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- PDB-4qw4: yCP in complex with carfilzomib -

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Basic information

Entry
Database: PDB / ID: 4qw4
TitleyCP 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 / 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
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: 2.8 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 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_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_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)736,48749
Polymers731,05128
Non-polymers5,43721
Water5,981332
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.810, 298.690, 145.700
Angle α, β, γ (deg.)90.00, 112.69, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999399, -0.005494, 0.034225), (-0.000664, -0.984144, -0.17737), (0.034657, -0.177286, 0.983549)66.97149, -287.10895, -26.15088
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: M45A / 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: 23325.248 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 , 5 types, 353 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


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


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


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 332 / 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: Mar 16, 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: 262363 / Num. obs: 254230 / % possible obs: 96.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 10.4
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.544 / Mean I/σ(I) obs: 2.3 / % possible all: 98

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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: 0.949 / Cor.coef. Fo:Fc free: 0.931 / SU B: 25.622 / SU ML: 0.215 / Cross valid method: THROUGHOUT / ESU R Free: 0.283 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21636 12712 5 %RANDOM
Rwork0.18716 ---
all0.191 254230 --
obs0.18861 241518 97.04 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.124 Å2
Baniso -1Baniso -2Baniso -3
1-1.91 Å20 Å2-0.67 Å2
2---4.49 Å2-0 Å2
3---2.11 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49295 0 371 332 49998
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950585
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248390
X-RAY DIFFRACTIONr_angle_refined_deg0.8651.97168448
X-RAY DIFFRACTIONr_angle_other_deg0.7623.003111444
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.02856306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.03624.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.084158736
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.40315284
X-RAY DIFFRACTIONr_chiral_restr0.0490.27708
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257216
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211340
X-RAY DIFFRACTIONr_mcbond_it2.424.92825313
X-RAY DIFFRACTIONr_mcbond_other2.424.92825312
X-RAY DIFFRACTIONr_mcangle_it3.2577.37831588
X-RAY DIFFRACTIONr_mcangle_other3.2577.37831589
X-RAY DIFFRACTIONr_scbond_it2.3455.30925272
X-RAY DIFFRACTIONr_scbond_other2.3455.30925272
X-RAY DIFFRACTIONr_scangle_other2.9897.81236861
X-RAY DIFFRACTIONr_long_range_B_refined3.77438.49753995
X-RAY DIFFRACTIONr_long_range_B_other3.76938.49653969
X-RAY DIFFRACTIONr_rigid_bond_restr0.936398975
X-RAY DIFFRACTIONr_sphericity_free25.3275212
X-RAY DIFFRACTIONr_sphericity_bonded16.017598184
LS refinement shellResolution: 2.8→2.872 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.354 944 -
Rwork0.312 17931 -
obs--98.06 %
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)
10.0019-0.0027-0.00010.0074-0.00080.0010.00330.0054-0.00620.0072-0.0038-0.0087-0.009-0.00480.00050.1687-0.0055-0.01880.0722-0.00790.144567.6619-91.530446.6096
20.05340.0175-0.01760.006-0.00560.0075-0.00810.00220.00960.0002-0.00150.0054-0.0059-0.00340.00960.178-0.0066-0.00550.07130.0070.138260.2429-87.145216.9611
30.01590.00880.00160.00640.00150.0035-0.00560.00380.0122-0.00140.01330.0140.01690.0074-0.00770.18010.0003-0.01660.07330.01310.132432.9317-86.43661.6678
40.0074-0.00270.00580.0053-0.00270.0077-0.0124-0.00650.007-0.00460.00340.02140.00050.00690.0090.15950.0043-0.02910.06870.01350.15813.6506-89.042614.2509
50.0002-0.0005-0.00010.0013-0.00030.0013-0.0013-0.0024-0.00510.00490.00230.0141-0.00880.007-0.0010.15670.0094-0.00420.07270.00360.176-2.605-93.341846.4047
60.00810.00410.00140.00250.00040.0010.0053-0.00250.00430.0064-0.00690.00110.00810.00560.00160.19240.00320.00540.0717-0.00650.132315.909-94.260170.618
70.0060-0.01060.0005-0.0010.02470.00670.010.00030.005-0.0065-0.0054-0.0083-0.0041-0.00020.2004-0.0061-0.01720.0658-0.01090.123248.4352-92.891771.8498
80.00050.0015-0.00010.0090.00010.00190.0078-0.0026-0.00130.0243-0.0062-0.0293-0.0079-0.0096-0.00160.1613-0.0057-0.0240.0686-0.0050.137867.8257-129.591548.4066
90.0246-0.0045-0.0110.0648-0.0120.01210.0006-0.0067-0.003-0.0104-0.0092-0.0155-0.0109-0.00910.00860.1667-0.005-0.00520.07330.00340.142568.776-126.797221.2184
100.0065-0.00220.00050.0567-0.03390.02120.0011-0.01460.0196-0.0217-0.002-0.00190.00110.00490.00090.1864-0.0032-0.00750.07280.00430.121745.1203-125.6381-0.2089
110.00450.0124-0.00660.1238-0.01090.01070.0119-0.00720.011-0.0171-0.00020.023-0.020.0162-0.01170.16280.0044-0.03650.07020.01370.132111.2104-129.78323.2111
120.00770.01050.00910.01620.01360.01780.0042-0.00160.00620.00140.00550.0197-0.00930.0109-0.00980.15030.0042-0.02190.07370.01190.1623-4.1699-133.110429.2291
130.0180.0061-0.03880.003-0.01360.110.0053-0.00080.0062-0.0070.00050.00990.0150.0415-0.00590.15670.0071-0.00420.06930.00130.13198.231-136.960661.0061
140.0234-0.0004-0.01570.122-0.00340.01330.01580.012-0.00660.0268-0.0067-0.0062-0.0028-0.0006-0.00910.1933-0.0062-0.01840.0794-0.00370.118140.5043-133.566770.8692
150.0116-0.0109-0.00710.01620.01020.0076-0.00410.016-0.0049-0.00440.00130.01160.01120.00160.00280.1594-0.0079-0.02890.07120.01360.15431.7027-205.379736.8968
160.01180.0050.00640.00380.00150.0055-0.0045-0.0121-0.0076-0.0166-0.0022-0.00770.0025-0.00150.00670.1697-0.0047-0.03880.0672-0.00430.14128.1446-204.06436.7195
170.00190.0006-0.00160.0019-00.00240.0015-0.01-0.0002-0.01760.0010.0072-0.0080.0093-0.00250.19940.0081-0.02260.0543-0.00620.122835.2553-202.1734-9.1728
180.0071-0.0030.01030.0078-0.01230.03030.003-0.01320.0039-0.0189-0.0176-0.01580.0119-0.00610.01460.1650.00990.00240.0543-0.00940.131664.8436-201.81443.0605
190.00060.0003-0.00060.0008-0.00030.00360.00660.0017-0.00330.00280.0007-0.0115-0.0069-0.0144-0.00730.14640.0033-0.01970.0677-0.00280.177371.9731-203.321235.1226
200.01150.0108-0.01260.0192-0.01110.0140.01550.0065-0.01070.0037-0.0172-0.0058-0.0252-0.00970.00180.1662-0.0053-0.03350.06340.01150.146854.0955-206.879659.5062
210.0029-0.0003-0.00550.0017-0.00490.04340.00350.0104-0.00710.0032-0.00030.0117-0.004-0.0041-0.00320.1738-0.0034-0.02560.06690.01450.137521.6932-208.716861.2737
220.0010.00110.00030.0067-0.00140.00270.0118-0.0024-0.00390.0187-0.00230.02290.0060.0107-0.00950.1592-0.0049-0.01820.06860.01380.14821.6532-168.320845.689
230.0054-0.00560.01060.0107-0.01410.02580.003-0.00680.001-0.01730.00520.02410.00750.0017-0.00820.1616-0.0038-0.03950.07190.00410.15950.0143-166.019918.4475
240.0014-0.0014-0.00060.02180.00740.00520.0023-0.0095-0.0032-0.03610.00670.0050.00410.008-0.0090.1859-0.0023-0.02990.0722-0.00280.128123.1024-163.1598-3.4878
250.00340.00590.0030.09060.00090.00280.0124-0.0115-0.0069-0.0179-0.0089-0.01410.0115-0.0116-0.00350.17420.0058-0.00070.0775-0.00840.131257.1149-159.6654-0.1925
260.01350.014-0.02290.0167-0.02140.05070.0083-0.0052-0.00660.0131-0.0065-0.02480.0089-0.0114-0.00190.14680.0064-0.01020.0755-0.00390.153573.1348-161.126325.5764
270.22670.00280.04330.0192-0.00920.044-0.0072-0.0030.00010.0074-0.0151-0.0084-0.0544-0.02120.02220.1552-0.0048-0.02950.0690.01210.125161.5933-163.214657.8319
280.0051-0.00610.00050.08370.02440.01080.00930.0153-0.00860.0185-0.00710.0126-0.00930.0048-0.00210.1853-0.0053-0.01060.07570.01130.124529.6001-168.460867.7562
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 309
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 313
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 306
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 307
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 307
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 309
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 418
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301 - 302
18X-RAY DIFFRACTION8H401 - 413
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 414
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201 - 216
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 419
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 311
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 314
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 203
33X-RAY DIFFRACTION14N301 - 307
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 305
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 309
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 309
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 307
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 306
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 310
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301
48X-RAY DIFFRACTION21U401 - 416
49X-RAY DIFFRACTION22V1 - 222
50X-RAY DIFFRACTION22V301 - 303
51X-RAY DIFFRACTION22V401 - 410
52X-RAY DIFFRACTION23W1 - 204
53X-RAY DIFFRACTION23W301 - 312
54X-RAY DIFFRACTION24X1 - 195
55X-RAY DIFFRACTION24X201 - 216
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 303
58X-RAY DIFFRACTION25Y401 - 417
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 416
62X-RAY DIFFRACTION27a1 - 233
63X-RAY DIFFRACTION27a301 - 318
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201 - 202
66X-RAY DIFFRACTION28b301 - 318

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