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- PDB-4qw3: yCP beta5-C63F mutant in complex with bortezomib -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qw3
TitleyCP beta5-C63F 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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-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: 2.9 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_seq_id / _struct_conn.ptnr2_label_asym_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)733,70843
Polymers731,13928
Non-polymers2,56915
Water4,558253
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area127090 Å2
ΔGint-471 kcal/mol
Surface area215250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)138.140, 299.960, 146.570
Angle α, β, γ (deg.)90.00, 113.18, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999686, -0.000676, 0.025029), (-0.003696, -0.984702, -0.174205), (0.024764, -0.174243, 0.984391)69.26772, -288.34915, -26.05096

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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: C63F / 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


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


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


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


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


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, 268 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-CL / CHLORIDE ION


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


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


Mass: 18.015 Da / Num. of mol.: 253 / 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: Aug 14, 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: 2.9→30 Å / Num. all: 241692 / Num. obs: 238309 / % possible obs: 98.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 13.9
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.51 / 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: 1RYP

1ryp


Resolution: 2.9→15 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.934 / SU B: 31.564 / SU ML: 0.254 / Cross valid method: THROUGHOUT / ESU R Free: 0.302 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21738 11916 5 %RANDOM
Rwork0.18311 ---
all0.188 238309 --
obs0.18483 226393 98.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 72.881 Å2
Baniso -1Baniso -2Baniso -3
1-5.26 Å20 Å2-0.73 Å2
2---8.34 Å2-0 Å2
3---2.48 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49376 0 177 253 49806
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950466
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248206
X-RAY DIFFRACTIONr_angle_refined_deg0.8481.96768278
X-RAY DIFFRACTIONr_angle_other_deg0.6933.001110986
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.97756314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.96124.4192254
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.948158752
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.23815284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27686
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257266
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211332
X-RAY DIFFRACTIONr_mcbond_it3.1986.26825346
X-RAY DIFFRACTIONr_mcbond_other3.1976.26825345
X-RAY DIFFRACTIONr_mcangle_it4.2849.38531630
X-RAY DIFFRACTIONr_mcangle_other4.2849.38531631
X-RAY DIFFRACTIONr_scbond_it3.056.66125120
X-RAY DIFFRACTIONr_scbond_other3.056.66125120
X-RAY DIFFRACTIONr_scangle_other3.8629.83636648
X-RAY DIFFRACTIONr_long_range_B_refined4.90248.70253617
X-RAY DIFFRACTIONr_long_range_B_other4.89948.70753598
X-RAY DIFFRACTIONr_rigid_bond_restr1.656398672
X-RAY DIFFRACTIONr_sphericity_free29.8215198
X-RAY DIFFRACTIONr_sphericity_bonded20.151597824
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.338 854 -
Rwork0.297 16233 -
obs--99.44 %
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)
10.0101-0.01040.00710.0492-0.0250.0137-0.00680.0064-0.0225-0.01050.0036-0.0212-0.0016-0.00620.00320.116-0.0058-0.00860.0954-0.00560.120567.9414-91.787946.5041
20.0002-0.0001-0.00050.0074-0.00110.0013-0.00330.0017-0.0039-0.0192-0.00360.01290.0098-0.00310.00690.094-0.00970.0280.0990.00540.120560.744-87.611516.8765
30.00480.0032-0.00150.0051-0.00390.00510.00860.00260.0135-0.00750.00530.02330.01940.0055-0.01390.14790.0031-0.00440.0920.01280.122333.4072-86.88791.5248
40.0023-0.0013-0.00290.0046-00.00450.0078-0.0077-0.0047-0.0122-0.00520.0216-0.00710.0149-0.00260.10470.0135-0.01450.06420.00440.13224.0552-89.498914.1252
50.00270.00270.00220.00810.00330.0032-0.0093-0.00350.0013-0.0055-0.00030.0293-0.00980.0080.00960.06390.00320.02830.0963-0.00240.1465-2.2256-94.022446.0469
60.0009-0.0006-0.00030.00090.00090.0015-0.00390.0069-0.00740.0076-0.00410.00850.00830.00460.0080.12640.00330.03390.0867-0.00950.111316.1349-94.70470.3004
70.02440.0011-0.02530.0173-0.00440.05730.01080.01750.00720.0372-0.0165-0.01350.01420.01130.00580.13-0.00030.00860.0714-0.01430.098748.6339-93.119171.6573
80.00840.018-0.0020.065-0.00150.0030.01320.00430.00570.0495-0.0091-0.0385-0.0073-0.0141-0.00410.1022-0.0034-0.01590.0884-0.00650.120868.3903-129.337947.8283
90.0016-0.01220.00110.1058-0.01740.01070.00430.00130.0013-0.0237-0.0062-0.0291-0.0223-0.00790.00180.1073-0.00550.01960.0958-0.00110.123669.1344-127.250621.4116
100.0983-0.1929-0.15640.51340.50870.5670.0666-0.00440.0125-0.0422-0.034-0.01470.0489-0.0298-0.03250.1375-0.0011-0.00470.08170.00990.092245.6572-126.2204-0.0779
110.0082-0.0177-0.00190.04940.01150.00710.00030.0001-0.0178-0.00790.01360.0221-0.00810.0198-0.01390.1288-0.0067-0.02420.08260.00650.119911.9356-130.35732.9478
120.00530.0005-0.0010.00220.00090.0054-0.0055-0.01690.01690.00250.00420.0155-0.01730.0110.00130.08040.00470.00550.09320.00340.1459-3.4996-133.83428.9376
130.0088-0.02390.00070.15050.00670.00240.01170.00530.01980.0299-0.01850.00060.00510.01140.00680.1086-0.00190.02570.0952-0.00290.11658.8155-137.467760.6875
140.0306-0.0417-0.01120.06910.01740.00450.01190.0106-0.00150.0286-0.01290.0070.0036-0.00150.0010.1638-0.0059-0.0020.0945-0.00020.112540.6772-133.805771.0555
150.05220.0419-0.0110.0372-0.00830.0056-0.01550.01860-0.01540.00030.00850.0121-0.00220.01510.0856-0.0124-0.01780.08810.0120.13172.3951-206.194237.147
160.0231-0.00210.03330.006-0.00570.0495-0.00880.00230.0075-0.0164-0.0022-0.0133-0.00010.00680.0110.1093-0.004-0.0340.0836-0.00960.11968.864-205.07567.1161
170.0037-0.0036-0.00220.00450.00160.00440.01710.0013-0.0016-0.0212-0.0090.0106-0.01280.0134-0.00810.13050.0076-0.00730.0643-0.02250.08136.2425-203.2921-8.7731
180.0084-0.02610.01360.0987-0.05560.03230.0074-0.0010.0246-0.0594-0.0294-0.05960.03530.01920.0220.04540.03090.01520.0436-0.03050.090465.73-202.87773.7512
190.00370.0010.00080.0113-0.00140.00730.01260.00330.00440.0067-0.0051-0.02580.008-0.0041-0.00750.06330.0219-0.00860.0654-0.01630.115872.5817-203.946835.6662
200.01060.0051-0.00850.0045-0.00390.00750.02020.0055-0.00750.0176-0.0176-0.0152-0.0234-0.0095-0.00260.12460.0023-0.04220.06630.01290.115254.6359-207.468259.9907
210.00130.0008-0.00020.0026-0.00220.00330.00640.00870.00680.00470.00530.01620.00820.0044-0.01170.1479-0.0083-0.01760.07620.01250.117922.2392-209.445361.6217
220.00860.01890.01110.06250.02280.01750.0196-0.0029-0.00370.0326-0.00810.02940.030.0122-0.01150.1043-0.0020.00540.08630.00810.13192.1067-169.507344.983
230.00470.0217-0.00110.1203-0.010.0115-0-0.0050.0089-0.042-0.00060.04230.02710.01830.00060.114-0.0058-0.01930.07920.00430.13380.8754-166.936818.5851
240.0065-0.0012-0.00070.0033-0.00130.00140.0118-0.0121-0.0206-0.0123-0.0090.0132-0.00430.0092-0.00280.15240.0111-0.02290.0872-0.01120.110524.0066-164.1831-3.2404
250.03110.04090.00030.0887-0.01850.01550.00640.0013-0.0105-0.04250.0143-0.01640.0197-0.0138-0.02070.10560.00790.03010.0847-0.00780.095257.7761-160.6221-0.1431
260.00550.0218-0.00310.1141-0.02580.01370.0011-0.009-0.00740.00690.0017-0.00750.0203-0.0123-0.00280.09650.01120.00390.0869-0.00940.132773.6258-161.705425.7479
270.006-0.0064-0.00330.18210.00780.00370.00070.0119-0.02060.0222-0.0018-0.01670.0023-0.01670.00110.13130.0038-0.02440.08510.00490.120661.9133-163.66157.8577
280.00870.0040.00520.00330.00280.00520.02260.0033-0.00440.0192-0.0103-0.00290.0077-0.0082-0.01220.1561-0.0026-0.00340.09580.00460.113530.2399-169.126768.0745
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 307
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 308
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 305
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 305
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 302
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 311
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 413
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 414
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301 - 309
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201
23X-RAY DIFFRACTION10J301 - 309
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301
26X-RAY DIFFRACTION11K401 - 412
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 310
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 318
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 203
33X-RAY DIFFRACTION14N301 - 305
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 308
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 308
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 308
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 305
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 303
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 304
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 408
49X-RAY DIFFRACTION22V1 - 226
50X-RAY DIFFRACTION22V301
51X-RAY DIFFRACTION22V401 - 411
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 304
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 211
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 302
58X-RAY DIFFRACTION25Y401 - 408
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 414
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 325
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 202
66X-RAY DIFFRACTION28b301 - 308

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