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- PDB-4qz1: yCP beta5-M45T mutant in complex with the epoxyketone inhibitor O... -

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Basic information

Entry
Database: PDB / ID: 4qz1
TitleyCP beta5-M45T mutant in complex with the epoxyketone inhibitor ONX 0914
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 ...1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 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_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_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_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-2
B: Proteasome subunit alpha type-3
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-6
F: Probable proteasome subunit alpha type-7
G: Proteasome subunit alpha type-1
H: Proteasome subunit beta type-2
I: Proteasome subunit beta type-3
J: Proteasome subunit beta type-4
K: Proteasome subunit beta type-5
L: Proteasome subunit beta type-6
M: Proteasome subunit beta type-7
N: Proteasome subunit beta type-1
O: Proteasome subunit alpha type-2
P: Proteasome subunit alpha type-3
Q: Proteasome subunit alpha type-4
R: Proteasome subunit alpha type-5
S: Proteasome subunit alpha type-6
T: Probable proteasome subunit alpha type-7
U: Proteasome subunit alpha type-1
V: Proteasome subunit beta type-2
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-4
Y: Proteasome subunit beta type-5
Z: Proteasome subunit beta type-6
a: Proteasome subunit beta type-7
b: Proteasome subunit beta type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)735,42443
Polymers730,99128
Non-polymers4,43315
Water3,909217
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area122920 Å2
ΔGint-397 kcal/mol
Surface area213000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)137.180, 298.800, 146.830
Angle α, β, γ (deg.)90.00, 113.02, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999723, 0.001283, 0.023481), (-0.005278, -0.985276, -0.170891), (0.022916, -0.170968, 0.98501)69.15965, -286.86115, -25.74234
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: M45I / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-3 /


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


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


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


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


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

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Protein , 1 types, 2 molecules FT

#6: Protein Probable proteasome subunit alpha type-7


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

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

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


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


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


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


Mass: 23295.158 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): 4932
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6 /


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


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


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

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Non-polymers , 5 types, 232 molecules

#15: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#16: 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
#17: Chemical
ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#18: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 217 / 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
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 14, 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: 3→30 Å / Num. all: 216803 / Num. obs: 212250 / % possible obs: 97.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.097 / Net I/σ(I): 7.8
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.468 / Mean I/σ(I) obs: 2.1 / % 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: pdb entry 1RYP

1ryp


Resolution: 3→15 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.943 / SU B: 35.803 / SU ML: 0.276 / Cross valid method: THROUGHOUT / ESU R Free: 0.329 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21573 10613 5 %RANDOM
Rwork0.17599 ---
obs0.17797 201636 98.05 %-
all-212249 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 84.253 Å2
Baniso -1Baniso -2Baniso -3
1-6.39 Å20 Å2-2.28 Å2
2---8.54 Å2-0 Å2
3---2.29 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49276 0 305 217 49798
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950506
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248258
X-RAY DIFFRACTIONr_angle_refined_deg0.8981.9768348
X-RAY DIFFRACTIONr_angle_other_deg0.8573.003111134
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.98656304
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.93324.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.001158726
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.68415284
X-RAY DIFFRACTIONr_chiral_restr0.050.27689
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257196
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211320
X-RAY DIFFRACTIONr_mcbond_it4.0637.625306
X-RAY DIFFRACTIONr_mcbond_other4.0627.625305
X-RAY DIFFRACTIONr_mcangle_it5.48111.38231580
X-RAY DIFFRACTIONr_mcangle_other5.48111.38231581
X-RAY DIFFRACTIONr_scbond_it3.8867.99425200
X-RAY DIFFRACTIONr_scbond_other3.8857.99425200
X-RAY DIFFRACTIONr_scangle_other4.95711.82636769
X-RAY DIFFRACTIONr_long_range_B_refined6.16559.03754036
X-RAY DIFFRACTIONr_long_range_B_other6.15959.03954015
X-RAY DIFFRACTIONr_rigid_bond_restr1.374398764
X-RAY DIFFRACTIONr_sphericity_free31.795178
X-RAY DIFFRACTIONr_sphericity_bonded24.508597888
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.325 764 -
Rwork0.271 14507 -
obs--99.19 %
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)
10.01780.02060.00860.02410.00990.0043-0.00430.008-0.0063-0.00850.0096-0.003-0.00340.0024-0.00530.0843-0.0102-0.00850.0658-0.00580.104467.8219-91.184446.4379
20.00230.0013-0.00120.00450.00060.0024-0.0083-0.0088-0.008-0.0161-0.00490.00880.0054-0.00220.01320.0852-0.00830.00660.07110.00440.099860.8121-87.200316.8509
30.0007-0.00050.00080.00050.00010.00620.0063-0.005-0.0055-0.00010.00960.00230.00240.0059-0.0160.0990.0021-0.00480.06040.00880.083233.6033-86.46391.4032
40.02-0.0249-0.02140.04450.02240.02790.0034-0.0028-0.0033-0.01260.00090.03980.01140.0127-0.00430.06640.0095-0.01980.04370.00630.09894.2158-88.926913.8122
50.07340.0140.07580.00470.01230.0809-0.014-0.00890.0158-0.00630.00290.0122-0.0152-0.00290.01110.03790.0120.02490.0703-0.00140.1062-2.2908-93.179345.6178
60.0143-0.00130.01960.0004-0.0010.02950.00380.0049-0.00580.0038-0.00190.00510.02110.0009-0.00190.0967-0.0040.02740.0562-0.00860.091915.9659-93.87769.9893
70.0115-0.0031-0.00830.00880.01760.0565-0.00280.0210.0010.0141-0.0087-0.00660.0009-0.0080.01150.1215-0.0051-0.00670.0428-0.00810.078648.4045-92.380571.4749
80.00470.0153-0.00110.0717-0.00020.00270.00690.00560.00140.0361-0.009-0.021-0.0069-0.00990.00210.067-0.0084-0.01250.0651-0.00620.093167.8814-129.259448.5482
90.00190.00530.00060.01540.00220.0033-0.00360.0014-0.013-0.01640.0012-0.0374-0.0146-0.00720.00240.08470.00190.01270.068-0.00210.102469.0488-126.870621.565
100.02720.0224-0.03690.0709-0.05930.06650.0207-0.00620.006-0.0421-0.0149-0.0003-0.0020.0059-0.00590.10640.00450.00170.0633-0.00310.084845.6079-125.83370.1754
110.0053-0.0198-0.00110.10630.00270.00280.0078-0.00010.0006-0.01170.00880.0067-0.00240.0082-0.01650.10290.003-0.02490.05910.00320.093711.8364-129.75233.1711
120.0121-0.0207-0.00940.04150.02340.0487-0.0038-0.0036-0.00010.01080.00830.0157-0.01530.0267-0.00460.0710.0024-0.00480.05650.01030.104-3.6521-132.922729.1035
130.71830.287-0.01140.1346-0.12570.77690.05060.0049-0.04260.0048-0.0142-0.010.12190.0269-0.03640.0484-0.00890.00230.0482-0.0120.07098.4228-136.013160.6554
140.0187-0.0278-0.00060.05460.00190.0010.011-0.0019-0.0030.01350.0003-0.00120.00030.0054-0.01130.1148-0.0094-0.00490.0677-0.0040.09240.4299-132.923870.8976
150.0287-0.0128-0.02030.01530.0070.0166-0.00870.0194-0.0075-0.01890.00630.01230.0172-0.00950.00240.0733-0.0217-0.02630.06060.00840.11391.9584-205.138437.628
160.0263-0.0030.00240.0029-0.00160.0011-0.0074-0.00150.0068-0.0083-0.0013-0.00890.00120.00010.00870.0794-0.0001-0.02770.0617-0.00560.09998.324-204.12057.6511
170.0008-0.0008-0.0010.0021-0.00020.00250.0077-0.00240-0.0106-0.00210.0054-0.00430.0082-0.00560.07020.0064-0.00350.0363-0.01950.052235.5688-202.4553-8.2685
180.0122-0.0158-0.0190.02690.02280.03230.0094-0.00770.0104-0.0301-0.0043-0.0278-0.01910.0088-0.00510.04640.02390.02660.0412-0.01160.089865.034-202.0474.0124
190.00430.00060.00860.0117-0.01890.10360.0177-0.003-0.00910.0060.0087-0.0219-0.00210.0002-0.02630.02950.0044-0.01620.0461-0.00420.107772.0895-203.105235.792
200.01640.0089-0.01310.0066-0.00890.01540.01660.0083-0.01970.0177-0.0138-0.0211-0.0215-0.0189-0.00280.1003-0.0026-0.04460.03760.00010.104854.2216-206.413860.2173
210.0030.0015-0.00160.002-0.00110.00130.0094-0.00720.00770.00330.00080.012-0.00080.0046-0.01020.1166-0.0093-0.02020.06360.00980.089721.8068-208.345761.9808
220.00290.00020.00240.0041-0.00050.00440.012-0.0005-0.0110.0111-0.00990.01020.01310.0104-0.00210.0837-0.00770.00280.06340.00850.10242.0563-168.014545.9892
230.0010.003-0.00110.0221-0.00740.00410.00520.00010.0092-0.02810.00520.04320.00910.0089-0.01040.0804-0.0011-0.02540.05520.00420.10450.4298-165.883518.9141
240.0109-0.0184-0.00650.03860.01610.00770.0077-0.0072-0.0167-0.0415-0.00050.0155-0.0169-0.0004-0.00720.10570.0061-0.0180.0572-0.00450.083323.6344-163.3182-2.7469
250.00390.00550.00450.01310.00840.00660.01210.0013-0.00930.00180.0088-0.02410.00810.0032-0.0210.09810.00840.00960.0631-0.00020.093457.3771-159.9530.2571
260.0068-0.01840.00170.0685-0.00270.01490.00150.0042-0.00510.0162-0.0038-0.02760.0169-0.00360.00230.05030.00850.01210.0605-0.00110.10273.2463-161.092326.0627
270.99160.21580.22030.0797-0.12591.05960.0106-0.02030.06880.0273-0.00980.0088-0.1418-0.0568-0.00070.0548-0.0012-0.00690.04010.02240.064261.6119-162.806458.0747
280.0150.00310.00350.00940.00160.00170.02140.00610.00510.029-0.0124-0.01060.0081-0.0049-0.0090.114-0.0114-0.00770.06570.00470.089829.8704-168.088368.0981
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 - 316
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 306
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 306
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 302
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 304
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301
15X-RAY DIFFRACTION7G401 - 407
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 408
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 306
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 215
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301 - 303
25X-RAY DIFFRACTION11K401 - 410
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 313
28X-RAY DIFFRACTION13M1 - 231
29X-RAY DIFFRACTION13M301 - 316
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201 - 202
32X-RAY DIFFRACTION14N301 - 304
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301 - 304
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 309
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 302
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301 - 305
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301 - 302
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 306
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 408
48X-RAY DIFFRACTION22V1 - 222
49X-RAY DIFFRACTION22V301 - 302
50X-RAY DIFFRACTION22V401 - 408
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 307
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201
55X-RAY DIFFRACTION24X301 - 314
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 302
58X-RAY DIFFRACTION25Y401 - 412
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301 - 306
61X-RAY DIFFRACTION27a1 - 233
62X-RAY DIFFRACTION27a301 - 313
63X-RAY DIFFRACTION28b1 - 196
64X-RAY DIFFRACTION28b201
65X-RAY DIFFRACTION28b301 - 305

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