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- PDB-4qwl: yCP beta5-A50V mutant in complex with carfilzomib -

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Basic information

Entry
Database: PDB / ID: 4qwl
TitleyCP beta5-A50V mutant in complex with carfilzomib
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 / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex ...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 / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
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
CARFILZOMIB, bound form / Chem-3BV / 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 ...CARFILZOMIB, bound form / Chem-3BV / 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 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

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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)736,17748
Polymers731,10728
Non-polymers5,07020
Water11,746652
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)134.480, 300.280, 143.960
Angle α, β, γ (deg.)90.00, 112.71, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999348, -0.005035, 0.035742), (-0.001258, -0.984763, -0.173895), (0.036073, -0.173826, 0.984115)66.53471, -288.82095, -25.84392

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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: A50V / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P23639
#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
#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
#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
#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
#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

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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

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Proteasome subunit beta type- ... , 7 types, 14 molecules HVIWJXKYLZMaNb

#8: Protein Proteasome subunit beta type-2 / PSMB2 / 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
#9: Protein Proteasome subunit beta type-3 / PSMB3 / 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
#10: Protein Proteasome subunit beta type-4 / PSMB4 / 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
#11: Protein Proteasome subunit beta type-5 / PSMB5 / 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
#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
#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
#14: Protein Proteasome subunit beta type-1 / PSMB1 / 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

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Non-polymers , 5 types, 672 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 / Chloride


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-3BV / N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide / / CARFILZOMIB, bound form / Carfilzomib


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 723.942 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C40H61N5O7 / References: CARFILZOMIB, bound form / Comment: medication, anticancer, inhibitor*YM
#18: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 652 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.67 Å3/Da / Density % sol: 66.52 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 20, 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: 2.6→30 Å / Num. all: 322028 / Num. obs: 315909 / % possible obs: 98.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 14.3

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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: 0.955 / Cor.coef. Fo:Fc free: 0.94 / SU B: 23.115 / SU ML: 0.207 / Cross valid method: THROUGHOUT / ESU R Free: 0.238 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21856 15796 5 %RANDOM
Rwork0.19258 ---
all0.197 315908 --
obs0.19388 300112 98.38 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.356 Å2
Baniso -1Baniso -2Baniso -3
1-2.96 Å2-0 Å2-2.11 Å2
2---5.43 Å20 Å2
3---2.49 Å2
Refinement stepCycle: LAST / Resolution: 2.6→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49299 0 348 652 50299
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950565
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248372
X-RAY DIFFRACTIONr_angle_refined_deg0.8771.9768422
X-RAY DIFFRACTIONr_angle_other_deg0.7673.003111396
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.12856306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.06624.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.096158738
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.63115284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27706
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257216
X-RAY DIFFRACTIONr_gen_planes_other0.0020.0211340
X-RAY DIFFRACTIONr_mcbond_it2.1884.99925313
X-RAY DIFFRACTIONr_mcbond_other2.1884.99925312
X-RAY DIFFRACTIONr_mcangle_it2.9147.4831588
X-RAY DIFFRACTIONr_mcangle_other2.9147.4831589
X-RAY DIFFRACTIONr_scbond_it2.0955.39725252
X-RAY DIFFRACTIONr_scbond_other2.0955.39725252
X-RAY DIFFRACTIONr_scangle_other2.5757.93636835
X-RAY DIFFRACTIONr_long_range_B_refined3.36939.02254629
X-RAY DIFFRACTIONr_long_range_B_other3.33939.01754545
X-RAY DIFFRACTIONr_rigid_bond_restr0.904398937
X-RAY DIFFRACTIONr_sphericity_free27.6915406
X-RAY DIFFRACTIONr_sphericity_bonded17.215598276
LS refinement shellResolution: 2.601→2.667 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.352 1082 -
Rwork0.322 20556 -
obs--93.8 %
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)
10.00240.00080.00010.0011-0.00070.0016-0.00590.0143-0.00460.00540.0062-0.0093-0.0134-0.0033-0.00040.1252-0.0092-0.00960.0994-0.00460.149266.9795-91.986345.9255
20.00950.00740.02030.01050.01870.0488-0.01360.0054-0.0037-0.0191-0.00120.0163-0.01640.0070.01480.1064-0.01280.01810.10270.01220.134459.544-87.681116.3385
30.01630.016-0.00540.019-0.00450.0022-0.0065-0.00950.0026-0.00150.00980.00570.00520.0072-0.00330.14560.0047-0.00620.09670.00770.132632.301-87.27761.071
40.00370.0003-0.00010.0040.00140.0025-0.0122-0.0127-0.0022-0.01070.00580.0231-0.01160.01020.00640.13080.0115-0.01880.0847-0.00070.15413.1203-89.989913.7033
50.0173-0.01620.02730.0164-0.02360.0531-0.0088-0.0144-0.02230.00810.01640.0323-0.0204-0.0045-0.00760.08930.01690.01290.1002-0.00310.1565-3.1003-94.336945.7192
60.0006-0.00090.00060.0109-0.00280.00120.00340.0060.00450.0263-0.0126-0.0127-0.00160.00430.00920.13280.01080.02660.0952-0.01270.125915.366-94.996469.8638
70.0045-0.0013-0.00390.00220.00090.00380.00580.01730.00440.0127-0.0066-0.0101-0.0043-0.01730.00080.157-0.0024-0.00980.0834-0.01550.129247.783-93.343271.0934
80.003-0.0003-0.00330.00790.00030.0040.00980.01090.00880.0202-0.0027-0.0284-0.0087-0.0164-0.0070.1228-0.0034-0.01480.0957-0.00450.150467.4426-130.024947.9041
90.0015-0.0064-0.00270.09510.02120.00940.00770.00780.0086-0.0132-0.0143-0.0036-0.0182-0.01810.00670.107-0.00320.01070.1105-0.00110.154768.2661-127.294420.7246
100.0052-0.0034-0.00040.01030.00120.00030.006-0.00650.0109-0.0348-0.00080.0058-0.0053-0.0014-0.00510.138200.01070.10320.00460.128844.7199-126.3653-0.7858
110.0098-0.0203-0.00860.07390.01270.00890.0091-0.01790.0064-0.02770.00040.0029-0.01830.0183-0.00950.12860.0088-0.0260.09270.01040.138110.9223-130.75782.6203
120.0561-0.01820.05910.0478-0.0160.0750.0071-0.00510.00110.01590.00570.0237-0.01010.0205-0.01280.09670.00440.00380.10660.00780.1682-4.4746-134.152728.73
130.00460.00290.00860.01350.01450.04190.01520.00430.016-0.0061-0.00550.01220.03150.0171-0.00970.10570.00030.01750.11080.0020.14537.9475-137.834860.4944
140.0372-0.0138-0.01270.07820.00410.00540.01120.0118-0.00960.0309-0.0057-0.01220.0034-0.0011-0.00550.1446-0.0026-0.00690.10340.00070.127640.1441-134.146570.3037
150.04320.02390.00540.0140.00140.0054-0.00540.0190.0045-0.00860.0061-0.00260.02090.0089-0.00070.1243-0.016-0.02060.09560.0130.15621.8955-206.313236.4167
160.0014-0.00040.00050.0004-0.00040.0004-0.009-0.0080.00420.00150.0026-0.0073-0.0009-0.00470.00640.1355-0.0033-0.02920.0954-0.00360.15358.331-205.10226.2981
170.024-0.00830.02480.0029-0.00940.04280.03280.0223-0.0428-0.007-0.00140.01520.00990.0492-0.03140.13910.0299-0.00210.0712-0.01460.104335.4741-202.9281-9.6038
180.0214-0.04-00.081-0.0020.00070.0085-0.00740.0093-0.044-0.0044-0.0140.00760.0051-0.00420.09270.04720.02040.0418-0.02690.129964.9161-202.41072.9045
190.0011-0.0021-0.00530.00520.00830.02730.00220.00320.00590.01750.009-0.01410.0144-0.0265-0.01120.08520.0305-0.01190.0633-0.02780.173871.9786-203.728934.6624
200.00820.0048-0.00340.0041-0.00090.00610.02190.0025-0.01620.0182-0.0142-0.0207-0.0127-0.0181-0.00770.13980.0068-0.04950.06250.00740.138554.158-207.481658.967
210.00340.00070.00150.00040.00010.0010.00020.0165-0.00220.00140.00440.0046-0.0050.007-0.00470.1593-0.0108-0.02470.08460.01170.143721.812-209.552960.7051
220.00230.00170.0020.0082-0.00080.00410.01230.00280.00020.015-0.00490.02910.00950.0162-0.00740.1092-0.00440.00770.10150.02030.13511.5887-169.247145.2047
230.01690.02450.0080.0410.00710.01220.0161-0.0031-0.00280.0009-0.00780.00710.0210.0228-0.00840.1086-0.0047-0.01850.0946-0.00030.16050.037-167.032717.9825
240.0042-0.0064-0.00140.01670.00190.00290.0095-0.0118-0.0118-0.0260.00270.0067-0.00440.0137-0.01210.14810.0008-0.02510.0983-0.00120.136423.0243-164.0445-3.9807
250.0114-0.00670.01060.0724-0.00230.01090.0246-0.0114-0.012-0.0238-0.0022-0.01580.0207-0.0061-0.02240.11050.00990.02390.1036-0.01070.116756.9231-160.2905-0.6602
260.0189-0.03570.02170.0818-0.03990.02490.0116-0.0086-0.0087-0.0007-0.0006-0.0070.0149-0.0101-0.0110.09420.00420.01010.1066-0.01210.163772.9727-161.557825.2119
270.1351-0.01080.07960.0031-0.00130.07060.00320.0216-0.01530.0035-0.0134-0.0025-0.0243-0.02440.01020.1287-0.0008-0.02240.0870.00550.139661.4162-163.647557.4061
280.00530.0011-0.00270.00070.00040.00370.01930.0140.00790.00910.0006-0.0044-0-0.0097-0.01990.1495-0.0046-0.01140.10450.00120.13629.4784-169.133667.2595
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 326
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 322
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 319
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 319
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 306
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 314
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 433
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 424
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 422
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 231
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 447
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 329
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 333
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 204
33X-RAY DIFFRACTION14N301 - 328
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 314
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 322
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 316
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 305
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 306
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 316
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 425
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 425
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 326
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201
56X-RAY DIFFRACTION24X301 - 331
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 423
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 425
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 334
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 331

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