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- PDB-4qw6: yCP beta5-M45V mutant in complex with carfilzomib -

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Basic information

Entry
Database: PDB / ID: 4qw6
TitleyCP beta5-M45V mutant in complex with carfilzomib
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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation ...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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
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
CARFILZOMIB, bound form / Chem-3BV / 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 ...CARFILZOMIB, bound form / Chem-3BV / 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 16, 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_conn_type / 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.conn_type_id / _struct_conn.id / _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_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 30, 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-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)736,39948
Polymers730,98728
Non-polymers5,41220
Water4,197233
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area122750 Å2
ΔGint-450 kcal/mol
Surface area213240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.320, 299.760, 145.300
Angle α, β, γ (deg.)90.00, 113.04, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999691, -0.002121, 0.024765), (-0.002239, -0.984619, -0.174698), (0.024755, -0.1747, 0.984311)68.0324, -288.23724, -26.13318

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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: M45V / 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


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


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


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


Mass: 23293.186 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


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, 253 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-3BV / N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide / CARFILZOMIB, bound form


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 723.942 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C40H61N5O7 / References: CARFILZOMIB, bound form / Comment: medication, anticancer, inhibitor*YM
#18: 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
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 233 / 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: 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: Sep 7, 2013
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: 236536 / Num. obs: 231569 / % possible obs: 97.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.085 / Net I/σ(I): 12.1
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.459 / Mean I/σ(I) obs: 3.5 / % possible all: 98.7

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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: 0.953 / Cor.coef. Fo:Fc free: 0.935 / SU B: 27.766 / SU ML: 0.225 / Cross valid method: THROUGHOUT / ESU R Free: 0.291 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20601 11579 5 %RANDOM
Rwork0.17689 ---
all0.182 231569 --
obs0.17834 219990 98.01 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 64.595 Å2
Baniso -1Baniso -2Baniso -3
1-1.94 Å20 Å2-0.56 Å2
2---6.96 Å2-0 Å2
3---3.86 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49293 0 370 233 49896
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950583
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248390
X-RAY DIFFRACTIONr_angle_refined_deg0.8581.97168448
X-RAY DIFFRACTIONr_angle_other_deg0.763.003111442
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.98356306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.70524.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.793158732
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.29115284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27710
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257216
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211340
X-RAY DIFFRACTIONr_mcbond_it2.4855.40625313
X-RAY DIFFRACTIONr_mcbond_other2.4855.40625312
X-RAY DIFFRACTIONr_mcangle_it3.3348.09431588
X-RAY DIFFRACTIONr_mcangle_other3.3348.09431589
X-RAY DIFFRACTIONr_scbond_it2.3875.79325270
X-RAY DIFFRACTIONr_scbond_other2.3875.79325270
X-RAY DIFFRACTIONr_scangle_other2.9738.53336861
X-RAY DIFFRACTIONr_long_range_B_refined3.77842.18554166
X-RAY DIFFRACTIONr_long_range_B_other3.77442.18754144
X-RAY DIFFRACTIONr_rigid_bond_restr0.944398973
X-RAY DIFFRACTIONr_sphericity_free25.6695164
X-RAY DIFFRACTIONr_sphericity_bonded19.974598130
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.326 827 -
Rwork0.29 15720 -
obs--98.45 %
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)
10.00940.0134-0.0040.0358-0.00190.00330.00590.0182-0.0086-0.00470.0025-0.0146-0.0094-0.0123-0.00840.1216-0.0119-0.00550.0887-0.00340.122667.2713-91.743446.1008
20.00390.00450.00490.00650.00770.0096-0.0082-0.0012-0.0058-0.0089-0.00340.0053-0.0047-0.00370.01160.1285-0.00570.00530.09690.00260.126660.0755-87.592316.4448
30.03770.03130.00080.0289-0.00120.00310.0003-0.01120.004-0.00150.0110.01230.0062-0.0063-0.01130.13560.0069-0.0020.08830.00820.123932.8299-87.13251.0744
40.05460.00550.04830.00970.00440.0558-0.0067-0.02130.012-0.0049-0.00160.0325-0.0198-0.00750.00830.09660.025-0.00820.04020.01180.11163.5534-89.813713.5408
50.001-0.00080.00260.00350.00650.0326-0.0067-0.0045-0.00790.0064-0.00050.0177-0.0011-0.00710.00720.10260.01110.01750.08770.00540.1325-2.8461-94.069445.5556
60.00190.00150.00060.00220.00010.0010.01070.00110.0010.0134-0.01060.00810.00530.0071-0.00010.11880.00190.03570.0811-0.01630.09415.5061-94.677569.8032
70.0082-0.00120.00010.0021-0.00040.00090.00550.02280.00730.0131-0.0099-0.00820.002-0.00330.00430.1534-0.00560.00280.0826-0.01130.110647.9476-93.096871.1643
80.00240.0029-0.0020.01630.00720.00930.01930.0055-0.00310.0226-0.0079-0.0336-0.0052-0.0231-0.01140.1153-0.0064-0.0010.0838-0.0010.109467.64-129.774648.075
90.001-0.0002-0.0010.06570.00190.0060.00780.0003-0.0075-0.0058-0.0094-0.0151-0.0104-0.02170.00160.1184-0.00330.00810.09620.00130.124668.7431-127.166420.963
100.02480.0192-0.01310.0208-0.01160.00780.0121-0.01110.0089-0.0101-0.0055-0.0092-0.0002-0.0005-0.00660.14110.00210.00090.10100.119545.2218-126.2724-0.5472
110.0099-0.0049-0.0050.02070.00050.00320.014-0.01320.0206-0.0102-0.00470.0028-0.00620.0133-0.00930.12460.0034-0.01910.09220.00890.12311.3831-130.61112.7623
120.0154-0.00080.01510.0095-0.0020.02590.0107-0.00830.00520.00730.0020.0071-0.00250.0146-0.01270.11070.00460.00090.09330.00570.1447-4.0625-133.896128.621
130.01310.01470.02710.01880.03350.07010.012900.0130.0093-0.00550.00160.03140.0227-0.00740.1295-0.00130.01490.0907-0.00050.12868.156-137.508760.4213
140.00570.00760.0020.1548-0.00770.00210.02230.0129-0.00730.0121-0.0144-0.00560.00350.0087-0.0080.1422-0.0065-0.0040.0954-0.00040.115140.2931-133.817670.4085
150.0120.0046-0.00170.002-0.0010.0037-0.00350.0219-0.0054-0.0050.0057-0.00510.00940.0072-0.00220.1202-0.0098-0.01120.0860.01130.13372.1065-206.089836.7544
160.00160.0004-0.00050.001-0.00120.0015-0.0109-0.00670.0017-0.0012-0.0018-0.01050.00110.0030.01270.1225-0.0069-0.02150.0881-0.00760.12838.5732-204.90956.7085
170.00810.0019-0.00230.0018-0.00120.00560.0101-0.0225-0.0095-0.0106-0.00150.0046-0.00950.0121-0.00860.14090.019-0.00880.0788-0.00750.100935.9751-202.8922-9.1442
180.0057-0.01210.00690.0411-0.02270.01280.0124-0.00010.0178-0.0436-0.0265-0.03490.02660.01380.01410.07720.03280.01350.0475-0.02550.095965.3064-202.34033.3903
190.01920.022-0.00090.03290.00330.0130.02470.0089-0.01360.03510.0021-0.04710.0035-0.0184-0.02670.09120.0173-0.0080.0521-0.0170.141272.228-203.553235.2925
200.01950.0111-0.00530.0091-0.00110.00390.03380.0025-0.03110.0265-0.0246-0.0272-0.0136-0.011-0.00920.13460.008-0.06350.04610.00940.109154.299-207.200259.5407
210.00360.00020.00130.0046-0.00410.00670.00330.0155-0.00230.01540.00090.00350.00050.0116-0.00420.1468-0.012-0.01150.07920.01010.124121.9283-209.2161.1659
220.0012-0.00010.00220.0087-0.00410.00810.0130.0025-0.00150.0041-0.00110.03240.01250.0192-0.01190.1192-0.0098-0.0050.08220.00920.12731.858-168.964145.2878
230.01710.0140.01110.0493-0.02040.0345-0.00010.00020.0007-0.01240.00060.00750.00330.0217-0.00050.12490.0002-0.01340.08870.0030.14310.3004-166.832218.0736
240.0057-0.0068-0.00050.0427-0.00860.0040.0117-0.0167-0.0106-0.0263-0.00250.0092-0.00420.0095-0.00920.1360.006-0.01360.0885-0.0030.118523.4763-163.9594-3.7009
250.0044-0.00060.00510.00130.00040.00720.0144-0.0101-0.0077-0.00460.0061-0.00940.0117-0.0095-0.02050.1210.00910.01910.0919-0.00880.11257.3806-160.2317-0.2168
260.00320.00510.00180.07760.00440.00140.0169-0.0058-0.00990.0042-0.0096-0.02030.0045-0.0069-0.00730.10850.0031-0.00450.0965-0.00350.139273.2054-161.43425.5431
270.21160.04320.12310.0561-0.01840.1431-0.0069-0.0058-0.01520.0087-0.0057-0.0003-0.0466-0.03750.01260.12870.0008-0.01560.07580.00290.122261.5464-163.383757.6673
280.00540.0011-0.00050.00090.00080.00160.01620.01620.00350.0092-0.0021-0.00540.002-0.0034-0.01410.1396-0.01040.00690.09560.00690.110529.6031-168.815467.4714
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 306
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 307
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 305
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 304
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 304
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 306
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 412
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 415
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 408
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 215
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 413
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 310
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 311
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 203
33X-RAY DIFFRACTION14N301 - 302
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 303
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 311
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 307
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 307
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 - 408
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 303
51X-RAY DIFFRACTION22V401 - 409
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 305
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 214
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 407
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301 - 308
61X-RAY DIFFRACTION27a1 - 233
62X-RAY DIFFRACTION27a301 - 314
63X-RAY DIFFRACTION28b1 - 196
64X-RAY DIFFRACTION28b201 - 202
65X-RAY DIFFRACTION28b301 - 309

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