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- PDB-9fsv: Yeast 20S proteasome with human beta2i (1-53) in complex with epo... -

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Basic information

Entry
Database: PDB / ID: 9fsv
TitleYeast 20S proteasome with human beta2i (1-53) in complex with epoxyketone inhibitor 42
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE / Proteasome / Mutant / Human Chimeric Subunit / Structure-based Drug Development / Inhibitor / Binding Analysis
Function / homology
Function and homology information


spermatoproteasome complex / Proteasome assembly / proteasome core complex / 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 / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A ...spermatoproteasome complex / Proteasome assembly / proteasome core complex / 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 / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / 3-deoxy-7-phosphoheptulonate synthase / 3-deoxy-7-phosphoheptulonate synthase activity / 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 / humoral immune response / Antigen processing: Ubiquitination & Proteasome degradation / chorismate biosynthetic process / proteasome endopeptidase complex / Ub-specific processing proteases / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / aromatic amino acid family biosynthetic process / threonine-type endopeptidase activity / T cell proliferation / proteasome core complex, alpha-subunit complex / amino acid biosynthetic process / Neutrophil degranulation / proteasome complex / cell morphogenesis / peroxisome / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / endoplasmic reticulum membrane / mitochondrion / metal ion binding / nucleus / cytosol
Similarity search - Function
DAHP synthetase, class II / Class-II DAHP synthetase family / 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. ...DAHP synthetase, class II / Class-II DAHP synthetase family / 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 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 / Aldolase-type TIM barrel
Similarity search - Domain/homology
: / Phospho-2-dehydro-3-deoxyheptonate aldolase / 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 ...: / Phospho-2-dehydro-3-deoxyheptonate aldolase / 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 / Proteasome subunit beta type-10
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.75 Å
AuthorsMaurits, E. / Huber, E.M. / Dekker, P.M. / Wang, X. / Heinemeyer, W. / Florea, B.I. / Groll, M. / Overkleeft, H.S.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)GR 1861/10-3 Germany
CitationJournal: to be published
Title: Structure-based design of peptide epoxyketones selectively targeting the three human immunoproteasome active sites
Authors: Maurits, E. / Huber, E.M. / Dekker, P.M. / Wang, X. / Heinemeyer, W. / Florea, B.I. / Groll, M. / Overkleeft, H.S.
History
DepositionJun 22, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 17, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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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-10,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-10,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)733,65051
Polymers729,30528
Non-polymers4,34523
Water5,549308
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 area128580 Å2
ΔGint-529 kcal/mol
Surface area212830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.700, 300.600, 144.480
Angle α, β, γ (deg.)90.00, 112.83, 90.00
Int Tables number4
Space group name H-MP1211

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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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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 (brewer's yeast) / References: UniProt: P21242

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

#8: Protein Proteasome subunit beta type-10,Proteasome subunit beta type-2 / Low molecular mass protein 10 / Macropain subunit MECl-1 / Multicatalytic endopeptidase complex ...Low molecular mass protein 10 / Macropain subunit MECl-1 / Multicatalytic endopeptidase complex subunit MECl-1 / Proteasome MECl-1 / Proteasome subunit beta-2i / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


Mass: 24342.568 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: PSMB10, LMP10, MECL1, PUP1, YOR157C / Production host: Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P40306, 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: 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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Non-polymers , 6 types, 331 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-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#18: Chemical
ChemComp-A1IFL / (2S)-N-[(2S)-1-[[(1S)-2-cyclohexyl-1-[(2R,3S,6R,7S)-3-methanoyl-2,6-dimethyl-6,7-bis(oxidanyl)-1,4-oxazepan-7-yl]ethyl]amino]-3-(4-methoxyphenyl)-1-oxidanylidene-propan-2-yl]-2-(2-morpholin-4-ylethanoylamino)-4-oxidanyl-butanamide / epoxyketone inhibitor 42


Mass: 719.865 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C36H57N5O10 / Source: (synth.) synthetic construct (others) / Feature type: SUBJECT OF INVESTIGATION
#19: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#20: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 308 / 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: 3.69 Å3/Da / Density % sol: 66.63 %
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: Nov 27, 2021
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: 2.75→30 Å / Num. obs: 259664 / % possible obs: 94.9 % / Redundancy: 3 % / Rmerge(I) obs: 0.094 / Net I/σ(I): 7.5
Reflection shellResolution: 2.75→2.85 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.641 / Mean I/σ(I) obs: 2 / Num. unique obs: 26829

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.75→30 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.927 / SU B: 35.413 / SU ML: 0.305 / Cross valid method: THROUGHOUT / ESU R: 0.626 / ESU R Free: 0.316 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24702 12976 5 %RANDOM
Rwork0.21311 ---
obs0.2148 246529 94.93 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 65.405 Å2
Baniso -1Baniso -2Baniso -3
1-2.5 Å2-0 Å2-1.57 Å2
2---1.4 Å2-0 Å2
3---0.17 Å2
Refinement stepCycle: 1 / Resolution: 2.75→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49516 0 79 308 49903
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01350516
X-RAY DIFFRACTIONr_bond_other_d0.0020.01548030
X-RAY DIFFRACTIONr_angle_refined_deg1.411.64668350
X-RAY DIFFRACTIONr_angle_other_deg1.2281.591110726
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.41956315
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.49522.8032537
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.387158748
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.66915284
X-RAY DIFFRACTIONr_chiral_restr0.0550.26663
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0257301
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211339
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_it1.0842.97625344
X-RAY DIFFRACTIONr_mcbond_other1.0842.97625343
X-RAY DIFFRACTIONr_mcangle_it1.9424.45731631
X-RAY DIFFRACTIONr_mcangle_other1.9424.45731632
X-RAY DIFFRACTIONr_scbond_it0.8943.10225172
X-RAY DIFFRACTIONr_scbond_other0.8913.09825154
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.6164.59336696
X-RAY DIFFRACTIONr_long_range_B_refined4.00733.91353309
X-RAY DIFFRACTIONr_long_range_B_other3.99833.89753286
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.75→2.821 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.376 975 -
Rwork0.354 18520 -
obs--97.13 %
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)
10.7158-0.1330.16130.50460.03720.1008-0.05610.0848-0.03160.07490.0494-0.0884-0.1253-0.00550.00670.5689-0.0637-0.12770.1406-0.06270.698966.8465-91.916145.8991
20.33870.04520.00730.04240.1490.7595-0.0953-0.03-0.0121-0.08790.00740.0181-0.09430.12240.08780.6119-0.0472-0.04580.15220.09540.670659.469-87.827616.238
30.3890.29620.01570.2312-0.00130.7423-0.04710.07360.0699-0.04660.06870.023-0.02790.1171-0.02170.69440.0067-0.15320.15460.09160.610932.3065-87.40010.8372
40.4585-0.0722-0.28130.19620.00060.281-0.0359-0.05750.0238-0.12090.03060.1945-0.08740.04890.00530.61990.0874-0.25820.08020.12350.75133.2017-90.036113.4387
50.27090.07310.19450.4153-0.12140.5285-0.074-0.04890.0102-0.02490.02860.1857-0.10730.00380.04550.44970.0729-0.0430.1572-0.02570.8137-3.1685-94.286845.5361
60.62280.0855-0.12690.1644-0.10280.2147-0.0221-0.03960.11770.0572-0.05580.1316-0.01290.03020.0780.61790.01990.00480.1466-0.1090.668315.2777-94.807969.7928
70.2931-0.0141-0.13710.3131-0.12130.62720.0010.0440.06610.1106-0.0475-0.0766-0.0469-0.02880.04650.7038-0.0316-0.15590.0873-0.10170.602947.5729-93.233571.0912
80.0231-0.0398-0.04590.3020.17850.15430.03760.0480.02340.1234-0.0152-0.2159-0.0286-0.0531-0.02240.5065-0.0102-0.16020.2104-0.02970.733567.4362-129.570347.4224
90.5687-0.0861-0.1930.94150.21080.15250.0345-0.0385-0.0067-0.0924-0.0123-0.2162-0.1107-0.0719-0.02220.5369-0.0256-0.01550.1922-0.00890.720468.2229-127.425120.7742
100.14560.14140.07971.05660.05530.21540.0614-0.09860.0793-0.221-0.0296-0.0125-0.0386-0.0164-0.03180.68040.0181-0.09530.17570.03070.580744.6571-126.6027-0.7609
110.1925-0.0471-0.02410.7013-0.12140.21170.017-0.03660.079-0.1735-0.01670.215-0.05580.0791-0.00030.61580.0206-0.25960.2020.03510.616610.9151-130.87742.4134
120.10990.18410.16230.52590.21390.37750.0667-0.01320.0214-0.0452-0.01980.2564-0.01580.055-0.0470.4650.0295-0.18190.18110.03980.8206-4.4274-134.344128.5466
130.27150.06480.01140.63890.22610.08690.040.02610.01530.1693-0.05590.0470.0032-0.01190.01590.5593-0.01760.00070.22740.01340.6687.7256-137.753560.5082
140.57720.0634-0.32110.80870.19110.24790.06050.02950.00750.2150.0193-0.11460.0155-0.0278-0.07980.6715-0.0047-0.15470.2032-0.01170.562639.7359-133.852871.1509
150.7571-0.146-0.40220.30970.14690.38060.02810.09120.01340.0564-0.01360.10930.1704-0.0018-0.01450.5915-0.0985-0.23010.08920.04590.71391.8281-206.43636.8248
160.27960.14990.29320.5388-0.10570.6604-0.1061-0.0497-0.0611-0.07990.0695-0.00610.0032-0.10160.03650.5961-0.0365-0.25680.1131-0.09030.6968.2977-205.33626.7064
170.43860.270.06390.3452-0.10950.52410.1320.0368-0.0932-0.2229-0.02930.21490.06110.0252-0.10260.84120.0919-0.37250.0289-0.13480.649935.4066-203.3206-9.2314
180.5457-0.1020.15650.36040.04690.54060.0757-0.18920.0538-0.3473-0.1329-0.11180.0947-0.07290.05720.68620.1883-0.01240.171-0.09750.669464.7477-202.83053.2584
190.26660.1923-0.30270.2508-0.17840.64940.04210.0622-0.08590.04550.1109-0.28830.14760.0084-0.1530.43620.1472-0.22340.0922-0.16790.917371.8179-203.951635.2392
201.11180.43580.11090.1949-0.02330.24480.077-0.0353-0.22260.0573-0.0097-0.13170.0083-0.0418-0.06730.69660.0644-0.39460.03330.07190.717853.922-207.575859.5732
210.2452-0.16570.04580.188-0.18420.68220.0221-0.0186-0.06480.01160.04010.11410.01230.0397-0.06220.7061-0.0191-0.23250.03910.11490.684221.6953-209.544261.2285
220.01920.0432-0.01380.2127-0.10340.09090.04720.0189-0.01970.0524-0.01820.16770.07150.0517-0.0290.5201-0.0414-0.1340.19570.05810.75641.5747-169.350845.3179
230.4496-0.16350.09070.6745-0.27930.1829-0.0119-0.0290.0105-0.16720.06490.19260.0860.0661-0.0530.5611-0.0156-0.28340.1460.00560.7418-0.0474-167.189618.0615
240.377-0.0933-0.03980.6538-0.28030.1420.0699-0.0343-0.0879-0.172-0.04210.03920.03360.0277-0.02780.74480.0182-0.24990.1541-0.04780.543623.0429-164.3237-3.8401
250.23610.33340.14891.0524-0.04460.26210.0089-0.0237-0.0422-0.21310.0738-0.1298-0.0135-0.0287-0.08270.6220.0608-0.01110.2026-0.06220.605856.8494-160.6202-0.6242
260.11380.2346-0.10680.6085-0.01580.60210.04720.0159-0.0460.0201-0.0224-0.21830.0152-0.0794-0.02480.43520.0854-0.0770.2224-0.06580.763172.8115-161.613525.3675
270.2138-0.1208-0.12260.653-0.11240.1662-0.01730.08310.01980.18410.0114-0.22270.0504-0.12160.00590.5890.0311-0.24820.1969-0.01590.661261.4238-163.644557.6924
280.422-0.13770.23370.7284-0.14930.18010.09390.029-0.02260.18-0.02350.01790.0308-0.0661-0.07040.667-0.0272-0.12230.17730.04110.593929.6881-169.347568.1985
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 DIFFRACTION8H2 - 226
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K2 - 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 DIFFRACTION22V2 - 223
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y2 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b1 - 196

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