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- PDB-4qvq: yCP beta5-M45I mutant in complex with bortezomib -

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Basic information

Entry
Database: PDB / ID: 4qvq
TitleyCP beta5-M45I mutant in complex with bortezomib
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / 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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway ...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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / 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
Chem-BO2 / 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 ...Chem-BO2 / 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: 2.6 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 15, 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
Revision 1.3Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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)733,68147
Polymers731,01528
Non-polymers2,66619
Water9,062503
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area126000 Å2
ΔGint-499 kcal/mol
Surface area214710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.670, 300.620, 145.520
Angle α, β, γ (deg.)90.00, 113.19, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999737, -0.001101, 0.022915), (-0.002873, -0.984979, -0.172649), (0.022761, -0.17267, 0.984717)68.38821, -289.05829, -25.73461

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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: M45I / 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: 23307.211 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 , 4 types, 522 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


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-BO2 / N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / BORTEZOMIB


Mass: 384.237 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C19H25BN4O4 / Comment: medication, anticancer*YM
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 503 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.6→30 Å / Num. all: 329900 / Num. obs: 326601 / % possible obs: 99 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 11.3
Reflection shellResolution: 2.6→2.7 Å / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.4 / % possible all: 99.6

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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: 2.6→15 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.94 / SU B: 21.11 / SU ML: 0.191 / Cross valid method: THROUGHOUT / ESU R Free: 0.234 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21919 16330 5 %RANDOM
Rwork0.195 ---
all0.199 326601 --
obs0.19621 310271 99.11 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 65.391 Å2
Baniso -1Baniso -2Baniso -3
1-2.72 Å20 Å20.21 Å2
2---6.13 Å20 Å2
3---2.43 Å2
Refinement stepCycle: LAST / Resolution: 2.6→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49366 0 181 503 50050
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950454
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248200
X-RAY DIFFRACTIONr_angle_refined_deg0.8321.96768264
X-RAY DIFFRACTIONr_angle_other_deg0.73.001110974
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.89456314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.41124.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.362158750
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.55315284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27688
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it2.2995.25425346
X-RAY DIFFRACTIONr_mcbond_other2.2995.25325345
X-RAY DIFFRACTIONr_mcangle_it3.0227.86631630
X-RAY DIFFRACTIONr_mcangle_other3.0227.86631631
X-RAY DIFFRACTIONr_scbond_it2.2325.69125108
X-RAY DIFFRACTIONr_scbond_other2.2315.69125108
X-RAY DIFFRACTIONr_scangle_other2.7418.36536634
X-RAY DIFFRACTIONr_long_range_B_refined3.49541.12154116
X-RAY DIFFRACTIONr_long_range_B_other3.4841.11554056
X-RAY DIFFRACTIONr_rigid_bond_restr0.804398654
X-RAY DIFFRACTIONr_sphericity_free25.7235310
X-RAY DIFFRACTIONr_sphericity_bonded18.061597950
LS refinement shellResolution: 2.6→2.665 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.345 1175 -
Rwork0.326 22342 -
obs--99.69 %
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)
10.0271-0.00490.01210.0021-0.00370.010.00030.0174-0.01020.00330.0034-0.0084-0.0164-0.0072-0.00370.1477-0.0081-0.00520.101-0.0020.158867.3254-91.987946.1583
20.01540.00360.00520.00120.00130.0020.00020.0063-0.0054-0.0005-0.00110.0058-0.00430.00530.0010.1587-0.005-0.00040.10610.0020.164260.118-87.820416.481
30.02710.0264-0.02160.0291-0.02280.0187-0.001-0.0136-0.0002-0.0070.00840.01230.01010.006-0.00740.16330.0026-0.00840.09950.00530.160232.8395-87.2921.0647
40.00220.00070.00260.00870.0070.0136-0.0025-0.0083-0.001-0.0076-0.01110.0355-0.0037-0.00130.01360.13150.0179-0.01170.06580.01510.16133.533-90.040213.5229
50.0009-0.00140.00180.0023-0.00220.00550.0013-0.0052-0.0097-0.00340.00850.0175-0.0045-0.0064-0.00970.14530.00530.00680.101-0.00030.1775-2.8762-94.413245.5347
60.0276-0.0011-0.00050.0029-0.00040.00030.00520.0029-0.00570.0198-0.00770.005-0.00180.00480.00250.16770.00020.01030.1009-0.00460.162515.4833-94.948369.8177
70.00690.0021-0.00090.01570.00310.00130.00570.02190.00190.017-0.009-0.0110.0017-0.00720.00330.1725-0.0035-0.00220.0881-0.00950.156147.9674-93.328771.2387
80.0035-0.0011-0.00430.00750.00350.00690.01550.01230.00590.0167-0.0091-0.0274-0.0064-0.0238-0.00640.1443-0.0035-0.01140.0962-0.00990.161667.9913-129.495847.6266
90.0048-0.0116-0.01530.07940.01370.06440.0023-0.0027-0.0016-0.007-0.0035-0.0055-0.0137-0.00950.00120.1496-0.0015-0.00130.1078-0.00040.164968.7658-127.450520.9956
100.04710.0276-0.00670.0179-0.00370.00170.0056-0.00730.007-0.0050.0043-0.00410.00530.0016-0.00990.16680.00120.00050.10730.0030.152345.2653-126.5018-0.6276
110.00380.0068-0.0030.0169-0.00020.0083-0.0004-0.00670.0035-0.0070.00660.0091-0.01190.0237-0.00620.15730.004-0.01680.08990.01110.161711.4394-130.77742.3286
120.00530.002-0.00150.00190.0010.01080.0145-0.01290.00320.00860.00120.0091-0.00770.019-0.01570.13820.0073-0.00880.09620.00620.1792-4.0817-134.273328.4779
130.0031-0.00610.00030.04850.00390.00120.0120.00860.00710.0198-0.01310.01260.00370.00820.00110.1545-0.00170.00620.10310.00030.16588.1994-137.836960.367
140.0143-0.0118-0.00450.03020.00970.00410.0180.0217-0.0020.0163-0.00440.00150.0012-0.0005-0.01360.1679-0.0078-0.00680.0948-0.00150.154240.1665-134.058370.7806
150.0293-0.0072-0.02520.01740.01560.0387-0.00440.0180.0013-0.0092-0.00170.00240.01760.01190.00610.147-0.0108-0.01460.09770.00380.16892.1346-206.523536.7444
160.05290.00320.0310.00060.00170.0197-0.012-0.00330.00310.00240.0017-0.00740.0046-0.00250.01030.1537-0.0012-0.02140.1029-0.00340.16178.6697-205.38296.6936
170.0068-0.00280.00030.0033-0.00170.0050.0177-0.0122-0.0209-0.0192-0.00090.0133-0.00290.014-0.01670.16240.0161-0.01320.0837-0.01450.143936.0875-203.4291-9.1719
180.0062-0.0005-0.0030.0179-0.01240.0104-0.0051-0.01680.0095-0.0282-0.0129-0.04060.02050.01460.0180.1120.03290.0110.0561-0.02080.143465.474-202.83293.4411
190.00720.00540.00320.00630.00260.00270.0182-0.0106-0.01660.02120.001-0.02410.0012-0.0069-0.01930.12680.0214-0.01940.0783-0.01080.165672.3677-203.934235.4025
200.02070.010.00190.00690.00250.00220.0394-0.0032-0.02920.0207-0.0254-0.02150.0031-0.0118-0.01410.15370.0068-0.03840.06850.00290.142954.3884-207.66659.6367
210.00270.005-0.00350.0193-0.01780.0176-0.00430.01230.00050.00690.00770.0053-0.00460.0029-0.00350.1697-0.0038-0.01180.09050.00360.16221.9652-209.69261.1982
220.00490.00580.00380.0242-0.00180.0070.02070.0037-0.00540.0104-0.00730.02790.01140.0188-0.01350.1412-0.0084-00.09420.01060.17051.6022-169.852644.646
230.00160.0108-0.00070.09340.00090.0110.0011-0.0040.0048-0.01140.00160.0150.01810.0272-0.00270.1455-0.0078-0.01330.0920.00620.17010.4085-167.249618.0309
240.01360.01080.00540.01740.00570.00380.0058-0.0066-0.0121-0.02010.00510.01090.00190.0096-0.01090.16510.0053-0.01510.1-0.00210.153423.5792-164.4244-3.8109
250.02430.00020.00960.00450.00030.00850.01330.00470.0081-0.01610.0065-0.01620.0152-0.0092-0.01990.15340.00270.00440.1055-0.01030.145157.4651-160.718-0.5922
260.00740.0095-0.00160.0186-0.01070.01290.0137-0.0096-0.00950.001-0.0027-0.0080.015-0.0158-0.0110.13520.0101-0.00240.1012-0.00870.171873.3414-161.760925.5276
270.007-0.0163-0.00190.06080.00140.00270.01090.0129-0.00760.017-0.0099-0.00350.001-0.0158-0.0010.1560.0011-0.01650.09350.00040.162461.6119-163.754557.7073
280.0057-0.0050.00260.0329-0.01290.00650.01720.013-0.0010.0143-0.00510.00020.0047-0.0048-0.01220.1683-0.0079-0.00530.09350.00520.153129.8184-169.33367.8157
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 320
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 315
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 320
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 307
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 306
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 318
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 424
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 438
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 417
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 317
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 303
27X-RAY DIFFRACTION11K401 - 425
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 329
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 329
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 315
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 309
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 312
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 310
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 307
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 306
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 311
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 418
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301 - 302
52X-RAY DIFFRACTION22V401 - 418
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 318
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 217
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 418
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 424
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 334
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 321

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