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- PDB-8bw1: Yeast 20S proteasome in complex with an engineered fellutamide de... -

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Basic information

Entry
Database: PDB / ID: 8bw1
TitleYeast 20S proteasome in complex with an engineered fellutamide derivative (C14QAL)
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / Proteasome / semisynthesis / Inhibitor / Binding Analysis
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
Similarity search - Function
Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site ...Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
MYRISTIC ACID / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 ...MYRISTIC ACID / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsBozhueyuek, K.A.J. / Praeve, L. / Kegler, C. / Kaiser, S. / Shi, Y. / Kuttenlochner, W. / Schenk, L. / Groll, M. / Hochberg, G.K.A. / Bode, H.B.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)SFB1035/A2 Germany
CitationJournal: Science / Year: 2024
Title: Evolution-inspired engineering of nonribosomal peptide synthetases.
Authors: Bozhuyuk, K.A.J. / Prave, L. / Kegler, C. / Schenk, L. / Kaiser, S. / Schelhas, C. / Shi, Y.N. / Kuttenlochner, W. / Schreiber, M. / Kandler, J. / Alanjary, M. / Mohiuddin, T.M. / Groll, M. ...Authors: Bozhuyuk, K.A.J. / Prave, L. / Kegler, C. / Schenk, L. / Kaiser, S. / Schelhas, C. / Shi, Y.N. / Kuttenlochner, W. / Schreiber, M. / Kandler, J. / Alanjary, M. / Mohiuddin, T.M. / Groll, M. / Hochberg, G.K.A. / Bode, H.B.
History
DepositionDec 6, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 20, 2023Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2024Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-2
B: Proteasome subunit alpha type-3
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-6
F: Probable proteasome subunit alpha type-7
G: Proteasome subunit alpha type-1
H: Proteasome subunit beta type-2
I: Proteasome subunit beta type-3
J: Proteasome subunit beta type-4
K: Proteasome subunit beta type-5
L: Proteasome subunit beta type-6
M: Proteasome subunit beta type-7
N: Proteasome subunit beta type-1
O: Proteasome subunit alpha type-2
P: Proteasome subunit alpha type-3
Q: Proteasome subunit alpha type-4
R: Proteasome subunit alpha type-5
S: Proteasome subunit alpha type-6
T: Probable proteasome subunit alpha type-7
U: Proteasome subunit alpha type-1
V: Proteasome subunit beta type-2
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-4
Y: Proteasome subunit beta type-5
Z: Proteasome subunit beta type-6
a: Proteasome subunit beta type-7
b: Proteasome subunit beta type-1
e: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
f: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
g: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
h: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)733,53147
Polymers732,31632
Non-polymers1,21415
Water1,51384
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, AU contains one biological assembly
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area123850 Å2
ΔGint-480 kcal/mol
Surface area213770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.970, 300.870, 143.980
Angle α, β, γ (deg.)90.00, 112.78, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
22
33
44
55
66
77
88
99
1010
1111
1212
1313
1414
/ NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

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Components

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Proteasome subunit alpha type- ... , 6 types, 12 molecules AOBPCQDRESGU

#1: Protein Proteasome subunit alpha type-2 / / Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / ...Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / Proteinase YSCE subunit 7


Mass: 27191.828 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P23639
#2: Protein Proteasome subunit alpha type-3 / / Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 ...Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 / Proteinase YSCE subunit 13


Mass: 28748.230 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P23638
#3: Protein Proteasome subunit alpha type-4 / / Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component ...Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component PRE6 / Proteinase YSCE subunit PRE6


Mass: 28478.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P40303
#4: Protein Proteasome subunit alpha type-5 / / Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component ...Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component PUP2 / Proteinase YSCE subunit PUP2


Mass: 28649.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P32379
#5: Protein Proteasome subunit alpha type-6 / / Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component ...Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component PRE5 / Proteinase YSCE subunit PRE5


Mass: 25634.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P40302
#7: Protein Proteasome subunit alpha type-1 / / Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7- ...Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7-alpha / Proteasome component Y8 / Proteinase YSCE subunit 7 / SCL1 suppressor protein


Mass: 28033.830 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P21243

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Proteasome subunit beta type- ... , 7 types, 14 molecules HVIWJXKYLZMaNb

#8: Protein Proteasome subunit beta type-2 / PSMB2 / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component ...Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


Mass: 25114.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / PSMB3 / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit PUP3 / Proteasome component PUP3


Mass: 22627.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P25451
#10: Protein Proteasome subunit beta type-4 / PSMB4 / Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 ...Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 / Proteinase YSCE subunit 11


Mass: 22545.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P22141
#11: Protein Proteasome subunit beta type-5 / PSMB5 / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component ...Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component PRE2 / Proteinase YSCE subunit PRE2


Mass: 23325.248 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6 / / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P23724
#13: Protein Proteasome subunit beta type-7 / / Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component ...Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component PRE4 / Proteinase YSCE subunit PRE4


Mass: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P30657
#14: Protein Proteasome subunit beta type-1 / PSMB1 / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component ...Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component PRE3 / Proteinase YSCE subunit PRE3


Mass: 21517.186 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P38624, proteasome endopeptidase complex

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Protein / Protein/peptide , 2 types, 6 molecules FTefgh

#15: Protein/peptide
3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE


Mass: 316.396 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Synthetic construct (others)
#6: Protein Probable proteasome subunit alpha type-7 / Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / ...Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / Proteinase YSCE subunit 1


Mass: 31575.068 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P21242

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Non-polymers , 4 types, 99 molecules

#16: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#17: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#18: Chemical
ChemComp-MYR / MYRISTIC ACID / Myristic acid


Mass: 228.371 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H28O2 / Feature type: SUBJECT OF INVESTIGATION
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 84 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.68 Å3/Da / Density % sol: 66.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 / Details: 100 mM MES, 20 mM MgAc2, 11% MPD

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 21, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.25→30 Å / Num. obs: 157953 / % possible obs: 95.1 % / Redundancy: 3 % / Rmerge(I) obs: 0.105 / Net I/σ(I): 11.1
Reflection shellResolution: 3.25→3.35 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.654 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 13542 / % possible all: 93.7

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Processing

Software
NameVersionClassification
REFMAC5.8.0258refinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1RYP

1ryp


Resolution: 3.25→30 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.94 / SU B: 54.303 / SU ML: 0.361 / Cross valid method: THROUGHOUT / ESU R Free: 0.41 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21218 7890 5 %RANDOM
Rwork0.1745 ---
obs0.1764 149904 95.15 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 91.345 Å2
Baniso -1Baniso -2Baniso -3
1-6.51 Å20 Å2-3.33 Å2
2---5.78 Å2-0 Å2
3---1.53 Å2
Refinement stepCycle: LAST / Resolution: 3.25→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49322 0 159 84 49565
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.01350368
X-RAY DIFFRACTIONr_bond_other_d0.0030.01747024
X-RAY DIFFRACTIONr_angle_refined_deg1.2041.64468122
X-RAY DIFFRACTIONr_angle_other_deg1.2051.588109132
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.04556308
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.81122.8022534
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.527158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.7415284
X-RAY DIFFRACTIONr_chiral_restr0.0390.26656
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0256562
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0210378
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.6766.31625322
X-RAY DIFFRACTIONr_mcbond_other2.6766.31625321
X-RAY DIFFRACTIONr_mcangle_it4.0329.46831600
X-RAY DIFFRACTIONr_mcangle_other4.0329.46831601
X-RAY DIFFRACTIONr_scbond_it2.4486.65425046
X-RAY DIFFRACTIONr_scbond_other2.4476.65425046
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.6789.85636522
X-RAY DIFFRACTIONr_long_range_B_refined5.73872.39652949
X-RAY DIFFRACTIONr_long_range_B_other5.73772.39652947
X-RAY DIFFRACTIONr_rigid_bond_restr0.357397392
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Auth asym-ID: A / Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDNumberTypeRms dev position (Å)Weight position
10103063tight positional0.030.05
11113254tight positional0.010.05
12123389tight positional00.05
13133507tight positional0.010.05
14142919tight positional00.05
113765tight thermal7.640.5
223714tight thermal7.910.5
333685tight thermal11.310.5
443540tight thermal8.770.5
553459tight thermal8.760.5
663693tight thermal8.140.5
773724tight thermal6.80.5
883442tight thermal6.090.5
993091tight thermal6.120.5
10103063tight thermal6.420.5
11113254tight thermal6.130.5
12123389tight thermal6.270.5
13133507tight thermal5.390.5
14142919tight thermal5.250.5
LS refinement shellResolution: 3.25→3.333 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.364 573 -
Rwork0.351 10878 -
obs--94.11 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.2567-0.31730.03410.89250.10270.502-0.06850.0413-0.01040.1020.053-0.1474-0.1024-0.04170.01550.4507-0.0812-0.00440.1812-0.03640.417966.8315-92.009145.8429
20.8333-0.19410.03751.04190.53291.3918-0.1193-0.04380.0222-0.1686-0.0023-0.1515-0.19590.30360.12160.5226-0.07820.08180.25840.07920.400559.4173-87.644516.2438
30.58620.2539-0.05280.1563-0.13170.59870.03740.06320.1121-0.10240.05090.03630.02750.0684-0.08830.6414-0.0027-0.02440.24970.05460.397831.9958-87.37080.9445
40.7775-0.1743-0.01760.4993-0.42070.59110.0075-0.11220.0231-0.2388-0.04740.1908-0.03470.10840.03980.5680.074-0.22050.10410.08330.53522.8295-90.138813.6684
50.2699-0.01270.05290.14230.05730.5368-0.08960.014-0.0064-0.0764-0.00660.2852-0.1749-0.04050.09620.35010.10260.04450.16990.00720.7596-3.5355-94.689345.5719
60.18710.0262-0.02930.2459-0.16780.24250.0054-0.03130.14160.065-0.0260.1867-0.03320.00240.02050.51390.05070.1740.1815-0.11320.44415.0629-95.349869.7773
70.147-0.0574-0.12650.54130.26550.91120.02950.08230.11210.1594-0.0326-0.0729-0.11180.01870.00310.592-0.0268-0.05220.1494-0.0630.327947.5716-93.554471.0267
80.06910.0151-0.03890.1497-0.04080.03090.01850.13350.0613-0.08030.0112-0.1314-0.0003-0.0569-0.02960.4348-0.0141-0.05530.3964-0.00610.491567.7086-129.482346.9468
90.9354-0.1740.23171.49190.3440.16620.10520.0288-0.0923-0.1917-0.0604-0.2174-0.0353-0.0214-0.04480.3726-0.00520.15390.2509-0.00280.424968.3541-127.169820.5336
100.43230.66050.12571.32590.01820.4214-0.0029-0.02140.068-0.4050.03320.0894-0.00180.0278-0.03030.6452-0.01450.06030.22030.03190.231244.6546-126.5197-0.9884
110.43670.63530.28821.78490.35570.2566-0.0264-0.0280.0832-0.11050.00950.3033-0.02560.08810.01690.50540.0188-0.23370.24680.04460.418610.866-130.98962.5698
120.3760.07940.42780.42630.32060.72270.1117-0.0866-0.0382-0.0872-0.0710.27660.0219-0.0396-0.04070.31410.0358-0.04870.24010.03990.6597-4.6444-134.727528.4015
130.86560.2112-0.19421.422-0.02540.28830.0884-0.0586-0.04340.2869-0.08690.14070.0490.0463-0.00150.3965-0.01830.14540.28790.01350.35697.6578-137.573660.1165
140.6298-0.1006-0.21691.0688-0.11060.21440.04430.03470.01270.2641-0.0642-0.10190.0389-0.010.01980.542-0.029-0.02090.2694-0.02950.20839.9757-134.218770.6791
151.1145-0.0569-0.2390.89820.02270.505-0.04650.09080.0180.00660.03140.10260.1779-0.04690.01510.4679-0.1356-0.23660.1490.0950.54982.4569-206.926736.3626
160.63390.06030.23410.56750.0241.1868-0.0087-0.0637-0.04560.0042-0.0440.07380.0588-0.24640.05260.6077-0.0256-0.25810.1569-0.07780.538.7942-205.70016.2871
170.65610.25680.25730.19540.08180.1470.130.0441-0.0111-0.2352-0.02160.14630.05450.0841-0.10830.98010.1137-0.29630.1133-0.1750.457136.0082-203.399-9.7265
180.79180.31040.29420.32420.04470.15020.1179-0.1317-0.0231-0.3345-0.2015-0.10290.185-0.03610.08370.7640.23190.1750.1777-0.09170.403765.48-202.91722.6562
190.06330.18050.00930.8147-0.15630.13780.0110.0461-0.0955-0.15030.1067-0.32670.14320.0103-0.11780.35560.135-0.09390.114-0.16370.80672.713-203.953334.4074
200.24930.29110.14680.35650.20540.22760.1079-0.0236-0.22440.0502-0.05-0.2591-0.0548-0.0816-0.05790.5390.0255-0.34370.09240.11370.562754.8582-207.79558.8191
210.11470.1426-0.13330.706-0.22851.05270.11150.0204-0.06540.0907-0.00540.15250.12180.0146-0.10610.5984-0.0346-0.17550.08660.11030.43122.4293-209.96560.6467
220.0633-0.0541-0.00510.09720.01480.00440.04360.1197-0.0319-0.096-0.0490.176-0.00140.00320.00540.4785-0.0578-0.07380.36380.10820.56631.667-170.23944.1927
230.4773-0.12140.2150.57960.29720.41820.05880.02720.0344-0.0886-0.03030.17490.0015-0.0101-0.02850.4158-0.0257-0.23710.18870.02280.50470.3094-167.697417.8236
240.09180.254-0.10020.9986-0.03030.4402-0.03370.0127-0.06-0.32480.0648-0.0880.01110.0197-0.0310.6450.0186-0.19010.1984-0.03820.293923.3703-164.4483-4.1425
250.19170.4818-0.11081.8384-0.44590.11230.0603-0.0741-0.1178-0.1708-0.0849-0.23520.06160.04390.02460.5910.04730.1470.3059-0.07710.410357.2836-160.6497-0.7804
260.35230.4748-0.42760.8378-0.62210.55770.07160.0005-0.0633-0.0236-0.1445-0.3119-0.00420.01660.07290.34650.08540.03990.2622-0.07390.591273.4854-161.575324.799
270.63930.27320.38111.3301-0.01050.38670.05510.04050.01670.2491-0.0373-0.1736-0.0497-0.1183-0.01770.40240.0173-0.16580.19920.0020.399762.103-164.476956.8564
280.6511-0.06910.06881.21530.20940.05820.1170.0721-0.02860.1333-0.10140.07910.0243-0.0618-0.01560.5519-0.0295-0.05010.26310.10140.234530.137-169.763567.6075
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION2B1 - 244
3X-RAY DIFFRACTION3C1 - 240
4X-RAY DIFFRACTION4D1 - 242
5X-RAY DIFFRACTION5E3 - 233
6X-RAY DIFFRACTION6F2 - 244
7X-RAY DIFFRACTION7G2 - 242
8X-RAY DIFFRACTION8H1 - 226
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K1 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 230
14X-RAY DIFFRACTION14N1 - 196
15X-RAY DIFFRACTION15O1 - 250
16X-RAY DIFFRACTION16P1 - 244
17X-RAY DIFFRACTION17Q1 - 240
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S3 - 233
20X-RAY DIFFRACTION20T2 - 244
21X-RAY DIFFRACTION21U2 - 242
22X-RAY DIFFRACTION22V1 - 226
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 230
28X-RAY DIFFRACTION28b1 - 196

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