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- PDB-4qv1: yCP beta5-M45A mutant -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qv1
TitleyCP beta5-M45A mutant
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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation ...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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
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: 2.5 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)731,24440
Polymers730,93128
Non-polymers31412
Water16,646924
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119720 Å2
ΔGint-481 kcal/mol
Surface area214200 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.540, 300.510, 144.280
Angle α, β, γ (deg.)90.00, 112.67, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999392, -0.004038, 0.03463), (-0.002063, -0.984678, -0.174369), (0.034803, -0.174335, 0.984071)66.82587, -289.33258, -26.33787

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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: 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 / 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 / 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 / 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 / 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 / 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: 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 / 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 / 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, 936 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#17: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 924 / 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: 2.5→30 Å / Num. all: 363360 / Num. obs: 358637 / % possible obs: 98.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 11.9
Reflection shellResolution: 2.5→2.6 Å / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 2.2 / % 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: 2.5→15 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.945 / SU B: 19.658 / SU ML: 0.183 / Cross valid method: THROUGHOUT / ESU R Free: 0.212 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21559 17932 5 %RANDOM
Rwork0.19425 ---
obs0.19532 340705 98.8 %-
all-358637 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 58.161 Å2
Baniso -1Baniso -2Baniso -3
1-2.9 Å2-0 Å2-1.4 Å2
2---4.96 Å20 Å2
3---1.95 Å2
Refinement stepCycle: LAST / Resolution: 2.5→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49360 0 12 924 50296
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950268
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248044
X-RAY DIFFRACTIONr_angle_refined_deg0.8281.96368004
X-RAY DIFFRACTIONr_angle_other_deg0.6713110634
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.0656314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.79124.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.75158752
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.01915284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27662
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211268
X-RAY DIFFRACTIONr_mcbond_it1.8894.89725346
X-RAY DIFFRACTIONr_mcbond_other1.8894.89725345
X-RAY DIFFRACTIONr_mcangle_it2.4627.32931630
X-RAY DIFFRACTIONr_mcangle_other2.4627.32931631
X-RAY DIFFRACTIONr_scbond_it1.8355.27524922
X-RAY DIFFRACTIONr_scbond_other1.8355.27524922
X-RAY DIFFRACTIONr_scangle_other2.1777.76436374
X-RAY DIFFRACTIONr_long_range_B_refined2.91738.24554758
X-RAY DIFFRACTIONr_long_range_B_other2.85738.23754596
X-RAY DIFFRACTIONr_rigid_bond_restr0.849398312
X-RAY DIFFRACTIONr_sphericity_free27.5595474
X-RAY DIFFRACTIONr_sphericity_bonded15.651597876
LS refinement shellResolution: 2.5→2.563 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.333 1284 -
Rwork0.33 24398 -
obs--98.58 %
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)
10.0265-0.02210.01480.0271-0.01650.0124-0.00630.00950.00190.00290.0086-0.0096-0.0081-0.0109-0.00230.0945-0.00850.00710.0779-0.00550.11366.6224-91.980445.9238
20.0410.0155-0.01520.0078-0.0040.0077-0.0035-0.01-0.017-0.0054-0.00890.0025-0.00780.0030.01250.0914-0.0040.02720.07980.00220.089259.0716-87.632216.3785
30.03120.0292-0.01890.0299-0.01830.0124-0.0059-0.00680.0049-0.01030.01080.01210.01430.0036-0.00490.12360.0027-0.00180.07030.00710.099931.8193-87.25641.1807
40.0025-0.0019-0.00520.0232-0.01270.02630.0075-0.00810.0009-0.01840.00410.029-0.00640.0208-0.01150.09910.0152-0.01550.0380.01080.12632.6996-90.198913.858
50.06180.02190.04150.01230.01430.0307-0.0086-0.0031-0.00210.00850.00350.0193-0.01380.00530.00510.05590.0140.02560.0738-0.00320.1256-3.5166-94.657545.792
60.0081-0.0048-0.00510.02110.01450.0212-0.00370.00140.00620.0179-0.01020.00210.00210.00820.01390.09840.00150.03410.0758-0.01140.09815.0261-95.311969.85
70.0059-0.0031-0.00070.0041-0.00140.0015-0.00480.01920.00190.0193-0.005-0.0081-0.0086-0.00460.00970.1386-0.00490.00020.0671-0.0080.094447.4187-93.492571.0449
80.0040.0026-0.00040.01890.00750.00640.00950.00660.00910.016-0.0032-0.0279-0.002-0.0153-0.00630.099-0.001-0.00570.0683-0.00410.115667.7145-129.309247.3189
90.015-0.03-0.02820.18230.01750.08070.01210.0060.0040.0017-0.0011-0.01650.0018-0.0149-0.01110.0721-0.00010.02660.0896-0.00630.111368.2293-127.023420.6804
100.014-0.01710.00760.0261-0.01090.00660.0041-0.01560.0019-0.02090.0037-0.01130.00070.0017-0.00780.1191-0.0020.01480.0744-0.00120.09644.4971-126.4186-0.7753
110.00350.0102-0.00550.059-0.01740.01180.0022-0.01020.0067-0.02540.00040.0114-0.01210.0122-0.00260.10760.0054-0.01620.06380.00510.107710.7353-130.88842.5272
120.0104-0.00930.0060.06210.0010.01440.002-0.0070.00570.0037-0.00250.0219-0.01420.01530.00050.07210.0050.01250.08220.00580.1258-4.5951-134.735128.4861
130.0063-0.0074-0.00040.10640.02740.00790.0140.01220.0090.021-0.01330.0160.00810.0046-0.00070.0875-0.00380.02820.0841-0.00120.10417.78-138.202960.2783
140.00450.0047-0.00020.0079-0.00070.00010.00960.0084-0.00550.0206-0.0081-0.0092-0.00040.0018-0.00150.13-0.00420.00030.0773-0.00070.097739.8217-134.157970.6605
150.02080.01590.01140.01230.0090.0104-0.00380.00830.0135-0.00380.0070.0070.01530.01-0.00320.1107-0.0117-0.01390.06390.01180.11922.313-206.924936.6918
160.0053-0.00180.00450.0016-0.00350.0086-0.01290.00120.0015-0.00180.0018-0.00680.00640.00150.0110.1147-0.0042-0.01910.0666-0.00620.11868.8649-205.87496.595
170.02210.00880.0230.00960.00890.04070.0101-0.0169-0.0192-0.02830.01250.0044-0.00550.009-0.02260.1320.0263-0.01350.0558-0.01930.104535.8586-203.7105-9.2598
180.0136-0.01630.00490.0301-0.00640.00190.0174-0.0070.0134-0.0494-0.0169-0.0250.0097-0.0028-0.00050.08490.01930.0240.0373-0.01830.096665.3221-202.94023.04
190.03690.0194-0.01350.012-0.00490.01380.0170.009-0.01550.01530.0009-0.02340.0058-0.0142-0.01790.08410.016-0.01420.0591-0.01590.1472.4179-204.046534.971
200.02360.00510.01870.00260.00170.02610.0218-0.0149-0.01320.0122-0.0144-0.0147-0.0024-0.023-0.00740.11690.0091-0.04690.02710.01780.106354.5403-207.69759.2387
210.0020.0007-0.00010.001-0.00020.0002-0.00070.0109-0.00090.00840.00450.0035-0.0002-0.0009-0.00380.1406-0.0083-0.01920.06240.00940.106722.2367-209.931660.9591
220.00270.0020.00150.0068-0.00130.00530.0136-0.0009-0.00010.0129-0.00140.02480.00870.0144-0.01220.0881-0.00110.00630.07060.00890.11681.3505-170.432944.6603
230.0040.0134-0.0010.053-0.00950.00710.00620.00120.0041-0.0074-0.00350.01270.01230.0175-0.00270.102-0.0026-0.01470.07010.00320.12180.1168-167.978318.0372
240.01450.01360.01450.02080.01720.0180.0084-0.0066-0.0056-0.02040.00080.0059-0.00270.0049-0.00920.12910.0049-0.01360.0688-0.00010.10423.2156-164.7374-3.9005
250.01470.01480.01180.05230.01840.01480.0184-0.0172-0.009-0.0256-0.0048-0.0150.01070.0015-0.01370.09640.01110.0250.0727-0.01190.092357.0705-160.8551-0.8258
260.0027-0.00580.00340.0608-0.01710.00970.0065-0.0035-0.0044-0.0093-0.0016-0.02610.0034-0.0184-0.00490.07520.00310.01470.082-0.01110.122273.1076-161.598524.9508
270.00360.0002-0.00280.00630.00280.00350.00780.0136-0.0090.0164-0.0065-0.020.0018-0.0147-0.00130.11830.0025-0.02310.0651-0.00040.1261.6552-163.79257.1982
280.01330.0119-0.0050.0481-0.01080.00460.01610.02280.00210.0133-0.0068-0.00370.0038-0.0063-0.00930.1237-0.0041-0.00490.06950.00310.096829.9308-169.704867.661
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 336
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 325
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 323
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 332
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 319
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 329
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 442
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 434
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 439
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 338
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 302
27X-RAY DIFFRACTION11K401 - 444
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 342
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 353
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201
34X-RAY DIFFRACTION14N301 - 338
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 325
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 321
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 320
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 314
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 316
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 325
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 442
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301
52X-RAY DIFFRACTION22V401 - 424
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 339
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 230
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301
59X-RAY DIFFRACTION25Y401 - 436
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 429
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 360
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 249

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