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- PDB-9qai: Yeast 20S proteasome mutant: beta5_T3M in complex with MG132 -

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Basic information

Entry
Database: PDB / ID: 9qai
TitleYeast 20S proteasome mutant: beta5_T3M in complex with MG132
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 / Proteasome / Proteasome Associated Autoinflammatory Syndromes / Mutation / Assembly / Maturation
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / Ub-specific processing proteases / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / Neutrophil degranulation / proteasome complex / peroxisome / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
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 alpha5 / Proteasome subunit alpha6 / 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 alpha5 / Proteasome subunit alpha6 / 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 B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
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 ...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: 2.8 Å
AuthorsHuber, E.M. / Heinemeyer, W. / Groll, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)SFB1035, project no.201302640, A02 Germany
CitationJournal: Structure / Year: 2025
Title: Proteasome-associated autoinflammatory syndromes: The impact of mutations in proteasome subunits on particle assembly, structure, and activity
Authors: Huber, E.M. / Heinemeyer, W. / Groll, M.
History
DepositionFeb 28, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 8, 2025Provider: repository / Type: Initial release

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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
i: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
j: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)734,48249
Polymers734,07334
Non-polymers40915
Water5,080282
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration, AU contains one biological assembly
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area129190 Å2
ΔGint-556 kcal/mol
Surface area213720 Å2
Unit cell
Length a, b, c (Å)136.130, 300.280, 145.700
Angle α, β, γ (deg.)90.00, 113.08, 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 / 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: 25013.355 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 / 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 / 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 / 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: 23254.238 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: 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 / 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: 21416.080 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, 8 molecules FTefghij

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


Mass: 594.740 Da / Num. of mol.: 6 / 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 , 3 types, 297 molecules

#16: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Mg
#17: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 282 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 3.75 Å3/Da / Density % sol: 67.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 / Details: 20 mM MgAC2, 13% MPD, 0.1 M MES

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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: Oct 24, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→30 Å / Num. obs: 255576 / % possible obs: 97 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.083 / Net I/σ(I): 11
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.458 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 25850 / % possible all: 98.5

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Processing

Software
NameVersionClassification
REFMAC5.7.0032refinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→15 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.942 / SU B: 24.867 / SU ML: 0.21 / Cross valid method: THROUGHOUT / ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20546 12779 5 %RANDOM
Rwork0.18675 ---
obs0.18768 242797 97.11 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 69.587 Å2
Baniso -1Baniso -2Baniso -3
1-3.69 Å20 Å2-0.04 Å2
2---5.52 Å2-0 Å2
3---1.35 Å2
Refinement stepCycle: 1 / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49564 0 15 283 49862
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950468
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248280
X-RAY DIFFRACTIONr_angle_refined_deg0.8811.96868268
X-RAY DIFFRACTIONr_angle_other_deg0.7063111158
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.69956312
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.89824.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.21158750
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.12215284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27699
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257222
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211314
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_it2.0915.06425338
X-RAY DIFFRACTIONr_mcbond_other2.0915.06425337
X-RAY DIFFRACTIONr_mcangle_it2.6667.58231620
X-RAY DIFFRACTIONr_mcangle_other2.6667.58231621
X-RAY DIFFRACTIONr_scbond_it2.1115.54925130
X-RAY DIFFRACTIONr_scbond_other2.1115.54925130
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.4538.14736648
X-RAY DIFFRACTIONr_long_range_B_refined3.10139.8854253
X-RAY DIFFRACTIONr_long_range_B_other3.08239.87254217
X-RAY DIFFRACTIONr_rigid_bond_restr1.645398748
X-RAY DIFFRACTIONr_sphericity_free32.3935190
X-RAY DIFFRACTIONr_sphericity_bonded5.636597954
Refine LS restraints NCS

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

Ens-IDDom-IDNumberTypeRms dev position (Å)Weight position
10103099tight positional00.05
11113280tight positional0.070.05
12123439tight positional00.05
13133576tight positional0.010.05
14143024tight positional00.05
113795tight thermal5.410.5
223756tight thermal3.970.5
333729tight thermal9.960.5
443578tight thermal4.240.5
553509tight thermal5.180.5
663749tight thermal5.090.5
773770tight thermal3.230.5
883478tight thermal3.610.5
993119tight thermal2.830.5
10103099tight thermal2.670.5
11113280tight thermal2.470.5
12123439tight thermal2.180.5
13133576tight thermal2.160.5
14143024tight thermal2.320.5
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.34 925 -
Rwork0.308 17577 -
obs--98.59 %
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)
10.3264-0.0817-0.02070.0608-0.04750.0892-0.03220.0336-0.02480.05740.0202-0.0443-0.0865-0.0610.0120.1748-0.03760.0210.1716-0.05330.217267.2043-91.993146.3281
20.2310.0314-0.0810.04110.04230.2362-0.0477-0.0762-0.0285-0.0624-0.01590.0208-0.09280.08350.06370.2323-0.0380.09640.20270.0280.1860.0186-87.809816.6386
30.24620.1986-0.01140.1749-0.05860.5462-0.04450.00230.0212-0.06470.03310.0375-0.00290.12170.01130.2595-0.00370.01860.16590.06110.1332.7546-87.21891.2321
40.10320.0045-0.12930.0653-0.00180.16370.0021-0.08910.001-0.0797-0.00760.1466-0.00810.12070.00560.19040.0542-0.11560.13360.0630.3763.4741-89.859613.7506
50.0010.00340.01670.01610.05730.3306-0.0091-0.00320.0047-0.0046-0.00610.0545-0.09170.00360.01520.07690.05670.1070.12890.01570.437-2.9154-94.196445.7793
60.3903-0.05320.03280.01090.00670.1615-0.00480.02710.04220.0221-0.01850.0186-0.00810.01260.02330.280.02040.2060.1692-0.05440.195315.4434-94.812370.0385
70.04110.0351-0.01040.09050.00580.01410.06080.0478-0.01660.1435-0.0429-0.0467-0.0099-0.0345-0.01790.3255-0.03390.010.1597-0.02820.122647.8953-93.304471.4043
80.07210.016-0.06660.0657-0.020.06360.01080.07690.02120.07010.0027-0.0905-0.0188-0.0834-0.01350.1208-0.024-0.05460.1861-0.03390.197167.7767-129.488447.6896
90.08530.0042-0.1260.6902-0.18750.24490.0420.0534-0.0023-0.0774-0.0433-0.1367-0.0528-0.08970.00130.1054-0.01980.08750.2208-0.01040.197668.5641-127.478921.1674
100.4175-0.18020.07050.36420.24420.28450.0289-0.08660.0071-0.0859-0.01140.0034-0.0234-0.0172-0.01740.28760.00610.05640.18130.0180.046245.1314-126.4795-0.395
110.0155-0.0204-0.00660.0534-0.0110.02560.0231-0.0293-0.0208-0.0807-0.01250.08150.01380.0742-0.01060.22640.0126-0.14040.2320.04170.22611.3518-130.67342.6873
120.07580.0790.15120.14750.15640.3431-0.0048-0.0116-0.00220.03290.01070.1379-0.0170.0672-0.00590.07310.01550.02270.21030.03220.3793-4.2431-134.106228.7118
130.00860.01470.00280.095-0.01080.00450.02760.02970.03510.1247-0.02820.1196-0.01160.030.00060.19620.00220.14170.24290.00580.24157.951-137.192560.452
140.4727-0.0807-0.24850.38920.02620.13260.04530.08240.07370.1385-0.00770.0348-0.0107-0.0413-0.03760.3017-0.00710.01270.2046-0.03530.033140.0632-133.996870.77
150.17040.0122-0.07110.02580.04620.1373-0.02560.02840.03590.0533-0.00240.02780.1202-0.00720.0280.1725-0.0735-0.03320.11550.05310.28551.9278-206.278136.9304
160.16620.0410.09980.0225-0.02090.2385-0.0505-0.05580.0255-0.039-0.01640.00120.0399-0.03760.06690.2196-0.0262-0.12880.1151-0.04550.20868.4629-205.16426.8519
170.22940.11080.1730.13690.07340.18120.0856-0.02710.013-0.142-0.05340.10130.04130.0283-0.03220.43280.0681-0.16820.0709-0.09480.14335.8024-203.2439-9.008
180.16750.02620.15870.07680.01040.15650.0206-0.13330.0605-0.1502-0.0744-0.07720.0598-0.1070.05390.33820.09660.170.1672-0.03610.196665.1779-202.78023.5024
190.0460.0381-0.05710.036-0.04540.20420.03850.0647-0.05390.02060.0548-0.07340.0548-0.0403-0.09330.11360.0848-0.10530.1065-0.10130.427472.0696-203.966535.5252
200.37490.1393-0.13620.0606-0.03570.07820.09990.0135-0.09140.0696-0.0509-0.0733-0.036-0.0592-0.0490.3033-0.0001-0.23060.10420.08720.248354.0887-207.61159.7649
210.10340.0277-0.1160.1409-0.06930.19980.01630.029-0.00080.08650.00420.09190.01180.0294-0.02060.2936-0.0144-0.06460.09810.04870.145821.7021-209.536661.3567
220.0217-0.00540.0710.0495-0.03050.24770.02330.0177-0.00790.03450.00660.10160.03230.0917-0.02990.1087-0.04040.0250.14050.06130.25191.4962-169.637544.7796
230.0994-0.00210.17150.0747-0.07190.37250.02530.02660.0504-0.067-0.01210.12630.06990.0877-0.01320.1332-0.0132-0.12590.14730.00770.25610.2948-167.005418.266
240.1672-0.0498-0.04730.3623-0.14450.08880.0529-0.1158-0.0645-0.1019-0.0430.02540.00440.0693-0.00980.29970.013-0.09190.151-0.02480.103623.3872-164.2187-3.5604
250.0181-0.00330.0110.00790.00030.0080.0224-0.05550.0084-0.0468-0.0114-0.01760.0022-0.0343-0.0110.27910.01950.1080.2546-0.04830.129957.209-160.6188-0.3043
260.09640.0982-0.13010.1392-0.11110.21660.03230.0182-0.02190.0105-0.03-0.10270.0073-0.0672-0.00230.11690.04420.00470.245-0.03790.296973.1969-161.714225.6636
270.0135-0.0257-0.01410.61880.15070.04380.01530.0372-0.02850.1468-0.0025-0.10650.0389-0.0367-0.01280.2230.0161-0.11620.193-0.01090.194961.4254-163.688157.8236
280.2422-0.0090.10390.26410.07330.07120.07080.0655-0.01340.134-0.0498-0.0060.04970.0021-0.02090.2802-0.01580.02980.18170.04290.045929.5956-169.17767.8141
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-10 - 9999
2X-RAY DIFFRACTION2B-10 - 9999
3X-RAY DIFFRACTION3C-10 - 9999
4X-RAY DIFFRACTION4D-10 - 9999
5X-RAY DIFFRACTION5E-10 - 9999
6X-RAY DIFFRACTION6F-10 - 9999
7X-RAY DIFFRACTION7G-10 - 9999
8X-RAY DIFFRACTION8H-10 - 9999
9X-RAY DIFFRACTION9I-10 - 9999
10X-RAY DIFFRACTION10J-10 - 9999
11X-RAY DIFFRACTION11K-10 - 9999
12X-RAY DIFFRACTION12L-10 - 9999
13X-RAY DIFFRACTION13M-10 - 9999
14X-RAY DIFFRACTION14N-10 - 9999
15X-RAY DIFFRACTION15O-10 - 9999
16X-RAY DIFFRACTION16P-10 - 9999
17X-RAY DIFFRACTION17Q-10 - 9999
18X-RAY DIFFRACTION18R-10 - 9999
19X-RAY DIFFRACTION19S-10 - 9999
20X-RAY DIFFRACTION20T-10 - 9999
21X-RAY DIFFRACTION21U-10 - 9999
22X-RAY DIFFRACTION22V-10 - 9999
23X-RAY DIFFRACTION23W-10 - 9999
24X-RAY DIFFRACTION24X-10 - 9999
25X-RAY DIFFRACTION25Y-10 - 9999
26X-RAY DIFFRACTION26Z-10 - 9999
27X-RAY DIFFRACTION27a-10 - 9999
28X-RAY DIFFRACTION28b-10 - 9999

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