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- PDB-4qv4: yCP beta5-M45T mutant -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qv4
TitleyCP beta5-M45T 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: 2.7 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 1.2Sep 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.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)731,28039
Polymers730,99128
Non-polymers29011
Water8,539474
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119830 Å2
ΔGint-472 kcal/mol
Surface area214970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.760, 301.270, 144.420
Angle α, β, γ (deg.)90.00, 112.81, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999516, -0.0026, 0.030986), (-0.002791, -0.984978, -0.172654), (0.030969, -0.172657, 0.984495)67.3145, -290.03336, -26.14583

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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: M45T / 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: 23295.158 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast)
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, 485 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 9 / 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.: 474 / 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: 2.7→30 Å / Num. all: 289794 / Num. obs: 286607 / % possible obs: 98.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.076 / Net I/σ(I): 13.9
Reflection shellResolution: 2.7→2.8 Å / Rmerge(I) obs: 0.553 / Mean I/σ(I) obs: 2.7 / % 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: pdb entry 1RYP

1ryp


Resolution: 2.7→15 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.939 / SU B: 23.557 / SU ML: 0.205 / Cross valid method: THROUGHOUT / ESU R Free: 0.252 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21338 14331 5 %RANDOM
Rwork0.18966 ---
obs0.19085 272276 99 %-
all-286607 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.353 Å2
Baniso -1Baniso -2Baniso -3
1-2.21 Å2-0 Å2-0.73 Å2
2---6.31 Å2-0 Å2
3---3.26 Å2
Refinement stepCycle: LAST / Resolution: 2.7→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49364 0 11 474 49849
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950272
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248046
X-RAY DIFFRACTIONr_angle_refined_deg0.831.96368010
X-RAY DIFFRACTIONr_angle_other_deg0.6723110640
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.97956314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.85124.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.613158754
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.73215284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27664
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211268
X-RAY DIFFRACTIONr_mcbond_it2.1855.10125346
X-RAY DIFFRACTIONr_mcbond_other2.1855.10125345
X-RAY DIFFRACTIONr_mcangle_it2.97.63631630
X-RAY DIFFRACTIONr_mcangle_other2.97.63631631
X-RAY DIFFRACTIONr_scbond_it2.085.47224926
X-RAY DIFFRACTIONr_scbond_other2.085.47224926
X-RAY DIFFRACTIONr_scangle_other2.5498.06136380
X-RAY DIFFRACTIONr_long_range_B_refined3.29739.74254050
X-RAY DIFFRACTIONr_long_range_B_other3.27539.74353976
X-RAY DIFFRACTIONr_rigid_bond_restr1.01398318
X-RAY DIFFRACTIONr_sphericity_free28.6195284
X-RAY DIFFRACTIONr_sphericity_bonded15.995597621
LS refinement shellResolution: 2.7→2.768 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.345 1032 -
Rwork0.322 19606 -
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)
10.0023-0.0026-0.00120.00980.00140.0023-0.00720.0083-0.00640.00420.0048-0-0.0072-0.01050.00240.1266-0.00670.00490.0853-0.00390.134766.3563-92.083445.8066
20.02580.00190.01590.00260.00350.0152-0.0115-0.0059-0.0095-0.0065-0.00210.0151-0.00680.01010.01360.1324-0.00440.01310.08560.00340.122358.8774-87.83716.152
30.00510.0012-0.00210.0017-00.0013-0.0069-0.01450.0131-0.00350.00570.01350.00840.00770.00120.1382-0.00110.00030.07990.00990.120131.6522-87.61540.8223
40.016-0.0070.01790.0580.03950.0695-0.00170.0105-0.0034-0.0282-0.01170.0536-0.02280.01670.01350.09910.02190.00670.02410.01580.12282.4916-90.66513.504
50.04950.03150.00480.02160.00030.0117-0-0.0130.007-0.0038-0.00010.0105-0.00610.00150.00010.11030.01080.01620.0738-0.00550.1381-3.7474-95.190845.4601
60.00860.00350.00570.00260.00080.0069-0.00350.00180.01030.0062-0.01060.00130.00360.01210.01410.1353-0.00110.0230.0788-0.01360.126214.7149-95.661469.6546
70.0065-0.00290.00020.004-0.00040.0003-0.00110.02140.00410.0153-0.0052-0.01270.002-0.00060.00630.1433-0.00010.00850.0764-0.01250.114547.0969-93.624270.9542
80.00530.00220.00370.01180.01270.02290.01260.01240.00620.0124-0.0012-0.0238-0.0121-0.0091-0.01140.1238-0.00520.00010.0831-0.00310.120667.6176-129.378647.3003
90.0003-0.0012-0.00180.0420.03940.0390.00590.00250.0025-0.0014-0.001-0.0098-0.0145-0.0076-0.00490.1251-0.0020.0150.088-0.00180.130668.2094-127.141420.5612
100.0059-0.0017-0.00020.0213-0.00340.0010.0038-0.01410.0157-0.0202-0.00050.0143-0.0010.0046-0.00330.1318-0.00340.02190.08460.00780.103144.5134-126.7478-1.0153
110.01540.0270.00250.05910.01220.00560.0042-0.01260.0119-0.0114-0.00070.0122-0.0120.0107-0.00350.13150.0056-0.00450.07280.00680.129510.7513-131.38022.227
120.00330.0016-0.00220.03290.01870.01470.0108-0.00960.00430.0018-0.00470.0176-0.00670.0131-0.00610.11830.00340.00270.08020.00670.1393-4.5331-135.259628.1584
130.0021-0.00110.0010.02250.0030.00110.00390.01080.00960.0105-0.0086-0.00120.00120.00560.00470.12990.00080.01790.0907-0.00360.1267.7292-138.602260.1105
140.02560.00960.01750.02370.02610.0320.00720.00070.00180.0125-0.005-0.00840.0041-0.0039-0.00230.1379-0.00290.01130.09280.00060.11839.7335-134.359570.662
150.0145-0.0064-0.00830.00350.00310.0076-0.00480.00260.0066-0.00560.0031-0.00350.01730.00690.00180.1288-0.0079-0.0070.07770.00620.13892.6348-207.397636.6294
160.04460.008-0.00270.0055-0.00860.0174-0.00470.00460.00370.0013-0.0014-0.00740.0001-0.00050.00610.1339-0-0.00950.0807-0.00620.1369.193-206.39256.5041
170.0065-0.00320.00320.0032-0.00120.0210.0134-0.011-0.0176-0.0150.01430.0091-0.00630.0212-0.02770.13370.0248-0.0010.0652-0.01580.099136.3632-204.1215-9.4068
180.01-0.02640.00120.0735-0.00210.00070.01520.00830.0119-0.023-0.0236-0.02310.0057-0.00130.00830.09550.02470.02490.0396-0.03390.087765.7493-203.18993.1511
190.02030.0219-0.00660.0246-0.00730.00710.0112-0.001-0.0070.01220.0001-0.01750.0048-0.0098-0.01130.10750.01720.00070.0601-0.01520.145272.7337-204.078235.0674
200.00190.0011-0.00120.0009-0.00020.00510.008-0.0004-0.00480.0084-0.0102-0.0058-0.0109-0.01320.00220.12850.0065-0.02360.05290.01470.12554.8531-207.84759.3629
210.0016-0.00040.00080.0001-0.00020.00040.00030.0113-0.00040.0022-0.00130.0011-0.00170.00580.00110.1447-0.0046-0.00310.07850.00620.126922.5175-210.249861.0275
220.0020.00080.00240.007-0.00290.00570.01510.00240.00140.0107-0.0090.02340.01310.0142-0.0060.1153-0.00840.01070.07010.01010.12071.5204-170.891644.5166
230.0037-0.01280.00610.0452-0.02270.01440.00230.0004-0.0003-0.0046-0.00660.00670.00530.01830.00430.1261-0.0033-0.00870.07670.00080.14180.2815-168.531817.7923
240.02740.00240.00150.0010.00010.00110.00980.0022-0.0052-0.00460.00070.0069-0.00560.0045-0.01050.14180.0022-0.00920.08410.00010.123123.4422-165.2082-4.1283
250.00450.01650.00780.10420.030.02980.0127-0.0076-0.0025-0.0116-0.0004-0.0160.0059-0.0011-0.01230.11770.00960.02270.0846-0.00940.109457.2678-161.1359-0.9027
260.0056-0.00880.00330.026-0.00330.00270.0094-0.0076-0.0093-0.0022-0.0010.00410.0084-0.0111-0.00840.12080.00590.00910.0874-0.00930.13273.1815-161.692124.9275
270.0051-0.0133-0.00110.0778-0.00380.00350.00360.0103-0.0130.0052-0-0.0023-0.0006-0.0157-0.00360.13030.0029-0.00610.0781-0.00120.132461.7269-163.876657.2522
280.00590.00120.00170.03960.01890.01070.01720.0159-0.0058-0.0011-0.00750.00560.0001-0.0036-0.00970.135-0.00730.00720.08530.00360.120929.9925-169.927167.7154
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 311
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 316
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 309
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 314
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 313
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 311
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 426
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 425
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 420
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 318
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 302
27X-RAY DIFFRACTION11K401 - 420
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 323
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 327
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201
34X-RAY DIFFRACTION14N301 - 323
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 307
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 306
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 317
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 308
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 307
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 318
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 413
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301
52X-RAY DIFFRACTION22V401 - 411
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 315
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 218
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301
59X-RAY DIFFRACTION25Y401 - 419
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301 - 326
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 328
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 225

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