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- PDB-4qw0: yCP beta5-A49T-A50V-double mutant in complex with bortezomib -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qw0
TitleyCP beta5-A49T-A50V-double 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 / 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 / threonine-type endopeptidase activity / Ub-specific processing proteases / Neutrophil degranulation / proteasome complex / 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

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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)733,80946
Polymers731,16728
Non-polymers2,64218
Water3,495194
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area126000 Å2
ΔGint-487 kcal/mol
Surface area215090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.930, 301.260, 145.610
Angle α, β, γ (deg.)90.00, 113.16, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999691, 0.000211, 0.024847), (-0.004465, -0.985216, -0.171257), (0.024443, -0.171315, 0.984913)68.7861, -289.60098, -25.96815
DetailsAU contains one biological assembly.

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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: A49, 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: 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


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, 212 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


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.: 194 / 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: 239156 / Num. obs: 233416 / % possible obs: 97.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 11.8
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.512 / Mean I/σ(I) obs: 2.6 / % possible all: 99.1

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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: 0.937 / SU B: 29.828 / SU ML: 0.239 / Cross valid method: THROUGHOUT / ESU R Free: 0.298 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21142 11671 5 %RANDOM
Rwork0.17785 ---
all0.183 233415 --
obs0.17952 221744 97.72 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 72.647 Å2
Baniso -1Baniso -2Baniso -3
1-4.34 Å2-0 Å20.53 Å2
2---7.95 Å20 Å2
3---2.48 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49372 0 180 194 49746
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950460
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248202
X-RAY DIFFRACTIONr_angle_refined_deg0.8571.96768271
X-RAY DIFFRACTIONr_angle_other_deg0.7063.001110981
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.03656314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.25724.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.109158755
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.94115284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27689
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it3.0396.40625346
X-RAY DIFFRACTIONr_mcbond_other3.0396.40625345
X-RAY DIFFRACTIONr_mcangle_it4.0599.59231630
X-RAY DIFFRACTIONr_mcangle_other4.0599.59231631
X-RAY DIFFRACTIONr_scbond_it3.0016.81325114
X-RAY DIFFRACTIONr_scbond_other3.0016.81325114
X-RAY DIFFRACTIONr_scangle_other3.80310.05936641
X-RAY DIFFRACTIONr_long_range_B_refined4.61249.74353479
X-RAY DIFFRACTIONr_long_range_B_other4.60849.74653455
X-RAY DIFFRACTIONr_rigid_bond_restr1.2398662
X-RAY DIFFRACTIONr_sphericity_free28.2185139
X-RAY DIFFRACTIONr_sphericity_bonded20.284597819
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.341 844 -
Rwork0.299 16036 -
obs--99.2 %
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)
10.0071-0.01050.00090.0494-0.00710.0013-0.00480.0155-0.0077-0.00910.0034-0.0151-0.001-0.00450.00140.0875-0.006-0.00130.078-0.00530.096667.4129-92.110446.0493
20.0024-0.00090.00070.00190.00050.0018-0.00130.0003-0.0107-0.0043-0.00240.01110.0069-0.00110.00380.0871-0.00290.01350.080.00610.097460.1358-87.994116.3486
30.0014-0.00090.00070.0015-0.00110.00090.0023-0.0082-0.0067-0.00240.00330.01160.0041-0.0012-0.00560.11740.00420.00170.06820.00460.091432.8036-87.40011.0186
40.0051-0.004-0.00750.02640.02290.0239-0.0027-0.00730.0014-0.0266-0.01130.0368-0.02720.00210.0140.05320.0172-0.00490.05010.01120.09833.4839-90.213413.5773
50.0011-0.00160.00040.0026-0.00050.0009-0.0008-0.0002-0.00990.00310.00080.0165-0.00050.0065-00.0170.01740.01980.0737-0.00430.1031-2.7974-94.519445.6792
60.0195-0.0002-0.00810.0015-0.0020.0073-0.00410.0037-0.00790.0104-0.00550.0007-0.00640.01180.00960.1108-0.00130.02010.0688-0.00620.097115.624-95.085869.8745
70.0085-0.0035-0.00930.01170.02010.08590.00360.0206-0.00070.0273-0.0092-0.00420.01040.00110.00560.1163-0.00640.00830.0622-0.0070.08648.1105-93.433371.1749
80.00080.0016-0.00060.01770.00370.00220.01020.00440.00130.0283-0.0057-0.0250.0016-0.0109-0.00440.0696-0.0036-0.00420.0798-0.00150.10368.1026-129.650847.5034
90.0049-0.0025-0.01140.029-0.02040.06610.00670.0064-0.00020.0171-0.0079-0.0266-0.0243-0.01120.00130.0767-0.0040.01380.0764-0.00120.103268.8497-127.564520.9146
100.0590.0341-0.05380.0258-0.03790.05870.0173-0.00680.0057-0.0153-0.00540.00020.01470.0043-0.01190.10130.0030.00580.07190.00290.088545.2168-126.7472-0.6664
110.0024-0.00160.00480.0020.00310.05880.0169-0.0004-0.0073-0.01250.00980.0032-0.01520.0265-0.02670.0907-0.001-0.01720.05680.01390.087911.4475-131.07932.6055
120.0111-0.00410.00860.0088-0.00270.0181-0.0057-0.01620.00750.01790.01290.0131-0.01110.0064-0.00720.060.00160.0080.06760.00630.1251-3.9885-134.582728.5201
130.01250.03350.00580.1010.01560.00390.00740.00510.01530.0215-0.00630.0195-0.00020.0088-0.0010.08830.0050.01560.074-0.00190.10338.3524-138.00560.3595
140.0186-0.05010.00660.1648-0.01610.00260.01090.0016-0.00470.0335-0.00830.01070.00620.0029-0.00250.1174-0.00310.00440.0766-0.0020.088640.3214-134.192670.7355
150.0777-0.0039-0.05580.01490.01650.0655-0.00540.01910.0088-0.0089-00.00450.01810.0010.00540.0861-0.0156-0.00710.06250.00740.10492.2498-206.909737.0743
160.04230.00680.01890.00110.00290.0141-0.01030.01180.0005-0.00160.0023-0.00140.0140.00730.0080.0927-0.0064-0.02130.0685-0.00490.09648.8194-205.96696.9582
170.00510.0015-0.00020.01250.0060.00620.0018-0.01150.0083-0.0230.00460.0106-0.00480.0097-0.00640.10980.0172-00.0587-0.00610.073736.1341-204.104-8.8838
180.0042-0.00940.00320.0422-0.0290.0249-0.0001-0.00460.017-0.0412-0.0165-0.04450.03760.02080.01660.05780.03490.0230.0313-0.01130.070765.6108-203.36953.5645
190.02750.03340.00710.04340.00910.0020.0183-0.0131-0.01170.0239-0.0116-0.0310.0035-0.0047-0.00670.03840.0267-0.00510.0609-0.01040.101572.5515-204.351435.6398
200.03550.0158-0.00860.0074-0.00290.01150.0173-0.002-0.01070.0128-0.0104-0.00840.0256-0.0028-0.00680.1280.0089-0.02860.05980.00320.100354.5654-207.875659.8908
210.0211-0.0017-0.00190.0056-0.00130.0015-0.00040.00060.00980.01690.00770.0142-0.00150.0044-0.00730.1347-0.0066-0.00620.06030.00290.087922.1206-209.980861.5303
220.0032-0.00010.00610.04720.00420.01530.0119-0.00450.00040.0284-0.00570.02710.03110.0016-0.00620.0736-0.00780.0070.06560.00150.10191.7237-170.145344.8101
230.0011-0.00050.00130.05690.05520.06040.00880.0002-0.0021-0.0058-0.00950.01950.00920.0030.00070.0874-0.0005-0.01460.07360.00410.11210.4686-167.797618.2047
240.02540.0366-0.00050.088-0.00390.0010.0048-0.0088-0.0117-0.03560.00390.01580.00260.0032-0.00870.10970.0064-0.00870.0692-0.00250.09223.6881-164.9887-3.7034
250.0260.01020.03180.04080.00850.04330.0174-0.003-0.0088-0.038-0.0008-0.00620.01380.0076-0.01660.07820.00270.01560.0765-0.00580.080957.514-161.2258-0.4086
260.00730.0193-0.0090.0695-0.03250.02610.0011-0.0112-0.01040.0173-0-0.02140.0156-0.003-0.00110.07220.00870.00060.075-0.0060.115773.4191-162.041925.431
270.0033-0.009-0.0020.15280.01540.004-0.0060.0114-0.00640.0134-0.0077-0.0092-0.0045-0.00210.01360.10050.006-0.01380.0720.00340.095561.7231-163.967357.6168
280.00330.0083-00.0924-0.02060.00840.01250.00650.0010.0403-0.0056-0.0110.0081-0.0057-0.00680.11570.00040.0050.0767-0.00090.086629.9751-169.509867.8968
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 303
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 306
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 306
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 302
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 310
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 406
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 409
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 402
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 308
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 302
27X-RAY DIFFRACTION11K401 - 409
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 313
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 315
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 305
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 303
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 304
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 302
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 309
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 303
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 306
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 407
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301 - 302
52X-RAY DIFFRACTION22V401 - 408
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 305
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 210
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 409
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 408
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 313
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 305

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