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- PDB-4r02: yCP in complex with BSc4999 (alpha-Keto Phenylamide) -

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Basic information

Entry
Database: PDB / ID: 4r02
TitleyCP in complex with BSc4999 (alpha-Keto Phenylamide)
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / Drug Development / Binding Analysis / Reversible Covalent Ligand / 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 / threonine-type endopeptidase activity / Ub-specific processing proteases / Neutrophil degranulation / proteasome complex / 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
N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-{(2S,3S)-1-[(2,4-DIMETHYLPHENYL)AMINO]-2-HYDROXY-5-METHYL-1-OXOHEXAN-3-YL}-L-LEUCINAMIDE / Chem-3E5 / 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 ...N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-{(2S,3S)-1-[(2,4-DIMETHYLPHENYL)AMINO]-2-HYDROXY-5-METHYL-1-OXOHEXAN-3-YL}-L-LEUCINAMIDE / Chem-3E5 / 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: 2.5 Å
AuthorsVoss, C. / Scholz, C. / Knorr, S. / Beck, P. / Stein, M. / Zall, A. / Kuckelkorn, U. / Kloetzel, P.-M. / Groll, M. / Hamacher, K. / Schmidt, B.
CitationJournal: Chemmedchem / Year: 2014
Title: alpha-Keto Phenylamides as P1'-Extended Proteasome Inhibitors.
Authors: Voss, C. / Scholz, C. / Knorr, S. / Beck, P. / Stein, M.L. / Zall, A. / Kuckelkorn, U. / Kloetzel, P.M. / Groll, M. / Hamacher, K. / Schmidt, B.
History
DepositionJul 29, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 13, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 19, 2014Group: 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)732,56841
Polymers731,05128
Non-polymers1,51713
Water48,7492706
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119360 Å2
ΔGint-459 kcal/mol
Surface area216790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)137.240, 300.870, 146.290
Angle α, β, γ (deg.)90.00, 113.20, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999691, -2.5E-5, 0.024844), (-0.004283, -0.984853, -0.173337), (0.024472, -0.17339, 0.984549)68.81651, -289.50333, -25.80285
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: A49S / 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) / Strain (production host): 4932
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-7


Mass: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-1


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 , 3 types, 2719 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-3E5 / N-[(benzyloxy)carbonyl]-L-leucyl-N-{(2S,3S)-1-[(2,4-dimethylphenyl)amino]-2-hydroxy-5-methyl-1-oxohexan-3-yl}-L-leucinamide


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 624.811 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C35H52N4O6
References: N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-{(2S,3S)-1-[(2,4-DIMETHYLPHENYL)AMINO]-2-HYDROXY-5-METHYL-1-OXOHEXAN-3-YL}-L-LEUCINAMIDE
#17: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2706 / 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: Sep 22, 2012
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: 2.5→30 Å / Num. all: 374723 / Num. obs: 363107 / % possible obs: 96.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.074 / Net I/σ(I): 10.9
Reflection shellResolution: 2.5→2.6 Å / Rmerge(I) obs: 0.558 / Mean I/σ(I) obs: 2 / % possible all: 99.1

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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: 2.5→15 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.945 / SU B: 15.532 / SU ML: 0.152 / Cross valid method: THROUGHOUT / ESU R Free: 0.207 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20686 18156 5 %RANDOM
Rwork0.17016 ---
all0.176 363107 --
obs0.17199 344951 96.97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 52.966 Å2
Baniso -1Baniso -2Baniso -3
1-2.67 Å20 Å2-0.55 Å2
2---3.36 Å2-0 Å2
3---0.67 Å2
Refinement stepCycle: LAST / Resolution: 2.5→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49366 0 101 2706 52173
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950366
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248156
X-RAY DIFFRACTIONr_angle_refined_deg0.9681.96568134
X-RAY DIFFRACTIONr_angle_other_deg0.7073110882
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.75356314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.69724.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.493158758
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.91215284
X-RAY DIFFRACTIONr_chiral_restr0.0580.27676
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257196
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211302
X-RAY DIFFRACTIONr_rigid_bond_restr1.434398522
X-RAY DIFFRACTIONr_sphericity_free24.9235905
X-RAY DIFFRACTIONr_sphericity_bonded11.785599435
LS refinement shellResolution: 2.5→2.563 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.305 1338 -
Rwork0.271 25413 -
obs--99.31 %
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)
10.1401-0.03870.03590.10720.00750.082-0.0060.00930.01390.00620.0013-0.0374-0.01730.01110.00470.0273-0.01170.00840.0098-0.00720.044467.607-92.19646.564
20.10020.0004-0.01760.11850.02910.1124-0.00250.01170.0146-0.0434-0.0017-0.0231-0.03020.02670.00430.0318-0.01170.01780.01470.00480.039960.357-87.88816.786
30.12670.07780.05270.12610.05790.1491-0.01390.01970.0101-0.07340.02270.0008-0.04760.0186-0.00890.0688-0.00410.00520.01170.00840.045732.986-87.2941.353
40.05720.0219-0.03850.1302-0.00420.0941-0.00570.00670.0249-0.02280.00440.0711-0.0367-0.01190.00130.04390.0156-0.01410.01370.01710.07553.617-89.93313.868
50.09430.03460.06850.0868-0.02330.222-0.0089-0.01470.02110.01470.00750.0751-0.0376-0.04190.00140.02070.01990.00990.02150.00010.0764-2.708-94.2146.045
60.1260.00510.00290.14160.06090.10640.0095-0.0230.01750.0429-0.01780.0339-0.0103-0.02280.00820.0380.00710.0220.0165-0.00890.042115.71-95.0570.352
70.04630.00290.02770.13480.03710.1317-0.0017-0.00770.00590.0456-0.0104-0.0193-0.01180.00210.0120.0539-0.00540.00370.0069-0.00840.034948.262-93.66371.683
80.03520.01240.0110.08090.0050.00530.0040.00450.00660.02240.0002-0.0452-0.00270.0058-0.00430.0231-0.00540.00040.0139-0.01190.048268.391-129.77247.962
90.1529-0.04230.0140.19980.01380.06290.00320.0230.0007-0.0197-0.0037-0.047-0.02460.02580.00050.0181-0.00820.01660.0202-0.00160.040468.963-127.58821.303
100.08970.0880.00950.29530.00270.1251-0.00070.01830.0204-0.06620.0032-0.0026-0.00440.0132-0.00250.0440.00090.01070.00820.00390.025645.358-126.656-0.367
110.09150.0979-0.08480.3062-0.07150.0810.00270.01270.0198-0.05980.00710.0808-0.0107-0.0127-0.00980.03090.0098-0.02010.01090.01060.053311.432-130.7922.512
120.0388-0.04610.02980.19730.05290.11280.0099-0.0028-0.0125-0.0136-0.00270.0681-0.0111-0.0182-0.00720.01880.0084-0.00120.020.01360.0745-4.133-134.33228.797
130.0399-0.02160.02290.249-0.01120.0409-0.0049-0.02450.00090.04390.0050.04820.0042-0.0233-00.01920.00110.02020.01920.00350.04698.138-137.97760.713
140.0456-0.0075-0.04540.25540.02990.17140.0105-0.0190.00350.0546-0.0006-0.004-0.00170.0069-0.010.0368-0.00480.00120.0109-0.00690.026940.266-134.28371.277
150.1959-0.0848-0.06280.13420.04630.0926-0.01240.0235-0.01650.0107-0.00210.0460.0314-0.02140.01450.0332-0.0184-0.00860.01290.00570.05942.136-206.86437.018
160.09760.08010.03540.12940.01440.068-0.00780.00880.0066-0.0322-0.00690.02870.0186-0.01540.01470.0429-0.0091-0.01770.0153-0.01030.04178.629-205.7766.803
170.08930.0404-0.00170.1722-0.06260.13550.00520.0362-0.03-0.10240.00970.04920.0546-0.0009-0.01490.10250.0021-0.01910.0158-0.0190.055736.052-203.898-9.067
180.0136-0.03420.01380.23120.00940.11860.00360.005-0.002-0.0687-0.0152-0.05270.02510.02380.01150.04970.01930.0220.0155-0.0090.060665.547-203.3863.323
190.1719-0.0083-0.08310.1721-0.00770.1602-0.00190.0024-0.03120.00970.0179-0.08220.04110.0353-0.0160.02750.0236-0.00150.0211-0.00930.076472.506-204.74335.55
200.14740.04-0.02260.0698-0.05810.10610.0122-0.0398-0.03070.0223-0.0065-0.03190.03040.0132-0.00570.05760.014-0.02240.01850.01260.059654.496-208.27659.848
210.01310.0004-0.03220.1236-0.02560.0848-0.007-0.0025-0.00210.0242-0.00040.01320.00910.00770.00740.0469-0.0021-0.00490.00360.01160.043121.971-210.1161.465
220.0503-0.0173-0.02970.10730.01240.03790.00470.0001-0.00620.02090.00250.06470.0191-0.0151-0.00720.0272-0.0152-0.00030.01130.01150.05651.512-170.20945.003
230.172-0.00210.0160.15060.02870.07050.01310.02420.0028-0.0274-0.01070.05180.0298-0.0298-0.00230.0244-0.0121-0.01780.01850.00250.04860.432-167.62118.333
240.06750.04240.04830.1675-0.01870.08190.00310.0174-0.0152-0.05810.00730.01410.0063-0.0014-0.01040.04750.0055-0.01420.0164-0.00250.03323.655-164.687-3.583
250.15980.14870.08110.2738-0.01020.1135-0.00570.0293-0.0234-0.06830.0217-0.04950.02460.024-0.0160.0450.00940.02550.0196-0.01190.03857.649-161.12-0.563
260.0266-0.0324-0.02170.2278-0.03650.07090.01140.00030.0083-0.01170.0005-0.05950.00770.0187-0.01190.02230.01170.00820.0246-0.01430.062773.673-162.22325.632
270.0333-0.0008-0.00660.28430.03970.0467-0.0005-0.0148-0.0120.0432-0.0015-0.04370.00770.01520.0020.02530.0053-0.01080.01440.0020.041761.986-164.28357.896
280.04010.01770.06320.30550.00260.1960.0106-0.0171-0.01020.04990.00220.0170.0138-0.0034-0.01280.035-0.00330.00630.01450.01010.032730.079-169.84768.253
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 421
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 384
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 388
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 382
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 344
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 393
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301
15X-RAY DIFFRACTION7G401 - 517
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301 - 410
18X-RAY DIFFRACTION9I1 - 204
19X-RAY DIFFRACTION9I301 - 302
20X-RAY DIFFRACTION9I401 - 506
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201
23X-RAY DIFFRACTION10J301 - 401
24X-RAY DIFFRACTION11K1 - 212
25X-RAY DIFFRACTION11K301 - 303
26X-RAY DIFFRACTION11K401 - 519
27X-RAY DIFFRACTION12L1 - 222
28X-RAY DIFFRACTION12L301 - 418
29X-RAY DIFFRACTION13M1 - 233
30X-RAY DIFFRACTION13M301 - 441
31X-RAY DIFFRACTION14N1 - 196
32X-RAY DIFFRACTION14N201 - 202
33X-RAY DIFFRACTION14N301 - 408
34X-RAY DIFFRACTION15O1 - 250
35X-RAY DIFFRACTION15O301 - 379
36X-RAY DIFFRACTION16P1 - 244
37X-RAY DIFFRACTION16P301 - 373
38X-RAY DIFFRACTION17Q1 - 240
39X-RAY DIFFRACTION17Q301 - 361
40X-RAY DIFFRACTION18R1 - 242
41X-RAY DIFFRACTION18R301 - 374
42X-RAY DIFFRACTION19S3 - 233
43X-RAY DIFFRACTION19S301 - 338
44X-RAY DIFFRACTION20T2 - 244
45X-RAY DIFFRACTION20T301 - 382
46X-RAY DIFFRACTION21U2 - 242
47X-RAY DIFFRACTION21U301 - 409
48X-RAY DIFFRACTION22V1 - 226
49X-RAY DIFFRACTION22V301
50X-RAY DIFFRACTION22V401 - 489
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 404
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201 - 292
55X-RAY DIFFRACTION25Y1 - 212
56X-RAY DIFFRACTION25Y301 - 302
57X-RAY DIFFRACTION25Y401 - 514
58X-RAY DIFFRACTION26Z1 - 222
59X-RAY DIFFRACTION26Z301
60X-RAY DIFFRACTION26Z401 - 526
61X-RAY DIFFRACTION27a1 - 233
62X-RAY DIFFRACTION27a301 - 437
63X-RAY DIFFRACTION28b1 - 196
64X-RAY DIFFRACTION28b201 - 296

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