BMRBj - BMREntryMaster

Found 1 Document (0.578 seconds)

BMRB: 34336

6Q6E

Structural and functional insights into the condensin ATPase cycle

Authors

Simon, B., Hassler, M., Haering, C.H., Hennig, J.

Assembly

Condensin complex subunit 2, Structural maintenance of chromosomes protein

Entity

1. Condensin complex subunit 2, Structural maintenance of chromosomes protein (polymer), 221 monomers, 25152.77 Da Detail

GHMRAVTPMK RVPILANFEE WMKMATDNKI NAANSWNFAL IDYFHDMSLL KEGDSVNFQK ASCTLDGCVK IYTSRVDSVA TETGKLLSGL ADSRDSKKKD REDGGGSGGS LRKKINPKVM NMIDSVEKKE MSLKHMMKTV LKDKHKIEET IATLDEYKRK ASGGSAGTRM FEDRKEKALK TMAKKDLKLQ EITELLRDEI EPKLEKLRQE KRAFLDFQQT Q

Formula weight

25152.77 Da

Source organism

Chaetomium thermophilum

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.1 %, Completeness: 77.1 %, Completeness (bb): 81.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	77.1 % (2031 of 2634)	77.1 % (1073 of 1392)	72.5 % (732 of 1009)	97.0 % (226 of 233)
Backbone	81.6 % (1076 of 1318)	92.5 % (417 of 451)	69.1 % (449 of 650)	96.8 % (210 of 217)
Sidechain	75.9 % (1156 of 1524)	69.7 % (656 of 941)	85.4 % (484 of 567)	100.0 % (16 of 16)
Aromatic	61.2 % (82 of 134)	64.2 % (43 of 67)	56.9 % (37 of 65)	100.0 % (2 of 2)
Methyl	98.6 % (209 of 212)	98.1 % (104 of 106)	99.1 % (105 of 106)

1. entity 1

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.8 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.8 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.6 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.6 mM

Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.4 mM [U-100% 13C; U-100% 15N;U-100% 2H] Ct Smc2 Brn1 fusion protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
3	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N; U-100% 2H]		0.4 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.773 ppm	internal	indirect	0.2514495
¹H	water	protons	4.773 ppm	internal	direct	1.0
¹⁵N	water	protons	4.773 ppm	internal	indirect	0.1013291

Referencing offset: -0.07 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.773 ppm	internal	indirect	0.2514495
¹H	water	protons	4.773 ppm	internal	direct	1.0
¹⁵N	water	protons	4.773 ppm	internal	indirect	0.1013291

Referencing offset: -0.07 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.773 ppm	internal	indirect	0.2514495
¹H	water	protons	4.773 ppm	internal	direct	1.0
¹⁵N	water	protons	4.773 ppm	internal	indirect	0.1013291

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 6Q6E, Strand ID: A Detail

Release date

2019-04-29

Citation

Structural Basis of an Asymmetric Condensin ATPase Cycle
Hassler, M., Shaltiel, I.A., Kschonsak, M., Simon, B., Merkel, F., Tharichen, L., Bailey, H.J., Macosek, J., Bravo, S., Metz, J., Hennig, J., Haering, C.H.
Mol. Cell (2019), 74, 1175-1188, PubMed 31226277 , DOI 10.1016/j.molcel.2019.03.037 , Abstract

Related entities 1. Condensin complex subunit 2, Structural maintenance of chromosomes protein, : 1 entities Detail

Experiments performed 8 experiments Detail

1 3D HNCA

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.4 mM [U-100% 13C; U-100% 15N;U-100% 2H] Ct Smc2 Brn1 fusion protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
3	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N; U-100% 2H]		0.4 mM

2 3D HNCACB

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
3	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N; U-100% 2H]		0.4 mM

3 3D HN(CO)CA

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
3	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N; U-100% 2H]		0.4 mM

4 3D HN(COCA)CB

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
3	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N; U-100% 2H]		0.4 mM

5 3D 1H-15N NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.8 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.8 mM

6 3D 1H-13C NOESY aliphatic

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.8 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.8 mM

7 3D 1H-13C NOESY aromatic

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.6 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.6 mM

8 3D 1H-13C NOESY aliphatic

Instrument

Bruker AvanceIII - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.6 mM [U-100% 13C; U-100% 15N] Ct Smc2 Brn1 fusion protein, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	Ct Smc2 Brn1 fusion protein	[U-100% 13C; U-100% 15N]		0.6 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34336_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr34336_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	2185		98.6 (chain: 1, length: 221)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 221, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 1266
  - ¹³C chemical shifts: 695
  - ¹⁵N chemical shifts: 224
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1392	1036	74.4
¹³C chemical shifts	1009	695	68.9
¹⁵N chemical shifts	245	224	91.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	451	421	93.3
¹³C chemical shifts	442	215	48.6
¹⁵N chemical shifts	217	208	95.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	941	615	65.4
¹³C chemical shifts	567	480	84.7
¹⁵N chemical shifts	28	16	57.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	118	115	97.5
¹³C chemical shifts	118	115	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	67	43	64.2
¹³C chemical shifts	65	37	56.9
¹⁵N chemical shifts	2	2	100.0

Keywords Condensin, SMC protein complex, cohesin, structural protein

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Found 1 Document (0.578 seconds)

BMRB: 34336

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Condensin complex subunit 2, Structural maintenance of chromosomes protein, : 1 entities Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail