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- PDB-9qd2: Yeast 20S proteasome mutant: beta1_G128V (b1-propeptide deleted) ... -

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Basic information

Entry
Database: PDB / ID: 9qd2
TitleYeast 20S proteasome mutant: beta1_G128V (b1-propeptide deleted) 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: 2.7 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
DepositionMar 5, 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
d: 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)734,56644
Polymers734,09734
Non-polymers47010
Water4,540252
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration, AU contains one biological assembly
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area128530 Å2
ΔGint-490 kcal/mol
Surface area213920 Å2
Unit cell
Length a, b, c (Å)136.230, 300.110, 145.770
Angle α, β, γ (deg.)90.00, 113.25, 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: 23224.146 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 / 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: 21458.160 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: PRE3, YJL001W, J1407 / Production host: Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P38624, proteasome endopeptidase complex

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Protein / Protein/peptide , 2 types, 8 molecules FTdefghi

#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 , 4 types, 262 molecules

#16: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#17: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#18: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 252 / 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: 3.74 Å3/Da / Density % sol: 67.14 %
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: Dec 19, 2015
RadiationMonochromator: LN2 COOLED FIXED-EXIT. SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.7→30 Å / Num. obs: 286712 / % possible obs: 97.6 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.071 / Net I/σ(I): 10.4
Reflection shellResolution: 2.7→2.8 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.591 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 29927 / % possible all: 98.8

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→15 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.95 / SU B: 30.439 / SU ML: 0.246 / Cross valid method: THROUGHOUT / ESU R Free: 0.256 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21412 14253 5 %RANDOM
Rwork0.17631 ---
obs0.1795 270814 97.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 72.19 Å2
Baniso -1Baniso -2Baniso -3
1-1.3 Å2-0 Å2-0.82 Å2
2---2.59 Å20 Å2
3---1.46 Å2
Refinement stepCycle: 1 / Resolution: 2.7→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49514 0 21 252 49787
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.01350430
X-RAY DIFFRACTIONr_bond_other_d0.0020.01747083
X-RAY DIFFRACTIONr_angle_refined_deg1.2981.64768220
X-RAY DIFFRACTIONr_angle_other_deg1.3111.587109249
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2656306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.4522.7912530
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.514158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.18615284
X-RAY DIFFRACTIONr_chiral_restr0.0430.26678
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0256642
X-RAY DIFFRACTIONr_gen_planes_other0.0020.0210436
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_it3.2455.37225314
X-RAY DIFFRACTIONr_mcbond_other3.2455.37225313
X-RAY DIFFRACTIONr_mcangle_it4.7018.0531590
X-RAY DIFFRACTIONr_mcangle_other4.7018.0531591
X-RAY DIFFRACTIONr_scbond_it3.1785.76825116
X-RAY DIFFRACTIONr_scbond_other3.1735.76725114
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.4988.50736631
X-RAY DIFFRACTIONr_long_range_B_refined6.34361.81352768
X-RAY DIFFRACTIONr_long_range_B_other6.32761.79852743
X-RAY DIFFRACTIONr_rigid_bond_restr0.556397513
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 positional0.010.05
11113239tight positional0.090.05
12123389tight positional0.010.05
13133564tight positional0.050.05
14143004tight positional0.070.05
113765tight thermal7.740.5
223714tight thermal7.940.5
333685tight thermal9.620.5
443540tight thermal7.550.5
553459tight thermal7.40.5
663693tight thermal7.280.5
773724tight thermal6.930.5
883362tight thermal6.150.5
993091tight thermal5.50.5
10103063tight thermal5.970.5
11113239tight thermal6.490.5
12123389tight thermal5.690.5
13133564tight thermal5.50.5
14143004tight thermal6.470.5
LS refinement shellResolution: 2.7→2.768 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.36 1039 -
Rwork0.337 19733 -
obs--98.96 %
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)
10.4649-0.03470.13020.4576-0.22890.2431-0.0390.0719-0.00080.02050.0439-0.1954-0.09990.0303-0.00480.2612-0.05630.00090.1374-0.09260.325166.801-92.014746.217
20.8342-0.12880.04110.51740.31960.6925-0.0962-0.04390.0499-0.11930.0373-0.0493-0.12360.13190.05890.2941-0.07510.07780.10440.05840.264359.7525-87.82316.5506
30.58290.48040.08070.42990.08061.137-0.03960.06710.0452-0.1140.07030.0299-0.08850.1355-0.03060.32960.0012-0.00720.07450.08840.265632.4969-87.49461.0952
40.54290.0758-0.22110.13370.00490.5584-0.0139-0.06140.047-0.09950.01410.2404-0.11870.052-0.00010.26890.0691-0.1280.06150.06550.46713.2477-90.182413.4665
50.02940.02060.13170.1750.10720.694-0.0497-0.0379-0.0017-0.015-0.0050.2229-0.1361-0.0880.05480.1570.11960.05680.13630.01520.519-3.3411-94.547645.4434
60.76170.05540.08840.05260.06610.2792-0.0225-0.04480.10970.1024-0.01310.09810.00730.00290.03560.36370.05950.17770.14-0.0990.293415.0725-95.169569.7433
70.19650.03330.09160.6983-0.15860.88160.04270.00620.030.2161-0.0271-0.0976-0.0677-0.0427-0.01560.4158-0.01420.00080.0773-0.07050.220147.4988-93.552371.2366
80.0504-0.1161-0.09210.42660.24680.2040.03120.0020.06180.12010.0153-0.1931-0.0231-0.0235-0.04650.2501-0.0092-0.04980.1551-0.05840.316967.4638-130.051248.2816
90.6176-0.444-0.05411.35730.09880.33450.0291-0.00520.0026-0.08810.0205-0.2517-0.0860.0335-0.04960.1915-0.01940.08570.1589-0.01860.322768.5219-127.423921.0566
100.63950.33730.36920.92450.04080.28360.03340.0744-0.0326-0.23340.0404-0.0960.03760.0839-0.07380.3473-0.00190.05350.18140.01620.214545.011-126.6469-0.552
110.19680.0224-0.12680.9329-0.22490.36340.00960.04670.0507-0.28160.01380.267-0.06380.0051-0.02340.24440.0332-0.13310.1420.04730.289611.2089-130.96282.4724
120.1983-0.13230.23280.39270.01470.47330.08090.0192-0.0399-0.0397-0.03110.24350.0337-0.0223-0.04970.15290.0438-0.03310.14070.05340.4797-4.42-134.46528.458
130.3171-0.03180.02150.8865-0.05640.01650.0252-0.0620.04410.1793-0.01120.1280.0192-0.0382-0.0140.27370.0040.10060.19460.01120.27977.8789-138.035860.1615
140.8498-0.3197-0.08781.0282-0.12770.46730.0459-0.0377-0.07550.25130.00970.0052-0.0718-0.0497-0.05560.3324-0.01990.00420.1697-0.04830.159639.5814-133.964670.554
150.49330.1095-0.17850.37440.11020.2403-0.03360.06290.05670.0535-0.01250.19130.1675-0.05090.04610.2979-0.1004-0.05180.07510.06960.38962.3142-206.524936.8724
160.72960.19150.22090.52470.00880.5402-0.07040.02290.0884-0.0673-0.03520.03250.0775-0.04330.10560.3004-0.0371-0.13380.0614-0.07570.31548.7278-205.44496.8028
170.58760.23990.13760.50410.16570.45280.1260.0215-0.0634-0.2963-0.050.23830.08580.054-0.0760.53320.0732-0.20170.0424-0.09450.306736.0793-203.3521-9.059
180.80260.02460.16030.79160.18880.42360.0646-0.12670.0516-0.2584-0.0716-0.19640.0751-0.03810.0070.38840.12630.10330.109-0.06210.252965.4332-202.78873.4051
190.61060.4594-0.33450.3957-0.13250.7804-0.00110.0403-0.2210.03340.0664-0.3030.17870.1081-0.06530.2590.1732-0.0950.1225-0.11880.525172.4577-203.866935.3663
201.19210.4197-0.18690.16990.01670.43350.0837-0.2005-0.22370.1087-0.0596-0.12030.16240.0231-0.02410.49350.1024-0.21310.11430.09110.34854.4295-207.398659.6663
210.3948-0.0533-0.16310.4928-0.0120.76460.0216-0.0124-0.04550.07760.02950.10070.10580.0562-0.05110.4303-0.0145-0.04890.04430.0950.255922.0486-209.511761.2922
220.019-0.06820.04270.4371-0.17850.130.034-0.0219-0.05250.0610.0130.22420.0828-0.0108-0.0470.2515-0.050.01640.13440.06250.37291.7892-169.442845.4285
230.8146-0.0345-0.3691.43290.06070.23140.03250.03870.0272-0.0612-0.00450.26060.0926-0.0169-0.0280.2243-0.0211-0.14920.10990.0120.38640.3318-167.364718.1391
240.97640.3976-0.42570.86340.1030.3503-0.02770.04920.0056-0.26490.07760.1392-0.0432-0.0085-0.04980.35840.0283-0.13220.1339-0.01490.223523.5228-164.3965-3.6975
250.27440.09540.29441.0244-0.08280.44440.02820.1335-0.0313-0.36660.0445-0.08940.05570.0612-0.07260.30110.06120.1110.1867-0.0510.212257.3678-160.6266-0.4588
260.36080.0096-0.20190.5959-0.18110.25820.10690.03320.01440.015-0.0527-0.20310.01870.0414-0.05420.19970.08430.02250.2023-0.07520.381273.3479-161.63225.4973
270.21070.09130.09010.97850.0380.04720.0423-0.0002-0.05450.1967-0.0279-0.12630.038-0.0045-0.01440.29940.0435-0.09090.1738-0.01760.260561.5424-163.557557.506
280.7152-0.20340.01571.18580.20120.44420.0494-0.07450.04080.20640.06460.05220.14290.0391-0.1140.3184-0.01810.0230.16230.05040.177230.0477-169.374967.6068
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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