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- PDB-4qv0: yCP beta5-A49T-A50V-double mutant -

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Basic information

Entry
Database: PDB / ID: 4qv0
TitleyCP beta5-A49T-A50V-double mutant
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis
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
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 ...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: 3.1 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 14, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Feb 27, 2019Group: Data collection / Refinement description / Category: refine / reflns_shell
Item: _refine.pdbx_starting_model / _reflns_shell.Rmerge_I_obs
Revision 1.3Sep 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_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.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)731,38436
Polymers731,16728
Non-polymers2178
Water2,648147
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119770 Å2
ΔGint-450 kcal/mol
Surface area213210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.800, 300.210, 144.400
Angle α, β, γ (deg.)90.00, 112.86, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999597, -0.002302, 0.028276), (-0.002553, -0.985358, -0.170478), (0.028255, -0.170481, 0.984956)67.3691, -289.12753, -25.87478

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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 / / Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / ...Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / Proteinase YSCE subunit 7


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: A49T, A50V / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-3 / / Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 ...Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 / Proteinase YSCE subunit 13


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 / / Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component ...Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component PRE6 / Proteinase YSCE subunit PRE6


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 / / Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component ...Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component PUP2 / Proteinase YSCE subunit PUP2


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 / / Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component ...Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component PRE5 / Proteinase YSCE subunit PRE5


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 / / Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7- ...Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7-alpha / Proteasome component Y8 / Proteinase YSCE subunit 7 / SCL1 suppressor protein


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 / Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / ...Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / Proteinase YSCE subunit 1


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 / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component ...Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


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 / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit PUP3 / Proteasome component PUP3


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 / Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 ...Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 / Proteinase YSCE subunit 11


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 / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component ...Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component PRE2 / Proteinase YSCE subunit PRE2


Mass: 23383.328 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 / / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5


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 / / Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component ...Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component PRE4 / Proteinase YSCE subunit PRE4


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 / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component ...Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component PRE3 / Proteinase YSCE subunit PRE3


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 , 3 types, 155 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: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 147 / 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: 3.1→30 Å / Num. all: 191054 / Num. obs: 187042 / % possible obs: 97.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.111 / Net I/σ(I): 7.7
Reflection shellResolution: 3.1→3.2 Å / Rmerge(I) obs: 0.495 / Mean I/σ(I) obs: 2.4 / % possible all: 99.2

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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: 3.1→15 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.942 / SU B: 35.193 / SU ML: 0.262 / 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
Rfree0.19654 9353 5 %RANDOM
Rwork0.15936 ---
obs0.16125 177689 98.06 %-
all-187042 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 76.031 Å2
Baniso -1Baniso -2Baniso -3
1-4.08 Å20 Å2-1.16 Å2
2---7.85 Å2-0 Å2
3---3.14 Å2
Refinement stepCycle: LAST / Resolution: 3.1→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49374 0 8 147 49529
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950282
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248062
X-RAY DIFFRACTIONr_angle_refined_deg0.8381.96368022
X-RAY DIFFRACTIONr_angle_other_deg0.6763110678
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.18656314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.89724.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.809158762
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.04615284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27666
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211268
X-RAY DIFFRACTIONr_mcbond_it3.3866.8125346
X-RAY DIFFRACTIONr_mcbond_other3.3866.8125345
X-RAY DIFFRACTIONr_mcangle_it4.5710.20131630
X-RAY DIFFRACTIONr_mcangle_other4.5710.20131631
X-RAY DIFFRACTIONr_scbond_it3.3187.23824936
X-RAY DIFFRACTIONr_scbond_other3.3187.23824936
X-RAY DIFFRACTIONr_scangle_other4.22910.6936392
X-RAY DIFFRACTIONr_long_range_B_refined5.23653.19554165
X-RAY DIFFRACTIONr_long_range_B_other5.23153.254148
X-RAY DIFFRACTIONr_rigid_bond_restr1.125398344
X-RAY DIFFRACTIONr_sphericity_free32.0955105
X-RAY DIFFRACTIONr_sphericity_bonded19.691597496
LS refinement shellResolution: 3.1→3.177 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.325 669 -
Rwork0.266 12698 -
obs--99.31 %
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)
10.0016-0.0002-0.00050.00090.00020.00040.00140.0090.00290.00290.0001-0.00890.0043-0.0044-0.00160.103-0.0098-0.00190.0655-0.00960.091966.4389-91.81145.66
20.0028-0.0009-0.00140.00220.00010.02030.0008-0.009-0.012-0.0078-0.00340.0101-0.00520.00470.00260.1035-0.00630.00780.0650.0030.087759.0345-87.658616.0876
30.05880.03250.00090.0212-0.00550.01290.0070.0098-0.0005-0.00030.01450.01130.0153-0.0062-0.02150.10750.00350.00070.0610.00810.082231.8618-87.37540.809
40.0033-0.0020.0080.01940.01770.0494-0.0087-0.002-0.0083-0.0215-0.00840.0361-0.0264-0.00210.01710.06090.0323-0.01470.02520.01530.08512.6755-90.302613.38
50.00090.00110.00040.00260.00010.0003-0.0063-0.00010.0028-0.00180.00530.0111-0.0035-0.00340.0010.06380.0170.01890.0577-0.00160.0878-3.5464-94.605145.4206
60.0002-0.0003-0.00080.00330.00330.0054-0.0045-0.0011-0.00230.0028-0.00710.01090.00840.00210.01160.07330.01290.03510.0527-0.01950.045914.9106-95.132869.5103
70.0191-0.0154-0.01660.03250.01840.01730.00470.01840.00430.02330.005-0.0003-0.0014-0.0064-0.00970.1153-0.0032-0.00270.0522-0.01420.068747.2071-93.237770.7677
80.00080.0019-0.00030.0092-0.00070.00470.00830.0032-0.00610.0259-0.0008-0.0145-0.0103-0.0089-0.00750.0917-0.0086-0.00760.0619-0.00230.086667.5588-129.021847.2519
90.0414-0.026-0.02650.07170.02160.05140.01190.0045-0.0050.0158-0.0136-0.0365-0.0375-0.02060.00160.0715-0.00970.02010.061-0.00020.078568.1718-126.971420.5337
100.01270.02540.00370.10190.0320.01460.0117-0.00810.0086-0.02070.0065-0.0079-0.01020.0115-0.01820.0952-0.00430.00520.06470.00210.070744.5552-126.4215-0.9706
110.0011-0.00490.00180.0978-0.05930.03790.0095-0.00470.0018-0.0068-0.00620.0075-0.00580.0128-0.00320.10010.0052-0.00890.06230.0040.082810.8625-130.90162.247
120.0150.00310.02160.01210.00090.04280.0073-0.00770.00320.02290.00130.0079-0.00890.0035-0.00860.08090.0036-00.06070.00360.0961-4.5154-134.653828.2925
130.0114-0.01660.00950.03-0.01530.00850.0024-0.00130.01110.01-0.0061-0.00040.00220.0040.00370.08460.00230.02650.0699-0.00610.07237.7632-137.950760.1402
140.0227-0.0381-0.01010.09860.01860.00720.01630.00530.00960.0164-0.00880.00490.00720.0039-0.00740.1186-0.0036-0.0040.0629-0.00950.05739.7003-133.807970.5824
150.0325-0.0129-0.02710.01080.0130.0235-0.00930.01220.0046-0.00630.01020.00910.0053-0.0033-0.00090.1044-0.0123-0.00750.05580.00640.09092.4458-206.622136.7937
160.0976-0.0024-0.010.0010.00070.0016-0.00590.01080.00560.00420.00310.00730.00630.00230.00280.1103-0.0025-0.01440.0567-0.0050.08229.0321-205.69526.7587
170.0054-0.00040.00850.00140.00380.03480.0114-0.0061-0.0106-0.00870.0134-0.0015-0.01690.0125-0.02480.10160.02140.00070.0492-0.01310.042736.101-203.5104-9.1132
180.0016-0.00590.00320.0225-0.01210.0069-0.00040.00040.0093-0.0335-0.0116-0.03440.0154-0.00240.0120.06780.02950.03320.0376-0.02230.070865.5205-202.59153.2234
190.07280.024700.0132-000.0018-0.016-0.00280.01510.0019-0.0142-0.0006-0.0004-0.00370.06060.0426-0.00480.0351-0.00520.084472.4612-203.5635.221
200.00010.0003-0.00010.0007-0.00010.00090.0016-0.0007-0.00210.0038-0.0021-0.0062-0.0077-0.00380.00060.07730.0224-0.02660.02710.02210.052354.561-207.154959.4602
210.00680.01-0.00350.0194-0.00550.00220.0001-0.00640.0050.0111-0.00210.019-0.0030.00680.00190.1198-0.0002-0.00520.05390.01270.061522.299-209.492761.1436
220.0034-0.00220.00340.0066-0.00270.00480.01120.00190.00290.003-0.00620.0130.01620.0042-0.0050.0909-0.01190.00880.05970.0030.08271.4479-170.154344.6265
230.0011-0.0014-0.00010.00550.00810.02140.00290.0051-0.00670.0046-0.00550.00910.00660.01260.00260.0969-0.0049-0.01520.06150.0020.10170.2353-167.7517.9377
240.02250.0165-0.00390.04190.01540.03410.0175-0.0063-0.0144-0.0102-0.0020.0079-0.00260.0064-0.01550.1120.004-0.01160.0634-0.00290.07623.3605-164.6902-3.9428
250.02440.04510.0120.08880.02070.00970.0050-0.004-0.01010.0049-0.01650.00320.0016-0.00990.07830.01410.0390.0621-0.01520.049457.103-160.7386-0.8469
260.02670.0458-0.02760.0973-0.05970.04050.0005-0.0204-0.01490.012-0.0069-0.020.00880.00240.00640.07970.00950.00330.0739-0.00840.087773.0803-161.307125.0533
270.0073-0.01610.00370.0735-0.01560.0054-0.00350.007-0.00940.01580.0073-0.0180.0087-0.0062-0.00380.10680.0086-0.01390.06240.00030.083261.5607-163.373157.2896
280.0101-0.01550.00050.0731-0.00780.00180.0160.0137-0.00590.0233-0.01090.0016-0.0044-0.0051-0.00510.1157-0.0014-0.00380.05940.00820.05929.8603-169.277167.7364
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 - 305
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 303
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 307
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 305
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 312
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 402
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 405
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 302
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 206
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301
25X-RAY DIFFRACTION11K401 - 408
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 308
28X-RAY DIFFRACTION13M1 - 233
29X-RAY DIFFRACTION13M301 - 307
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201
32X-RAY DIFFRACTION14N301 - 305
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 304
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 308
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301 - 305
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 305
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 406
48X-RAY DIFFRACTION22V1 - 226
49X-RAY DIFFRACTION22V301
50X-RAY DIFFRACTION22V401 - 404
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 303
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201 - 210
55X-RAY DIFFRACTION25Y1 - 212
56X-RAY DIFFRACTION25Y301
57X-RAY DIFFRACTION25Y401 - 408
58X-RAY DIFFRACTION26Z1 - 222
59X-RAY DIFFRACTION26Z301 - 303
60X-RAY DIFFRACTION27a1 - 233
61X-RAY DIFFRACTION27a301 - 308
62X-RAY DIFFRACTION28b1 - 196
63X-RAY DIFFRACTION28b201 - 203

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