BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16572

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: 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:
Lamin-B1_protein, polymer, 122 residues, 13672.427 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):
Lamin-B1_protein: MGHHHHHHSHMTGNVCIEEI DVDGKFIRLKNTSEQDQPMG GWEMIRKIGDTSVSYKYTSR YVLKAGQTVTIWAANAGVTA SPPTDLIWKNQNSWGTGEDV KVILKNSQGEEVAQRSTVFK TT

Data sets:
Data typeCount
13C chemical shifts398
15N chemical shifts134
1H chemical shifts824

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lamin-B1_protein1

Entities:

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

1   METGLYHISHISHISHISHISHISSERHIS
2   METTHRGLYASNVALCYSILEGLUGLUILE
3   ASPVALASPGLYLYSPHEILEARGLEULYS
4   ASNTHRSERGLUGLNASPGLNPROMETGLY
5   GLYTRPGLUMETILEARGLYSILEGLYASP
6   THRSERVALSERTYRLYSTYRTHRSERARG
7   TYRVALLEULYSALAGLYGLNTHRVALTHR
8   ILETRPALAALAASNALAGLYVALTHRALA
9   SERPROPROTHRASPLEUILETRPLYSASN
10   GLNASNSERTRPGLYTHRGLYGLUASPVAL
11   LYSVALILELEULYSASNSERGLNGLYGLU
12   GLUVALALAGLNARGSERTHRVALPHELYS
13   THRTHR

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR5546A_sample_1isotropicsample_conditions_1
2D 1H-13C HSQCHR5546A_sample_1isotropicsample_conditions_1
3D HNCACBHR5546A_sample_1isotropicsample_conditions_1
3D GFT CBCA(CO)NHHR5546A_sample_1isotropicsample_conditions_1
3D HBHA(CO)NHHR5546A_sample_1isotropicsample_conditions_1
3D HNCOHR5546A_sample_1isotropicsample_conditions_1
3D HNHAHR5546A_sample_1isotropicsample_conditions_1
3D HCCH-TOCSYHR5546A_sample_1isotropicsample_conditions_1
3D 1H-15N NOESYHR5546A_sample_1isotropicsample_conditions_1
3D 1H-13C NOESY aroHR5546A_sample_1isotropicsample_conditions_1
2D 1H-15N HSQCHR5546A_sample_2isotropicsample_conditions_2
2D 1H-13C HSQCHR5546A_sample_2isotropicsample_conditions_2
2D HNOEHR5546A_sample_2isotropicsample_conditions_2
3D (H)CCH-TOCSYHR5546A_sample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYHR5546A_sample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphHR5546A_sample_2isotropicsample_conditions_1
2D 1H-15N HSQCHR5546A_sample_2isotropicsample_conditions_1
3D CBCA(CO)NHHR5546A_sample_1isotropicsample_conditions_1
3D GFT HNCACBHR5546A_sample_1isotropicsample_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

Related Database Links:

PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts