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- PDB-4qvv: yCP beta5-A49V mutant in complex with bortezomib -

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Basic information

Entry
Database: PDB / ID: 4qvv
TitleyCP beta5-A49V 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 / 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 / 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: 2.8 Å
AuthorsHuber, E.M. / Heinemeyer, W. / Groll, M.
CitationJournal: Structure / Year: 2015
Title: Bortezomib-Resistant Mutant Proteasomes: Structural and Biochemical Evaluation with Carfilzomib and ONX 0914.
Authors: Huber, E.M. / Heinemeyer, W. / Groll, M.
History
DepositionJul 16, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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)733,74946
Polymers731,10728
Non-polymers2,64218
Water6,612367
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area125290 Å2
ΔGint-482 kcal/mol
Surface area216020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.520, 300.750, 145.350
Angle α, β, γ (deg.)90.00, 113.24, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999817, 0.001402, 0.01906), (-0.004667, -0.985026, -0.172342), (0.018533, -0.1724, 0.984853)68.92258, -288.99832, -25.83502

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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: A49V / 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: 23353.303 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, 385 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / 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.: 367 / 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: 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: 2.8→30 Å / Num. all: 263779 / Num. obs: 257713 / % possible obs: 97.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.061 / Net I/σ(I): 16.3
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.427 / Mean I/σ(I) obs: 3.1 / % possible all: 98.9

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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: 2.8→15 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.922 / SU B: 30.495 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R Free: 0.305 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23547 12886 5 %RANDOM
Rwork0.19939 ---
all0.204 257713 --
obs0.20118 244827 97.83 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 62.298 Å2
Baniso -1Baniso -2Baniso -3
1-3.42 Å20 Å2-1.23 Å2
2---5.6 Å2-0 Å2
3---1.98 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49370 0 180 367 49917
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950458
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248204
X-RAY DIFFRACTIONr_angle_refined_deg0.8681.96768268
X-RAY DIFFRACTIONr_angle_other_deg0.7193.001110984
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.06356314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.12224.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.05158754
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.50315284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27688
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it2.9545.56525346
X-RAY DIFFRACTIONr_mcbond_other2.9545.56425345
X-RAY DIFFRACTIONr_mcangle_it3.9648.33131630
X-RAY DIFFRACTIONr_mcangle_other3.9638.33131631
X-RAY DIFFRACTIONr_scbond_it2.7895.96125112
X-RAY DIFFRACTIONr_scbond_other2.7895.96125112
X-RAY DIFFRACTIONr_scangle_other3.5648.78636638
X-RAY DIFFRACTIONr_long_range_B_refined4.5243.28953761
X-RAY DIFFRACTIONr_long_range_B_other4.51743.29253727
X-RAY DIFFRACTIONr_rigid_bond_restr1.072398662
X-RAY DIFFRACTIONr_sphericity_free29.5495213
X-RAY DIFFRACTIONr_sphericity_bonded17.44597918
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.363 932 -
Rwork0.307 17718 -
obs--99.04 %
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)
10.012-0.0126-0.0080.0210.01120.00840.00580.0059-0.0099-0.0032-0.0006-0.0064-0.012-0.0053-0.00520.0698-0.00740.0010.0505-0.00520.056267.722-92.10346.0759
20.00330.00090.00740.00530.010.0309-0.0042-0.0035-0.0055-0.0077-0.00330.011-0.0169-0.00190.00750.07-0.00580.01520.05180.0060.053660.5523-87.943716.4563
30.06290.03490.020.0214-0.00190.10980.0040.00270.0092-0.00290.0070.01020.00830.0115-0.0110.07590.0047-0.0010.04860.01110.05233.1488-87.27081.1241
40.0014-0.00160.00060.00440.00180.0042-0.00520.0022-0.0063-0.0066-0.0020.0184-0.0050.01110.00720.0540.0086-0.0210.04040.01780.08043.572-89.897513.6406
50.0002-0.0003-0.00030.0017-0.00450.01920.002-0.0006-0.0040.00640.00120.009-0.02470.0025-0.00320.03940.01370.01680.04510.00020.0934-2.9893-94.18645.7022
60.0009-0.00040.00080.0002-0.00040.00150.00090.006-0.0023-0.0014-0.0030.00070.00920.00490.00210.0841-0.00070.03010.047-0.00920.055915.4648-94.803569.8661
70.0062-0.0016-0.00140.0534-0.0320.02470.00780.01440.00130.0234-0.0105-0.01150.0001-0.00390.00270.0979-0.00970.00260.0456-0.00760.041848.1709-93.306171.1656
80.00150.0032-0.00090.0181-0.00110.00310.007-0.00020.00270.0297-0.005-0.0181-0.0044-0.0118-0.00210.0546-0.0024-0.01580.056-0.00160.057568.1906-129.593347.5937
90.0289-0.0616-0.01190.140.03210.01090.0029-0.00620.0081-0.0086-0.0041-0.0189-0.0079-0.01080.00120.0422-0.0030.01610.05230.00080.054669.0861-127.570221.0055
100.04250.05-0.00770.0769-0.00670.0040.0097-0.0240.0081-0.0265-0.00580.0034-0.00490.0026-0.00390.0809-0.00160.00930.05020.00330.038545.505-126.5315-0.6174
110.06990.08040.02210.17130.00820.0144-0.0012-0.00990.012-0.028-0.00260.0338-0.00290.00520.00390.07180.0032-0.0270.04550.01270.055211.4408-130.72732.4842
120.00290.0021-0.00130.003-0.00030.00130.0047-0.00730.00690.0026-0.00460.0153-0.00120.0082-0.00010.04220.00090.00050.05460.00840.092-4.2745-134.135228.5451
130.00610.0170.00650.06280.01790.0070.00560.00720.00530.0286-0.00790.02130.00780.00820.00230.0665-0.00020.02340.0549-0.00070.06517.9578-137.669760.4043
140.0195-0.0233-0.00550.14240.00570.00180.01250.0152-0.00140.0349-0.00750.004-0.0041-0.0033-0.0050.1036-0.00370.00110.0588-0.00220.039740.0977-134.008470.791
150.0069-0.0041-0.01040.00760.01690.0405-0.00210.01110.0105-0.0013-0.00020.00590.00840.00180.00230.0639-0.0082-0.00880.04510.0080.08361.6298-206.34436.8649
160.06340.0190.00510.00580.00140.0013-0.0099-0.00540.0188-0.0070.00060.00660.001-0.00080.00930.0781-0.0018-0.02780.0443-0.00910.06828.4672-205.37366.8344
170.02870.0090.02550.00470.00890.0260.0107-0.0108-0.0008-0.0097-0.0040.00240.0078-0.0015-0.00670.11120.0085-0.01960.0272-0.01080.034636.0451-203.5614-8.9006
180.0117-0.00730.00470.0104-0.00440.00220.0051-0.01530.0101-0.0243-0.0059-0.01520.0085-0.00380.00080.0670.01820.02660.0379-0.00410.043665.6666-203.01613.5762
190.0050.0010.00530.00050.00160.00960.0142-0.004-0.0040.00320.001-0.00580.0097-0.0125-0.01530.04820.0104-0.0140.0429-0.0050.082472.4064-204.193235.6667
200.01040.0014-0.00590.0012-00.0040.01560.0097-0.01340.0069-0.0124-0.0068-0.0096-0.0103-0.00330.0848-0.0045-0.02890.04540.01340.064454.0773-207.72359.8217
210.0019-0.00510.0010.0521-0.00470.00110.00150.008800.0168-0.00590.0146-0.00540.00460.00440.0881-0.0037-0.00530.04870.01090.058121.4383-209.638461.3468
220.0053-0.00070.00890.0511-0.01650.02430.0155-0.0018-0.00510.0044-0.00420.03460.01770.014-0.01130.05-0.00650.00820.05150.00940.07011.2695-169.69744.7521
230.00380.00990.00370.07010.01510.006-0.0005-0.0046-0.0026-0.01020.00350.02450.00350.0053-0.0030.0528-0.002-0.02260.05390.00380.08380.1846-167.163518.135
240.03230.031-0.00350.0394-0.00460.00170.0038-0.003-0.0022-0.01780.00170.0171-0.00320.0031-0.00550.0960.007-0.02570.0528-0.00180.050223.631-164.5014-3.7436
250.01120.0255-0.00610.0666-0.01580.0043-0.0027-0.0055-0.0004-0.03620.0018-0.0010.00720.00260.00080.06540.00330.01640.0525-0.00770.039957.7103-160.8955-0.4358
260.00440.00330.00040.112-0.01830.00680.0054-0.0056-0.01430.0005-0.0136-0.01620.0041-0.00980.00820.03710.0067-0.00520.059-0.00370.063573.5765-161.92925.5615
270.00250.0079-0.00180.1148-0.00280.0029-0.00090.0056-0.00760.0217-0.0058-0.011-0.0066-0.00990.00670.0748-0.0009-0.0180.05250.00120.056661.5743-163.854457.7243
280.0061-0.01110.00540.039-0.01460.00650.0140.01160.00080.0073-0.01510.00130.00710.00460.00120.1007-0.00510.00430.06110.00410.044129.5272-169.261867.8879
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 313
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 310
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 311
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 313
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 309
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 314
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 410
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 420
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 407
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 312
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 303
27X-RAY DIFFRACTION11K401 - 414
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 314
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 323
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 315
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 307
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 304
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 307
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 317
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 - 416
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301 - 302
52X-RAY DIFFRACTION22V401 - 413
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 310
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 218
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 415
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301 - 317
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 328
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 202
66X-RAY DIFFRACTION28b301 - 313

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