BMRB Entry 19753

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19753
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

Title:
Solution NMR Structure plectin repeat domain 6 (4403-4606) of Plectin from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR6354E
Deposition date:
2014-01-24
Original release date:
2014-02-24
Authors:
Pulavarti, Surya VSRK; Eletsky, Alexander; Huang, Yuanpeng; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Pulavarti, Surya VSRK; Eletsky, Alexander; Huang, Yuanpeng; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure plectin repeat domain 6 (4403-4606) of Plectin from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR6354E"  .

Assembly members:

Assembly members:
Plectin, polymer, 215 residues, 23730 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: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Plectin: MGHHHHHHSHMQLASWSDPT EETGPVAGILDTETLEKVSI TEAMHRNLVDNITGQRLLEA QACTGGIIDPSTGERFPVTD AVNKGLVDKIMVDRINLAQK AFCGFEDPRTKTKMSAAQAL KKGWLYYEAGQRFLEVQYLT GGLIEPDTPGRVPLDEALQR GTVDARTAQKLRDVGAYSKY LTCPKTKLKISYKDALDRSM VEEGTGLRLLEAAAQ

Data sets:
Data typeCount
13C chemical shifts662
15N chemical shifts195
1H chemical shifts483

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Plectin repeat domain 61

Entities:

Entity 1, Plectin repeat domain 6 215 residues - 23730 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METGLNLEUALASERTRPSERASPPROTHR
3   GLUGLUTHRGLYPROVALALAGLYILELEU
4   ASPTHRGLUTHRLEUGLULYSVALSERILE
5   THRGLUALAMETHISARGASNLEUVALASP
6   ASNILETHRGLYGLNARGLEULEUGLUALA
7   GLNALACYSTHRGLYGLYILEILEASPPRO
8   SERTHRGLYGLUARGPHEPROVALTHRASP
9   ALAVALASNLYSGLYLEUVALASPLYSILE
10   METVALASPARGILEASNLEUALAGLNLYS
11   ALAPHECYSGLYPHEGLUASPPROARGTHR
12   LYSTHRLYSMETSERALAALAGLNALALEU
13   LYSLYSGLYTRPLEUTYRTYRGLUALAGLY
14   GLNARGPHELEUGLUVALGLNTYRLEUTHR
15   GLYGLYLEUILEGLUPROASPTHRPROGLY
16   ARGVALPROLEUASPGLUALALEUGLNARG
17   GLYTHRVALASPALAARGTHRALAGLNLYS
18   LEUARGASPVALGLYALATYRSERLYSTYR
19   LEUTHRCYSPROLYSTHRLYSLEULYSILE
20   SERTYRLYSASPALALEUASPARGSERMET
21   VALGLUGLUGLYTHRGLYLEUARGLEULEU
22   GLUALAALAALAGLN

Samples:

sample_1: Plectin, [U-100% 13C; U-100% 15N; U-2H; ILV-1H], 1 mM; MES pH 6.5 20 mM; NaCL 100 mM; CaCL2 5 mM; DTT 10 mM; NaN3 0.02%; Proteinase Inhibitors 1 ratio; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D ct [13C,1H] HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(COCA)CBsample_1isotropicsample_conditions_1
3D HMCM[CG]CBCAsample_1isotropicsample_conditions_1
3D HMCMCBCAsample_1isotropicsample_conditions_1
3D [H]-NOESY-[NH/CH] ( mix= 250 ms)sample_1isotropicsample_conditions_1

Software:

vnmrj, Varian - Data collection

prosa, Guntert - processing

CARA, Keller and Wuthrich - data analysis

autoassign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI, CSI (Wishart and Sykes) - Secondary structure analysis

TALOS+, (TALOS+) -Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

uniprot Q15149
PDB
AlphaFold Q6S383

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks