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- PDB-3un4: Yeast 20S proteasome in complex with PR-957 (morpholine) -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 3un4
TitleYeast 20S proteasome in complex with PR-957 (morpholine)
Components(Proteasome component ...) x 14
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Proteasome / antigen presentation / drug development / protein degradation / HYDROLASE -HYDROLASE-INHIBITOR complex / 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
1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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 ...1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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: 3.4 Å
AuthorsHuber, E. / Basler, M. / Schwab, R. / Heinemeyer, W. / Kirk, C. / Groettrup, M. / Groll, M.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2012
Title: Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity.
Authors: Huber, E.M. / Basler, M. / Schwab, R. / Heinemeyer, W. / Kirk, C.J. / Groettrup, M. / Groll, M.
History
DepositionNov 15, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 29, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2012Group: Database references
Revision 1.2Dec 12, 2012Group: Other
Revision 1.3Sep 13, 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_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_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 component Y7
B: Proteasome component Y13
C: Proteasome component PRE6
D: Proteasome component PUP2
E: Proteasome component PRE5
F: Proteasome component C1
G: Proteasome component C7-alpha
H: Proteasome component PUP1
I: Proteasome component PUP3
J: Proteasome component C11
K: Proteasome component PRE2
L: Proteasome component C5
M: Proteasome component PRE4
N: Proteasome component PRE3
O: Proteasome component Y7
P: Proteasome component Y13
Q: Proteasome component PRE6
R: Proteasome component PUP2
S: Proteasome component PRE5
T: Proteasome component C1
U: Proteasome component C7-alpha
V: Proteasome component PUP1
W: Proteasome component PUP3
X: Proteasome component C11
Y: Proteasome component PRE2
Z: Proteasome component C5
a: Proteasome component PRE4
b: Proteasome component PRE3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)732,04834
Polymers728,54028
Non-polymers3,5086
Water23,8161322
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)134.410, 300.780, 143.820
Angle α, β, γ (deg.)90.00, 112.75, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.99967, -0.003009, 0.025512), (-0.001333, -0.985702, -0.168494), (0.025654, -0.168472, 0.985373)67.17863, -290.05682, -25.3405

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Components

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Proteasome component ... , 14 types, 28 molecules AOBPCQDRESFTGUHVIWJXKYLZMaNb

#1: Protein Proteasome component Y7 / / Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit 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 component Y13 / / Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit 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 component PRE6 / / Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit 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 component PUP2 / / Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit 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 component PRE5 / / Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit 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
#6: Protein Proteasome component C1 / / Macropain subunit C1 / Multicatalytic endopeptidase complex subunit 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
#7: Protein Proteasome component C7-alpha / / Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component Y8 / ...Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / 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
#8: Protein Proteasome component PUP1 / / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit 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 component PUP3 / / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit 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 component C11 / / Macropain subunit C11 / Multicatalytic endopeptidase complex subunit 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 component PRE2 / / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit 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 component C5 / / Multicatalytic endopeptidase complex subunit 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 component PRE4 / / Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit 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 component PRE3 / / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit 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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Non-polymers , 2 types, 1328 molecules

#15: Chemical
ChemComp-04C / 1,2,4-trideoxy-4-methyl-2-{[N-(morpholin-4-ylacetyl)-L-alanyl-O-methyl-L-tyrosyl]amino}-1-phenyl-D-xylitol


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 584.704 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C31H44N4O7
References: 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL, proteasome endopeptidase complex
#16: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1322 / Source method: isolated from a natural source / Formula: H2O / References: proteasome endopeptidase complex

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Details

Sequence detailsTHE STARTING EPOXIDE RING OF AN EPOXOMICIN-LIKE INHIBITOR UNDERGOES RE-CYCLIZATION REACTION WITH ...THE STARTING EPOXIDE RING OF AN EPOXOMICIN-LIKE INHIBITOR UNDERGOES RE-CYCLIZATION REACTION WITH THE SIDE CHAIN OF N-TERMINAL RESIDUE THR-1 (CHAINS b,N,K,V,Y and H) AND THE FINAL PRODUCT 04C IS OBSERVED. SEE ALSO LINK RECORDS AND REMARK 630.

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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: 3.68 Å3/Da / Density % sol: 66.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 100 mM MES, 12% MPD, 20 mM MgAc2, 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: Feb 2, 2011
RadiationMonochromator: Double-crystal fixed-exit monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.4→30 Å / Num. all: 144376 / Num. obs: 141633 / % possible obs: 98.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.143 / Net I/σ(I): 8.2

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Processing

Software
NameClassification
XDSdata scaling
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1RYP

1ryp


Resolution: 3.4→15 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.918 / SU B: 53.346 / SU ML: 0.352 / Cross valid method: THROUGHOUT / ESU R Free: 0.471 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.21948 7082 5 %RANDOM
Rwork0.17885 ---
obs0.18086 134550 98.29 %-
all-141632 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK PARAMETER FOR MASK CALCULATION
Displacement parametersBiso mean: 80.525 Å2
Baniso -1Baniso -2Baniso -3
1-3.86 Å20 Å2-2.13 Å2
2---8.88 Å20 Å2
3---3.38 Å2
Refinement stepCycle: LAST / Resolution: 3.4→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49538 0 252 1322 51112
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.0250726
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.8991.96568638
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.26856334
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.69124.4082264
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.737158774
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.82615288
X-RAY DIFFRACTIONr_chiral_restr0.0590.27750
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02137954
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr1.302350726
X-RAY DIFFRACTIONr_sphericity_free40.5335430
X-RAY DIFFRACTIONr_sphericity_bonded10.839550692
LS refinement shellResolution: 3.4→3.484 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.331 491 -
Rwork0.296 9347 -
obs--98.41 %
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)
10.7315-0.19680.30611.1553-0.20050.1621-0.08040.00030.03590.08260.0198-0.2578-0.0759-0.04570.06060.2325-0.0557-0.01390.1926-0.060.265466.872-92.39245.556
20.8375-0.0343-0.07680.5782-0.24940.4594-0.18760.02540.0865-0.0839-0.0339-0.1413-0.12430.09050.22150.3104-0.06670.03960.19460.08940.245159.395-88.31616.099
30.27140.2443-0.31380.5677-0.31650.40320.0137-0.04610.042-0.1896-0.0280.1016-0.04170.05660.01430.31580.0147-0.02190.18840.08040.226632.135-87.8010.611
40.4178-0.0593-0.21960.3810.1140.1389-0.0793-0.07740.0574-0.09050.08110.3075-0.01920.0546-0.00180.23020.0936-0.05810.13530.12490.40163.563-90.92614.015
50.22980.11620.04270.7226-0.4250.3702-0.0108-0.03240.10760.10820.03690.3219-0.07480.0071-0.02610.17420.0890.16030.15060.0150.5153-2.778-94.38845.251
60.5083-0.33220.16810.4325-0.1480.06690.0090.0331-0.00740.2548-0.02050.0982-0.0498-0.01090.01140.50330.02420.2380.1384-0.06690.177115.538-95.06469.283
70.3572-0.0959-0.20190.61450.05980.12970.00350.0556-0.00750.3758-0.0385-0.1108-0.0444-0.03670.0350.5237-0.0375-0.06580.1418-0.05260.127147.694-93.41670.565
80.0586-0.1414-0.15680.72190.42210.49850.06080.05240.02520.2156-0.0623-0.346-0.0659-0.07260.00140.2809-0.0376-0.16640.16340.00040.342267.434-130.19748.18
90.28420.04290.12511.13770.10230.22450.0099-0.0684-0.04790.06-0.0415-0.3547-0.047-0.0610.03160.0967-0.03390.07740.23540.01020.352568.213-128.00620.738
100.39130.020.34270.9712-0.30580.4141-0.0046-0.00130.0608-0.2849-0.0412-0.04710.06310.02620.04580.24180.00660.13930.24220.01660.115844.777-127.131-1.119
110.58950.30810.0391.33510.48430.5773-0.0582-0.01930.134-0.29780.07180.4641-0.06960.0771-0.01360.17830.0338-0.13240.19470.06260.269810.909-131.4211.94
120.1206-0.16170.11420.49660.01130.360.1005-0.0085-0.0551-0.1350.00620.2636-0.0322-0.0051-0.10670.11110.04020.07110.20130.05090.4333-4.221-134.69128.366
130.851-0.01140.4080.4797-0.02520.23090.18440.02990.04140.3142-0.12740.14520.0261-0.0028-0.0570.3201-0.01820.20930.18010.01640.20847.783-137.98260.092
140.6051-0.4323-0.18631.7133-0.15580.28130.0660.03920.09550.418-0.02440.00790.03530.1034-0.04170.424-0.01920.06070.2238-0.0450.036939.638-134.21770.586
150.7371-0.1151-0.45670.82560.12930.3434-0.03680.0461-0.04610.09910.04740.23570.1168-0.0132-0.01050.2753-0.0943-0.12270.11810.09870.36991.862-206.75536.55
160.43090.46820.36440.61110.26670.78480.04490.05520.0074-0.05410.00170.12430.08010-0.04660.25140.0091-0.15320.1579-0.06380.30488.541-205.7556.671
170.0908-0.029-0.08010.6140.02750.30890.1365-0.0255-0.0808-0.348-0.02870.17470.02750.1666-0.10780.51110.0521-0.22160.1029-0.12120.320535.808-203.79-9.322
180.9082-0.23050.26210.7941-0.02360.08920.1119-0.1103-0.0261-0.2592-0.0985-0.330.0454-0.0654-0.01340.37470.12740.16240.1978-0.05640.305264.537-202.8754.109
191.17020.7111-0.11010.7090.2360.35110.20910.1898-0.28620.24960.0675-0.48870.1023-0.0815-0.27660.17330.1033-0.23350.137-0.08560.661371.482-204.5835.136
200.4140.2146-0.17010.14840.04410.56120.2667-0.0415-0.28460.2109-0.0808-0.23310.0876-0.1503-0.18590.4891-0.0144-0.37980.1020.11390.406853.694-208.01159.229
210.2913-0.2758-0.01370.5132-0.00340.4121-0.03180.0509-0.03530.25210.08570.03990.04520.0076-0.05390.4291-0.0333-0.11230.1440.09930.23621.618-210.05960.829
220.01270.0802-0.01081.2638-0.40490.47750.05480.0062-0.01520.2956-0.02140.27140.1129-0.0173-0.03340.1938-0.03750.06650.20310.07780.33171.405-169.92245.48
230.28170.02330.05731.245-0.50060.35550.0195-0.0781-0.0634-0.12560.01290.34790.04050.0497-0.03240.1065-0.0228-0.09240.18010.02010.3990.091-167.50718.003
240.14090.2752-0.02421.0140.15220.1153-0.05270.0269-0.049-0.25730.04650.0501-0.01640.02730.00620.30350.0279-0.11630.2199-0.02630.164523.09-164.691-4.146
250.91810.6216-0.04481.7792-0.37470.26280.15230.0992-0.1003-0.2634-0.0562-0.21850.01380.0437-0.09610.2060.07030.13430.2565-0.06210.220757.025-160.919-0.983
260.2570.0525-0.32831.17050.04790.52230.09890.0531-0.02470.0448-0.1192-0.3471-0.028-0.04670.02020.10080.07370.03910.2261-0.02030.387372.681-162.07725.327
270.7494-0.05680.18710.9277-0.30270.25220.07860.064-0.06980.351-0.0503-0.12480.01030.0126-0.02830.26930.0041-0.17080.15920.00970.222961.317-164.12857.338
280.23010.00850.05351.45570.15610.05210.11780.036-0.06810.3161-0.048-0.00810.0561-0.0612-0.06980.429-0.0310.0210.2080.08690.092129.689-169.66867.701
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A251 - 1318
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B258 - 1295
5X-RAY DIFFRACTION3C1 - 241
6X-RAY DIFFRACTION3C253 - 1308
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D253 - 1314
9X-RAY DIFFRACTION5E1 - 233
10X-RAY DIFFRACTION5E234 - 1281
11X-RAY DIFFRACTION6F1 - 244
12X-RAY DIFFRACTION6F285 - 1321
13X-RAY DIFFRACTION7G1 - 243
14X-RAY DIFFRACTION7G244 - 1273
15X-RAY DIFFRACTION8H1 - 222
16X-RAY DIFFRACTION8H233
17X-RAY DIFFRACTION8H234 - 1288
18X-RAY DIFFRACTION9I1 - 204
19X-RAY DIFFRACTION9I205 - 1322
20X-RAY DIFFRACTION10J1 - 198
21X-RAY DIFFRACTION10J199 - 1315
22X-RAY DIFFRACTION11K1 - 212
23X-RAY DIFFRACTION11K213
24X-RAY DIFFRACTION11K214 - 1313
25X-RAY DIFFRACTION12L1 - 222
26X-RAY DIFFRACTION12L223 - 1302
27X-RAY DIFFRACTION13M1 - 233
28X-RAY DIFFRACTION13M234 - 1312
29X-RAY DIFFRACTION14N1 - 196
30X-RAY DIFFRACTION14N197
31X-RAY DIFFRACTION14N198 - 1211
32X-RAY DIFFRACTION15O1 - 250
33X-RAY DIFFRACTION15O251 - 1267
34X-RAY DIFFRACTION16P1 - 244
35X-RAY DIFFRACTION16P258 - 1317
36X-RAY DIFFRACTION17Q1 - 241
37X-RAY DIFFRACTION17Q253 - 1304
38X-RAY DIFFRACTION18R1 - 242
39X-RAY DIFFRACTION18R268 - 1282
40X-RAY DIFFRACTION19S1 - 233
41X-RAY DIFFRACTION19S234 - 1299
42X-RAY DIFFRACTION20T1 - 244
43X-RAY DIFFRACTION20T285 - 1320
44X-RAY DIFFRACTION21U1 - 243
45X-RAY DIFFRACTION21U244 - 1310
46X-RAY DIFFRACTION22V1 - 222
47X-RAY DIFFRACTION22V233
48X-RAY DIFFRACTION22V234 - 1307
49X-RAY DIFFRACTION23W1 - 204
50X-RAY DIFFRACTION23W205 - 1316
51X-RAY DIFFRACTION24X1 - 198
52X-RAY DIFFRACTION24X199 - 1245
53X-RAY DIFFRACTION25Y1 - 212
54X-RAY DIFFRACTION25Y213
55X-RAY DIFFRACTION25Y214 - 1301
56X-RAY DIFFRACTION26Z1 - 222
57X-RAY DIFFRACTION26Z223 - 1291
58X-RAY DIFFRACTION27a1 - 233
59X-RAY DIFFRACTION27a234 - 1287
60X-RAY DIFFRACTION28b1 - 196
61X-RAY DIFFRACTION28b197
62X-RAY DIFFRACTION28b198 - 1232

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