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- PDB-4qwu: yCP beta5-C52F mutant in complex with bortezomib -

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Basic information

Entry
Database: PDB / ID: 4qwu
TitleyCP beta5-C52F mutant in complex with bortezomib
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / 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
Chem-BO2 / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 ...Chem-BO2 / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 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 17, 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)733,75645
Polymers731,13928
Non-polymers2,61717
Water3,981221
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area125880 Å2
ΔGint-477 kcal/mol
Surface area210790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.200, 299.250, 144.850
Angle α, β, γ (deg.)90.00, 113.01, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999656, -0.001659, 0.026166), (-0.002964, -0.98445, -0.175643), (0.02605, -0.17566, 0.984106)67.4883, -287.96707, -26.22713

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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)
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, 238 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / 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-BO2 / N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / BORTEZOMIB / Bortezomib


Mass: 384.237 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C19H25BN4O4 / Comment: medication, anticancer*YM
#18: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 221 / 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: Feb 9, 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: 3→30 Å / Num. all: 211036 / Num. obs: 205760 / % possible obs: 97.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 10.9
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.469 / Mean I/σ(I) obs: 3.1 / % possible all: 99.4

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Processing

Software
NameClassification
XDSdata scaling
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1RYP

1ryp


Resolution: 3→15 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.918 / SU B: 32.379 / SU ML: 0.254 / Cross valid method: THROUGHOUT / ESU R Free: 0.338 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2178 10288 5 %RANDOM
Rwork0.18084 ---
obs0.18268 195471 97.62 %-
all-205759 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 62.141 Å2
Baniso -1Baniso -2Baniso -3
1-4.42 Å20 Å2-0.46 Å2
2---5.93 Å2-0 Å2
3---1.25 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49376 0 179 221 49776
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950466
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248206
X-RAY DIFFRACTIONr_angle_refined_deg0.8521.96768278
X-RAY DIFFRACTIONr_angle_other_deg0.7043.001110986
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.1556314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.28324.4192254
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.681158752
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.2115284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27686
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257266
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211332
X-RAY DIFFRACTIONr_mcbond_it2.5045.28525346
X-RAY DIFFRACTIONr_mcbond_other2.5045.28525345
X-RAY DIFFRACTIONr_mcangle_it3.357.91431630
X-RAY DIFFRACTIONr_mcangle_other3.357.91431631
X-RAY DIFFRACTIONr_scbond_it2.445.67225120
X-RAY DIFFRACTIONr_scbond_other2.445.67225120
X-RAY DIFFRACTIONr_scangle_other3.0468.35536648
X-RAY DIFFRACTIONr_long_range_B_refined3.85741.3954734
X-RAY DIFFRACTIONr_long_range_B_other3.84541.39254720
X-RAY DIFFRACTIONr_rigid_bond_restr0.78398672
X-RAY DIFFRACTIONr_sphericity_free29.4475168
X-RAY DIFFRACTIONr_sphericity_bonded17.328597825
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 745 -
Rwork0.289 14159 -
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)
10.0359-0.0162-0.00920.01010.00420.0028-0.00940.0093-0.01230.01360.007-0.0036-0.0031-0.00010.00230.1173-0.0098-0.00120.08460.00190.106766.592-91.595346.0287
20.0019-0.00150.00020.00350.00150.0083-0.0003-0.0051-0.0131-0.0113-0.00480.01390.0053-0.00380.00510.1198-0.00420.01070.08850.00310.111859.2824-87.336716.5467
30.00470.0030.00030.0044-0.00130.00210.0041-0.01510.0018-0.00110.00340.00860.0092-0.0044-0.00750.12360.005-0.00440.08170.00950.104932.1808-86.85951.3543
40.0355-0.0150.02470.0268-0.0020.0208-0.0161-0.01280.0042-0.01670.00010.0365-0.0211-0.01060.01610.06680.0342-0.01610.03050.01360.09553.0816-89.658613.8322
50.00550.00780.00430.02160.00090.0084-0.0069-0.00620.0034-0.02520.00260.02350.00330.00030.00430.07180.01290.02140.0774-0.00230.1025-3.1974-94.197445.6652
60.00130.001-0.00020.0012-0.000100.00820.00060.00410.0075-0.00610.0072-0.0013-0.0004-0.00210.08360.01410.03490.0647-0.01750.06815.1287-94.830369.7221
70.0078-0.0036-0.00170.00410.00150.00090.01230.02150.00040.006-0.0125-0.01110.0047-0.00730.00030.1376-0.00320.00320.0739-0.01360.096347.4126-93.095871.0193
80.0027-0.0005-0.00320.00490.00080.00490.00940.0127-0.00160.0073-0.0067-0.0033-0.0019-0.0192-0.00270.1167-0.0012-0.00620.0815-0.00430.107967.384-128.972647.3083
90.01650.00040.03070.04750.01450.06440.0161-0.0002-0.0036-0.0091-0.014-0.0060.0022-0.0081-0.00210.1190.00090.01010.0880.00290.111968.1603-126.685920.9112
100.01880.01-0.010.0574-0.00180.00990.0213-0.0180.0237-0.00550.0025-0.00450.00580.0177-0.02380.12630.00110.0010.08490.00710.089444.6868-125.8889-0.5759
110.01610.03730.00050.09010.00480.0060.0050.0010.00820.01940.01030.02320.00560.0136-0.01530.07470.0058-0.03240.04990.01180.089211.1305-130.43462.7168
120.00110.00590.0040.04220.03480.03840.0013-0.00570.00220.0151-0.00790.0257-0.00310.0080.00660.09310.0044-0.01120.08440.0090.1067-4.2628-133.937328.4217
130.0214-0.03740.01150.0789-0.02180.00680.01110.00370.01180.0093-0.01040.00540.00640.0059-0.00070.12390.00010.00990.0906-0.00320.1127.9687-137.540160.1025
140.0034-0.00720.00290.0975-0.00810.0030.01470.0083-0.00490.0028-0.0056-0.00160.00770.0104-0.00920.132-0.00470.00080.0898-0.00250.103639.7878-133.683870.4129
150.0181-0.0119-0.01640.00970.01180.0218-0.00040.01810.0121-0.00790.0002-0.00350.01520.00070.00020.1115-0.0126-0.01310.08170.00240.11312.1952-206.009436.5939
160.01010.00430.00690.00250.00210.0066-0.0083-0.00050.0004-0.0072-0.0003-0.0058-0.00190.00660.00860.1078-0.0085-0.02380.077-0.00620.1028.758-204.87376.6847
170.0022-0.0012-0.00440.00180.00420.02170.0086-0.01070.0004-0.01280.00890.0005-0.0230.0203-0.01750.1130.0186-0.00660.0605-0.01370.059935.8286-202.8445-9.0303
180.0031-0.0052-0.00040.0208-0.00750.0056-0.0024-0.00980.0148-0.0308-0.0013-0.03780.02020.01150.00370.07440.03550.03420.0496-0.0310.084465.1074-202.2343.3179
190.02020.0203-0.02270.0227-0.02210.02940.0117-0.0056-0.01090.0115-0.0067-0.0239-0.0117-0.0014-0.00510.07960.027-0.01770.0715-0.00110.109671.9883-203.271835.1623
200.00980.00150.00690.00120.00170.00550.0201-0.0025-0.00950.0024-0.0084-0.00790.0121-0.0073-0.01170.09310.0247-0.03860.04490.02260.069454.1314-206.932859.2993
210.00330.0027-0.00140.0026-0.00150.00120.00460.01050.01330.01160.00540.0099-0.0060.0005-0.010.1338-0.0018-0.01130.07430.01030.099421.9008-209.055960.9105
220.0013-0.00020.00050.0025-0.00140.00090.0130.0040.00310.0003-0.00850.01110.00360.006-0.00450.1215-0.00310.00230.08630.00720.11451.5285-169.46344.4348
230.000200.0010.0004-0.00060.00690.00150.0040.00070.00230.00140.0061-0.01150.0214-0.0030.1225-0.0014-0.01410.08350.00450.11960.2739-167.030718.0349
240.0128-0.0090.01450.0099-0.00950.02850.0091-0.0144-0.0241-0.0190.01430.0104-0.01220.001-0.02340.11780.0022-0.01650.0746-0.00510.090823.3495-163.9981-3.7548
250.0038-0.00360.00580.0207-0.00590.00940.0116-0.0041-0.0089-0.02470.0088-0.00490.0144-0.0049-0.02040.11010.00820.02350.069-0.01490.091256.9813-160.0829-0.3631
260.0135-0.0247-0.0180.05390.03890.03270.00480.0061-0.00160.02490.0035-0.01030.0151-0.0192-0.00840.07970.01860.00610.0807-0.00820.101772.7819-161.141125.1841
270.0042-0.0009-0.0010.00250.00160.0010.0080.0156-0.010.0114-0.0073-0.00670.0055-0.0078-0.00070.12290.0025-0.00970.08350.00620.109261.1938-163.172857.2498
280.005-0.0027-0.00250.00210.0020.00190.01470.01710.00540.0005-0.0122-0.00360.0012-0.0128-0.00250.136-0.00670.00020.0919-0.00020.104329.5805-168.870367.4328
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 306
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 309
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 304
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 305
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 311
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 406
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 409
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 305
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201
23X-RAY DIFFRACTION10J301 - 309
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 302
26X-RAY DIFFRACTION11K401 - 409
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 310
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 313
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 203
33X-RAY DIFFRACTION14N301 - 308
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 307
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 309
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 305
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 304
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 305
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 304
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 413
49X-RAY DIFFRACTION22V1 - 226
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 408
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 304
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 209
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 302
58X-RAY DIFFRACTION25Y401 - 413
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 409
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 315
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 202
66X-RAY DIFFRACTION28b301 - 304

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