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- PDB-4qz6: yCP beta5-A49T-A50V double mutant in complex with the epoxyketone... -

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Basic information

Entry
Database: PDB / ID: 4qz6
TitleyCP beta5-A49T-A50V double mutant in complex with the epoxyketone inhibitor ONX 0914
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
Similarity search - Function
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 alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ...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 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 / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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 ...1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsHuber, E.M. / Heinemeyer, W. / Groll, M.
CitationJournal: Structure / Year: 2015
Title: Bortezomib-Resistant Mutant Proteasomes: Structural and Biochemical Evaluation with Carfilzomib and ONX 0914.
Authors: Huber, E.M. / Heinemeyer, W. / Groll, M.
History
DepositionJul 27, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Sep 20, 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_ref_seq_dif / 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_atom_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_atom_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.pdbx_leaving_atom_flag / _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_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)735,33146
Polymers731,16728
Non-polymers4,16418
Water2,990166
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area121870 Å2
ΔGint-455 kcal/mol
Surface area211010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.760, 300.170, 144.960
Angle α, β, γ (deg.)90.00, 112.96, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999694, -0.000283, 0.024719), (-0.003954, -0.985232, -0.171181), (0.024402, -0.171226, 0.98493)68.09466, -288.14328, -25.71966

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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 /


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: A49T, A50V / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-3 /


Mass: 28748.230 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23638, proteasome endopeptidase complex
#3: Protein Proteasome subunit alpha type-4 /


Mass: 28478.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40303, proteasome endopeptidase complex
#4: Protein Proteasome subunit alpha type-5 /


Mass: 28649.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P32379, proteasome endopeptidase complex
#5: Protein Proteasome subunit alpha type-6 /


Mass: 25634.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40302, proteasome endopeptidase complex
#7: Protein Proteasome subunit alpha type-1 /


Mass: 28033.830 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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Protein , 1 types, 2 molecules FT

#6: Protein Probable proteasome subunit alpha type-7


Mass: 31575.068 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21242, proteasome endopeptidase complex

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

#8: Protein Proteasome subunit beta type-2 / PSMB2


Mass: 25114.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / PSMB3


Mass: 22627.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25451, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-4 / PSMB4


Mass: 22545.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P22141, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-5 / PSMB5


Mass: 23383.328 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast)
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6 /


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-7 /


Mass: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-1 / PSMB1


Mass: 21517.186 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 5 types, 184 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 / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-04C / 1,2,4-trideoxy-4-methyl-2-{[N-(morpholin-4-ylacetyl)-L-alanyl-O-methyl-L-tyrosyl]amino}-1-phenyl-D-xylitol


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 584.704 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C31H44N4O7
References: 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
#18: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 166 / Source method: isolated from a natural source / Formula: H2O

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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: 3.67 Å3/Da / Density % sol: 66.52 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: May 13, 2012
RadiationMonochromator: LN2 COOLED FIXED-EXIT. SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→30 Å / Num. all: 235515 / Num. obs: 232924 / % possible obs: 98.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.074 / Net I/σ(I): 12.6
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.509 / Mean I/σ(I) obs: 2.4 / % possible all: 99.7

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Processing

Software
NameClassification
XDSdata scaling
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1RYP

1ryp


Resolution: 2.9→15 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.939 / SU B: 27.644 / SU ML: 0.226 / Cross valid method: THROUGHOUT / ESU R Free: 0.286 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20363 11647 5 %RANDOM
Rwork0.17359 ---
all0.178 232922 --
obs0.1751 221275 99.02 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 71.065 Å2
Baniso -1Baniso -2Baniso -3
1-2.71 Å20 Å20.04 Å2
2---5.98 Å2-0 Å2
3---2.39 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49304 0 286 166 49756
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950510
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248272
X-RAY DIFFRACTIONr_angle_refined_deg0.91.9768352
X-RAY DIFFRACTIONr_angle_other_deg0.823.003111162
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.15956306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.45824.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.675158740
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.35915284
X-RAY DIFFRACTIONr_chiral_restr0.0520.27690
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257214
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it2.916.17525314
X-RAY DIFFRACTIONr_mcbond_other2.916.17525313
X-RAY DIFFRACTIONr_mcangle_it3.9089.24631590
X-RAY DIFFRACTIONr_mcangle_other3.9089.24631591
X-RAY DIFFRACTIONr_scbond_it2.8476.5825196
X-RAY DIFFRACTIONr_scbond_other2.8476.5825196
X-RAY DIFFRACTIONr_scangle_other3.6089.70836763
X-RAY DIFFRACTIONr_long_range_B_refined4.39448.17154224
X-RAY DIFFRACTIONr_long_range_B_other4.3948.16954197
X-RAY DIFFRACTIONr_rigid_bond_restr0.949398782
X-RAY DIFFRACTIONr_sphericity_free28.2525117
X-RAY DIFFRACTIONr_sphericity_bonded19.087597919
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.323 835 -
Rwork0.278 15854 -
obs--99.67 %
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)
10.0282-0.0088-0.00170.0052-00.00110.00350.0163-0.00430.0042-0.0051-0.0141-0.0088-0.00410.00160.1098-0.0141-0.01870.0718-0.00210.102967.0347-91.665845.9983
20.00570.00790.01820.0130.03050.0741-0.0060.0054-0.00610.0006-0.003-0.00150.00270.0050.0090.1157-0.0028-0.00050.07750.00490.108659.8774-87.473616.4483
30.03790.0209-0.03630.0138-0.02320.04070.0143-0.00820.0081-0.00340.01030.01380.0006-0.0008-0.02460.1240.0083-0.01310.07490.00820.105732.7853-86.84971.1487
40.00140.00160.00010.00670.00670.0462-0.0011-0.00570.0047-0.0051-0.00670.02650.0006-0.00490.00790.0890.0167-0.01990.05780.01330.11833.7069-89.527113.6117
50.0011-0.0005-0.00080.0031-0.0010.00150.0038-0.0056-0.0064-0.0003-0.00360.0173-0.00490.0072-0.00020.06870.01750.00180.0656-0.00610.1111-2.5535-93.685245.5981
60.0157-0.0134-0.02320.01550.01930.03670.00560.0009-0.00990.0109-0.01280.0134-0.00620.00980.00720.1207-0.0020.0150.0683-0.01110.088915.7284-94.377869.7149
70.02090.00750.01840.02470.01950.03670.01450.01840.00290.0317-0.0241-0.01660.0166-0.00750.00960.1333-0.0088-0.00990.0532-0.01240.091347.9301-92.904970.9982
80.00120.0061-0.00090.0337-0.00670.00490.0066-0.0034-0.00520.047-0.0116-0.0389-0.014-0.0140.00510.0984-0.0014-0.01710.0746-0.00410.097267.3065-129.712648.098
90.0232-0.01020.00630.08570.03250.02250.01670.0184-0.00730.0004-0.0197-0.0061-0.0107-0.00240.0030.1013-0.00040.00030.08160.00230.101368.3887-127.056120.9432
100.01050.0248-0.00850.114-0.02450.0080.0116-0.00480.016-0.01790.00250.0010.0030.0034-0.01410.1221-0.0036-0.00530.07710.00480.090944.9731-126.1315-0.5076
110.0007-0.0011-0.00070.0031-0.00040.00580.0001-0.0049-0.0068-0.01160.00730.01440.01330.0158-0.00740.10190.0048-0.0350.06530.0160.103611.4635-130.34162.7223
120.03070.03410.03830.05860.05090.06130.0079-0.010.0076-0.0016-0.00460.0208-0.0080.0069-0.00340.09030.0016-0.01240.07420.00140.1294-3.846-133.653228.6133
130.38720.08990.00980.03340.04990.35670.0230.0148-0.02720.003-0.0109-0.0050.05880.0367-0.01210.0992-0.00110.0030.0555-0.00850.10398.1699-137.195660.3591
140.0046-0.02120.00420.1345-0.02570.0050.00550.0023-0.00250.0483-0.0065-0.0061-0.00880.00350.00090.1402-0.0104-0.02160.0766-0.00460.084340.0847-133.581370.4657
150.03990.0078-0.00150.02980.01760.01830.00080.01790.0046-0.01540.00210.01510.00950.0082-0.00290.0989-0.0132-0.0210.06930.00860.10862.0317-205.855536.9772
160.03680.01450.02740.00640.01070.0228-0.00490.0065-0.0041-0.005-0.0041-0.00210.00190.00120.0090.1173-0.0052-0.03460.074-0.00430.10948.451-204.89796.9887
170.00320.0014-0.00320.0171-0.00010.00320.0042-0.01270.0069-0.0345-0.00170.0284-0.00470.0123-0.00240.1250.0165-0.01420.0609-0.01020.082235.4658-203.0893-8.7664
180.0078-0.0034-0.00260.0166-0.02430.0437-0.0117-0.0150.0155-0.0173-0.0146-0.0290.03390.02950.02630.07230.03910.00150.0453-0.01190.070464.7478-202.47263.5361
190.00420.00270.0020.00390.00210.00150.01490.0005-0.01020.0069-0.0048-0.02030.0055-0.005-0.01020.07280.0189-0.02170.05750.00130.117871.6852-203.692535.4932
200.03190.01560.00260.01140.00290.00770.0274-0.0038-0.02060.0117-0.0223-0.02190.003-0.0174-0.00520.11390.0007-0.04120.04940.01330.110653.8755-207.142459.6741
210.00640.0032-0.01120.0046-0.00840.0311-0.00250.01260.00560.01340.00810.00720.0048-0.0017-0.00560.1298-0.0053-0.01570.06470.00520.104421.7528-209.073961.3035
220.00610.00960.00190.01790.00450.00470.0131-0.00980.00840.0244-0.01090.02740.01470.0115-0.00230.0879-0.0036-0.01860.07110.00490.10561.9232-168.750845.4774
230.0172-0.0257-0.00740.08050.01550.00550.00950.00590.0004-0.0354-0.00690.03570.0020.0046-0.00270.1064-0.0027-0.02640.07280.00370.11230.309-166.72118.2269
240.03930.04270.02680.1136-0.00760.04240.0057-0.0024-0.0102-0.0207-0.0011-0.00260.0010.0091-0.00460.12990.0075-0.02720.0748-0.00080.096423.3128-163.9802-3.5335
250.0008-0.0004-0.00030.0015-0.00010.00090.0022-0.00510.0065-0.01010.00490.0033-0.005-0.0033-0.00710.12130.00650.00380.0677-0.00560.097256.8825-160.3766-0.2212
260.00710.0008-0.00330.0494-0.01490.01360.02560.00330.0013-0.0086-0.017-0.01790.0016-0.0124-0.00860.09290.0001-0.01670.0676-0.00250.114172.6582-161.455825.4924
270.58920.0940.10810.1146-0.11930.4721-0.01150.0140.0140.0167-0.0310.0065-0.1083-0.01450.04250.1051-0.0095-0.02240.04790.02450.077761.3038-163.352157.5827
280.0010.0005-0.00010.0054-0.00010.00030.0063-0.0049-0.00480.0203-0.00170.01410.00040.0044-0.00450.1378-0.0087-0.00810.07850.00090.099529.6321-168.690967.6313
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 304
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 306
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 304
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 304
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 310
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 408
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 412
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 403
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 210
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 403
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 306
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 310
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 203
33X-RAY DIFFRACTION14N301 - 306
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 302
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 305
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 302
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 302
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 306
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 307
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 409
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 403
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 208
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 405
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 409
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 309
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201
66X-RAY DIFFRACTION28b301 - 304

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