BMRB Entry 34336

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34336
MolProbity Validation Chart

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Title:
Structural and functional insights into the condensin ATPase cycle
Deposition date:
2018-12-10
Original release date:
2019-06-27
Authors:
Simon, B.; Hassler, M.; Haering, C.; Hennig, J.
Citation:

Citation: Hassler, Markus; Shaltiel, Indra; Kschonsak, Marc; Simon, Bernd; Merkel, Fabian; Tharichen, Lena; Bailey, Henry; Macosek, Jakub; Bravo, Sol; Metz, Jutta; Hennig, Janosch; Haering, Christian. "Structural Basis of an Asymmetric Condensin ATPase Cycle."  Mol. Cell 74, 1175-1188 (2019).
PubMed: 31226277

Assembly members:

Assembly members:
entity_1, polymer, 221 residues, 25200.189 Da.

Natural source:

Natural source:   Common Name: Chaetomium thermophilum   Taxonomy ID: 209285   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Chaetomium thermophilum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMRAVTPMKRVPILANFEE WMKMATDNKINAANSWNFAL IDYFHDMSLLKEGDSVNFQK ASCTLDGCVKIYTSRVDSVA TETGKLLSGLADSRDSKKKD REDGGGSGGSLRKKINPKVM NMIDSVEKKEMSLKHMMKTV LKDKHKIEETIATLDEYKRK ASGGSAGTRMFEDRKEKALK TMAKKDLKLQEITELLRDEI EPKLEKLRQEKRAFLDFQQT Q

Data sets:
Data typeCount
13C chemical shifts695
15N chemical shifts224
1H chemical shifts1266

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 221 residues - 25200.189 Da.

1   GLYHISMETARGALAVALTHRPROMETLYS
2   ARGVALPROILELEUALAASNPHEGLUGLU
3   TRPMETLYSMETALATHRASPASNLYSILE
4   ASNALAALAASNSERTRPASNPHEALALEU
5   ILEASPTYRPHEHISASPMETSERLEULEU
6   LYSGLUGLYASPSERVALASNPHEGLNLYS
7   ALASERCYSTHRLEUASPGLYCYSVALLYS
8   ILETYRTHRSERARGVALASPSERVALALA
9   THRGLUTHRGLYLYSLEULEUSERGLYLEU
10   ALAASPSERARGASPSERLYSLYSLYSASP
11   ARGGLUASPGLYGLYGLYSERGLYGLYSER
12   LEUARGLYSLYSILEASNPROLYSVALMET
13   ASNMETILEASPSERVALGLULYSLYSGLU
14   METSERLEULYSHISMETMETLYSTHRVAL
15   LEULYSASPLYSHISLYSILEGLUGLUTHR
16   ILEALATHRLEUASPGLUTYRLYSARGLYS
17   ALASERGLYGLYSERALAGLYTHRARGMET
18   PHEGLUASPARGLYSGLULYSALALEULYS
19   THRMETALALYSLYSASPLEULYSLEUGLN
20   GLUILETHRGLULEULEUARGASPGLUILE
21   GLUPROLYSLEUGLULYSLEUARGGLNGLU
22   LYSARGALAPHELEUASPPHEGLNGLNTHR
23   GLN

Samples:

sample_1: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N], 0.8 mM

sample_2: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N], 0.6 mM

sample_3: Ct Smc2 Brn1 fusion protein, [U-100% 13C; U-100% 15N; U-100% 2H], 0.4 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HN(COCA)CBsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - structure calculation

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 600 MHz

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