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- PDB-4qz7: yCP beta5-A50V mutant in complex with the epoxyketone inhibitor O... -

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Basic information

Entry
Database: PDB / ID: 4qz7
TitleyCP beta5-A50V 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 / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / 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 / Ub-specific processing proteases / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / Neutrophil degranulation / proteasome complex / peroxisome / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / 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 alpha5 / Proteasome subunit alpha6 / 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 alpha5 / Proteasome subunit alpha6 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
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: 2.8 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
Revision 1.3Nov 27, 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)735,24745
Polymers731,10728
Non-polymers4,14017
Water4,179232
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area120640 Å2
ΔGint-439 kcal/mol
Surface area214020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.790, 300.310, 146.090
Angle α, β, γ (deg.)90.00, 112.83, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999684, -2.2E-5, 0.025126), (-0.004363, -0.984652, -0.174472), (0.024744, -0.174526, 0.984342)68.19183, -288.24075, -26.06151
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: 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)
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, 249 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-CL / CHLORIDE ION


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


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


Mass: 18.015 Da / Num. of mol.: 232 / 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: 2.8→30 Å / Num. all: 264122 / Num. obs: 256991 / % possible obs: 97.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 9.8
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.489 / Mean I/σ(I) obs: 2.6 / % possible all: 98.8

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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: 2.8→15 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.942 / SU B: 26.487 / SU ML: 0.221 / Cross valid method: THROUGHOUT / ESU R Free: 0.276 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21293 12850 5 %RANDOM
Rwork0.17549 ---
all0.18 256990 --
obs0.17736 244140 97.42 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 68.921 Å2
Baniso -1Baniso -2Baniso -3
1-4.61 Å2-0 Å20.97 Å2
2---7.59 Å20 Å2
3---1.9 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49291 0 285 232 49808
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950497
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248259
X-RAY DIFFRACTIONr_angle_refined_deg0.9411.9768333
X-RAY DIFFRACTIONr_angle_other_deg0.8213.003111131
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.46956305
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.72124.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.242158736
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.21415284
X-RAY DIFFRACTIONr_chiral_restr0.0530.27686
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257203
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211321
X-RAY DIFFRACTIONr_mcbond_it2.7386.32625310
X-RAY DIFFRACTIONr_mcbond_other2.7386.32525309
X-RAY DIFFRACTIONr_mcangle_it3.5939.47631585
X-RAY DIFFRACTIONr_mcangle_other3.5939.47631586
X-RAY DIFFRACTIONr_scbond_it2.76.78125187
X-RAY DIFFRACTIONr_scbond_other2.76.78125187
X-RAY DIFFRACTIONr_scangle_other3.3179.99136749
X-RAY DIFFRACTIONr_long_range_B_refined4.08249.47853960
X-RAY DIFFRACTIONr_long_range_B_other4.07549.47753937
X-RAY DIFFRACTIONr_rigid_bond_restr1.189398756
X-RAY DIFFRACTIONr_sphericity_free28.6115176
X-RAY DIFFRACTIONr_sphericity_bonded14.484597899
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.333 933 -
Rwork0.286 17728 -
obs--98.91 %
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)
10.036-0.0320.00370.06-0.02520.0182-0.00550.0109-0.00560.0052-0.001-0.0104-0.00610.00140.00650.0491-0.00920.00450.0221-0.00830.052367.2293-91.761146.5597
20.0685-0.01060.00070.01090.00110.0569-0.00260.00370.0026-0.0141-0.00360.0007-0.0050.01680.00620.0446-0.00670.02490.02360.00430.04360.0028-87.568316.8501
30.05090.0424-0.04110.0402-0.04610.07510.01090.00050.006-0.00020.00680.0112-0.00460.0041-0.01780.05730.00440.00250.01760.00750.042932.7023-87.08811.4522
40.07820.03940.00260.05510.01430.0064-0.0101-0.01490.0028-0.013-0.00010.0436-0.00690.00030.01020.03760.0151-0.01410.01480.01370.05993.3906-89.687113.9014
50.0238-0.0136-0.01580.0334-0.00390.0188-0.0054-0.0074-0.00720.02170.0130.0399-0.0071-0.0045-0.00760.01690.01390.02120.0216-0.00250.0669-3.0145-93.917845.994
60.0242-0.02490.00760.0639-0.00040.00410.00850.00740.00020.0245-0.01150.02170.00520.00130.0030.06020.00050.04350.0205-0.00920.036815.397-94.563370.2637
70.0119-0.0043-0.0190.00980.01190.04620.00690.01020.00230.0193-0.005-0.0039-0.0085-0.0142-0.00190.0845-0.00470.0110.0148-0.01060.036347.9487-93.107671.6336
80.0020.00070.00230.0331-0.0050.0160.00130.00280.0040.0216-0.007-0.0308-0.01950.00230.00570.0406-0.0077-0.00620.0271-0.00360.055367.6697-129.886848.6152
90.02030.0239-0.02210.13930.02190.0480.00450.0037-0.0011-0.0004-0.0092-0.0174-0.0087-0.00560.00470.0413-0.00320.01330.0274-0.00120.055468.6311-127.26221.4354
100.0544-0.0070.0060.1329-0.03040.04120.0128-0.00240.0165-0.04-0.0021-0.0004-0.00150.0059-0.01070.05920.00220.01080.02140.00160.038445.0876-126.3211-0.1008
110.04720.0093-0.02790.1866-0.01660.01740.00910.00180.0136-0.02480.00680.0428-0.0036-0.0029-0.01580.03760.0095-0.02470.02430.00990.039611.2019-130.50662.9578
120.0482-0.0242-0.00850.1150.02040.01170.0185-0.0070.00830.0009-0.00990.027-0.0051-0.0064-0.00870.0180.0038-0.00450.02520.00490.0712-4.3926-133.864829.0613
130.430.14270.0310.1486-0.08880.58330.02490.0065-0.02650.0199-0.0120.00890.06610.0079-0.01290.0296-0.00120.02150.0123-0.00730.03497.8291-137.241660.8422
140.08640.0132-0.04280.1238-0.02620.02570.0088-0.00270.0050.0316-0.0055-0.0036-0.00280.0059-0.00330.0656-0.00480.00260.0246-0.01230.017340.0827-133.813371.0125
150.07310.0218-0.01110.02160.02140.0462-0.00460.00890.010.00150.0030.00860.0177-0.0070.00170.0439-0.0124-0.00660.01960.00750.05611.9008-206.137537.1779
160.10140.00430.03720.0482-0.02530.0478-0.00290.00580.0059-0.0192-0.0041-0.00180.0164-0.00540.0070.0367-0.0066-0.0270.0186-0.00550.04278.3783-205.01867.0437
170.03750.04010.0040.0828-0.02370.08320.0071-0.0037-0.0039-0.0437-0.0050.00820.0130.0082-0.00210.07350.0128-0.0110.0109-0.01180.031535.6764-203.0048-8.8157
180.0164-0.02380.00870.044-0.01540.01570.0057-0.00390.0172-0.0323-0.0097-0.02980.0230.01150.0040.05360.0220.02990.0251-0.00910.045165.1412-202.50813.5911
190.01970.0191-0.03170.0349-0.01620.08430.00140.0022-0.00830.01430.0108-0.03930.0120.0044-0.01220.02520.0209-0.00950.0194-0.00860.074672.1639-203.836335.5904
200.06190.01550.01180.0325-0.0280.04910.0259-0.0089-0.01160.0193-0.014-0.020.0024-0.0026-0.01190.0570.0032-0.03020.01120.01260.047154.2228-207.517959.9104
210.0122-0.0109-0.00990.01390.0090.0508-0.00180.001-0.00910.01560.0050.00790.0080.0042-0.00310.0732-0.0021-0.00730.01710.00870.040421.747-209.40161.5708
220.00580.0006-0.00970.0153-0.00340.0213-0.0026-0.0029-0.00480.0020.00040.02990.01870.00450.00220.0374-0.00760.00020.01890.0050.06721.6196-169.015545.8588
230.02220.03160.01860.1352-0.02110.0460.0024-0.00230.005-0.0146-0.00450.04010.01110.00090.00210.029-0.0062-0.01850.01820.00290.06290.1265-166.859618.5937
240.03450.0289-0.02350.1052-0.00450.02140.00090.002-0.0054-0.03640.0020.0155-0.0057-0.0035-0.00290.0610.0005-0.01990.02010.00080.040123.2555-164.0004-3.25
250.06260.08130.00890.1684-0.0020.00850.0108-0.0004-0.0021-0.0299-0.0031-0.02570.00870.0065-0.00780.04790.00810.02740.0287-0.01050.034557.2025-160.3852-0.0899
260.0606-0.0058-0.07280.11430.03180.11380.0134-0.0072-0.00450.0007-0.0047-0.0215-0.00230.0086-0.00880.01420.00720.00740.0283-0.00330.05973.2794-161.574825.9023
270.69830.22020.13820.1399-0.02050.80870.0094-0.00010.04540.0241-0.02060.0036-0.1021-0.00920.01110.0332-0.0012-0.01070.01090.01110.028561.6474-163.575558.0971
280.02880.02720.02810.09890.02970.0290.0128-0.002-0.00330.0155-0.00330.01350.0096-0.0052-0.00940.0638-0.00420.0110.0270.00530.037629.6644-168.992268.0657
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 - 308
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 310
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 303
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 303
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 308
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 410
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 410
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 406
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 210
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 409
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 311
29X-RAY DIFFRACTION13M1 - 232
30X-RAY DIFFRACTION13M301 - 309
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 202
33X-RAY DIFFRACTION14N301 - 306
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 303
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 308
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 306
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 305
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 306
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 309
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 410
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 410
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 305
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 212
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 414
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 416
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 311
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201
66X-RAY DIFFRACTION28b301 - 308

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