4OAc 20 mM; DTT 100 mM; NaCl 200 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 205 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 205 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	HR5546A_sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	HR5546A_sample_1	isotropic	sample_conditions_1
3D HNCACB	HR5546A_sample_1	isotropic	sample_conditions_1
3D GFT CBCA(CO)NH	HR5546A_sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	HR5546A_sample_1	isotropic	sample_conditions_1
3D HNCO	HR5546A_sample_1	isotropic	sample_conditions_1
3D HNHA	HR5546A_sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	HR5546A_sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	HR5546A_sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aro	HR5546A_sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	HR5546A_sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	HR5546A_sample_2	isotropic	sample_conditions_2
2D HNOE	HR5546A_sample_2	isotropic	sample_conditions_2
3D (H)CCH-TOCSY	HR5546A_sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	HR5546A_sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliph	HR5546A_sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	HR5546A_sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	HR5546A_sample_1	isotropic	sample_conditions_1
3D GFT HNCACB	HR5546A_sample_1	isotropic	sample_conditions_1

Software:

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AVS, Moseley and Montelione - chemical shift assignment validation

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v2.3, Goddard - data analysis, peak picking

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TOPSPIN v2.1, Bruker Biospin - collection

VNMRJ v2.1, Varian - collection

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2KPW
DBJ	BAA08784 BAK63580
EMBL	CAA34677
GB	AAB09600 AAC96023 AAH52729 AAH58392 EDL09872
REF	NP_001267370 NP_034851 NP_446357 XP_003259953 XP_003477267
SP	P14733 P70615
AlphaFold	P14733 P70615