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 18053

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PDB ID:
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/BMR18053
MolProbity Validation Chart

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Title: Solution NMR structure of C-terminal globular domain of human Lamin-B2. Northeast Structural Genomics Consortium target HR8546A.

Deposition date: 2011-11-11 Original release date: 2011-12-06

Authors: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Xu, Chao; Min, Jinrong; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Xu, Chao; Min, Jinrong; Arrowsmith, Cheryl. "NMR solution structure of c-terminal globular domain of human Lamin-B2."  Not known ., .-..

Assembly members:
hs499, polymer, 139 residues, 13275.984 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):
hs499: MHHHHHHSSGRENLYFQGSA SGSVSIEEIDLEGKFVQLKN NSDKDQSLGNWRIKRQVLEG EEIAYKFTPKYILRAGQMVT VWAAGAGVAHSPPSTLVWKG QSSWGTGESFRTVLVNADGE EVAMRTVKKSSVMRENENG

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts130
1H chemical shifts779

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hs4991

Entities:

Entity 1, hs499 139 residues - 13275.984 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYSERALA
3   SERGLYSERVALSERILEGLUGLUILEASP
4   LEUGLUGLYLYSPHEVALGLNLEULYSASN
5   ASNSERASPLYSASPGLNSERLEUGLYASN
6   TRPARGILELYSARGGLNVALLEUGLUGLY
7   GLUGLUILEALATYRLYSPHETHRPROLYS
8   TYRILELEUARGALAGLYGLNMETVALTHR
9   VALTRPALAALAGLYALAGLYVALALAHIS
10   SERPROPROSERTHRLEUVALTRPLYSGLY
11   GLNSERSERTRPGLYTHRGLYGLUSERPHE
12   ARGTHRVALLEUVALASNALAASPGLYGLU
13   GLUVALALAMETARGTHRVALLYSLYSSER
14   SERVALMETARGGLUASNGLUASNGLY

Samples:

sample_1: hs499, [U-13C; U-15N], 0.5 mM; sodium phosphate 10 mM; sodium chloride 450 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 1 mM

sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAH06551 AAP36109 AAP88888 AAX29566 AAX42107
REF NP_116126 XP_004059772 XP_011526680 XP_011526681
SP Q03252

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