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- PDB-4qw1: yCP beta5-A50V mutant in complex with bortezomib -

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Basic information

Entry
Database: PDB / ID: 4qw1
TitleyCP beta5-A50V mutant in complex with bortezomib
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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway ...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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / 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
Chem-BO2 / 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 ...Chem-BO2 / 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_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
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-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)733,77347
Polymers731,10728
Non-polymers2,66619
Water6,035335
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area125020 Å2
ΔGint-489 kcal/mol
Surface area213020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.350, 299.860, 144.820
Angle α, β, γ (deg.)90.00, 112.95, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999589, -0.00299, 0.028516), (-0.002037, -0.984627, -0.174655), (0.0286, -0.174642, 0.984217)67.35458, -288.49002, -25.84451

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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: 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


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: 23353.303 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) / Strain (production host): ATCC 204508 / S288c
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 , 4 types, 354 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 9 / 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-BO2 / N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / BORTEZOMIB


Mass: 384.237 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C19H25BN4O4 / Comment: medication, anticancer*YM
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 335 / 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: Oct 20, 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: 234397 / Num. obs: 225490 / % possible obs: 96.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 10.4
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.495 / Mean I/σ(I) obs: 2.9 / % possible all: 97.8

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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: 0.946 / Cor.coef. Fo:Fc free: 0.926 / SU B: 28.94 / SU ML: 0.235 / Cross valid method: THROUGHOUT / ESU R Free: 0.312 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21636 11275 5 %RANDOM
Rwork0.1867 ---
all0.191 225490 --
obs0.18818 214215 96.33 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 60.888 Å2
Baniso -1Baniso -2Baniso -3
1-3.42 Å20 Å2-1.46 Å2
2---4.94 Å2-0 Å2
3---1.57 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49370 0 181 335 49886
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950458
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248204
X-RAY DIFFRACTIONr_angle_refined_deg0.8441.96768268
X-RAY DIFFRACTIONr_angle_other_deg0.6823.001110984
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.06556314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.13924.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.878158754
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.39615284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27688
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it2.4245.21525346
X-RAY DIFFRACTIONr_mcbond_other2.4245.21525345
X-RAY DIFFRACTIONr_mcangle_it3.2257.80831630
X-RAY DIFFRACTIONr_mcangle_other3.2257.80831631
X-RAY DIFFRACTIONr_scbond_it2.3995.60425112
X-RAY DIFFRACTIONr_scbond_other2.3995.60425112
X-RAY DIFFRACTIONr_scangle_other2.9968.25236638
X-RAY DIFFRACTIONr_long_range_B_refined3.78240.75154225
X-RAY DIFFRACTIONr_long_range_B_other3.77240.75554200
X-RAY DIFFRACTIONr_rigid_bond_restr1.34398662
X-RAY DIFFRACTIONr_sphericity_free28.575235
X-RAY DIFFRACTIONr_sphericity_bonded17.648597866
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.364 817 -
Rwork0.301 15529 -
obs--98.06 %
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)
10.0076-0.0025-0.00140.00520.00420.0056-0.00220.0199-0.01180.00870.001-0.0068-0.0040.00560.00130.0972-0.0089-0.00690.0879-0.0020.101967.1105-91.87746.1564
20.0032-0.00140.00450.00680.00440.01490.00320.0025-0.0107-0.0083-0.00720.01740.01180.00180.0040.0916-0.00570.0110.09150.00510.091859.7466-87.596616.5356
30.00350.0008-0.00280.0017-0.00180.0039-0.0044-0.01240.0058-0.01030.01270.00720.01080.0047-0.00830.10510.0031-0.00880.08250.00490.09432.501-87.0861.174
40.02630.00490.04620.00810.00940.0825-0.0171-0.00120.0068-0.01070.00260.027-0.03360.00470.01450.06170.0192-0.01090.05780.01120.10373.2897-89.817913.7541
50.00650.0166-0.00710.052-0.02190.0099-0.00540.001-0.0052-0.01690.01020.01580.00620.0034-0.00480.06350.01470.00630.0790.00150.0999-3.0038-94.228145.7332
60.00510.0101-0.00380.0241-0.00780.00370.0137-0.0045-0.00270.0286-0.02090.0064-0.0060.00740.00730.07880.01430.02450.0708-0.01350.070115.3879-94.883569.9455
70.011-0.0040.00650.0049-0.00060.03990.00350.02520.00330.0173-0.0092-0.00650.00410.00320.00570.1088-0.0037-0.00320.068-0.01420.083247.8288-93.255471.2846
80.0049-0.0027-0.01150.00990.00620.04910.00890.01390.01070.0196-0.0023-0.0208-0.0192-0.0196-0.00660.0779-0.0109-0.01240.0866-0.00080.095967.7737-129.315347.5688
90.0042-0.0139-0.00130.04920.00440.0030.00410.00230.00650.0125-0.013-0.0149-0.0089-0.01150.00890.0925-0.00110.00120.0931-0.00390.101168.4158-127.15820.9347
100.0068-0.0014-0.0020.02770.00370.00120.0091-0.01430.0154-0.0102-0.0012-0.011-0.00110.0068-0.00790.10840.0016-0.00130.08880.00420.089444.9008-126.1642-0.677
110.00190.0036-0.00020.00830.00110.0140.00480.00170.00380.00430.00650.0157-0.00650.0265-0.01130.08610.0031-0.020.07290.01350.090211.1048-130.45512.3838
120.01470.00520.01490.00340.00180.02740.0117-0.0106-0.00170.0112-0.00060.008-0.01180.0048-0.01110.08070.00340.00090.08310.01260.109-4.3325-134.058928.5902
130.0008-0.005-0.00110.05430.01430.00470.00230.00460.00260.0122-0.00450.009-0.00190.00670.00220.09890.00070.00460.0944-0.00170.10458.0027-137.683260.4506
140.0038-0.0009-0.00470.00840.00330.00970.00270.00610.00040.0153-0.00480.01240.01210.00590.00210.1085-0.0018-0.00960.09820.00180.088240.0238-133.937570.771
150.0339-0.0089-0.01580.00530.0050.011-0.01090.01530.0064-0.0090.0071-0.0010.01160.00780.00380.0881-0.0079-0.01660.08370.00820.10851.9028-206.16436.518
160.0029-0.00170.00550.003-0.00870.0262-0.0055-0.00990.00710.0003-0.0022-0.00350.00280.00070.00760.1038-0.0007-0.02170.0791-0.00640.10578.4335-204.93586.4504
170.0056-0.0048-0.00190.00460.00070.00510.0115-0.004-0.0094-0.0097-0.00190.01350.00430.0127-0.00960.10640.0125-0.00230.0314-0.01810.071235.7032-202.9008-9.4453
180.0022-0.00640.00380.0272-0.01710.01080.0053-0.00230.0118-0.0408-0.0155-0.0240.02620.00970.01020.06450.03020.02290.0444-0.03370.073365.0888-202.38863.1587
190.02390.02080.00040.02310.00620.01160.019-0.00140.00140.01530.0033-0.02150.0041-0.0102-0.02230.05250.0297-0.01820.0551-0.01510.10772.016-203.614234.9938
200.00970.0060.00030.00470.00150.00260.021-0.0047-0.02120.0118-0.0137-0.0167-0.0061-0.0107-0.00730.09140.0153-0.04560.04430.01790.071154.1417-207.352259.2541
210.00410.0008-0.00220.0022-0.00140.00210.00230.01620.00030.01220.0050.0067-0.0011-0.0097-0.00730.1125-0.007-0.01380.06580.01170.091121.7495-209.393560.9115
220.00140.00080.00290.00210.00330.00810.00540.0014-0.00810.01140.0030.00460.01940.012-0.00840.0836-0.01050.00280.08070.01220.10131.3563-169.596744.6161
230.00180.00140.00220.0042-00.0046-0.00090.0102-0.0015-0.01570.00790.00950.00920.017-0.00710.0969-0.0011-0.01810.08480.00230.10990.187-166.916417.9982
240.00480.00390.00160.02910.00420.00210.0056-0.0074-0.0154-0.0290.00380.002-0.0020.007-0.00940.10250.0063-0.01870.0852-0.00340.091723.2569-164.003-3.9444
250.00270.00390.00150.0262-0.00180.00250.0051-0.0017-0.0032-0.00380.0104-0.010.0086-0.0032-0.01550.09470.0060.01250.0817-0.00990.079657.15-160.3256-0.7756
260.00320.0047-0.00140.0174-0.0060.01010.0026-0.0114-0.00630.01380.002-0.00290.0159-0.0054-0.00470.07650.0084-0.00470.0902-0.00450.107673.0703-161.405425.3353
270.0131-0.01760.00370.0379-0.00880.00450.00420.0131-0.01090.0128-0.005-0.0147-0.0005-0.01150.00080.1019-0.0022-0.01380.0860.00450.095661.3962-163.529257.5499
280.003-0.00150.00060.002300.00130.0080.01320.00160.0072-0.0090.00440.0056-0.00390.0010.1135-0.0038-0.00350.09580.00060.090629.6113-169.143167.7073
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 313
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 318
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 311
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 309
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 303
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 314
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 413
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 423
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 414
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 315
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 302
27X-RAY DIFFRACTION11K401 - 410
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 316
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 316
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 308
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 306
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 307
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 311
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 304
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 307
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 307
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 412
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301 - 302
52X-RAY DIFFRACTION22V401 - 416
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 309
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 217
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 408
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 417
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 317
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 314

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