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- PDB-3unh: Mouse 20S immunoproteasome -

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Basic information

Entry
Database: PDB / ID: 3unh
TitleMouse 20S immunoproteasome
Components
  • (Proteasome subunit alpha type- ...) x 7
  • (Proteasome subunit beta type- ...) x 7
KeywordsHYDROLASE / 20S proteasome comprises 28 subunits / Protease / Cytosol
Function / homology
Function and homology information


Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 ...Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / Assembly of the pre-replicative complex / CDK-mediated phosphorylation and removal of Cdc6 / Autodegradation of the E3 ubiquitin ligase COP1 / G2/M Checkpoints / Degradation of AXIN / Asymmetric localization of PCP proteins / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Regulation of RUNX3 expression and activity / Regulation of RAS by GAPs / Regulation of PTEN stability and activity / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / UCH proteinases / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of DVL / Orc1 removal from chromatin / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Dectin-1 mediated noncanonical NF-kB signaling / NIK-->noncanonical NF-kB signaling / spermatoproteasome complex / TNFR2 non-canonical NF-kB pathway / Hedgehog ligand biogenesis / Hedgehog 'on' state / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Degradation of beta-catenin by the destruction complex / Activation of NF-kappaB in B cells / The role of GTSE1 in G2/M progression after G2 checkpoint / FCERI mediated NF-kB activation / CLEC7A (Dectin-1) signaling / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Interleukin-1 signaling / Downstream TCR signaling / Separation of Sister Chromatids / MAPK6/MAPK4 signaling / GLI3 is processed to GLI3R by the proteasome / ABC-family proteins mediated transport / Neddylation / Ub-specific processing proteases / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / proteasome core complex / antigen processing and presentation / fat cell differentiation / myofibril / immune system process / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / T cell proliferation / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / skeletal muscle tissue development / proteasomal protein catabolic process / Neutrophil degranulation / proteolysis involved in protein catabolic process / proteasome complex / sarcomere / response to bacterium / negative regulation of inflammatory response to antigenic stimulus / P-body / lipopolysaccharide binding / protein catabolic process / response to virus / nuclear matrix / cell morphogenesis / ubiquitin-dependent protein catabolic process / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / cilium / ciliary basal body / ribosome / ubiquitin protein ligase binding / centrosome / mitochondrion / RNA binding / nucleoplasm / identical protein binding / cytoplasm / cytosol
Similarity search - Function
Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha5 / Proteasome subunit alpha6 ...Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit 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 / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
IODIDE ION / : / Proteasome subunit beta type-1 / Proteasome subunit beta type-10 / Proteasome subunit alpha type-3 / Proteasome subunit beta type-8 / Proteasome subunit beta type-9 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-6 ...IODIDE ION / : / Proteasome subunit beta type-1 / Proteasome subunit beta type-10 / Proteasome subunit alpha type-3 / Proteasome subunit beta type-8 / Proteasome subunit beta type-9 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-7 / Proteasome subunit alpha type-5
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsHuber, E. / Basler, M. / Schwab, R. / Heinemeyer, W. / Kirk, C. / Groettrup, M. / Groll, M.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2012
Title: Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity.
Authors: Huber, E.M. / Basler, M. / Schwab, R. / Heinemeyer, W. / Kirk, C.J. / Groettrup, M. / Groll, M.
History
DepositionNov 15, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 29, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2012Group: Database references
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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-4
C: Proteasome subunit alpha type-7
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-1
F: Proteasome subunit alpha type-3
G: Proteasome subunit alpha type-6
H: Proteasome subunit beta type-10
I: Proteasome subunit beta type-3
J: Proteasome subunit beta type-2
K: Proteasome subunit beta type-8
L: Proteasome subunit beta type-1
M: Proteasome subunit beta type-4
N: Proteasome subunit beta type-9
O: Proteasome subunit alpha type-2
P: Proteasome subunit alpha type-4
Q: Proteasome subunit alpha type-7
R: Proteasome subunit alpha type-5
S: Proteasome subunit alpha type-1
T: Proteasome subunit alpha type-3
U: Proteasome subunit alpha type-6
V: Proteasome subunit beta type-10
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-2
Y: Proteasome subunit beta type-8
Z: Proteasome subunit beta type-1
a: Proteasome subunit beta type-4
b: Proteasome subunit beta type-9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)718,92875
Polymers715,94528
Non-polymers2,98347
Water9,638535
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)118.280, 205.220, 161.940
Angle α, β, γ (deg.)90.00, 105.70, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999989, -0.004188, 0.002276), (-0.00403, 0.997845, 0.065492), (-0.002545, 0.065482, -0.99785)18.76788, -5.33349, 168.7892

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Components

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

#1: Protein Proteasome subunit alpha type-2 / Macropain subunit C3 / Multicatalytic endopeptidase complex subunit C3 / Proteasome component C3


Mass: 25955.613 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: P49722, proteasome endopeptidase complex
#2: 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: 29512.807 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9R1P0, proteasome endopeptidase complex
#3: Protein Proteasome subunit alpha type-7 / Proteasome subunit RC6-1


Mass: 27897.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9Z2U0, proteasome endopeptidase complex
#4: Protein Proteasome subunit alpha type-5 / Macropain zeta chain / Multicatalytic endopeptidase complex zeta chain / Proteasome zeta chain


Mass: 26435.977 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9Z2U1, proteasome endopeptidase complex
#5: Protein Proteasome subunit alpha type-1 / Macropain subunit C2 / Multicatalytic endopeptidase complex subunit C2 / Proteasome component C2 / ...Macropain subunit C2 / Multicatalytic endopeptidase complex subunit C2 / Proteasome component C2 / Proteasome nu chain


Mass: 29586.576 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9R1P4, proteasome endopeptidase complex
#6: Protein Proteasome subunit alpha type-3 / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8 / ...Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8 / Proteasome subunit K


Mass: 28442.248 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: O70435, proteasome endopeptidase complex
#7: Protein Proteasome subunit alpha type-6 / Macropain iota chain / Multicatalytic endopeptidase complex iota chain / Proteasome iota chain


Mass: 27405.434 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9QUM9, proteasome endopeptidase complex

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

#8: 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: 24830.314 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: O35955, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / Proteasome chain 13 / Proteasome component C10-II / Proteasome theta chain


Mass: 22988.895 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9R1P1, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-2 / Macropain subunit C7-I / Multicatalytic endopeptidase complex subunit C7-I / Proteasome component C7-I


Mass: 22935.377 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q9R1P3, proteasome endopeptidase complex
#11: 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


Mass: 22674.686 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: P28063, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-1 / 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: 23576.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: O09061, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-4 / Proteasome beta chain / Low molecular mass protein 3 / Macropain beta chain / Multicatalytic ...Proteasome beta chain / Low molecular mass protein 3 / Macropain beta chain / Multicatalytic endopeptidase complex beta chain / Proteasome chain 3


Mass: 24384.715 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: P99026, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-9 / LMP-2d / Low molecular mass protein 2 / Macropain chain 7 / Multicatalytic endopeptidase complex ...LMP-2d / 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: 21345.162 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
References: UniProt: P28076, proteasome endopeptidase complex

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Non-polymers , 4 types, 582 molecules

#15: Chemical
ChemComp-IOD / IODIDE ION


Mass: 126.904 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: I
#16: Chemical...
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: K
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 535 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.64 Å3/Da / Density % sol: 53.46 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4
Details: 0.2 M NaI, 40% MPD, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Apr 12, 2011
RadiationMonochromator: double-crystal fixed-exit monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→30 Å / Num. all: 122308 / Num. obs: 121329 / % possible obs: 99.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.104 / Net I/σ(I): 10.4
Reflection shellResolution: 3.2→3.3 Å / Rmerge(I) obs: 0.515 / Mean I/σ(I) obs: 2.3 / % possible all: 99.4

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Processing

Software
NameVersionClassification
XDSdata scaling
PHASERphasing
REFMAC5.6.0119refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1IRU

1iru


Resolution: 3.2→15 Å / Cor.coef. Fo:Fc: 0.902 / Cor.coef. Fo:Fc free: 0.888 / SU B: 65.629 / SU ML: 0.473 / Cross valid method: THROUGHOUT / ESU R Free: 0.541 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.25395 6067 5 %RANDOM
Rwork0.23862 ---
obs0.23938 115261 99.2 %-
all-121328 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 82.186 Å2
Baniso -1Baniso -2Baniso -3
1--3.21 Å20 Å2-0.64 Å2
2--7.62 Å20 Å2
3----4.75 Å2
Refinement stepCycle: LAST / Resolution: 3.2→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms48502 0 47 535 49084
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01949380
X-RAY DIFFRACTIONr_angle_refined_deg0.8511.96566718
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.39856216
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.89223.7972186
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.551158648
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.96915350
X-RAY DIFFRACTIONr_chiral_restr0.0560.27484
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02137046
X-RAY DIFFRACTIONr_rigid_bond_restr0.809349380
X-RAY DIFFRACTIONr_sphericity_free22.2945296
X-RAY DIFFRACTIONr_sphericity_bonded2.911548789
LS refinement shellResolution: 3.2→3.279 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.355 419 -
Rwork0.337 7996 -
obs--99.34 %
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)
10.4521-0.3431-0.36221.44250.20910.3207-0.22550.29370.0719-0.06120.21740.05310.2601-0.3130.00820.4226-0.4616-0.10530.83670.05570.0757-8.913-55.52318.779
20.479-0.4974-0.45320.94370.55760.4953-0.12130.19410.218-0.09480.2060.03860.1348-0.1123-0.08470.2983-0.1631-0.13470.64460.36050.3233-3.447-24.64920.322
31.2614-0.6305-0.26741.08010.53160.37540.07460.19980.45630.02450.0506-0.1550.1871-0.061-0.12520.3143-0.06830.06350.25830.27450.524523.873-9.82928.741
40.036-0.00720.09480.26470.47611.6918-0.02370.0804-0.0337-0.00870.04350.11580.1340.0945-0.01970.1357-0.10010.05660.36170.1360.375450.9-24.15235.47
50.64630.35250.4880.20510.25850.5626-0.20640.0183-0.0578-0.09230.0381-0.07490.10310.05380.16830.41250.09410.23350.49090.07090.434258.205-54.60736.503
60.0861-0.11130.03790.9921-0.41710.4265-0.15920.0826-0.1298-0.01220.0613-0.06230.2946-0.00810.09780.77360.00850.32660.2455-0.17610.34540.351-79.04430.208
70.67610.5894-0.45341.1145-0.40920.3091-0.39410.3512-0.1159-0.03090.3002-0.22810.2265-0.23480.09390.9699-0.43290.13860.3661-0.18440.13659.527-79.39821.294
80.4218-0.1824-0.13370.16450.03650.1005-0.17610.16670.22150.03620.1381-0.04850.1951-0.18860.0380.4747-0.3398-0.05860.6046-0.0120.3319-18.369-62.37356.23
90.4912-0.3032-0.50020.21610.20151.1309-0.03590.07250.15060.00180.0627-0.09230.3022-0.2987-0.02670.1976-0.0311-0.04250.45480.14570.4447-19.391-34.38756.629
100.9986-0.1057-1.15960.19270.11571.37320.11330.04280.11270.00790.1378-0.0351-0.1197-0.0789-0.25110.35370.03530.0120.12110.10840.67053.222-12.58663.609
111.06140.13390.40580.0730.21970.67390.2081-0.0018-0.1154-0.01740.0309-0.0532-0.0770.0954-0.2390.3273-0.07830.00140.17060.00530.642534.962-16.34773.02
120.07130.12810.00740.33980.10790.56440.0083-0.12910.0246-0.1032-0.09980.12480.11930.41810.09150.21020.01720.01350.59420.04890.488249.553-43.23277.179
130.2917-0.025-0.40460.5302-0.46311.3851-0.0574-0.1762-0.0211-0.2491-0.09040.0410.33080.2440.14780.4890.17480.14480.1950.07920.523638.194-74.36974.072
140.75950.0286-0.43030.0973-0.1260.3719-0.1515-0.02120.0283-0.17480.0656-0.11510.2526-0.07530.08590.7234-0.11780.10960.0601-0.08110.54958.994-84.63463.254
150.7523-0.2465-0.44581.78690.08630.47750.0983-0.0174-0.11530.14-0.191-0.290.1169-0.0450.09270.2401-0.1293-0.12860.82730.18120.154628.265-59.787146.346
160.04770.1426-0.01281.19050.0960.0293-0.0113-0.0830.05770.18640.0814-0.12490.06230.047-0.07020.2413-0.1908-0.14250.8855-0.14290.19922.673-28.867146.858
172.27550.7180.00560.3657-0.04950.030.1311-0.45390.5013-0.0654-0.1970.10270.0861-0.02840.06590.311-0.15150.11640.5594-0.36880.3741-4.78-13.61139.408
180.3075-0.22330.66960.2043-0.53781.52290.0606-0.1202-0.0445-0.0494-0.02050.01790.1287-0.1331-0.040.0778-0.03120.11270.6619-0.25270.4212-31.687-27.587131.796
190.7878-0.08870.28180.2885-0.23210.79480.0262-0.13860.0893-0.0178-0.04470.11820.0335-0.13720.01850.1649-0.20720.05750.7508-0.0740.2867-38.846-57.909128.716
200.54370.15430.07520.62260.6340.83490.0134-0.2009-0.08520.0108-0.038-0.00720.20480.03580.02450.4841-0.28810.0420.52190.13520.2159-20.89-82.73133.384
210.5461-0.2572-0.22021.17980.15390.09560.001-0.1974-0.1859-0.0431-0.0974-0.01050.05040.04380.09640.4663-0.1365-0.06660.65440.24810.1439.947-83.584142.227
220.47220.5182-0.08740.609-0.13420.0674-0.0186-0.17470.0337-0.1289-0.1017-0.0340.11470.05660.12030.32890.0637-0.00410.54720.14980.412137.77-64.04108.586
230.51640.2027-0.53310.1099-0.2620.69610.1188-0.33450.0624-0.0417-0.1150.07040.08170.3323-0.00380.2551-0.1042-0.03010.6465-0.02010.342338.7-36.088110.009
241.3262-0.2916-1.2560.07980.26251.22520.2142-0.19250.2278-0.08340.03810.0295-0.15720.1004-0.25220.3287-0.14290.02570.2821-0.15490.590115.984-13.975104.464
250.53990.1975-0.0570.1242-0.16840.47330.2031-0.0822-0.04930.06310.00330.0931-0.0777-0.1348-0.20640.36170.0740.00910.3742-0.04910.6958-15.735-17.1394.846
260.089-0.1672-0.04540.42290.07450.95720.0507-0.00440.07050.0264-0.0601-0.06680.0971-0.32670.00940.2303-0.0818-0.02710.48790.03180.4809-30.221-43.7688.914
270.3544-0.3459-0.14540.39160.20071.0011-0.11280.07680.09110.01190.0364-0.1220.3323-0.18640.07640.499-0.3080.01230.3806-0.04190.3712-18.739-75.01489.957
280.0244-0.0896-0.12150.51530.60250.7441-0.0627-0.032-0.01640.0291-0.0290.01560.13830.04530.09170.5579-0.00110.03450.27870.16010.499910.493-85.878100.094
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 230
2X-RAY DIFFRACTION1A234 - 235
3X-RAY DIFFRACTION1A236 - 529
4X-RAY DIFFRACTION2B1 - 248
5X-RAY DIFFRACTION2B261
6X-RAY DIFFRACTION2B262 - 534
7X-RAY DIFFRACTION3C1 - 238
8X-RAY DIFFRACTION3C248 - 249
9X-RAY DIFFRACTION3C250 - 530
10X-RAY DIFFRACTION4D1 - 233
11X-RAY DIFFRACTION4D234 - 235
12X-RAY DIFFRACTION4D236 - 514
13X-RAY DIFFRACTION5E1 - 238
14X-RAY DIFFRACTION5E261 - 263
15X-RAY DIFFRACTION5E264 - 502
16X-RAY DIFFRACTION6F1 - 244
17X-RAY DIFFRACTION6F255
18X-RAY DIFFRACTION6F256 - 508
19X-RAY DIFFRACTION7G1 - 243
20X-RAY DIFFRACTION7G246
21X-RAY DIFFRACTION7G247 - 531
22X-RAY DIFFRACTION8H1 - 219
23X-RAY DIFFRACTION8H235 - 237
24X-RAY DIFFRACTION8H238 - 442
25X-RAY DIFFRACTION9I1 - 204
26X-RAY DIFFRACTION9I205
27X-RAY DIFFRACTION9I206 - 527
28X-RAY DIFFRACTION10J1 - 196
29X-RAY DIFFRACTION10J202 - 511
30X-RAY DIFFRACTION11K1 - 201
31X-RAY DIFFRACTION11K205 - 207
32X-RAY DIFFRACTION11K208 - 499
33X-RAY DIFFRACTION12L1 - 213
34X-RAY DIFFRACTION12L214
35X-RAY DIFFRACTION12L215 - 522
36X-RAY DIFFRACTION13M1 - 216
37X-RAY DIFFRACTION13M220
38X-RAY DIFFRACTION13M221 - 512
39X-RAY DIFFRACTION14N1 - 199
40X-RAY DIFFRACTION14N200 - 203
41X-RAY DIFFRACTION14N204 - 533
42X-RAY DIFFRACTION15O1 - 230
43X-RAY DIFFRACTION15O234
44X-RAY DIFFRACTION15O235 - 438
45X-RAY DIFFRACTION16P1 - 248
46X-RAY DIFFRACTION16P261
47X-RAY DIFFRACTION16P262 - 532
48X-RAY DIFFRACTION17Q1 - 238
49X-RAY DIFFRACTION17Q248 - 249
50X-RAY DIFFRACTION17Q250 - 505
51X-RAY DIFFRACTION18R1 - 233
52X-RAY DIFFRACTION18R234
53X-RAY DIFFRACTION18R235 - 535
54X-RAY DIFFRACTION19S1 - 238
55X-RAY DIFFRACTION19S261 - 262
56X-RAY DIFFRACTION19S263 - 506
57X-RAY DIFFRACTION20T1 - 244
58X-RAY DIFFRACTION20T255
59X-RAY DIFFRACTION20T256 - 519
60X-RAY DIFFRACTION21U1 - 243
61X-RAY DIFFRACTION21U246
62X-RAY DIFFRACTION21U247 - 507
63X-RAY DIFFRACTION22V1 - 219
64X-RAY DIFFRACTION22V235 - 237
65X-RAY DIFFRACTION22V238 - 465
66X-RAY DIFFRACTION23W1 - 204
67X-RAY DIFFRACTION23W205
68X-RAY DIFFRACTION23W206 - 493
69X-RAY DIFFRACTION24X1 - 196
70X-RAY DIFFRACTION24X202 - 521
71X-RAY DIFFRACTION25Y1 - 201
72X-RAY DIFFRACTION25Y205 - 206
73X-RAY DIFFRACTION25Y207 - 526
74X-RAY DIFFRACTION26Z1 - 213
75X-RAY DIFFRACTION26Z214
76X-RAY DIFFRACTION26Z215 - 525
77X-RAY DIFFRACTION27a1 - 216
78X-RAY DIFFRACTION27a220 - 221
79X-RAY DIFFRACTION27a222 - 483
80X-RAY DIFFRACTION28b1 - 199
81X-RAY DIFFRACTION28b200 - 203
82X-RAY DIFFRACTION28b204 - 520

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