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- PDB-4no9: yCP in complex with Z-Leu-Leu-Leu-epoxyketone -

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Basic information

Entry
Database: PDB / ID: 4no9
TitleyCP in complex with Z-Leu-Leu-Leu-epoxyketone
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE Inhibitor / Proteasome / Peptide Electrophile / Binding Analysis / Irreversible Inhibitor / Epoxyketone / 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
PHQ-LEU-LEU-LEU-EPOXYKETONE, unbound form / PHQ-LEU-LEU-LEU-EPOXYKETONE, bound form / Chem-2L0 / Chem-2LR / 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 ...PHQ-LEU-LEU-LEU-EPOXYKETONE, unbound form / PHQ-LEU-LEU-LEU-EPOXYKETONE, bound form / Chem-2L0 / Chem-2LR / 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: 2.9 Å
AuthorsStein, M.L. / Cui, H. / Beck, P. / Dubiella, C. / Voss, C. / Krueger, A. / Schmidt, B. / Groll, M.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Systematic Comparison of Peptidic Proteasome Inhibitors Highlights the alpha-Ketoamide Electrophile as an Auspicious Reversible Lead Motif.
Authors: Stein, M.L. / Cui, H. / Beck, P. / Dubiella, C. / Voss, C. / Kruger, A. / Schmidt, B. / Groll, M.
History
DepositionNov 19, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 12, 2014Provider: repository / Type: Initial release
Revision 1.1Feb 19, 2014Group: 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_conn_type / 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.conn_type_id / _struct_conn.id / _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_conn_type.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)733,38640
Polymers731,05128
Non-polymers2,33512
Water3,027168
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area118980 Å2
ΔGint-420 kcal/mol
Surface area214400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.490, 301.490, 144.390
Angle α, β, γ (deg.)90.00, 114.15, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999998, -0.00061, 0.002039), (0.000276, -0.987095, -0.160138), (0.00211, -0.160137, 0.987093)67.94151, -291.48773, -23.45439

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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 / 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 / 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 / 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, 180 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-2L0 / N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-leucinamide / PHQ-LEU-LEU-LEU-EPOXYKETONE, bound form


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 535.716 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C29H49N3O6 / References: PHQ-LEU-LEU-LEU-EPOXYKETONE, bound form
#17: Chemical ChemComp-2LR / N-[(benzyloxy)carbonyl]-L-leucyl-N-{(1R,2S)-1-hydroxy-4-methyl-1-[(2R)-2-methyloxiran-2-yl]pentan-2-yl}-L-leucinamide / PHQ-LEU-LEU-LEU-EPOXYKETONE, unbound form


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 533.700 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H47N3O6 / References: PHQ-LEU-LEU-LEU-EPOXYKETONE, unbound form
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 168 / 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: 3.71 Å3/Da / Density % sol: 66.83 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 mM MgAc2, 100 mM 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: Jul 9, 2011
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→25 Å / Num. all: 397998 / Num. obs: 395212 / % possible obs: 99.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 8.84
Reflection shellResolution: 2.6→2.7 Å / Rmerge(I) obs: 0.503 / Mean I/σ(I) obs: 1.99 / % 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: 2.9→15 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.935 / SU B: 27.099 / SU ML: 0.219 / Cross valid method: THROUGHOUT / ESU R Free: 0.286 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20342 11599 5 %RANDOM
Rwork0.17747 ---
all0.185 ---
obs0.17876 -98.95 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 57.381 Å2
Baniso -1Baniso -2Baniso -3
1-2.88 Å2-0 Å2-1.16 Å2
2---8.05 Å20 Å2
3---4.06 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49294 0 160 168 49622
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950358
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248154
X-RAY DIFFRACTIONr_angle_refined_deg1.0131.96668132
X-RAY DIFFRACTIONr_angle_other_deg0.7243.001110876
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.02656306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.32324.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.676158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.93515284
X-RAY DIFFRACTIONr_chiral_restr0.0580.27681
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257116
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211280
X-RAY DIFFRACTIONr_rigid_bond_restr0.878398392
X-RAY DIFFRACTIONr_sphericity_free34.3295100
X-RAY DIFFRACTIONr_sphericity_bonded7.85597562
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.308 827 -
Rwork0.294 15703 -
obs--99.5 %
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)
10.1317-0.05120.02960.2169-0.0060.0099-0.0040.004-0.00040.01730.0096-0.0522-0.0098-0.0078-0.00560.0534-0.00740.03370.0756-0.01480.045466.7556-92.702745.5874
20.1467-0.10850.07360.16770.04750.1922-0.01910.00490.0016-0.0326-0.007-0.0125-0.03460.03080.02620.0732-0.01450.04980.08380.01380.052459.9041-88.709115.8408
30.08370.07680.03870.08440.03190.04-0.02020.01140.0151-0.04630.02260.00670.00020.0217-0.00240.0764-0.00440.02660.07960.01660.031932.6985-88.17490.163
40.09690.0305-0.09880.02590.01090.2347-0.0116-0.01560.0356-0.0223-0.00340.0402-0.0537-0.00290.0150.04870.0248-0.01630.05190.02350.08783.2037-90.82112.4743
50.02390.05030.00280.1136-0.01210.0989-0.0082-0.00760.0169-0.0036-0.00180.0494-0.0214-0.00990.010.03140.02070.03540.0769-0.00170.0976-3.6128-94.929944.4787
60.10630.05550.05610.05760.02590.0303-0.0011-0.0190.01260.0366-0.00830.0261-0.0023-0.01190.00950.09340.010.06180.0897-0.01110.048814.6082-95.420868.8618
70.0416-0.00590.01250.1014-0.01720.00810.0150.01060.01990.0624-0.0198-0.0077-0.0127-0.00150.00480.0975-0.00760.02770.0712-0.01240.025847.082-93.727970.4493
80.01820.0167-0.00690.1098-0.0020.00320.02220.01280.0020.0374-0.0194-0.0706-0.007-0.0108-0.00280.0465-0.00420.0050.08210.00250.072267.0741-130.83447.9418
90.0853-0.01260.03330.1886-0.02040.04310.01380.00010.0147-0.0295-0.0167-0.066-0.014-0.0090.00290.0444-0.00370.04780.0814-0.00330.064668.4528-128.419620.5622
100.0975-0.03220.05160.1578-0.05160.13560.0045-0.00710.0026-0.0840.01040.0017-0.01660.0097-0.01490.09310.00110.03340.08390.00350.028645.1006-127.5465-1.2438
110.0473-0.03550.01840.2877-0.06820.04190.01240.00470.0067-0.05440.00560.0682-0.00930.0156-0.0180.05350.004-0.01540.07510.00940.037411.1744-131.76621.6339
120.0533-0.04010.03740.14920.06480.14550.0055-0.0089-0.0057-0.0147-0.00340.0695-0.0166-0.0053-0.0020.00610.00440.00990.07530.010.0927-4.6438-135.002527.5584
130.095-0.0260.00180.1267-0.01450.0017-0.0021-0.0110.00590.04680.00540.0393-0.0045-0.0002-0.00330.0534-0.0010.0540.0802-0.00080.05587.2012-138.402859.6077
140.1211-0.0148-0.05110.14680.00210.0240.01950.00140.01180.056-0.0157-0.0134-0.00660.0132-0.00380.0866-0.00850.02480.0847-0.00560.015439.1225-134.53270.5003
150.0589-0.0658-0.02690.09690.02850.0288-0.01320.00830.00710.00610.01670.03080.029-0.0125-0.00350.0402-0.0299-0.0020.05940.01780.09021.3865-207.275336.3154
160.0780.01590.04280.0462-0.00510.0727-0.03530.0261-0.0082-0.01490.01560.0235-0.0026-0.0070.01970.0485-0.0078-0.01720.0628-0.01660.06638.2895-206.36446.365
170.030.0060.01380.1478-0.03680.03310.0319-0.0071-0.0072-0.10170.00450.0450.04510.0198-0.03650.14810.0111-0.02970.0479-0.02310.052335.7457-204.6074-9.2686
180.09750.00140.12730.047-0.02650.19290.0072-0.0170.0064-0.0688-0.0283-0.04420.04330.01770.02110.10350.03320.07320.071-0.00890.069865.1808-204.00263.4184
190.06350.006-0.03460.0214-0.04260.16870.00880.0071-0.0158-0.0078-0.0081-0.02910.02810.0298-0.00080.03370.0360.00370.058-0.01230.098871.7448-205.044235.6969
200.16390.0024-0.00170.0932-0.0070.08320.0373-0.0177-0.03140.0342-0.0201-0.04450.0309-0.0053-0.01730.07230.0067-0.01640.05590.01670.048853.3152-208.484259.7361
210.0463-0.0692-0.02220.1223-0.00540.1045-0.0034-0-0.02310.01580.00450.0438-0.00740.0153-0.0010.0643-0.00630.02440.05610.02260.046920.9131-210.51460.8883
220.0042-0.0082-0.00050.118-0.02070.00820.0007-0.0074-0.0117-0.00080.00280.08360.011-0.0024-0.00350.0329-0.00970.02220.07610.01330.08451.1008-170.091244.7143
230.07280.0810.01560.3411-0.04060.02580.00390.0097-0.002-0.05370.01140.07020.01930.0103-0.01530.0198-0.0086-0.01260.0682-0.00170.0762-0.1244-168.013917.2218
240.0629-0.1104-0.0280.20540.05130.0150.01670.0154-0.0164-0.0577-0.01530.0209-0.0060.0014-0.00140.08340.002-0.00260.0723-0.01570.024923.3393-165.3891-4.3747
250.0995-0.049-0.00430.20060.02870.01680.0180.0187-0.0122-0.0592-0.0077-0.02770.0010.017-0.01040.08130.0160.0450.0869-0.01510.039557.2455-161.7149-0.7082
260.02280.0489-0.04310.1679-0.07860.09310.00450.0026-0.0014-0.0016-0.0056-0.05770.00530.00810.0010.03030.01550.03290.0884-0.0050.078572.9058-162.746125.4203
270.0584-0.03670.01610.25950.02260.05590.0035-0.0005-0.02430.0584-0.0074-0.0320.0043-0.00170.00390.04490.00180.00240.07530.00670.036760.9053-164.528557.5588
280.1010.00430.06590.2134-0.04060.05240.0135-0.0058-0.00830.0441-0.00210.02960.0014-0.0094-0.01130.0787-0.00580.03520.08380.01010.019928.9576-170.093967.6622
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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