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- PDB-4qwr: yCP beta5-C52F mutant in complex with carfilzomib -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qwr
TitleyCP beta5-C52F 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: 2.9 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 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)736,20948
Polymers731,13928
Non-polymers5,07020
Water4,918273
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)136.000, 300.580, 144.520
Angle α, β, γ (deg.)90.00, 113.17, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999625, -0.001817, 0.027332), (-0.002915, -0.985076, -0.172096), (0.027237, -0.172112, 0.984701)67.79079, -290.14981, -25.84808
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)
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 , 5 types, 293 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.: 273 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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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: 2.9→30 Å / Num. all: 235250 / Num. obs: 219488 / % possible obs: 93.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.079 / Net I/σ(I): 13.2
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.555 / Mean I/σ(I) obs: 2.1 / % possible all: 95.3

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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: 2.9→15 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.936 / SU B: 30.024 / SU ML: 0.238 / Cross valid method: THROUGHOUT / ESU R Free: 0.309 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20936 10975 5 %RANDOM
Rwork0.18061 ---
obs0.18204 208513 93.45 %-
all-219488 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 64.101 Å2
Baniso -1Baniso -2Baniso -3
1-3.33 Å20 Å2-1.49 Å2
2---5.83 Å20 Å2
3---2.3 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49306 0 348 273 49927
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950574
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248374
X-RAY DIFFRACTIONr_angle_refined_deg0.8651.9768434
X-RAY DIFFRACTIONr_angle_other_deg0.773.003111398
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.02756306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.90724.4042248
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.028158736
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.63315284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27704
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257234
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211350
X-RAY DIFFRACTIONr_mcbond_it2.5315.59425314
X-RAY DIFFRACTIONr_mcbond_other2.5315.59425313
X-RAY DIFFRACTIONr_mcangle_it3.48.37731590
X-RAY DIFFRACTIONr_mcangle_other3.48.37731591
X-RAY DIFFRACTIONr_scbond_it2.4875.97225260
X-RAY DIFFRACTIONr_scbond_other2.4875.97225260
X-RAY DIFFRACTIONr_scangle_other3.138.80936845
X-RAY DIFFRACTIONr_long_range_B_refined3.96543.64454079
X-RAY DIFFRACTIONr_long_range_B_other3.95443.64954052
X-RAY DIFFRACTIONr_rigid_bond_restr1.033398948
X-RAY DIFFRACTIONr_sphericity_free27.4215186
X-RAY DIFFRACTIONr_sphericity_bonded16.072598123
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.355 798 -
Rwork0.322 15154 -
obs--95.53 %
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)
10.00380.0013-0.00290.0020.00030.00350.00120.0155-0.0045-0.00570.0036-0.0102-0.0108-0.0105-0.00480.0926-0.0114-0.01010.0723-0.00460.086567.2709-92.527345.9127
20.00060.00150.00060.00530.00430.0052-0.0072-0.003-0.001-0.0144-0.00710.0074-0.0049-0.00160.01430.0815-0.0050.02070.08380.00340.064259.9936-88.308616.2953
30.0160.0132-0.00170.0131-0.00350.0050.0041-0.0086-0.0049-0.00920.00850.00190.0088-0.0017-0.01260.11770.0038-0.0070.07620.00590.083732.6953-87.73971.0219
40.00340.0036-0.0030.0054-0.00140.00450.0021-0.00830.0131-0.0083-0.00170.0212-0.00640.0141-0.00040.09090.0095-0.01880.06040.00620.09363.4068-90.438813.5923
50.0611-0.01020.0310.0059-0.00580.01670.0022-0.0036-0.0047-0.00220.00190.0198-0.00110.005-0.00420.05220.01480.01040.071-0.00250.0949-2.922-94.82945.5651
60.0011-0.00140.00040.0023-0.00030.00080.00130.007-0.0053-0.0039-0.00590.0075-0.00040.0070.00450.1026-0.00130.0240.0757-0.00870.05215.5215-95.426369.7292
70.01170.00430.00890.01740.01450.0276-0.00080.01590.00260.0174-0.01-0.00860.001-0.01180.01080.1038-0.00710.00330.052-0.01880.049648.007-93.834170.9767
80.00150.001-0.00210.0140.00220.00470.01090.00580.00160.0252-0.0068-0.0264-0.0055-0.0168-0.00410.0916-0.0008-0.01440.0750.00110.083667.6096-130.650347.8646
90.024-0.0156-0.0040.0872-0.02280.02410.0150.0072-0.0058-0.02-0.0183-0.0094-0.0275-0.00890.00330.0798-0.00240.01170.0820.00020.073368.675-127.912920.7788
100.0652-0.0442-0.00790.0386-0.00150.00660.0238-0.0050.0043-0.036-0.00570.01570.01250.0023-0.01810.1061-0.0010.00130.0818-0.0030.064845.0983-127.0262-0.7855
110.0220.04120.01410.08340.03170.0173-0.00570.00350.0083-0.01360.01550.0213-0.00130.0236-0.00980.09350.0054-0.020.06880.0040.082511.284-131.34982.7379
120.0016-0.00090.00020.0028-0.00150.00190.01090.0003-0.0028-0.0053-0.00580.01530.00140.0113-0.00520.08670.0042-0.00890.07740.0010.1053-4.1743-134.711628.5143
130.0026-0.00030.00250.0017-0.00140.0037-0.00210.00620.0123-0.0059-0.00970.00270.00790.00920.01190.0935-0.00380.00570.0767-0.00510.08058.0975-138.346860.2605
140.0081-0.0273-0.00280.20360.02010.00240.01940.01360.00180.0098-0.0161-0.0287-0.0003-0.0003-0.00320.1138-0.0048-0.01450.07-0.01020.057840.2699-134.68570.201
150.00350.00080.00040.0011-0.00050.00110.00040.01480.0067-0.00910.00570.00310.00670.0031-0.00610.0917-0.0133-0.01870.070.00540.09681.9017-207.023236.6384
160.0060.00340.00910.00270.00580.0146-0.00620.00550.008-0.00150.0012-0.0031-0.0030.00650.0050.10540.0005-0.02770.066-0.00480.09818.4196-205.97196.5703
170.012500.00650.0016-0.0020.01290.0121-0.0104-0.0235-0.01110.00460.005-0.00330.0152-0.01680.11380.0207-0.00990.0604-0.020.074435.6342-204.0515-9.1803
180.0064-0.01340.00940.0299-0.02160.01620.01330.00260.0115-0.0438-0.0167-0.01920.03380.01210.00330.07250.03180.00820.0316-0.02820.061465.1149-203.52773.2673
190.02320.0218-0.00890.0227-0.00570.01050.01060.0107-0.02220.020.0052-0.0341-0.0036-0.0127-0.01570.05760.0335-0.02110.0439-0.00570.106772.0967-204.670235.2521
200.00850.0028-0.00150.00220.00110.00490.0216-0.0029-0.01570.0072-0.0135-0.0126-0.009-0.0139-0.00810.10490.0013-0.04180.0460.01350.087654.1327-208.265759.4538
210.0061-0.0080.00780.014-0.01110.01090.00430.0086-0.00530.00380.00440.0126-0.00520.0095-0.00870.1131-0.0066-0.0180.05790.01030.076421.7206-210.236861.0124
220.0021-0.00150.00220.0081-0.0030.00460.0122-0.0005-0.00570.002-0.00710.02380.01070.012-0.00510.0876-0.0124-0.00350.06670.01010.08421.7317-169.869645.1485
230.03750.020.05110.02430.02470.07030.00690.00710.0028-0.0265-0.00380.01830.0150.0073-0.00310.0812-0.0038-0.01880.07460.00330.09880.1199-167.821617.9559
240.00350.0007-0.0020.00550.00170.00220.0063-0.0005-0.0154-0.0172-0.0063-0.0112-0.0149-0.002700.11190.0043-0.01910.0732-0.00430.082323.3075-164.9293-3.8685
250.01040.00220.00350.01150.00040.0015-0.00240.0022-0.0221-0.01310.0175-0.0117-0.002-0.0025-0.01510.0820.01030.01430.0776-0.01010.055257.1564-161.2906-0.3039
260.0208-0.0075-0.01760.01080.01450.02350.01130.0012-0.00820.0113-0.0042-0.01790.0086-0.0123-0.00720.07740.0112-0.00320.0825-0.00060.102173.1024-162.410425.3182
270.14510.01570.07430.0415-0.03840.1538-0.00430.0234-0.0327-0.0160.0023-0.0064-0.0147-0.03470.00190.08720.0087-0.02080.05120.00860.064861.4878-164.33457.4479
280.00550.0002-0.00310.0010.00080.00260.00910.0194-0.00090.0095-0.006-0.00340.0023-0.015-0.00310.1149-0.0019-0.0060.0886-0.00070.078529.5125-169.724967.2812
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 310
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 314
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 307
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 303
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 306
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 315
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 413
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 409
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 410
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 210
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 409
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 310
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 319
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 204
33X-RAY DIFFRACTION14N301 - 311
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 304
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 305
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 302
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 303
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 303
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 310
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 414
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 302
51X-RAY DIFFRACTION22V401 - 419
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 307
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 216
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 407
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 408
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 317
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 202
66X-RAY DIFFRACTION28b301 - 312

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