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- PDB-4qw5: yCP beta5-M45A mutant in complex with carfilzomib -

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Basic information

Entry
Database: PDB / ID: 4qw5
TitleyCP beta5-M45A mutant in complex with carfilzomib
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
CARFILZOMIB, bound form / Chem-3BV / 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 ...CARFILZOMIB, bound form / Chem-3BV / 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 16, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)736,31847
Polymers730,93128
Non-polymers5,38819
Water3,045169
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.550, 300.110, 145.150
Angle α, β, γ (deg.)90.00, 113.00, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999735, -0.001333, 0.022961), (-0.002695, -0.984654, -0.174496), (0.022841, -0.174512, 0.98439)67.77622, -288.5321, -26.07689

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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: M45A / 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: 23265.131 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, 188 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-3BV / N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide / / CARFILZOMIB, bound form / Carfilzomib


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 723.942 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C40H61N5O7 / References: CARFILZOMIB, bound form / Comment: medication, anticancer, inhibitor*YM
#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.: 169 / 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: 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: 212666 / Num. obs: 210752 / % possible obs: 99.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 13.2
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.475 / Mean I/σ(I) obs: 2.4 / % possible all: 99.4

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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: 31.837 / SU ML: 0.244 / Cross valid method: THROUGHOUT / ESU R Free: 0.306 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20062 10538 5 %RANDOM
Rwork0.1693 ---
all0.174 210751 --
obs0.17086 200213 99.24 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 71.373 Å2
Baniso -1Baniso -2Baniso -3
1-3.6 Å2-0 Å2-0.17 Å2
2---7.94 Å20 Å2
3---3.24 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49289 0 369 169 49827
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950579
X-RAY DIFFRACTIONr_bond_other_d0.0030.0248382
X-RAY DIFFRACTIONr_angle_refined_deg0.8721.97168442
X-RAY DIFFRACTIONr_angle_other_deg0.7643.003111424
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.03556306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.00424.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.954158730
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.48815284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27708
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257216
X-RAY DIFFRACTIONr_gen_planes_other0.0020.0211340
X-RAY DIFFRACTIONr_mcbond_it2.9896.25125313
X-RAY DIFFRACTIONr_mcbond_other2.9896.25125312
X-RAY DIFFRACTIONr_mcangle_it4.0349.36131588
X-RAY DIFFRACTIONr_mcangle_other4.0349.36131589
X-RAY DIFFRACTIONr_scbond_it2.96.6325266
X-RAY DIFFRACTIONr_scbond_other2.8996.6325266
X-RAY DIFFRACTIONr_scangle_other3.6869.79236855
X-RAY DIFFRACTIONr_long_range_B_refined4.62548.74654248
X-RAY DIFFRACTIONr_long_range_B_other4.62148.74854233
X-RAY DIFFRACTIONr_rigid_bond_restr0.924398961
X-RAY DIFFRACTIONr_sphericity_free27.4375133
X-RAY DIFFRACTIONr_sphericity_bonded18.895598085
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.332 749 -
Rwork0.298 14234 -
obs--99.51 %
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)
10.0083-0.0035-0.00440.00260.00220.0043-0.0020.0014-0.0071-0.00030.0035-0.0058-0.0126-0.0009-0.00150.0937-0.0106-0.00430.0821-0.00420.11267.0717-91.919546.1445
20.03410.0116-0.00740.00620.00020.0053-0.0124-0.0044-0.0075-0.0138-0.0050.0059-0.0047-0.00180.01740.0921-0.00160.01350.08310.00650.100359.8448-87.742616.5085
30.01390.0084-0.00580.0061-0.00330.0038-0.0035-0.00710.0007-0.00440.00860.00160.01050.0045-0.00520.11690.0047-0.00370.06920.0070.099232.6442-87.23611.1995
40.08030.02510.01290.01440.00680.0088-0.0023-0.01280.0142-0.0054-0.00340.0302-0.00690.01670.00570.09390.0046-0.00850.06290.00740.10673.4259-89.888113.6681
50.0041-0.0044-0.00220.00730.00290.0035-0.0008-0.0128-0.0115-0.0077-0.00010.0228-0.00330.00720.0010.0620.00960.01680.07510.00040.1121-2.9337-94.150645.6371
60.00150.00090.00070.00080.00020.00050.0080.00140.00230.0067-0.00540.00390.00480.004-0.00250.07610.01110.03220.0705-0.01370.064815.4114-94.766269.8417
70.00710.0027-0.00220.0196-0.00310.00240.00710.01810.0030.0165-0.0113-0.00650.0058-0.00670.00430.1209-0.0053-00.0686-0.01020.098747.8042-93.225471.1801
80.0006-0.0001-0.00160.01540.00270.00430.010.0050.00160.0212-0.0073-0.0305-0.0083-0.0157-0.00270.0969-0.0013-0.00270.08110.0020.097267.4175-129.980248.16
90.00230.0159-0.00080.1121-0.00480.00380.0004-0.0016-0.0014-0.0181-0.0051-0.0043-0.0116-0.01150.00470.0997-0.00140.00980.0808-0.00040.110968.4499-127.350121.0693
100.06650.0188-0.04750.0833-0.02960.03730.0239-0.00680.0199-0.0298-0.0094-0.006-0.010.0064-0.01460.0957-00.00750.08210.00790.077944.9915-126.4168-0.4414
110.00620.0095-0.00280.11560.02080.00850.0101-0.00570.0157-0.0145-0.00090.0303-0.00880.0125-0.00920.10350.0035-0.01890.07090.00840.099711.2098-130.73672.8345
120.00340.00420.00240.00630.00550.01630.011-0.007-0.00070.0033-00.0047-0.00910.0148-0.01090.08310.005-0.00350.07390.00050.1195-4.2143-134.004428.6948
130.05540.04930.04070.04670.0340.08950.013600.00990.0036-0.01040.00460.02930.0368-0.00320.08910.00260.00980.0707-0.00330.10637.9988-137.621760.4342
140.0135-0.01930.0050.0968-0.03280.01440.01780.0164-0.00360.0072-0.01490.00480.0090.0069-0.00290.1165-0.0023-0.00320.0808-0.00190.094940.0817-133.994570.4023
150.00330.0003-0.00360.0001-0.00050.0076-0.01260.0087-0.0049-0.00090.001-0.00210.02040.00410.01160.0812-0.0164-0.01270.07170.0060.11591.8219-206.198936.7701
160.0011-0.00010.00150.0038-0.00580.0115-0.0140.00060.0024-0.0015-0.0078-0.0175-0.00820.00960.02180.0929-0.0051-0.02140.0685-0.0050.10528.3655-205.07486.7364
170.0061-0.0011-0.00170.0047-0.00540.00790.0192-0.0102-0.0078-0.0145-0.00770.01410.00880.0205-0.01150.11130.0196-0.00770.0623-0.01880.090235.6237-203.0726-8.9837
180.0056-0.00980.00660.0171-0.01160.00940.01420.00590.0097-0.03-0.0132-0.0170.02420.0131-0.0010.06260.0340.00490.0319-0.03010.080164.9618-202.5753.5023
190.00580.0083-0.01350.0125-0.02030.04930.00470.0052-0.00970.00430.0036-0.01730.0074-0.008-0.00830.06080.0272-0.01360.0501-0.00930.11471.8438-203.842235.3885
200.02020.008-0.00520.004-0.00150.00620.0244-0.0026-0.03490.0106-0.0183-0.0188-0.0104-0.0147-0.00610.10450.0034-0.03710.05070.01280.090953.9102-207.469459.5888
210.0029-0.00220.00630.0094-0.01140.02220.00990.0089-0.00280.01180.00490.0048-0.00910.0177-0.01480.1126-0.0042-0.01340.06570.01030.100721.5865-209.413861.1719
220.00190.00130.00260.00650.00070.00570.0090.0017-0.00020.0113-0.00450.02340.01350.0142-0.00450.0912-0.01170.00390.07350.01250.10531.6164-169.088545.3381
230.05040.05650.0340.07950.03270.02750.00730.0005-0.0122-0.0250.0050.01320.01540.0134-0.01230.0854-0.0064-0.01050.07310.00250.11510.1287-166.966818.1646
240.0087-0.0056-0.00130.00440.00230.00390.0042-0.0132-0.0234-0.01090.00820.0107-0.00370.0156-0.01230.1121-0.0007-0.01470.0751-0.00470.096423.2611-164.1084-3.5864
250.00420.00040.00440.00250.00150.00530.0117-0.0027-0.013-0.00640.0085-0.01140.0061-0.0021-0.02020.09920.00570.01590.0831-0.00620.092957.0702-160.4196-0.1213
260.00230.00130.00140.0358-0.00920.00420.0088-0.0091-0.00830.0019-0.0056-0.01490.00940.0003-0.00330.08550.0029-0.00150.0839-0.00150.120972.9035-161.655225.6428
270.30110.0570.11130.0393-0.05570.2785-0.0034-0.0086-0.00320.0001-0.00620.0021-0.0401-0.02060.00960.09410.0025-0.01040.05760.00890.096861.2482-163.604757.712
280.0126-0.0092-00.00760.00050.00260.01630.00310.0043-0.0071-0.00930.0001-0.0041-0.0119-0.00710.1131-0.00810.00060.08560.00130.098529.3399-168.963467.4693
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 308
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 306
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 302
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 308
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 406
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 405
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 304
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 212
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301 - 303
25X-RAY DIFFRACTION11K401 - 406
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 309
28X-RAY DIFFRACTION13M1 - 233
29X-RAY DIFFRACTION13M301 - 311
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201 - 203
32X-RAY DIFFRACTION14N301 - 303
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301 - 303
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 305
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 306
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 304
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 406
48X-RAY DIFFRACTION22V1 - 222
49X-RAY DIFFRACTION22V301 - 302
50X-RAY DIFFRACTION22V401 - 408
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 304
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201 - 213
55X-RAY DIFFRACTION25Y1 - 212
56X-RAY DIFFRACTION25Y301 - 303
57X-RAY DIFFRACTION25Y401 - 406
58X-RAY DIFFRACTION26Z1 - 222
59X-RAY DIFFRACTION26Z301
60X-RAY DIFFRACTION26Z401 - 408
61X-RAY DIFFRACTION27a1 - 233
62X-RAY DIFFRACTION27a301 - 308
63X-RAY DIFFRACTION28b1 - 196
64X-RAY DIFFRACTION28b201 - 202
65X-RAY DIFFRACTION28b301 - 307

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