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- PDB-4jsq: Yeast 20S proteasome in complex with the dimerized linear mimetic... -

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Basic information

Entry
Database: PDB / ID: 4jsq
TitleYeast 20S proteasome in complex with the dimerized linear mimetic of TMC-95A - yCP:4e
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
  • TMC-95A mimic ligand yCP:4e
KeywordsHYDROLASE/HYDROLASE INHIBITOR / UPS / proteasome / drug discovery / non-covalent reversible inhibition / bivalence / TMC-95A derivatives / Ntn hydrolase / non-lysosomal protein breakdown / 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
TMC-95A mimic ligand yCP:4e / 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 ...TMC-95A mimic ligand yCP:4e / 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
AuthorsDesvergne, A. / Genin, E. / Marechal, X. / Gallastegui, N. / Dufau, L. / Richy, N. / Groll, M. / Vidal, J. / Reboud-Ravaux, M.
CitationJournal: J.Med.Chem. / Year: 2013
Title: Dimerized linear mimics of a natural cyclopeptide (TMC-95A) are potent noncovalent inhibitors of the eukaryotic 20S proteasome
Authors: Desvergne, A. / Genin, E. / Marechal, X. / Gallastegui, N. / Dufau, L. / Richy, N. / Groll, M. / Vidal, J. / Reboud-Ravaux, M.
History
DepositionMar 22, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 1, 2013Provider: repository / Type: Initial release
Revision 1.1Apr 23, 2014Group: Database references
Revision 1.2Nov 8, 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 / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / struct_conn
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2 / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_label_atom_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
c: TMC-95A mimic ligand yCP:4e
d: TMC-95A mimic ligand yCP:4e
hetero molecules


Theoretical massNumber of molelcules
Total (without water)731,13532
Polymers730,74530
Non-polymers3902
Water24,0861337
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.770, 300.220, 144.260
Angle α, β, γ (deg.)90.00, 112.86, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21O
12B
22P
13C
23Q
14D
24R
15E
25S
16F
26T
17G
27U
18H
28V
19I
29W
110J
210X
111K
211Y
112L
212Z
113M
213a
114N
214b
115c
215d

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999509, -0.002162, 0.031246), (-0.002996, -0.986441, -0.164088), (0.031177, -0.164101, 0.985951)67.91755, -290.25024, -24.70621

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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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23638, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40303, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P32379, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40302, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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

#8: Protein Proteasome subunit beta type-2 / PSMB2 / 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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / PSMB3 / 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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25451, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-4 / PSMB4 / 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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P22141, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-5 / PSMB5 / 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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P30656, proteasome endopeptidase complex
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#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: 25945.496 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 / 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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P38624, proteasome endopeptidase complex

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Protein / Protein/peptide , 2 types, 4 molecules FTcd

#15: Protein/peptide TMC-95A mimic ligand yCP:4e


Type: Peptide-like / Class: Inhibitor / Mass: 1102.367 Da / Num. of mol.: 2 / Source method: obtained synthetically / References: TMC-95A mimic ligand yCP:4e
#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 (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21242, proteasome endopeptidase complex

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Non-polymers , 2 types, 1339 molecules

#16: 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
#17: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1337 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsTHE COMPLETE DIMERIC INHIBITOR COMPOSED OF CHAINS c AND d, LINKED BY HEXANEDIOIC ACID AT THE N- ...THE COMPLETE DIMERIC INHIBITOR COMPOSED OF CHAINS c AND d, LINKED BY HEXANEDIOIC ACID AT THE N-TERMINAL. HOWEVER, THE LINKER REGION WAS FLEXIBLE AND WAS NOT MODELED IN THIS STRUCTURE.

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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: 3.71 Å3/Da / Density % sol: 66.82 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 20mM MgAc2, 0.1M MES, 12% MPD, pH 7.0, 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: Oct 6, 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: 2.8→20 Å / Num. all: 260574 / Num. obs: 257968 / % possible obs: 99 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 16.9
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.581 / Mean I/σ(I) obs: 2.9 / % possible all: 98.8

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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: 0.932 / Cor.coef. Fo:Fc free: 0.928 / SU B: 30.003 / SU ML: 0.288 / Cross valid method: THROUGHOUT / ESU R: 0.75 / ESU R Free: 0.315 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.24136 12899 5 %RANDOM
Rwork0.23544 ---
all0.237 245069 --
obs0.23573 245069 99.09 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 73.961 Å2
Baniso -1Baniso -2Baniso -3
1-3.35 Å20 Å2-3.24 Å2
2---9.44 Å20 Å2
3---3.57 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49650 0 24 1337 51011
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.0250594
X-RAY DIFFRACTIONr_angle_refined_deg0.8231.96668442
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.08356340
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.37224.4082264
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.454158780
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.90715288
X-RAY DIFFRACTIONr_chiral_restr0.0510.27690
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02138074
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeWeight positionRms dev position (Å)
1A1585TIGHT POSITIONAL0.05
1A1644TIGHT POSITIONAL0.05
1A1757TIGHT POSITIONAL0.05
1A1824TIGHT POSITIONAL0.05
1A1512TIGHT POSITIONAL0.05
1A1915TIGHT THERMAL0.52.65
2B1905TIGHT THERMAL0.53.08
3C1891TIGHT THERMAL0.55.96
4D1862TIGHT THERMAL0.51.18
5E1795TIGHT THERMAL0.53.17
6F1897TIGHT THERMAL0.53.85
7G1921TIGHT THERMAL0.51.46
8H1685TIGHT THERMAL0.50.99
9I1581TIGHT THERMAL0.52.97
10J1585TIGHT THERMAL0.53.5
11K1644TIGHT THERMAL0.52
12L1757TIGHT THERMAL0.51.1
13M1824TIGHT THERMAL0.51.27
14N1512TIGHT THERMAL0.50.7
15c68MEDIUM POSITIONAL0.50.51
15c68MEDIUM THERMAL20.72
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.379 916 -
Rwork0.385 17370 -
obs--98.93 %
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)
11.1135-0.41560.27091.1755-0.15450.4331-0.02390.0364-0.02020.11990.008-0.2721-0.1475-0.02780.01590.2174-0.07760.03560.2399-0.04730.269967.6704-92.537745.5848
21.1220.1292-0.14151.0288-0.11190.9647-0.1353-0.08530.0023-0.2213-0.0585-0.1415-0.16980.17710.19380.2781-0.07750.1270.30340.09330.208860.1283-88.433216.0816
30.4855-0.0177-0.24991.1969-0.0921.0394-0.06790.0280.1748-0.28090.03810.0214-0.14690.13170.02980.3473-0.0150.050.2630.09940.158332.6969-87.7280.5604
41.07930.3492-0.19271.08670.21250.4144-0.0645-0.08160.1143-0.13880.02540.3082-0.10230.05440.03910.18830.1071-0.08120.17780.11370.37714.0988-90.703814.0146
50.98690.42110.36160.6360.00111.2963-0.0497-0.05130.10160.03950.04730.3358-0.2279-0.11570.00240.13970.1080.15110.2618-0.00340.4863-2.1974-94.048145.3375
61.26990.29140.10690.576-0.31280.8079-0.0131-0.11850.07890.2489-0.0320.1644-0.1515-0.08610.04510.42650.05720.24790.296-0.08420.207816.2295-94.765669.3996
70.62630.04120.06230.7846-0.08870.8790.00370.0030.03260.2727-0.0462-0.1542-0.1358-0.03380.04250.4374-0.0438-0.01310.1941-0.08270.117648.5097-93.494270.6996
80.0751-0.1328-0.08770.51290.20520.170.06380.07850.08360.0982-0.0038-0.3798-0.0626-0.0017-0.060.2296-0.0436-0.07250.3159-0.02010.395667.9612-130.392948.236
90.3277-0.0124-0.13471.78430.06970.63690.03440.05010.0174-0.0442-0.0773-0.4277-0.0651-0.00880.04280.1241-0.01120.17330.34240.02550.353168.7519-128.17620.7343
101.1362-0.30330.58142.53170.14440.47150.0427-0.02660.0567-0.4015-0.02810.02210.01310.0638-0.01470.36630.01930.1430.32160.01620.098545.1892-127.1922-1.1406
110.94460.69410.10091.54460.71760.6674-0.00860.06210.0616-0.35080.06220.3007-0.06910.032-0.05360.23720.0477-0.1830.24630.05940.268711.2422-131.25841.9953
120.27260.06020.12141.24270.29350.51650.1196-0.06750.0049-0.0779-0.03370.4337-0.04870.0175-0.08590.08190.03450.03050.30610.07540.4616-3.9455-134.403428.515
130.6381-0.23290.09251.4906-0.17480.10510.0549-0.04690.06610.3527-0.020.2362-0.0358-0.0402-0.03480.2363-0.00630.23350.35280.01560.24698.1662-137.711160.3148
141.3327-0.3531-0.18441.1742-0.25150.2580.0127-0.05090.06420.34110.0016-0.1316-0.0575-0.0628-0.01430.4335-0.03850.03230.3159-0.02260.045140.1893-134.220170.7039
151.0165-0.2614-0.40181.1290.34230.69740.05070.00670.00040.0270.00610.29120.1811-0.0248-0.05680.1216-0.0935-0.09970.18030.09810.44081.8635-206.564536.8527
160.61970.31360.2440.9720.00591.2231-0.0886-0.0365-0.0019-0.16320.02910.11270.0116-0.1310.05950.2596-0.0135-0.19570.1673-0.08710.28438.4536-205.63656.8575
170.62280.12730.35641.1079-0.47711.36530.1506-0.0402-0.1391-0.6115-0.01720.29450.25150.0636-0.13340.64060.0531-0.21070.1028-0.10150.300235.8278-203.9208-9.2402
181.21720.21770.69731.4379-0.03460.41860.1924-0.1436-0.0147-0.4788-0.2324-0.25540.1597-0.04230.03990.42680.14830.26910.2382-0.03540.336764.6712-203.13164.1615
191.16980.3545-0.09680.8561-0.390.76510.18890.1629-0.2257-0.011-0.0359-0.44270.14710.0748-0.1530.10690.1202-0.09370.185-0.08520.63371.7376-204.857335.2106
200.97840.19110.11450.48430.11070.90370.2092-0.1478-0.26950.1823-0.1043-0.31380.0951-0.0753-0.10490.3371-0.0043-0.29060.13070.1290.386853.9295-208.225859.3733
210.4554-0.1141-0.20870.956-0.03240.7961-0.00080.0098-0.12420.20310.03870.14270.02160.0465-0.03790.3319-0.0363-0.09750.15470.10480.25321.7314-209.986961.1376
220.1034-0.17740.09490.5558-0.26620.14890.0707-0.0498-0.1092-0.00530.05760.39750.0410.0173-0.12830.1146-0.02590.08990.37090.08520.40971.7153-169.70345.7146
230.5705-0.16290.22441.3759-0.30890.83240.0441-0.0406-0.0244-0.09250.04020.38040.08290.0139-0.08430.0922-0.014-0.13140.22650.01070.39270.2439-167.321918.1632
240.9379-0.1718-0.17491.982-0.08870.44550.0090.0198-0.0944-0.32210.02760.0607-0.04260.0423-0.03660.38940.0259-0.11070.2274-0.04250.073923.2914-164.6357-4.0688
250.91260.65370.05712.4701-0.68750.3610.09670.0447-0.0436-0.4891-0.0266-0.24960.11090.0993-0.07020.34410.07390.24080.3436-0.05320.259457.325-161.1103-0.9456
260.2121-0.0669-0.1911.3147-0.26270.81930.09030.06590.0277-0.0116-0.1073-0.44620.02510.02580.01710.10410.05880.11650.3324-0.01130.462873.1185-162.348825.3744
270.4084-0.09130.02791.34970.16210.2178-0.01380.0289-0.08450.3079-0.0203-0.28160.027-0.04130.03410.2639-0.0169-0.14930.25540.02490.252561.8075-164.34657.4879
281.18760.10050.23771.63380.23650.37710.1104-0.0349-0.08870.3458-0.03540.05130.0691-0.0405-0.07490.3587-0.03970.07550.31030.070.057230.0566-169.588667.8922
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION2B1 - 244
3X-RAY DIFFRACTION3C1 - 241
4X-RAY DIFFRACTION4D1 - 242
5X-RAY DIFFRACTION5E1 - 233
6X-RAY DIFFRACTION6F1 - 244
7X-RAY DIFFRACTION7G1 - 243
8X-RAY DIFFRACTION8H1 - 222
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 198
11X-RAY DIFFRACTION11K1 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 233
14X-RAY DIFFRACTION14N1 - 196
15X-RAY DIFFRACTION15O1 - 250
16X-RAY DIFFRACTION16P1 - 244
17X-RAY DIFFRACTION17Q1 - 241
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S1 - 233
20X-RAY DIFFRACTION20T1 - 244
21X-RAY DIFFRACTION21U1 - 243
22X-RAY DIFFRACTION22V1 - 222
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 198
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b1 - 196

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