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- PDB-4nnw: yCP in complex with Z-Leu-Leu-Leu-ketoaldehyde -

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Basic information

Entry
Database: PDB / ID: 4nnw
TitleyCP in complex with Z-Leu-Leu-Leu-ketoaldehyde
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE Inhibitor / Proteasome / Peptide Electrophile / Binding Analysis / Reversible Inhibitor / Ketoaldehyde / HYDROLASE-HYDROLASE Inhibitor complex
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / Ub-specific processing proteases / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / Neutrophil degranulation / proteasome complex / peroxisome / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / 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 alpha5 / Proteasome subunit alpha6 / 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 alpha5 / Proteasome subunit alpha6 / 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 B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
PHQ-Leu-Leu-Leu-ketoaldehyde, bound form / Chem-2MK / 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 ...PHQ-Leu-Leu-Leu-ketoaldehyde, bound form / Chem-2MK / 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 S288c (yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsStein, M.L. / Cui, H. / Beck, P. / Dubiella, C. / Voss, C. / Krueger, A. / Schmidt, B. / Groll, M.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Systematic Comparison of Peptidic Proteasome Inhibitors Highlights the alpha-Ketoamide Electrophile as an Auspicious Reversible Lead Motif.
Authors: Stein, M.L. / Cui, H. / Beck, P. / Dubiella, C. / Voss, C. / Kruger, A. / Schmidt, B. / Groll, M.
History
DepositionNov 19, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 12, 2014Provider: repository / Type: Initial release
Revision 1.1Feb 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_conn_type / 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.conn_type_id / _struct_conn.id / _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_conn_type.id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Mar 13, 2024Group: Source and taxonomy / Category: entity_src_nat
Revision 1.4Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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)734,29142
Polymers731,05128
Non-polymers3,24014
Water11,620645
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119380 Å2
ΔGint-420 kcal/mol
Surface area214360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.640, 301.290, 145.120
Angle α, β, γ (deg.)90.00, 113.71, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.99998, -0.000132, 0.00637), (-0.0009, -0.986834, -0.161733), (0.006307, -0.161736, 0.986814)68.43185, -290.89206, -23.67491

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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 / Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / ...Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / Proteinase YSCE subunit 7


Mass: 27191.828 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P23639
#2: Protein Proteasome subunit alpha type-3 / Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 ...Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 / Proteinase YSCE subunit 13


Mass: 28748.230 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P23638
#3: Protein Proteasome subunit alpha type-4 / Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component ...Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component PRE6 / Proteinase YSCE subunit PRE6


Mass: 28478.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P40303
#4: Protein Proteasome subunit alpha type-5 / Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component ...Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component PUP2 / Proteinase YSCE subunit PUP2


Mass: 28649.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P32379
#5: Protein Proteasome subunit alpha type-6 / Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component ...Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component PRE5 / Proteinase YSCE subunit PRE5


Mass: 25634.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P40302
#7: Protein Proteasome subunit alpha type-1 / Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7- ...Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7-alpha / Proteasome component Y8 / Proteinase YSCE subunit 7 / SCL1 suppressor protein


Mass: 28033.830 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P21243

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Protein , 1 types, 2 molecules FT

#6: Protein Probable proteasome subunit alpha type-7 / Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / ...Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / Proteinase YSCE subunit 1


Mass: 31575.068 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P21242

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Proteasome subunit beta type- ... , 7 types, 14 molecules HVIWJXKYLZMaNb

#8: Protein Proteasome subunit beta type-2 / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component ...Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


Mass: 25114.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P25043
#9: Protein Proteasome subunit beta type-3 / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit PUP3 / Proteasome component PUP3


Mass: 22627.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P25451
#10: Protein Proteasome subunit beta type-4 / Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 ...Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 / Proteinase YSCE subunit 11


Mass: 22545.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P22141
#11: Protein Proteasome subunit beta type-5 / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component ...Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component PRE2 / Proteinase YSCE subunit PRE2


Mass: 23325.248 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P30656
#12: Protein Proteasome subunit beta type-6 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P23724
#13: Protein Proteasome subunit beta type-7 / Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component ...Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component PRE4 / Proteinase YSCE subunit PRE4


Mass: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P30657
#14: Protein Proteasome subunit beta type-1 / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component ...Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component PRE3 / Proteinase YSCE subunit PRE3


Mass: 21517.186 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288c (yeast) / Strain: ATCC 204508 / S288c / References: UniProt: P38624

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Non-polymers , 3 types, 659 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-2MK / N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2R,3S)-1,2-dihydroxy-5-methylhexan-3-yl]-L-leucinamide / PHQ-Leu-Leu-Leu-ketoaldehyde, bound form


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 507.663 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C27H45N3O6 / References: PHQ-Leu-Leu-Leu-ketoaldehyde, bound form
#17: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 645 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 3.74 Å3/Da / Density % sol: 67.12 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 mM MgAc2, 100 mM MES, 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 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Apr 11, 2011
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: 2.6→30 Å / Num. all: 328337 / Num. obs: 323084 / % possible obs: 98.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Rmerge(I) obs: 0.077 / Net I/σ(I): 0.119
Reflection shellResolution: 2.6→2.7 Å / Rmerge(I) obs: 0.477 / Mean I/σ(I) obs: 2.9 / % possible all: 88.1

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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: 2.6→15 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.943 / SU B: 19.075 / SU ML: 0.175 / Cross valid method: THROUGHOUT / ESU R Free: 0.224 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20844 16155 5 %RANDOM
Rwork0.1953 ---
all0.1975 323083 --
obs0.19596 306928 98.95 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 49.408 Å2
Baniso -1Baniso -2Baniso -3
1-3.38 Å20 Å2-1.3 Å2
2---5.98 Å2-0 Å2
3---2.29 Å2
Refinement stepCycle: LAST / Resolution: 2.6→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49296 0 218 645 50159
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950424
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248236
X-RAY DIFFRACTIONr_angle_refined_deg1.1991.96868224
X-RAY DIFFRACTIONr_angle_other_deg0.7893.002111060
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.56256306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.87624.4082246
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.869158736
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8215284
X-RAY DIFFRACTIONr_chiral_restr0.0690.27694
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257148
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211304
X-RAY DIFFRACTIONr_rigid_bond_restr1.162398498
X-RAY DIFFRACTIONr_sphericity_free30.2695302
X-RAY DIFFRACTIONr_sphericity_bonded4.177597939
LS refinement shellResolution: 2.604→2.67 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.352 1045 -
Rwork0.319 19853 -
obs--89.38 %
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)
10.0955-0.0542-0.00630.1386-0.050.0547-0.00180.01440.0035-0.00560.0038-0.0627-0.0275-0.0072-0.0020.0521-0.02190.03430.0763-0.02210.0867.2928-92.495245.9036
20.0572-0.02580.06640.09380.02960.1488-0.00590.0025-0.007-0.0619-0.0119-0.014-0.03460.02760.01780.0994-0.01320.05910.08640.0220.067360.2791-88.54416.1298
30.080.06730.06760.06450.05950.0957-0.03550.0170.0249-0.03830.03710.0281-0.01170.0292-0.00170.1198-0.00490.00760.07670.03190.050433.0454-87.89490.5081
40.08590.0359-0.04510.07990.06860.1535-0.0146-0.0240.0336-0.0404-0.01520.0713-0.0361-0.00420.02980.06670.0365-0.03650.05350.02810.12993.5867-90.444712.8942
50.0569-0.00250.12360.01830.0240.3755-0.0221-0.0187-0.01050.00780.00280.0507-0.0568-0.03460.01930.02420.02610.03350.0611-0.00020.1681-3.0417-94.558944.9657
60.1340.11720.05990.1120.04860.02870.0157-0.02950.02440.0432-0.01810.0405-0.0066-0.01890.00240.10930.01310.07820.0924-0.0220.06715.2862-95.168269.3298
70.03730.0842-0.00040.2003-0.00660.00720.0157-0.0039-0.00940.0535-0.019-0.0204-0.0167-0.010.00330.1199-0.01140.03150.0755-0.02720.030447.7534-93.633770.8723
80.00790.0114-0.00090.13180.06380.07290.02030.0059-0.00080.0231-0.0071-0.0824-0.00710.0011-0.01330.0538-0.01380.00760.0989-0.0070.092967.5574-130.709348.2756
90.09110.03560.01520.29730.00060.0280.01770.0171-0.0152-0.0443-0.0168-0.0917-0.0179-0.0127-0.00090.064-0.00450.05590.0966-0.0070.08568.679-128.314120.9365
100.19790.0256-0.04270.2124-0.04490.0173-0.0042-0.00610.0097-0.10960.0120.0090.01480.0009-0.00780.13340.0040.04370.09080.00980.030845.3182-127.3309-0.919
110.0303-0.0523-0.00660.40150.02930.00450.0112-0.0203-0.0002-0.0811-0.01240.1019-0.0135-0.00810.00110.08390.0104-0.04060.08230.02270.067311.3561-131.44771.9917
120.0177-0.02370.0180.21760.06070.06720.0028-0.0001-0.0245-0.02360.00480.1066-0.01760.0002-0.00770.01250.01050.00010.0810.02340.1444-4.3324-134.667428.0008
130.0491-0.05350.03920.2144-0.01060.0426-0.003-0.014-0.00210.0435-0.00470.06550.00320.00350.00770.0506-0.00120.0660.08980.00250.08727.7293-138.186559.9537
140.08230.0039-0.03310.17640.0090.01540.01340.00390.01550.0693-0.0045-0.0135-0.00120.0098-0.00890.1087-0.00840.0230.1005-0.0150.014539.7865-134.518270.4513
150.0443-0.0617-0.02490.14420.0950.1803-0.00330.0139-0.0035-0.00850.00960.0620.0341-0.0177-0.00620.0349-0.043-0.02430.06190.02640.12591.3999-207.032536.5651
160.0610.058-0.0250.0616-0.02090.0223-0.0432-0.00040.0091-0.05610.01480.0167-0-0.00850.02850.0765-0.0127-0.05540.068-0.02530.08458.2135-206.03556.6105
170.16830.00620.03850.1731-0.08040.09470.04850.0182-0.0357-0.12240.01730.06090.05240.0389-0.06580.17850.0058-0.03930.0571-0.03010.055935.6477-204.3447-9.0534
180.0374-0.03390.05360.108-0.04510.10230.0152-0.01790.0186-0.1078-0.0261-0.06270.03080.00580.01090.14190.04740.0820.0838-0.02020.082765.095-203.86633.5619
190.0413-0.0305-0.00720.06190.02860.20690.00760.0021-0.007-0.00810.0076-0.0640.03760.0409-0.01530.03030.04090.0130.0674-0.00720.130371.7787-204.980935.8794
200.16680.0884-0.08080.15-0.05810.04280.0152-0.023-0.03570.028-0.0358-0.0726-0.01110.00560.02060.08560.005-0.0280.0660.04110.065353.4363-208.354559.9643
210.0401-0.0503-0.03210.1206-0.00020.0748-0.00420.0001-0.00940.02080.01420.0608-0.00710.0239-0.01010.0942-0.01590.01370.06280.03730.060221.0199-210.3261.213
220.0329-0.00250.0190.1314-0.01440.01330.02250.0054-0.0090.0359-0.00970.11420.00950.0098-0.01280.0341-0.01680.02330.08290.02090.11531.2203-169.836545.1327
230.0427-0.004-0.01260.2541-0.02960.04760.0061-0.00350.01-0.06870.0150.08590.0370.0062-0.02110.0474-0.0123-0.04450.07330.00810.10870.0505-167.661917.702
240.07790.00590.00310.10740.06990.06650.0039-0.0047-0.0187-0.08560.00160.0228-0.02020.0093-0.00550.13280.0028-0.0510.0678-0.0130.032523.4096-165.0687-4.0491
250.10280.08770.01250.4860.0070.00590.01910.0066-0.0075-0.0859-0.0051-0.0543-0.00540.017-0.0140.10820.01790.06750.0974-0.01570.055557.3438-161.5199-0.5066
260.0290.0135-0.0460.291-0.02820.07780.00470.01280.0152-0.00990.007-0.09510.0043-0.0064-0.01180.02730.01670.03810.1061-0.01210.098373.0629-162.628425.6613
270.07920.002-0.01460.27660.05670.02230.0036-0.0201-0.02190.0416-0.0074-0.0672-0.003-0.00520.00380.05620.0056-0.01020.08780.00550.057161.0775-164.38757.7568
280.0605-0.10430.02720.36630.00060.02980.00590.004-0.01880.07590.01310.0440.0147-0.0082-0.0190.1033-0.00990.03890.10260.02160.038729.0485-169.692667.6096
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION2B1 - 244
3X-RAY DIFFRACTION3C1 - 240
4X-RAY DIFFRACTION4D1 - 242
5X-RAY DIFFRACTION5E3 - 233
6X-RAY DIFFRACTION6F2 - 244
7X-RAY DIFFRACTION7G2 - 242
8X-RAY DIFFRACTION8H2 - 222
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K2 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 233
14X-RAY DIFFRACTION14N2 - 196
15X-RAY DIFFRACTION15O1 - 250
16X-RAY DIFFRACTION16P1 - 244
17X-RAY DIFFRACTION17Q1 - 240
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S3 - 233
20X-RAY DIFFRACTION20T2 - 244
21X-RAY DIFFRACTION21U2 - 242
22X-RAY DIFFRACTION22V2 - 222
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y2 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b2 - 196

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