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- PDB-4r00: yCP beta5-C52F mutant in complex with Omuralide -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4r00
TitleyCP beta5-C52F mutant in complex with Omuralide
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
Omuralide, open form / 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 ...Omuralide, open form / 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 29, 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)732,80247
Polymers731,13928
Non-polymers1,66319
Water6,179343
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area121230 Å2
ΔGint-505 kcal/mol
Surface area214120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.250, 301.240, 144.330
Angle α, β, γ (deg.)90.00, 113.16, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999535, -0.001579, 0.030459), (-0.003693, -0.985044, -0.172262), (0.030276, -0.172295, 0.98458)68.00609, -290.28302, -26.08145
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 /


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: C52F / 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 /


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 /


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 /


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 /


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 /


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


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 / PSMB2


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 / PSMB3


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 / PSMB4


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 / PSMB5


Mass: 23369.279 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) / Strain (production host): 4932
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6 /


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 /


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 / PSMB1


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, 362 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.: 5 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-SLA / Omuralide, open form / (2R,3S,4R)-3-hydroxy-2-[(1S)-1-hydroxy-2-methylpropyl]-4-methyl-5-oxopyrrolidine-2-carbaldehyde


Mass: 215.246 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H17NO4
#18: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 343 / 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: Nov 30, 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: 2.8→30 Å / Num. all: 261898 / Num. obs: 255351 / % possible obs: 97.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.087 / Net I/σ(I): 11.1
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.505 / Mean I/σ(I) obs: 2.3 / % possible all: 97

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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: 0.95 / Cor.coef. Fo:Fc free: 0.935 / SU B: 25.562 / SU ML: 0.214 / Cross valid method: THROUGHOUT / ESU R Free: 0.273 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20992 12768 5 %RANDOM
Rwork0.18389 ---
all0.188 255351 --
obs0.1852 242583 97.59 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 59.818 Å2
Baniso -1Baniso -2Baniso -3
1-2.54 Å2-0 Å2-0.7 Å2
2---4.6 Å20 Å2
3---1.72 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49376 0 103 343 49822
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950382
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248152
X-RAY DIFFRACTIONr_angle_refined_deg0.8461.96568182
X-RAY DIFFRACTIONr_angle_other_deg0.7933.001110866
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.91856314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.6324.4192254
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.58158752
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.48615284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27692
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257176
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211284
X-RAY DIFFRACTIONr_mcbond_it2.4475.33325346
X-RAY DIFFRACTIONr_mcbond_other2.4475.33325345
X-RAY DIFFRACTIONr_mcangle_it3.3027.98531630
X-RAY DIFFRACTIONr_mcangle_other3.3027.98531631
X-RAY DIFFRACTIONr_scbond_it2.4225.71125036
X-RAY DIFFRACTIONr_scbond_other2.4225.71125036
X-RAY DIFFRACTIONr_scangle_other3.0788.41736552
X-RAY DIFFRACTIONr_long_range_B_refined3.82841.58753954
X-RAY DIFFRACTIONr_long_range_B_other3.82341.58953926
X-RAY DIFFRACTIONr_rigid_bond_restr1.204398534
X-RAY DIFFRACTIONr_sphericity_free26.0225230
X-RAY DIFFRACTIONr_sphericity_bonded16.45597755
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 908 -
Rwork0.314 17255 -
obs--97.09 %
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)
10.0129-0.0023-0.00660.00830.00130.0038-0.00260.0088-0.00490.00290.0023-0.0225-0.0044-0.00490.00030.0726-0.0071-0.00740.0306-0.0080.077567.1655-92.455945.7781
20.02440.0040.01920.00140.00330.0164-0.00680.0019-0.002-0.00580.00080.00450.00020.00440.0060.0781-0.00780.010.03790.00840.068659.8114-88.198416.2354
30.02840.028-0.01870.0285-0.01840.0134-0.00670.00110.0011-0.00960.00710.00760.00610.0044-0.00040.08990.0011-0.00620.03290.010.061132.5125-87.68391.01
40.00160.00070.00480.0083-0.01110.0442-0.0048-0.00060.005-0.01510.00010.01830.00710.01240.00480.06420.0083-0.02180.02040.01120.0833.2593-90.413813.5696
50.0003-0.00050.00020.0014-0.00010.0005-0.0018-0.0002-0.00470.0030.00390.0096-0.0030.0022-0.00210.05240.00840.00680.02970.00450.0972-2.999-94.907245.4874
60.0001-0.0003-0.00020.00080.00090.0011-0.0030.0009-0.00060.0077-0.00120.0040.00920.00140.00430.09070.00120.01670.0328-0.00740.067615.4765-95.478169.574
70.0112-0.0105-0.01210.01640.0130.01380.00360.0126-0.00420.0207-0.0082-0.00330.0012-0.01110.00450.1011-0.0019-0.00630.025-0.00840.056347.9282-93.803470.834
80.0140.0111-0.02350.041-0.01430.04040.0060.0058-0.00020.0371-0.0043-0.0317-0.0076-0.0142-0.00170.0462-0.0019-0.01870.0229-0.00730.064967.9775-129.950647.2672
90.0018-0.006-0.00750.02560.0380.06310.0076-0.00110.0065-0.0154-0.0042-0.0156-0.014-0.0115-0.00340.0648-0.00310.01240.0384-0.00150.078168.6824-127.75820.6446
100.0790.0061-0.01750.0046-0.00090.00490.0148-0.02450.0114-0.0161-0.0063-0.006-0.00290.0079-0.00860.09770.00170.00410.02930.00540.049244.9684-126.9691-0.7762
110.01750.04010.00270.1005-0.00390.0682-0.00010.00350.0027-0.01790.00780.0279-0.00470.0236-0.00770.07010.0015-0.02440.02860.00570.064611.2022-131.26882.3667
120.0006-0.0003-0.00080.01920.00630.0043-0.0009-0.0044-0.00220.01330.00110.0208-0.00090.0062-0.00010.04920.0013-0.00320.03350.00550.0919-4.1493-134.947728.3107
130.0166-0.0350.00580.087-0.01090.00230.00530.00770.00460.0217-0.01030.01020.00420.00470.0050.07220.00040.01520.0374-0.00050.07058.1588-138.42260.0873
140.0108-0.0154-0.00910.08640.01540.00860.00790.0094-0.00010.0345-0.0051-0.0061-0.0055-0.0033-0.00290.0935-0.0003-0.00540.0367-0.00340.05540.1603-134.577570.4411
150.02760.01470.0070.03210.01960.0133-0.00130.0090.00090.0045-0.00420.00610.01-0.00150.00550.0719-0.0124-0.01480.02320.01020.08022.2836-207.248636.6479
160.0111-0.00290.02040.0014-0.00620.0391-0.00480.00130.0038-0.004-0.0047-0.00390.0054-0.00050.00950.0777-0.0033-0.02460.0237-0.00970.07818.7639-206.24216.6242
170.00140.0002-0.00130.0032-0.00370.00880.0112-0.0035-0.0012-0.01570.00160.00910.0070.0106-0.01280.1070.0139-0.02880.0183-0.01710.059435.9412-204.2567-9.1732
180.0068-0.01850.00920.0704-0.02920.0134-0.0008-0.0060.0156-0.0417-0.0126-0.04970.0158-0.0040.01340.0620.01940.00530.0274-0.00970.050965.4296-203.67483.2048
190.00240.0012-0.00050.0060.00350.00360.010.0041-0.0010.0110.0053-0.02360.0038-0.0014-0.01530.05660.0157-0.02770.0203-0.02060.172.4706-204.665735.0798
200.0570.01060.01640.00240.00290.00570.0188-0.0052-0.0130.0096-0.008-0.00720.0025-0.0048-0.01080.0920.0058-0.03970.01330.00740.07354.5542-208.334559.2874
210.0078-0.01180.01060.0294-0.02310.019-0.00270.00720.00530.01860.0030.0064-0.00880.0026-0.00030.1001-0.005-0.0160.02080.01230.060322.1936-210.412460.9473
220.0040.00950.01010.02530.02240.02990.008-0.00350.00180.0231-0.00770.01880.017-0.0008-0.00030.0512-0.0060.00310.02640.00990.07881.6492-170.600744.5682
230.00670.0049-0.00120.007-0.0010.0013-0.0037-0.0026-0.002-0.01770.00080.01020.00240.00630.00280.0692-0.0013-0.02640.03460.00260.08370.2944-168.14717.9527
240.0294-0.02610.03020.0278-0.03060.03940.0099-0.0131-0.0091-0.01850.00190.0089-0-0.0004-0.01190.0960.0029-0.01620.0328-0.00380.049223.4947-165.1841-3.8576
250.02830.064-0.00130.1676-0.00420.00280.003-0.0001-0.0011-0.03840.006-0.00990.00440.0034-0.0090.07450.00550.00690.0318-0.00930.058557.3366-161.4379-0.7706
260.00090.00740.00070.11930.00020.00160.0024-0.0013-0.00630.01460.0011-0.03280.0067-0.0032-0.00350.05140.0087-0.00580.0405-0.00850.085473.2918-162.274325.0483
270.0092-0.0132-0.00230.0397-0.00060.00250.00070.0101-0.00840.015-0.0017-0.0137-0.0037-0.00910.0010.07250.0059-0.02420.0348-0.00290.071661.7817-164.353757.2052
280.0111-0.00860.00090.07120.02120.00830.01290.0073-0.00090.0305-0.0075-0.0050.016-0.0041-0.00540.0973-0.0021-0.00150.03250.00650.054130.0351-170.011667.5383
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 314
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 308
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 312
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 307
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 305
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 316
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 416
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 408
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 407
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 321
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 303
27X-RAY DIFFRACTION11K401 - 409
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 321
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 328
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 314
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 305
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 311
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 308
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 307
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 303
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 309
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 416
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301 - 302
52X-RAY DIFFRACTION22V401 - 411
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 310
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 215
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301 - 302
59X-RAY DIFFRACTION25Y401 - 410
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 417
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 320
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 315

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