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- PDB-7b12: HUMAN IMMUNOPROTEASOME 20S PARTICLE IN COMPLEX WITH [2-(3-ethylph... -

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Basic information

Entry
Database: PDB / ID: 7b12
TitleHUMAN IMMUNOPROTEASOME 20S PARTICLE IN COMPLEX WITH [2-(3-ethylphenyl)-1-[(2S)-3-phenyl-2-[(pyrazin-2-yl)formamido]propanamido]ethyl]boronic acid
Components
  • (Proteasome subunit alpha type- ...) x 7
  • (Proteasome subunit beta type- ...) x 7
KeywordsIMMUNE SYSTEM / MULTICATALYTIC PROTEINASE / 20S PROTEASOME / PROTEASE / HYDROLASE
Function / homology
Function and homology information


regulation of cysteine-type endopeptidase activity / spermatoproteasome complex / purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril ...regulation of cysteine-type endopeptidase activity / spermatoproteasome complex / purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / fat cell differentiation / humoral immune response / antigen processing and presentation / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / T cell proliferation / negative regulation of inflammatory response to antigenic stimulus / response to organonitrogen compound / proteasome complex / proteolysis involved in protein catabolic process / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / ciliary basal body / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / proteasomal protein catabolic process / Degradation of DVL / P-body / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of AXIN / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / lipopolysaccharide binding / Hedgehog ligand biogenesis / Activation of NF-kappaB in B cells / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / Vif-mediated degradation of APOBEC3G / Autodegradation of the E3 ubiquitin ligase COP1 / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / response to virus / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / ABC-family proteins mediated transport / Degradation of beta-catenin by the destruction complex / cell morphogenesis / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / response to organic cyclic compound / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / nuclear matrix / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / The role of GTSE1 in G2/M progression after G2 checkpoint / UCH proteinases / KEAP1-NFE2L2 pathway / Interferon alpha/beta signaling / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / Neddylation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / positive regulation of NF-kappaB transcription factor activity / ER-Phagosome pathway / regulation of inflammatory response / postsynapse / proteasome-mediated ubiquitin-dependent protein catabolic process / secretory granule lumen / endopeptidase activity / ficolin-1-rich granule lumen / ribosome / Ub-specific processing proteases / intracellular membrane-bounded organelle / centrosome / synapse
Similarity search - Function
Proteasome subunit alpha 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 subunit alpha 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
Similarity search - Domain/homology
Chem-SKN / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit beta type-8 / Proteasome subunit beta type-9 / Proteasome subunit alpha type-5 ...Chem-SKN / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit beta type-8 / Proteasome subunit beta type-9 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-10 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.43 Å
AuthorsMusil, D. / Klein, M. / Crosignani, S.
CitationJournal: J.Med.Chem. / Year: 2021
Title: Structure-Based Optimization and Discovery of M3258, a Specific Inhibitor of the Immunoproteasome Subunit LMP7 ( beta 5i).
Authors: Klein, M. / Busch, M. / Friese-Hamim, M. / Crosignani, S. / Fuchss, T. / Musil, D. / Rohdich, F. / Sanderson, M.P. / Seenisamy, J. / Walter-Bausch, G. / Zanelli, U. / Hewitt, P. / Esdar, C. / Schadt, O.
History
DepositionNov 23, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 1, 2021Provider: repository / Type: Initial release
Revision 1.1Dec 8, 2021Group: Refinement description / Category: software
Revision 1.2Jun 14, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
1: Proteasome subunit beta type-1
2: Proteasome subunit beta type-4
A: Proteasome subunit alpha type-6
B: Proteasome subunit alpha type-2
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-7
E: Proteasome subunit alpha type-5
F: Proteasome subunit alpha type-1
G: Proteasome subunit alpha type-3
H: Proteasome subunit beta type-9
J: Proteasome subunit beta type-3
K: Proteasome subunit beta type-2
L: Proteasome subunit beta type-8
M: Proteasome subunit beta type-1
N: Proteasome subunit beta type-4
O: Proteasome subunit alpha type-6
P: Proteasome subunit alpha type-2
Q: Proteasome subunit alpha type-4
T: Proteasome subunit alpha type-1
U: Proteasome subunit alpha type-3
V: Proteasome subunit beta type-9
X: Proteasome subunit beta type-3
Y: Proteasome subunit beta type-2
Z: Proteasome subunit beta type-8
i: Proteasome subunit beta type-10
r: Proteasome subunit alpha type-7
s: Proteasome subunit alpha type-5
w: Proteasome subunit beta type-10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)694,45145
Polymers691,15528
Non-polymers3,29617
Water17,943996
1


  • Idetical with deposited unit
  • defined by author&software
  • 28-mer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area113910 Å2
ΔGint-539 kcal/mol
Surface area214930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)118.995, 201.736, 161.932
Angle α, β, γ (deg.)90.000, 106.830, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Proteasome subunit beta type- ... , 7 types, 14 molecules 1M2NHVJXKYLZiw

#1: Protein Proteasome subunit beta type-1 / PSMB1 / Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / ...Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / Proteasome gamma chain


Mass: 23578.986 Da / Num. of mol.: 2 / Fragment: 20S CORE / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P20618, proteasome endopeptidase complex
#2: Protein Proteasome subunit beta type-4 / PSMB4 / 26 kDa prosomal protein / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase complex ...26 kDa prosomal protein / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase complex beta chain / Proteasome beta chain / Proteasome chain 3 / HsN3


Mass: 23881.164 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P28070, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-9 / / Low molecular mass protein 2 / Macropain chain 7 / Multicatalytic endopeptidase complex chain 7 / ...Low molecular mass protein 2 / Macropain chain 7 / Multicatalytic endopeptidase complex chain 7 / Proteasome chain 7 / Proteasome subunit beta-1i / Really interesting new gene 12 protein


Mass: 21295.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P28065, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-3 / PSMB3 / Proteasome chain 13 / Proteasome component C10-II / Proteasome theta chain


Mass: 22841.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P49720, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-2 / PSMB2 / Macropain subunit C7-I / Multicatalytic endopeptidase complex subunit C7-I / Proteasome component C7-I


Mass: 22462.838 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P49721, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-8 / / Low molecular mass protein 7 / Macropain subunit C13 / Multicatalytic endopeptidase complex subunit ...Low molecular mass protein 7 / Macropain subunit C13 / Multicatalytic endopeptidase complex subunit C13 / Proteasome component C13 / Proteasome subunit beta-5i / Really interesting new gene 10 protein


Mass: 22557.504 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P28062, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-10 / / 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


Mass: 23428.891 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P40306, proteasome endopeptidase complex

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Proteasome subunit alpha type- ... , 7 types, 14 molecules AOBPCQDrEsFTGU

#3: Protein Proteasome subunit alpha type-6 / / 27 kDa prosomal protein / p27K / Macropain iota chain / Multicatalytic endopeptidase complex iota ...27 kDa prosomal protein / p27K / Macropain iota chain / Multicatalytic endopeptidase complex iota chain / Proteasome iota chain


Mass: 26941.902 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60900
#4: Protein Proteasome subunit alpha type-2 / / Macropain subunit C3 / Multicatalytic endopeptidase complex subunit C3 / Proteasome component C3


Mass: 25367.873 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25787
#5: Protein Proteasome subunit alpha type-4 / / Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / ...Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / Proteasome subunit L


Mass: 27859.896 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25789
#6: Protein Proteasome subunit alpha type-7 / / Proteasome subunit RC6-1 / Proteasome subunit XAPC7


Mass: 26365.064 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14818
#7: Protein Proteasome subunit alpha type-5 / / Macropain zeta chain / Multicatalytic endopeptidase complex zeta chain / Proteasome zeta chain


Mass: 25293.625 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P28066
#8: Protein Proteasome subunit alpha type-1 / / 30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex ...30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex subunit C2 / Proteasome component C2 / Proteasome nu chain


Mass: 26503.182 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25786
#9: Protein Proteasome subunit alpha type-3 / / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8


Mass: 27200.020 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25788

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Non-polymers , 4 types, 1013 molecules

#15: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#16: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Na
#17: Chemical
ChemComp-SKN / ((R)-2-(3-ethylphenyl)-1-((S)-3-phenyl-2-(pyrazine-2-carboxamido)propanamido)ethyl)boronic acid / [(1~{R})-2-(3-ethylphenyl)-1-[[(2~{S})-3-phenyl-2-(pyrazin-2-ylcarbonylamino)propanoyl]amino]ethyl]boronic acid / [2-(3-ethylphenyl)-1-[(2S)-3-phenyl-2-[(pyrazin-2-yl)formamido]propanamido]ethyl]boronic acid


Mass: 446.307 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C24H27BN4O4 / Feature type: SUBJECT OF INVESTIGATION
#18: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 996 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.7 Å3/Da / Density % sol: 54.47 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.6 / Details: 42 % MPD, 0.20 M NaSCN,

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9173 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Sep 22, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9173 Å / Relative weight: 1
ReflectionResolution: 2.43→107.89 Å / Num. obs: 177341 / % possible obs: 93.4 % / Redundancy: 4.5 % / Biso Wilson estimate: 60.34 Å2 / CC1/2: 0.998 / Rpim(I) all: 0.06 / Rrim(I) all: 0.133 / Net I/σ(I): 9.8
Reflection shellResolution: 2.43→2.657 Å / Redundancy: 5.3 % / Mean I/σ(I) obs: 1.6 / Num. unique obs: 8868 / CC1/2: 0.569 / Rpim(I) all: 0.542 / % possible all: 72.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
BUSTER2.11.7 (18-SEP-2020)refinement
XDSdata reduction
PHASERphasing
PDB_EXTRACT3.27data extraction
autoPROCdata scaling
autoPROCdata processing
STARANISO2.3.46data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: NONE

Resolution: 2.43→107.89 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.899 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.321
RfactorNum. reflection% reflectionSelection details
Rfree0.2245 8735 4.93 %RANDOM
Rwork0.18 ---
obs0.1822 177341 93.4 %-
Displacement parametersBiso max: 190.65 Å2 / Biso mean: 60.98 Å2 / Biso min: 13.03 Å2
Baniso -1Baniso -2Baniso -3
1--5.8408 Å20 Å21.7755 Å2
2--8.3515 Å20 Å2
3----2.5107 Å2
Refine analyzeLuzzati coordinate error obs: 0.33 Å
Refinement stepCycle: final / Resolution: 2.43→107.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms48113 0 229 996 49338
Biso mean--50.14 40.33 -
Num. residues----6195
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d17311SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes8473HARMONIC5
X-RAY DIFFRACTIONt_it49210HARMONIC10
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion6435SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact39553SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d49210HARMONIC20.008
X-RAY DIFFRACTIONt_angle_deg66474HARMONIC21
X-RAY DIFFRACTIONt_omega_torsion3.11
X-RAY DIFFRACTIONt_other_torsion17.66
LS refinement shellResolution: 2.43→2.57 Å / Rfactor Rfree error: 0 / Total num. of bins used: 51
RfactorNum. reflection% reflection
Rfree0.2587 163 4.6 %
Rwork0.221 3384 -
all0.2228 3547 -
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)
10.69040.0091-0.09850.263-0.61331.4522-0.07190.03620.0558-0.09680.0414-0.04040.30160.26410.0306-0.07620.18360.05650.13810.0181-0.063722.353719.0831-83.3068
20.35980.0955-0.04321.2055-0.44630.8212-0.20560.30560.0122-0.25240.17740.10760.3538-0.08640.02810.1518-0.14750.04870.1659-0.0434-0.2562-5.416814.2021-135.8842
30.0842-0.2684-0.11541.10710.07980.2129-0.05980.23150.108-0.08960.04080.12050.2026-0.32020.019-0.1296-0.1412-0.06880.21390.0888-0.0388-33.893130.9677-101.4802
40.11-0.05090.08441.16570.50590.9042-0.0043-0.13170.03090.18210.02430.01930.23120.1249-0.020.11950.03930.03270.07770.091-0.1892-7.1859.766-15.5812
51.0440.6081-0.23051.01750.14730.8511-0.0680.32690.1541-0.10940.08320.11580.1185-0.2186-0.0152-0.0918-0.1711-0.1210.33230.1532-0.2415-24.483137.9761-138.8872
60.04040.1058-0.08761.1803-0.13120.1373-0.0204-0.18060.01240.0633-0.0283-0.0150.13510.40560.0487-0.12780.0833-0.02950.26850.0511-0.099121.363229.1895-48.5882
70.57820.0929-0.05960.8525-0.08520.59370.0151-0.10840.07230.1721-0.0617-0.13350.08460.13690.0465-0.0489-0.0121-0.06330.24270.0056-0.191311.974833.3083-10.9518
80.16560.16650.09020.9488-0.11940.8008-0.02490.13430.1752-0.21860.1260.1582-0.1158-0.1445-0.1011-0.0828-0.0538-0.06230.16680.2728-0.0176-18.05668.614-136.4617
90.5445-0.18070.08330.70830.07280.2978-0.0213-0.11420.1530.21330.0093-0.0509-0.07880.11520.012-0.0041-0.0998-0.00440.1127-0.1241-0.06045.791264.2663-10.698
101.7412-0.37880.21150.6797-0.78750.20370.0881-0.08210.4128-0.09720.0484-0.0347-0.11670.2074-0.1365-0.0981-0.16280.10560.05160.15890.08368.98582.9198-127.6401
110.20580.4520.06581.3804-0.63981.4734-0.10590.0975-0.0678-0.06280.0885-0.0173-0.28180.54930.0174-0.2212-0.23280.05420.33820.1423-0.109735.635969.3772-121.1085
121.8444-0.07780.34741.10210.46011.3077-0.10540.24990.1545-0.18260.0065-0.34990.04820.53970.0989-0.24420.06990.14590.43510.0786-0.11742.755238.9538-120.0022
131.5478-0.09170.25680.7729-0.47330.3393-0.0087-0.21120.14260.14580.09950.24970.018-0.3869-0.0908-0.2277-0.06610.12890.26730.02420.035-55.300835.7254-29.6909
140.9493-0.17670.48330.6177-0.10050.5345-0.04220.2156-0.0982-0.2134-0.0207-0.0510.4040.31470.06290.09860.16510.17730.1827-0.0458-0.182725.070414.526-126.6012
151.08990.28260.36590.73620.06460.84460.0893-0.12890.00060.0959-0.03110.11090.2554-0.2099-0.05820.0521-0.14970.08130.02880.0856-0.094-37.653910.9456-24.72
160.70330.1569-0.17770.3407-0.58961.48920.0240.12850.0143-0.08790.0023-0.00660.3306-0.0304-0.02630.1069-0.03540.0283-0.0436-0.0007-0.0714-6.76898.9198-94.2739
171.37350.0254-0.55590.16040.41391.5094-0.0414-0.059-0.05070.02870.0455-0.00540.25740.0668-0.00410.09780.06060.019-0.08640.0674-0.0433-5.79217.5786-57.443
180.853-0.3046-0.49580-0.07580.3781-0.01920.00170.10050.0240.0080.02840.1185-0.00560.0113-0.2312-0.0197-0.0863-0.04350.06130.1295-6.284940.6624-74.7599
190.82780.165-0.80810.71340.31211.37110.03460.2740.1784-0.03870.02860.00980.0637-0.3571-0.0632-0.23390.0001-0.02710.17530.18210.0486-34.939359.0019-100.8112
203.15530.3102-0.23570.41620.15040.19920.1552-0.17510.8730.1701-0.00120.00630.0036-0.1785-0.154-0.0250.01130.1914-0.1642-0.15660.2547-21.597979.0228-18.5653
210.65790.0931-0.22490.5648-0.41940.8160.0684-0.16270.08120.1309-0.0740.0841-0.00430.37960.0056-0.1804-0.08440.0040.2455-0.0112-0.054422.347757.1311-47.3526
221.01020.6624-0.71360.65460.33041.32480.04370.18570.13070.01760.0295-0.0282-0.22740.015-0.0731-0.10.00780.0365-0.14680.16660.2011-12.579480.8946-93.7399
230.41730.4361-0.02180.93570.09741.3761-0.0452-0.06750.13380.1-0.00550.1546-0.2955-0.3870.0507-0.14910.14840.1580.0963-0.04880.0998-48.006465.4156-26.309
240.9578-0.6623-0.31610.6261-0.06532.11870.0176-0.10990.0890.03580.01350.0957-0.35350.0124-0.0311-0.0924-0.10930.0612-0.1367-0.03340.1534-0.094979.4905-52.899
250.8875-0.3933-0.34830.74340.43281.81560.05010.12730.1837-0.0502-0.02590.0155-0.21560.243-0.0242-0.1984-0.17030.03080.06030.11470.094819.174677.0659-83.5907
260.78870.35040.02450.5961-0.28291.58450.1371-0.07360.1630.09510.0410.0963-0.1571-0.1831-0.1781-0.16390.10110.1118-0.06950.06830.2166-31.819276.3047-63.2225
271.03730.2875-0.45590.2554-0.20070.91190.0189-0.02680.0824-0.0535-0.0299-0.03140.15530.28170.0109-0.27840.01280.01250.31670.0285-0.052333.779949.862-79.7427
280.7051-0.4592-0.21680.6144-0.10811.08320.04860.09080.12370.11760.02740.08330.136-0.2296-0.076-0.268-0.05680.01120.1750.12290.067-46.323449.4457-69.03
290.5826-0.1752-0.20940.21990.28581.3917-0.09250.08680.1090.05730.08730.06710.2962-0.15980.0053-0.0582-0.14270.02070.06690.0647-0.0138-34.904518.5168-67.6393
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ N|1 - N|214 }N1 - 214
2X-RAY DIFFRACTION2{ A|4 - A|244 }A4 - 244
3X-RAY DIFFRACTION3{ i|1 - i|219 }i1 - 219
4X-RAY DIFFRACTION4{ O|4 - O|245 }O4 - 245
5X-RAY DIFFRACTION5{ B|4 - B|232 }B4 - 232
6X-RAY DIFFRACTION6{ w|1 - w|220 }w1 - 220
7X-RAY DIFFRACTION7{ P|4 - P|232 }P4 - 232
8X-RAY DIFFRACTION8{ C|2 - C|246 }C2 - 246
9X-RAY DIFFRACTION9{ Q|2 - Q|249 }Q2 - 249
10X-RAY DIFFRACTION10{ D|2 - D|235 }D2 - 235
11X-RAY DIFFRACTION11{ E|9 - E|240 }E9 - 240
12X-RAY DIFFRACTION12{ F|4 - F|239 }F4 - 239
13X-RAY DIFFRACTION13{ T|4 - T|239 }T4 - 239
14X-RAY DIFFRACTION14{ G|3 - G|244 }G3 - 244
15X-RAY DIFFRACTION15{ U|2 - U|244 }U2 - 244
16X-RAY DIFFRACTION16{ H|1 - H|199 }H1 - 199
17X-RAY DIFFRACTION17{ V|1 - V|199 }V1 - 199
18X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }i301
19X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }H201
20X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }L301
21X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }w301
22X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }V201
23X-RAY DIFFRACTION18{ i|301 - i|301 H|201 - H|201 L|301 - L|301 w|301 - w|301 V|201 - V|201 Z|301 - Z|301 }Z301
24X-RAY DIFFRACTION19{ J|2 - J|205 }J2 - 205
25X-RAY DIFFRACTION20{ r|2 - r|236 }r2 - 236
26X-RAY DIFFRACTION21{ X|2 - X|205 }X2 - 205
27X-RAY DIFFRACTION22{ K|1 - K|196 }K1 - 196
28X-RAY DIFFRACTION23{ s|9 - s|238 }s9 - 238
29X-RAY DIFFRACTION24{ Y|1 - Y|197 }Y1 - 197
30X-RAY DIFFRACTION25{ L|1 - L|203 }L1 - 203
31X-RAY DIFFRACTION26{ Z|1 - Z|203 }Z1 - 203
32X-RAY DIFFRACTION27{ M|1 - M|213 }M1 - 213
33X-RAY DIFFRACTION28{ 1|1 - 1|213 }11 - 213
34X-RAY DIFFRACTION29{ 2|1 - 2|214 }21 - 214

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