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- PDB-4qz0: yCP beta5-M45V mutant in complex with the epoxyketone inhibitor O... -

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Basic information

Entry
Database: PDB / ID: 4qz0
TitleyCP beta5-M45V 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_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)735,49346
Polymers730,98728
Non-polymers4,50618
Water2,540141
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area121020 Å2
ΔGint-419 kcal/mol
Surface area212960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.050, 299.920, 145.010
Angle α, β, γ (deg.)90.00, 112.94, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.99957, -0.003615, 0.029105), (-0.001447, -0.98509, -0.172031), (0.029293, -0.171999, 0.984661)67.60091, -288.08737, -25.54985

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Components

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Proteasome subunit alpha type- ... , 6 types, 12 molecules AOBPCQDRESGU

#1: Protein Proteasome subunit alpha type-2 /


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: M45V / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-3 /


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


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


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


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


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

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Protein , 1 types, 2 molecules FT

#6: Protein Probable proteasome subunit alpha type-7


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

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

#8: Protein Proteasome subunit beta type-2 / 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: 23293.186 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast) / 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, 159 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


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


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 / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 141 / 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: Sep 7, 2013
RadiationMonochromator: LN2 COOLED FIXED-EXIT. SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3→30 Å / Num. all: 213246 / Num. obs: 208341 / % possible obs: 97.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.7
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 3.2 / % possible all: 98.9

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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: 3→15 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.94 / SU B: 31.536 / SU ML: 0.244 / Cross valid method: THROUGHOUT / ESU R Free: 0.31 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20146 10417 5 %RANDOM
Rwork0.16879 ---
all0.173 208341 --
obs0.17041 197924 97.85 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 73.904 Å2
Baniso -1Baniso -2Baniso -3
1-3.84 Å20 Å2-0.95 Å2
2---7.76 Å2-0 Å2
3---3.18 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49294 0 308 141 49743
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950524
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248288
X-RAY DIFFRACTIONr_angle_refined_deg0.8851.9768372
X-RAY DIFFRACTIONr_angle_other_deg0.8213.003111202
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.98556306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.81724.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.733158732
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.36215284
X-RAY DIFFRACTIONr_chiral_restr0.050.27692
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257214
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it3.0266.10225314
X-RAY DIFFRACTIONr_mcbond_other3.0266.10225313
X-RAY DIFFRACTIONr_mcangle_it4.0899.13831590
X-RAY DIFFRACTIONr_mcangle_other4.0899.13831591
X-RAY DIFFRACTIONr_scbond_it2.9236.5325210
X-RAY DIFFRACTIONr_scbond_other2.9236.5325210
X-RAY DIFFRACTIONr_scangle_other3.7179.6236783
X-RAY DIFFRACTIONr_long_range_B_refined4.63347.6654305
X-RAY DIFFRACTIONr_long_range_B_other4.63247.66254291
X-RAY DIFFRACTIONr_rigid_bond_restr1.267398812
X-RAY DIFFRACTIONr_sphericity_free26.8545119
X-RAY DIFFRACTIONr_sphericity_bonded23.476597921
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.328 747 -
Rwork0.287 14199 -
obs--99.08 %
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)
10.0043-0.0020.00120.0024-0.00150.0035-0.0070.01050.0014-0.0060.0017-0.0084-0.0086-0.01280.00530.1638-0.0135-0.01090.1131-0.00580.147367.1886-91.567146.0759
20.0060.01230.00790.03810.02340.0172-0.01020.008-0.00170.0051-0.0028-0.0066-0.0068-0.01160.0130.1607-0.00560.00890.1250.00780.140359.9748-87.333516.4295
30.0017-0.00010.00120.0014-0.00010.0030.0037-0.0086-0.00740.00720.01080.00510.0099-0.0006-0.01450.16960.00640.0010.12120.00570.138232.7099-86.90791.0145
40.0484-0.00810.04640.0101-0.0030.0615-0.0031-0.0113-0.0112-0.0079-0.00320.0361-0.02320.01190.00630.13840.0197-0.00450.06520.01490.14453.4515-89.66213.5032
50.0002-0.0004-0.00020.0025-0.00040.0009-0.0035-0.0006-0.00280.00330.00870.01770.00750.0045-0.00520.13350.00740.02480.11940.00480.1531-2.9093-93.896545.4847
60.0001-0.0002-0.00030.00290.00110.0024-0.0008-0.0021-0.00220.0091-0.00810.0170.01210.01030.00880.16390.0010.03510.115-0.00510.117715.4657-94.472769.7579
70.0058-0.00390.00080.0037-0.00050.00080.00920.01930.00930.007-0.0179-0.0055-0.0005-0.00130.00870.1994-0.0094-0.00010.103-0.02090.119347.8997-92.911171.1312
80.00340.0056-0.00430.03290.00460.01230.01860.0101-0.00440.0495-0.0131-0.048-0.0046-0.034-0.00550.1471-0.0135-0.00980.10310.00040.131967.6646-129.552748.1613
90.02750.05730.01210.12590.02940.01580.00120.00610.00520.002-0.0064-0.0101-0.0227-0.02720.00520.1529-0.00240.00250.12780.00260.147668.7037-126.969620.8267
100.03360.0301-0.02660.0285-0.02410.02140.0068-0.00410.0021-0.0062-0.0021-0.0048-0.0054-0.0026-0.00460.17460.0040.00170.1315-0.00010.137745.1414-126.057-0.6322
110.00510.0085-0.0010.07310.03190.02290.0092-0.0170.0045-0.0199-0.00060.0285-0.01660.0161-0.00850.15140.014-0.01930.11760.02310.119911.3221-130.32412.4355
120.03090.02710.03320.02760.02440.04920.0161-0.01030.0120.028-0.00640.02770.00270.014-0.00970.13270.0104-0.00450.11750.00860.1476-4.1427-133.779828.5553
130.52380.14750.08050.04920.06630.41990.03680.0034-0.03380.0065-0.0134-0.01160.08290.0167-0.02340.15630.00110.01330.107-0.00440.13178.0516-137.352360.3959
140.00120.00430.00040.04340.00020.00420.0135-0.0013-0.00340.0298-0.002-0.01710.00430.0196-0.01150.1824-0.0087-0.00220.1235-0.00380.136340.1826-133.593170.558
150.07560.0187-0.04540.0049-0.01140.0347-0.01120.02610.0053-0.00640.0101-0.00380.02480.00760.00110.1499-0.0126-0.00760.11650.00810.15082.2269-205.908336.708
160.0010.00030.00090.00040.00010.0009-0.00630.0091-0.00260.00420.0062-0.0013-0.00940.00670.00020.1671-0.0019-0.0180.1189-0.00070.14838.5624-204.72986.6179
170.00520.00170.00060.00590.00880.02230.0085-0.0131-0.009-0.0189-0.00420.004-0.02530.017-0.00430.15970.01920.00320.087-0.00730.113935.9358-202.689-9.3221
180.009-0.00320.00370.023-0.01280.00990.0145-0.01120.004-0.0368-0.0355-0.0290.01980.00350.0210.11720.02090.01220.0726-0.01390.137265.3252-202.05833.2385
190.01560.01450.00330.02170.00570.00350.02990.0071-0.01190.0334-0.0152-0.0440.0081-0.0155-0.01460.09950.0164-0.01390.1096-0.00740.174772.3217-203.313334.9889
200.01980.0159-0.00970.0172-0.00630.00930.0304-0.0025-0.03020.0392-0.031-0.0397-0.0236-0.01430.00070.1372-0.0105-0.06350.0551-0.00810.13754.5249-207.066859.2895
210.01210.0114-0.01090.0208-0.02640.03580.00980.0260.00340.01460.00540.0108-0.01150.006-0.01520.1669-0.006-0.01220.09660.01580.124822.1634-209.070861.0209
220.00430.00090.00270.0066-0.00290.0080.02150.0028-0.00450.0135-0.01070.02630.00840.0268-0.01090.154-0.00730.00310.10960.0090.14191.892-168.860445.3945
230.02060.02110.00720.02310.0070.00570.00550.00290.00470.00150.00260.0182-0.00370.018-0.00810.1591-0.0034-0.01170.12250.00910.15280.2556-166.609417.9842
240.04220.04660.03150.0560.03760.02770.0079-0.0132-0.0082-0.0129-0.00270.00260.00060.0121-0.00520.16950.006-0.01150.1258-0.00540.137523.3989-163.7407-3.8047
250.0050.00480.00310.00950.00560.00340.0195-0.0124-0.01030.0056-0.003-0.03150.0059-0.0018-0.01650.15370.01490.01510.1266-0.01490.131357.3011-160.0334-0.601
260.01080.0227-0.01420.0495-0.02740.02320.0092-0.0051-0.01650.0255-0.0178-0.0462-0.0037-0.00180.00860.13520.01020.01130.1165-0.01330.135373.2325-161.144325.3754
270.85710.25170.30410.1387-0.10130.7526-0.00960.00820.04180.0276-0.00510.011-0.1303-0.07120.01470.150.0023-0.01210.08270.01950.125661.7693-163.188457.5567
280.0064-0.0067-0.0040.05270.00840.00410.01870.0185-0.00610.0243-0.01340.0179-0.0082-0.0127-0.00530.1757-0.0105-0.00420.10270.00730.123529.8847-168.761267.5918
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 304
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 308
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 304
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 302
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 303
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 302
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 405
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 405
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 305
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 210
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301 - 303
25X-RAY DIFFRACTION11K401 - 405
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 306
28X-RAY DIFFRACTION13M1 - 233
29X-RAY DIFFRACTION13M301 - 307
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201 - 202
32X-RAY DIFFRACTION14N301 - 302
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301 - 302
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 305
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 303
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301 - 303
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301 - 303
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 303
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 405
48X-RAY DIFFRACTION22V1 - 222
49X-RAY DIFFRACTION22V301 - 303
50X-RAY DIFFRACTION22V401 - 407
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 305
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201 - 214
55X-RAY DIFFRACTION25Y1 - 212
56X-RAY DIFFRACTION25Y301 - 303
57X-RAY DIFFRACTION25Y401 - 404
58X-RAY DIFFRACTION26Z1 - 222
59X-RAY DIFFRACTION26Z301
60X-RAY DIFFRACTION26Z401 - 407
61X-RAY DIFFRACTION27a1 - 233
62X-RAY DIFFRACTION27a301 - 309
63X-RAY DIFFRACTION28b1 - 196
64X-RAY DIFFRACTION28b201
65X-RAY DIFFRACTION28b301 - 303

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