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- PDB-4qlq: yCP in complex with tripeptidic epoxyketone inhibitor 8 -

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Basic information

Entry
Database: PDB / ID: 4qlq
TitleyCP in complex with tripeptidic epoxyketone inhibitor 8
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Proteasome / Epoxyketone / Immunoproteasome Inhibitor / 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
Chem-38N / 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-38N / 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: 2.4 Å
AuthorsDe Bruin, G. / Huber, E. / Xin, B. / Van Rooden, E. / Al-Ayed, K. / Kim, K. / Kisselev, A. / Driessen, C. / Van der Marel, G. / Groll, M. / Overkleeft, H.
CitationJournal: J.Med.Chem. / Year: 2014
Title: Structure-based design of beta 1i or beta 5i specific inhibitors of human immunoproteasomes
Authors: De Bruin, G. / Huber, E.M. / Xin, B.T. / Van Rooden, E.J. / Al-Ayed, K. / Kim, K.B. / Kisselev, A.F. / Driessen, C. / Van der Stelt, M. / Van der Marel, G.A. / Groll, M. / Overkleeft, H.S.
History
DepositionJun 13, 2014Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jul 23, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2014Group: Database references
Revision 1.2Nov 8, 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_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_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)734,38144
Polymers731,05128
Non-polymers3,33016
Water14,628812
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area117660 Å2
ΔGint-349 kcal/mol
Surface area214500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.650, 299.590, 144.820
Angle α, β, γ (deg.)90.00, 112.85, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999292, -0.005755, 0.037173), (-0.000743, -0.985013, -0.172479), (0.037609, -0.172384, 0.984312)67.31113, -288.79517, -26.03921
DetailsAU contains one biological assembly.

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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 / 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 / Fragment: UNP residues 30-261 / 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: 23325.248 Da / Num. of mol.: 2 / Fragment: UNP residues 76-287 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
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 / Fragment: UNP residues 20-241 / 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 / Fragment: UNP residues 21-260 / 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 / Fragment: UNP residues 20-215 / 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, 828 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#17: Chemical
ChemComp-38N / N-(morpholin-4-ylacetyl)-L-alanyl-N-[(2S,4R)-1-cyclohexyl-5-hydroxy-4-methyl-3-oxopentan-2-yl]-O-methyl-L-tyrosinamide


Type: peptide-like / Mass: 588.735 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C31H48N4O7
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 812 / 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: 3.74 Å3/Da / Density % sol: 67.08 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20mM MgAc2, 100mM MES, 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 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 26, 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: 2.4→20 Å / Num. all: 416796 / Num. obs: 409646 / % possible obs: 98.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.1 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 13.6
Reflection shellResolution: 2.4→2.5 Å / Rmerge(I) obs: 0.443 / Mean I/σ(I) obs: 2.8 / % possible all: 99.1

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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: 2.4→15 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.952 / SU B: 16.137 / SU ML: 0.157 / Cross valid method: THROUGHOUT / σ(I): 2 / ESU R Free: 0.19 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21482 20483 5 %RANDOM
Rwork0.19866 ---
all0.201 409646 --
obs0.19946 389163 98.39 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 59.86 Å2
Baniso -1Baniso -2Baniso -3
1-2.61 Å2-0 Å2-0.32 Å2
2---6.78 Å20 Å2
3---3.18 Å2
Refinement stepCycle: LAST / Resolution: 2.4→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49296 0 224 812 50332
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950434
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248230
X-RAY DIFFRACTIONr_angle_refined_deg1.1191.96868240
X-RAY DIFFRACTIONr_angle_other_deg0.7973.002111088
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.34656306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.37124.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.15158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.22315284
X-RAY DIFFRACTIONr_chiral_restr0.0630.27684
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211284
X-RAY DIFFRACTIONr_mcbond_it1.9254.96525314
X-RAY DIFFRACTIONr_mcbond_other1.9254.96525313
X-RAY DIFFRACTIONr_mcangle_it2.1697.42931590
X-RAY DIFFRACTIONr_mcangle_other2.1697.4331591
X-RAY DIFFRACTIONr_scbond_it2.1935.37825120
X-RAY DIFFRACTIONr_scbond_other2.1935.37825120
X-RAY DIFFRACTIONr_scangle_other2.1167.87836651
X-RAY DIFFRACTIONr_long_range_B_refined2.60738.89954921
X-RAY DIFFRACTIONr_long_range_B_other2.5538.87654793
X-RAY DIFFRACTIONr_rigid_bond_restr1.136398664
X-RAY DIFFRACTIONr_sphericity_free27.3445401
X-RAY DIFFRACTIONr_sphericity_bonded4.78598169
LS refinement shellResolution: 2.4→2.461 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.362 1486 -
Rwork0.347 28221 -
obs--99.13 %
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)
10.04870.0371-0.01460.181-0.0390.05270.01860.0222-0.00340.0228-0.0034-0.0731-0.0322-0.0011-0.01530.1009-0.02860.00870.0425-0.02150.113667.8089-92.144445.9988
20.064-0.04920.02260.15420.06620.0714-0.02830.01590.0215-0.03480.003-0.016-0.04130.02350.02530.1259-0.0320.05530.06340.02930.085660.4743-87.909416.4091
30.12450.10910.11490.11610.07260.1681-0.04180.0350.0238-0.0670.03890.0284-0.01690.04340.00290.1467-0.00630.00570.05350.03840.08133.0907-87.25481.0955
40.03750.0314-0.0350.12780.06520.1386-0.0269-0.01720.0471-0.03950.00030.1423-0.02440.01430.02660.08420.0312-0.03910.03430.02350.20023.838-89.848513.7774
50.2566-0.00080.15220.05040.01080.2774-0.0234-0.0030.04120.03280.00390.1025-0.0453-0.03510.01950.05550.03240.06240.02950.00350.222-2.4084-94.06345.8422
60.26880.1154-0.00980.14610.0330.01630.0191-0.03120.05490.0944-0.02740.06420.0193-0.00750.00820.18770.00440.09190.0483-0.03670.081316.0839-94.774470.0142
70.04430.076-0.01770.2452-0.00020.17160.02690.0078-0.00170.1015-0.0204-0.0297-0.0304-0.0051-0.00650.2028-0.02430.01430.0377-0.02450.044748.6247-93.376571.2013
80.01980.05650.00950.24320.04620.0140.03450.0041-0.01250.0892-0.0138-0.11890.0011-0.0001-0.02070.0909-0.0055-0.02340.058-0.00650.120767.9821-130.149948.0593
90.11540.0506-0.0530.45250.03960.0420.0020.0342-0.0248-0.0404-0.0128-0.1166-0.0189-0.0230.01070.0724-0.01030.04410.0604-0.00030.12568.9732-127.606320.783
100.07010.1329-0.02540.3803-0.04230.01070.007-0.00260.0057-0.1233-0.0014-0.0145-0.0111-0.0067-0.00560.15670.00560.05080.06390.00940.037345.3109-126.5287-0.5783
110.09930.05010.00620.48230.03220.05070.02850.00340.0241-0.0970.00930.1436-0.01330.0115-0.03780.10850.0092-0.04420.05890.0220.113911.4559-130.60262.6709
120.00320.01130.0110.23920.07470.15540.00960.0032-0.00160.00460.0070.1609-0.03110.0189-0.01650.04360.01240.00730.0480.02490.1857-3.9005-133.96428.8699
130.0434-0.02080.05250.35180.05410.11590.0209-0.00590.01540.0935-0.02930.0844-0.0022-0.00480.00840.117-0.01030.09180.049-0.00030.08938.4012-137.576860.6677
140.05770.03710.00040.0273-0.00120.00070.02650.0401-0.05370.047-0.0077-0.0352-0.00980.0065-0.01880.2552-0.0177-0.00120.1074-0.02190.065740.4599-133.874571.0853
150.1922-0.011-0.08290.09110.06570.13560.01410.0188-0.00680.02920.00730.06680.0565-0.0152-0.02130.0888-0.0352-0.02620.03030.03040.14682.0655-206.123337.0098
160.06650.06610.04520.09020.02060.0552-0.0207-0.0238-0.0013-0.06360.0017-0.00940.0177-0.03930.0190.1201-0.0144-0.06070.0396-0.02990.12188.3471-205.00136.8484
170.23370.0710.04680.1615-0.00540.01740.02120.0132-0.0484-0.16950.00830.06010.01970.0156-0.02950.2503-0.0015-0.06640.0316-0.04810.117635.5127-203.1749-9.0919
180.0586-0.0980.0660.2685-0.13150.07940.0254-0.0030.0249-0.1375-0.0529-0.08790.04550.01150.02750.16130.06210.08050.0628-0.02410.140265.0866-202.69353.1213
190.04310.00340.02230.1199-0.1540.35960.02040.0191-0.06020.0146-0.0136-0.1070.04380.0591-0.00690.05830.0428-0.05560.0357-0.02180.267672.2635-203.95735.1053
200.19880.1945-0.08610.1971-0.09540.05790.0401-0.0523-0.11760.0649-0.0535-0.1086-0.02980.0050.01340.1498-0.0074-0.11860.0290.05320.172554.403-207.501759.4561
210.0184-0.0124-0.03130.2188-0.00060.06130.0006-0.0019-00.05570.01140.044-0.01340.0051-0.0120.1585-0.0117-0.0320.02410.04130.098422.0631-209.440461.2685
220.01960.04510.00460.2432-0.02530.01560.0349-0.00660.00780.0666-0.01850.14090.02170.0054-0.01640.0861-0.01260.02240.04630.0250.14762.0475-169.071745.6646
230.02170.06620.02110.31060.04990.0298-0.00360.0180.0199-0.0590.00440.12120.0250.0154-0.00080.0790.0005-0.05260.04750.01010.15490.2578-166.798818.3542
240.1202-0.03510.00160.30960.05770.01690.0044-0.0067-0.0362-0.14530.00740.0336-0.010.0115-0.01180.16220.0016-0.04450.0468-0.02360.050523.3196-164.0758-3.5993
250.12060.00670.10450.38720.00180.09380.02940.0187-0.0376-0.10020.0133-0.09440.01720.0264-0.04280.1290.01490.07360.0671-0.02860.082757.2755-160.5643-0.6194
260.01920.022-0.02530.363-0.05510.14320.02070.0112-0.017-0.0033-0.0176-0.16730.0119-0.0141-0.00310.05130.01750.01310.0656-0.02520.160773.3538-161.767625.2778
270.031-0.0323-0.02090.31230.04520.01780.00940.0114-0.02350.1082-0.0096-0.0953-0.0001-0.0120.00010.1270.0004-0.07320.03710.00940.094961.9698-163.749157.5345
280.00460.0048-0.00170.0069-0.00050.00160.01060.01120.01710.0302-0.00160.01640.0028-0.0116-0.00890.23-0.03060.00670.08760.03670.083730.2354-169.350668.1497
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION2B1 - 244
3X-RAY DIFFRACTION3C1 - 240
4X-RAY DIFFRACTION4D1 - 242
5X-RAY DIFFRACTION5E3 - 233
6X-RAY DIFFRACTION6F2 - 244
7X-RAY DIFFRACTION7G2 - 242
8X-RAY DIFFRACTION8H1 - 222
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K1 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 233
14X-RAY DIFFRACTION14N1 - 196
15X-RAY DIFFRACTION15O1 - 250
16X-RAY DIFFRACTION16P1 - 244
17X-RAY DIFFRACTION17Q1 - 240
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S3 - 233
20X-RAY DIFFRACTION20T2 - 244
21X-RAY DIFFRACTION21U2 - 242
22X-RAY DIFFRACTION22V1 - 222
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b1 - 196

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