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- PDB-5jhr: Yeast 20S proteasome in complex with the peptidic epoxyketone inh... -

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Basic information

Entry
Database: PDB / ID: 5jhr
TitleYeast 20S proteasome in complex with the peptidic epoxyketone inhibitor 27
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR complex / Proteasome / 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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation ...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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / 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. ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / 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 / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-6KF / 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 ...Chem-6KF / 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)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsHuber, E.M. / Groll, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationGR1861/10-1 Germany
CitationJournal: J.Med.Chem. / Year: 2016
Title: Structure-Based Design of beta 5c Selective Inhibitors of Human Constitutive Proteasomes.
Authors: Xin, B.T. / de Bruin, G. / Huber, E.M. / Besse, A. / Florea, B.I. / Filippov, D.V. / van der Marel, G.A. / Kisselev, A.F. / van der Stelt, M. / Driessen, C. / Groll, M. / Overkleeft, H.S.
History
DepositionApr 21, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Aug 3, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2016Group: Database references
Revision 2.0Jan 10, 2024Group: Atomic model / Author supporting evidence ...Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Refinement description
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp_atom / chem_comp_bond / database_2 / pdbx_audit_support / pdbx_initial_refinement_model / pdbx_nonpoly_scheme / struct_conn / struct_conn_type
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization / _pdbx_nonpoly_scheme.auth_seq_num / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)733,09643
Polymers731,05128
Non-polymers2,04515
Water3,891216
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)135.290, 300.810, 144.540
Angle α, β, γ (deg.)90.00, 112.95, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21O
12B
22P
13C
23Q
14D
24R
15E
25S
16F
26T
17G
27U
18H
28V
19I
29W
110J
210X
111K
211Y
112L
212Z
113M
213a
114N
214b

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A1 - 300
2111O1 - 300
1121B1 - 300
2121P1 - 300
1131C1 - 300
2131Q1 - 300
1141D1 - 300
2141R1 - 300
1151E1 - 300
2151S1 - 300
1161F1 - 300
2161T1 - 300
1171G1 - 300
2171U1 - 300
1181H1 - 300
2181V1 - 300
1191I1 - 300
2191W1 - 300
11101J1 - 300
21101X1 - 300
11111K1 - 300
21111Y1 - 300
11121L1 - 300
21121Z1 - 300
11131M1 - 300
21131a1 - 300
11141N1 - 300
21141b1 - 300

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999544, -0.003071, 0.030052), (-0.002111, -0.985287, -0.170895), (0.030135, -0.17088, 0.984831)67.321281, -289.820984, -25.50374

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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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P23638, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P40303, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P32379, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P40302, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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Protein , 1 types, 2 molecules FT

#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P21242, proteasome endopeptidase complex

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

#8: Protein Proteasome subunit beta type-2 / 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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / 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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P25451, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-4 / 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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P22141, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-5 / 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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-1 / 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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 5 types, 231 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


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


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#17: Chemical ChemComp-6KF / (2S)-2-azido-N-[(2S)-3-(biphenyl-4-yl)-1-{[(2S)-1-{[(2S,3S,4R)-3,5-dihydroxy-4-methylpentan-2-yl]amino}-1-oxo-3-phenylpropan-2-yl]amino}-1-oxopropan-2-yl]-3-phenylpropanamide (non-preferred name)


Mass: 676.804 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C39H44N6O5
#18: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 216 / Source method: isolated from a natural source / Formula: H2O

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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: 3.67 Å3/Da / Density % sol: 66.52 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 / Details: 20 mM MgAC2, 13% MPD, 0.1 M MES / PH range: 6.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Sep 7, 2014
RadiationMonochromator: LN2 COOLED FIXED-EXIT. SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→50 Å / Num. obs: 229229 / % possible obs: 97.7 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.074 / Net I/σ(I): 12.9
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.523 / Mean I/σ(I) obs: 2.7 / % possible all: 99.1

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
REFMACphasing
REFMAC5.7.0032refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5CZ4

5cz4


Resolution: 2.9→15 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.939 / SU B: 28.512 / SU ML: 0.23 / Cross valid method: THROUGHOUT / ESU R Free: 0.293 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20615 11462 5 %RANDOM
Rwork0.18101 ---
obs0.18226 217766 97.84 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 67.841 Å2
Baniso -1Baniso -2Baniso -3
1-2.4 Å20 Å2-1.39 Å2
2---6.37 Å20 Å2
3---3.36 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49304 0 135 216 49655
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950345
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248103
X-RAY DIFFRACTIONr_angle_refined_deg0.921.96668114
X-RAY DIFFRACTIONr_angle_other_deg0.6943.001110767
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.97356308
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.91924.4062247
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.315158741
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.32315284
X-RAY DIFFRACTIONr_chiral_restr0.0510.27669
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257125
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211305
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_it2.0825.03125316
X-RAY DIFFRACTIONr_mcbond_other2.0825.03125315
X-RAY DIFFRACTIONr_mcangle_it2.7447.53231593
X-RAY DIFFRACTIONr_mcangle_other2.7447.53231594
X-RAY DIFFRACTIONr_scbond_it2.0415.39825029
X-RAY DIFFRACTIONr_scbond_other2.0415.39825029
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.4827.96136521
X-RAY DIFFRACTIONr_long_range_B_refined3.13239.27454125
X-RAY DIFFRACTIONr_long_range_B_other3.11139.2754095
X-RAY DIFFRACTIONr_rigid_bond_restr1.646398448
X-RAY DIFFRACTIONr_sphericity_free33.595164
X-RAY DIFFRACTIONr_sphericity_bonded5.707597601
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A3099TIGHT POSITIONAL00.05
1A3291TIGHT POSITIONAL0.020.05
1A3439TIGHT POSITIONAL00.05
1A3618TIGHT POSITIONAL00.05
1A2949TIGHT POSITIONAL00.05
1A3795TIGHT THERMAL5.030.5
2B3756TIGHT THERMAL3.980.5
3C3729TIGHT THERMAL8.690.5
4D3578TIGHT THERMAL4.640.5
5E3509TIGHT THERMAL5.630.5
6F3749TIGHT THERMAL5.340.5
7G3770TIGHT THERMAL3.270.5
8H3322TIGHT THERMAL2.820.5
9I3119TIGHT THERMAL2.50.5
10J3099TIGHT THERMAL3.90.5
11K3291TIGHT THERMAL2.280.5
12L3439TIGHT THERMAL2.220.5
13M3618TIGHT THERMAL2.30.5
14N2949TIGHT THERMAL2.230.5
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.321 830 -
Rwork0.295 15762 -
obs--99.26 %
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)
10.2508-0.06830.04140.3227-0.17120.1528-0.0330.0021-0.01920.06180.0281-0.107-0.0682-0.06070.00490.1526-0.04660.00410.151-0.05810.202966.6889-92.16446.0014
20.33560.1319-0.02260.05290.00530.309-0.0752-0.0272-0.0023-0.0404-0.0112-0.0045-0.10220.06420.08640.187-0.06290.08530.17380.04230.15459.3682-87.862316.3838
30.30570.2927-0.13660.2998-0.13360.3827-0.0334-0.013-0.0013-0.06860.04610.0048-0.06370.0472-0.01270.2162-0.0090.02910.15640.05270.105832.176-87.50451.0488
40.17540.0952-0.17410.3345-0.08610.18160.0023-0.08610.0104-0.1215-0.00040.2626-0.02940.0724-0.00180.15830.0617-0.07120.12010.08080.27762.948-90.330913.5595
50.23170.11690.17640.0770.07540.437-0.06470.01780.074-0.01090.03110.1187-0.11310.00920.03360.09330.06520.08240.12290.03820.3994-3.3519-94.738445.479
60.42160.0950.11560.03430.02910.0327-0.01560.00030.10030.0505-0.01970.06640.01360.0020.03540.28770.02090.17570.1514-0.06150.172315.0324-95.371969.6929
70.06040.06010.04150.14480.09510.28870.05650.0649-0.02760.1462-0.0069-0.058-0.0162-0.0228-0.04960.2987-0.0110.00240.1414-0.04290.08847.4511-93.61271.0595
80.02640.0057-0.00040.11790.08090.06620.07050.0492-0.02070.0303-0.0097-0.15830.0236-0.0527-0.06070.1620.0064-0.03630.2052-0.03840.275267.5436-130.095548.217
90.3174-0.1767-0.08770.8133-0.03650.03570.02250.0026-0.07840.0666-0.0717-0.1725-0.0154-0.00920.04920.0929-0.01460.07030.2317-0.01520.209968.3811-127.436520.773
100.272-0.0261-0.01750.51360.26550.43230.0487-0.07560.0268-0.1645-0.00230.015-0.06250.0132-0.04630.2184-0.01430.07940.16730.00850.059944.7544-126.6828-0.6952
110.43770.84210.31371.91060.73390.2938-0.045-0.09430.0648-0.03210.00890.24940.01570.03480.03610.09420.0207-0.11750.18460.05940.222310.9688-131.20232.7144
120.1132-0.01910.06710.4540.09120.07040.05410.0586-0.045-0.0323-0.03670.17360.02890.0547-0.01740.04510.0367-0.00520.21430.04760.3162-4.3844-134.704128.366
130.2501-0.10360.05480.5306-0.03680.06170.05220.03650.04140.1731-0.04330.10970.010.0579-0.00890.153-0.00850.13250.16660.00160.13687.7927-138.232260.2144
140.15380.185-0.07410.5696-0.12480.04120.06810.06180.0120.1249-0.0585-0.0665-0.024-0.0086-0.00960.2901-0.0079-0.00990.1792-0.02130.049939.7757-134.28270.7454
150.2230.0748-0.12990.19710.09620.1938-0.05650.03610.07140.11180.03660.06650.13240.01010.01990.1807-0.0705-0.03540.10620.06740.23512.3684-206.965936.6234
160.32010.08670.14190.123-0.070.1835-0.0517-0.01530.011-0.1160.0111-0.01230.0812-0.03570.04060.2002-0.0349-0.0930.1098-0.05490.19398.7965-205.8546.5563
170.50260.23790.06630.37940.13910.31760.1263-0.0463-0.0251-0.1578-0.04070.16520.01630.0921-0.08560.33070.0654-0.18650.0553-0.07920.219735.9986-203.7393-9.3033
180.3992-0.05920.16240.49330.09890.11040.0713-0.11720.0336-0.2017-0.0773-0.16830.0225-0.07530.0060.29030.08780.12910.1547-0.05450.198465.4192-203.06193.1442
190.78210.60380.2570.53030.09020.36950.03360.0892-0.27820.03290.1058-0.29190.09220.0029-0.13940.10980.0877-0.11630.1079-0.13460.500172.4442-204.19934.921
200.32540.2509-0.080.1986-0.05360.03520.1061-0.0409-0.19230.0996-0.0779-0.167-0.0037-0.0207-0.02820.34130.0169-0.28040.10.08320.331254.6163-207.901359.2059
210.2277-0.0235-0.02240.1288-0.12380.22450.05660.0343-0.0380.1017-0.00360.04380.04570.018-0.0530.3828-0.0181-0.07160.06680.07190.143522.2413-210.064460.9238
220.0452-0.01370.02030.0292-0.00990.00970.040.08120.02360.0037-0.03730.06850.01750.0371-0.00270.1516-0.01410.0160.21450.05010.26891.6681-170.04245.4096
230.189-0.11370.07180.63480.01370.10110.0480.01160.05310.013-0.01850.16390.05250.0095-0.02950.0989-0.0101-0.09010.16860.01940.25910.2342-167.802917.9424
240.24750.0713-0.23740.9299-0.46390.4010.0783-0.0345-0.0083-0.1464-0.05410.0197-0.02650.0512-0.02420.24180.003-0.08050.1222-0.03640.045423.3679-164.7249-3.8531
250.6020.8992-0.20842.2469-0.68850.2388-0.0158-0.0983-0.0731-0.0485-0.0021-0.21830.0098-0.00410.01790.1510.04080.1120.2105-0.07140.167157.2879-160.8651-0.3815
260.4052-0.196-0.16480.7132-0.22690.26090.10790.04530.0675-0.0371-0.0663-0.2002-0.0659-0.0136-0.04160.05580.04920.03160.2099-0.04020.300173.1261-161.875925.122
270.1057-0.02010.03890.3915-0.04960.03030.02220.0358-0.06240.1733-0.0049-0.13730.0013-0.0244-0.01730.18450.0143-0.14280.1595-0.00870.169961.7058-164.003157.327
280.25360.09560.21910.17370.12540.21630.06170.0572-0.00410.163-0.0372-0.01440.0723-0.0031-0.02450.2738-0.0197-0.00320.13680.05710.031729.9788-169.826167.7234
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 - 222
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K1 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 233
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 - 222
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b1 - 196

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