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- PDB-4qz3: yCP beta5-A49V mutant in complex with the epoxyketone inhibitor O... -

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Basic information

Entry
Database: PDB / ID: 4qz3
TitleyCP beta5-A49V 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: 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

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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
Water5,981332
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.760, 300.170, 144.960
Angle α, β, γ (deg.)90.00, 112.96, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999652, -0.001633, 0.026337), (-0.00291, -0.985175, -0.171528), (0.026227, -0.171545, 0.984827)67.72233, -288.12567, -25.70673

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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: A49V / 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: 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 / 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, 349 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 / 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.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 332 / 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: 2.8→30 Å / Num. obs: 254320 / % possible obs: 97.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 9.2
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.482 / Mean I/σ(I) obs: 2.3 / % 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: pdb entry 1RYP

1ryp


Resolution: 2.8→15 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.941 / SU B: 25.084 / SU ML: 0.21 / Cross valid method: THROUGHOUT / ESU R Free: 0.271 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20748 12716 5 %RANDOM
Rwork0.18054 ---
obs0.18188 241603 97.32 %-
all-254319 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 64.466 Å2
Baniso -1Baniso -2Baniso -3
1-2.64 Å20 Å2-0.16 Å2
2---6.23 Å2-0 Å2
3---2.69 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49300 0 285 332 49917
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950506
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248270
X-RAY DIFFRACTIONr_angle_refined_deg0.9021.9768346
X-RAY DIFFRACTIONr_angle_other_deg0.8133.003111156
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.14156306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.34224.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.733158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.48215284
X-RAY DIFFRACTIONr_chiral_restr0.0520.27688
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257214
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it2.3645.49325314
X-RAY DIFFRACTIONr_mcbond_other2.3645.49325313
X-RAY DIFFRACTIONr_mcangle_it3.1598.22431590
X-RAY DIFFRACTIONr_mcangle_other3.1598.22431591
X-RAY DIFFRACTIONr_scbond_it2.3155.85325192
X-RAY DIFFRACTIONr_scbond_other2.3155.85325192
X-RAY DIFFRACTIONr_scangle_other2.8848.6336757
X-RAY DIFFRACTIONr_long_range_B_refined3.59642.71753982
X-RAY DIFFRACTIONr_long_range_B_other3.58442.71753942
X-RAY DIFFRACTIONr_rigid_bond_restr1.635398776
X-RAY DIFFRACTIONr_sphericity_free28.6195202
X-RAY DIFFRACTIONr_sphericity_bonded16.203597994
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.337 923 -
Rwork0.301 17551 -
obs--98.9 %
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)
10.0117-0.01320.00080.0356-0.00630.0034-0.00640.0153-0.0036-0.0078-0.0015-0.0053-0.0077-0.00820.00790.1011-0.0134-0.01130.0783-0.00360.125967.3118-91.782546.0523
20.0015-0.0011-0.00550.00410.00750.0251-0.0073-0.002-0.0017-0.0074-0.00770.00510.00340.00670.0150.0844-0.0090.0120.0810.00820.124260.0418-87.589916.4424
30.01940.01480.01430.01420.00860.01530.0075-0.00560.0006-0.00020.00840.01670.00970.0023-0.01590.1120.0065-0.0050.0850.00380.121532.7741-86.99811.1387
40.0007-0.0018-0.00010.02970.02060.0186-0.00260.0015-0.0078-0.0097-0.00610.038-0.01010.00810.00870.07520.0138-0.00470.06150.01340.12323.464-89.584113.6654
50.0005-0.00080.00010.0018-0.00020.0007-0.0019-0.003-0.00660.00380.0020.0157-0.00370.0039-0.00010.05130.01990.02140.0751-0.00610.1403-2.883-93.735545.7678
60.0382-0.0075-0.00970.00350.00240.00490.0075-0.0036-0.00040.0088-0.00890.0040.01130.00830.00140.10970.00080.01330.0741-0.00640.12115.5745-94.405569.9234
70.0061-0.0045-0.0010.01350.0020.0020.01050.0154-0.00040.0196-0.0182-0.01890.0093-0.00770.00760.1326-0.0089-0.00380.0543-0.01870.106948.0477-92.943271.1626
80.00380.0042-0.00530.0241-0.00220.00870.01320.00730.00030.0318-0.0112-0.035-0.013-0.0178-0.0020.0703-0.0104-0.00640.0672-0.00790.12367.578-129.783848.2594
90.00430.01-0.00220.0262-0.00430.00370.0037-0.00140.00130.0013-0.0083-0.0136-0.012-0.00920.00460.0913-0.00350.00430.08660.00210.1468.5908-127.259620.9718
100.01920.0234-0.01670.0403-0.02450.01770.0066-0.0080.0145-0.0163-0.0034-0.0056-0.0027-0.006-0.00320.11640.0051-0.00260.08330.00430.118945.0434-126.2095-0.5129
110.0029-0.0019-0.00290.00130.00170.00590.0148-0.00360.0042-0.01090.0028-0.0003-0.00640.0118-0.01760.11120.0012-0.02320.07370.01190.122311.1876-130.3542.6325
120.00240.0032-0.00340.0047-0.00470.00590.0086-0.00860.01170.0115-0.00430.0164-0.01430.0137-0.00430.07790.0056-0.00620.07980.00050.1468-4.2741-133.649728.7733
130.36310.15690.04160.07480.01380.50150.03770.0233-0.03070.0143-0.0141-0.01620.08640.0113-0.02370.0769-0.00930.00440.0656-0.00670.12047.9226-137.224660.6081
140.00310.0197-0.00330.1364-0.02260.00380.0063-0.0026-0.00640.0239-0.0082-0.0141-0.0059-00.00190.1222-0.0087-0.00830.0805-0.00010.11940.0855-133.626470.7014
150.0075-0.00010.00210.00290.00330.00880.00130.02030.00480.00060.00120.01060.01830.0081-0.00250.0872-0.015-0.01450.07560.00430.13281.7197-205.742436.9808
160.04630.00340.00580.0015-0.00020.0021-0.00790.009-0.0123-0.0095-0.002-0.0042-0.00320.00540.00990.1007-0.0073-0.02780.0757-0.0050.1248.268-204.74896.8971
170.01070.0048-0.0060.0151-0.0010.00410.0043-0.02460.0044-0.0396-0.00470.015-0.00450.01330.00030.11850.0181-0.01140.0569-0.01220.113335.4316-202.8451-8.8689
180.0099-0.0090.01110.0413-0.0360.03330.0037-0.0120.0078-0.033-0.0196-0.03410.0310.00530.01580.06060.0177-0.00460.0396-0.0140.114864.9485-202.33043.4159
190.00670.0092-0.0130.0198-0.02210.03750.0082-0.00350.00010.0047-0.0057-0.0272-0.0024-0.0053-0.00240.06120.019-0.00740.0688-0.00580.14771.9439-203.641935.4897
200.02420.0151-0.02080.0139-0.0140.02410.02670.0018-0.02020.0184-0.0248-0.0152-0.0207-0.0116-0.00190.105-0.0062-0.03860.06120.00730.131553.9457-207.151159.7305
210.00910.003-0.01360.0044-0.01130.04310.00210.01690.00530.01110.0010.00620.0020.0049-0.00310.1211-0.0079-0.01250.07210.00580.125121.5738-209.076361.3495
220.00220.0010.00040.011-0.00130.00530.012-0.0095-0.00580.0105-0.00690.03110.01480.0117-0.00510.0796-0.0071-0.00960.07660.00260.12441.5957-168.720345.6459
230.01110.01580.01120.03130.01110.0156-0.00690.00090.0077-0.03280.00110.03010.00960.00940.00570.0894-0.0081-0.01240.07870.00830.13880.032-166.530318.302
240.00150.0008-0.00080.0049-0.00150.00090.0037-0.0105-0.0025-0.0207-0.01070.00090.00350.00610.0070.12030.006-0.01870.0828-0.00180.128423.1731-163.8442-3.5605
250.005-0.00070.00090.0037-0.0020.00140.0153-0.01580.0011-0.0122-0.00470.01530.0043-0.0006-0.01060.10880.00420.00910.084-0.0080.124657.0918-160.2619-0.4067
260.0048-0.0172-0.00240.08710.01970.0090.00750.0001-0.00730.0052-0.0047-0.02020.0154-0.012-0.00280.0710.00730.00270.0855-0.00260.13473.0469-161.445825.5581
270.65350.10590.12450.0272-0.02860.4701-0.01060.02920.03210.016-0.0115-0.0053-0.0973-0.02840.02210.0925-0.0123-0.01010.05390.02770.098361.494-163.376857.7785
280.0010.00030.00040.00130.00040.00020.0050.0008-0.00750.0097-0.00020.00660.00370.0028-0.00470.1207-0.0088-0.00140.08790.00110.122329.5449-168.712567.826
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 307
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 315
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 308
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 303
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 314
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 413
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 418
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 413
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 219
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 411
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 313
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 319
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 202
33X-RAY DIFFRACTION14N301 - 309
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 311
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 305
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 303
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 307
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 305
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 315
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 420
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 413
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 311
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 223
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 414
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 414
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 313
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201
66X-RAY DIFFRACTION28b301 - 308

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