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- PDB-4hrc: Crystal structure of yeast 20S proteasome in complex with epoxyke... -

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Basic information

Entry
Database: PDB / ID: 4hrc
TitleCrystal structure of yeast 20S proteasome in complex with epoxyketone carmaphycin analogue 3
Components(Proteasome component ...) x 14
KeywordsHYDROLASE/HYDROLASE INHIBITOR / proteasome / inhibitor / carmaphycin / epoxyketone / vinylketone / 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 / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / endopeptidase activator activity / Ub-specific processing proteases / 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
N-HEXANOYL-L-VALYL-N~1~-[(2R,3S,4S)-1,3-DIHYDROXY-2,6-DIMETHYLHEPTAN-4-YL]-N~5~,N~5~-DIMETHYL-L-GLUTAMAMIDE / Chem-OV2 / 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-HEXANOYL-L-VALYL-N~1~-[(2R,3S,4S)-1,3-DIHYDROXY-2,6-DIMETHYLHEPTAN-4-YL]-N~5~,N~5~-DIMETHYL-L-GLUTAMAMIDE / Chem-OV2 / 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
AuthorsTrivella, D.B.B. / Stein, M. / Groll, M.
CitationJournal: Chem.Biol. / Year: 2014
Title: Enzyme inhibition by hydroamination: design and mechanism of a hybrid carmaphycin-syringolin enone proteasome inhibitor.
Authors: Trivella, D.B. / Pereira, A.R. / Stein, M.L. / Kasai, Y. / Byrum, T. / Valeriote, F.A. / Tantillo, D.J. / Groll, M. / Gerwick, W.H. / Moore, B.S.
History
DepositionOct 27, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 29, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 2, 2014Group: Database references
Revision 1.2Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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_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)707,11634
Polymers703,94428
Non-polymers3,1726
Water7,476415
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area120190 Å2
ΔGint-371 kcal/mol
Surface area217770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.350, 300.880, 144.250
Angle α, β, γ (deg.)90.000, 112.740, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21O
12J
22X
13K
23Y
14L
24Z
15M
25a
16N
26b
17B
27P
18C
28Q
19D
29R
110E
210S
111F
211T
112G
212U
113H
213V
114I
214W

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 250
2114O1 - 250
1124J1 - 198
2124X1 - 198
1134K1 - 222
2134Y1 - 222
1144L1 - 222
2144Z1 - 222
1154M1 - 233
2154a1 - 233
1164N1 - 196
2164b1 - 196
1174B1 - 244
2174P1 - 244
1184C1 - 241
2184Q1 - 241
1194D1 - 242
2194R1 - 242
11104E1 - 233
21104S1 - 233
11114F1 - 244
21114T1 - 244
11124G1 - 243
21124U1 - 243
11134H1 - 222
21134V1 - 222
11144I1 - 204
21144W1 - 204

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

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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: 27060.631 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: 27050.416 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: 26903.330 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: 26544.789 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: 25502.805 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: 26892.482 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: 27316.037 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: 23987.254 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: 22496.645 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, 421 molecules

#15: Chemical
ChemComp-OV2 / N-hexanoyl-L-valyl-N~1~-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-N~5~,N~5~-dimethyl-L-glutamamide / Carmaphycin A analogue, bound from


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 528.725 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C27H52N4O6 / Details: epoxyketone carmaphycin analogue 3, bound form
References: N-HEXANOYL-L-VALYL-N~1~-[(2R,3S,4S)-1,3-DIHYDROXY-2,6-DIMETHYLHEPTAN-4-YL]-N~5~,N~5~-DIMETHYL-L-GLUTAMAMIDE
#16: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 415 / 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: 3.85 Å3/Da / Density % sol: 68.04 %
Crystal growTemperature: 297 K / Method: vapor diffusion / pH: 7.5
Details: 30 mM of magnesium acetate, 100 mM of MES (pH 7.2) and 12% of MPD, vapor diffusion, temperature 297K

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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: Jun 2, 2012
RadiationMonochromator: Double Multilayer Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.7→48 Å / Num. obs: 284264 / % possible obs: 97.8 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 63.57 Å2 / Rmerge(I) obs: 0.078 / Net I/σ(I): 9.33
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.7-2.80.5411.76881842921197.5
2.8-2.90.4062.26741782531097.4
2.9-30.3162.91674872224298
3-3.50.1565.472335327662398
3.5-40.08210.671317654323898.2
4-50.05616.111274854268897.8
5-60.05318.52587121890997.9
6-100.04520.97604212041497.8
10-200.04223.3714404497497.5
20-400.04425.26193661895.8
400.05223.11963735.9

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
REFMACrefinement
PDB_EXTRACT3.11data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→48 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.928 / WRfactor Rfree: 0.2399 / WRfactor Rwork: 0.2059 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.7701 / SU B: 40.327 / SU ML: 0.327 / SU R Cruickshank DPI: 0.6608 / SU Rfree: 0.3175 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.661 / ESU R Free: 0.318 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2434 12670 5 %RANDOM
Rwork0.2102 ---
obs0.2119 255047 98.01 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 246.06 Å2 / Biso mean: 75.556 Å2 / Biso min: 20 Å2
Baniso -1Baniso -2Baniso -3
1-3.27 Å20 Å2-3.44 Å2
2---9.28 Å20 Å2
3---3.35 Å2
Refinement stepCycle: LAST / Resolution: 2.8→48 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49522 0 222 415 50159
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.02250657
X-RAY DIFFRACTIONr_angle_refined_deg0.9991.96868544
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.19156333
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.58224.4062263
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.474158770
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.57515288
X-RAY DIFFRACTIONr_chiral_restr0.0650.27719
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02138068
X-RAY DIFFRACTIONr_mcbond_it0.1771.531473
X-RAY DIFFRACTIONr_mcangle_it0.339250633
X-RAY DIFFRACTIONr_scbond_it0.462319184
X-RAY DIFFRACTIONr_scangle_it0.8254.517911
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1907MEDIUM POSITIONAL0.180.5
1A1907MEDIUM THERMAL0.122
2J1585MEDIUM POSITIONAL0.150.5
2J1585MEDIUM THERMAL0.242
3K1681MEDIUM POSITIONAL0.170.5
3K1681MEDIUM THERMAL0.212
4L1757MEDIUM POSITIONAL0.180.5
4L1757MEDIUM THERMAL0.232
5M1824MEDIUM POSITIONAL0.150.5
5M1824MEDIUM THERMAL0.242
6N1549MEDIUM POSITIONAL0.210.5
6N1549MEDIUM THERMAL0.142
7B1904MEDIUM POSITIONAL0.230.5
7B1904MEDIUM THERMAL0.212
8C1890MEDIUM POSITIONAL0.240.5
8C1890MEDIUM THERMAL0.152
9D1861MEDIUM POSITIONAL0.250.5
9D1861MEDIUM THERMAL0.152
10E1787MEDIUM POSITIONAL0.250.5
10E1787MEDIUM THERMAL0.182
11F1896MEDIUM POSITIONAL0.20.5
11F1896MEDIUM THERMAL0.192
12G1921MEDIUM POSITIONAL0.180.5
12G1921MEDIUM THERMAL0.122
13H1721MEDIUM POSITIONAL0.20.5
13H1721MEDIUM THERMAL0.262
14I1581MEDIUM POSITIONAL0.160.5
14I1581MEDIUM THERMAL0.242
LS refinement shellResolution: 2.8→2.872 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.343 890 -
Rwork0.353 17807 -
all-18697 -
obs--97.19 %
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)
12.5387-0.48960.68542.5203-0.05791.2872-0.0581-0.13190.10250.45950.0411-0.6314-0.18230.1870.0170.4046-0.1093-0.01960.3443-0.04010.420367.4648-92.858645.7297
22.5635-0.4345-0.67963.990.13181.6525-0.3019-0.19710.1796-0.38720.0137-0.63-0.56650.55210.28810.4735-0.14330.0460.49740.12790.394359.8459-88.81416.1957
31.22130.12030.15853.8853-0.41552.6152-0.11410.35630.4098-0.77430.0722-0.072-0.5130.32360.04190.3945-0.02430.11660.47280.13580.327432.4376-88.05220.7217
41.95690.4375-0.45483.0548-0.01370.914-0.0523-0.02140.2298-0.1310.02940.5359-0.27630.01870.02290.35860.1122-0.03110.32630.13120.56063.8559-91.195114.2512
51.5710.81060.69372.43630.74172.5394-0.3963-0.0680.33240.17840.09380.7996-0.6617-0.42040.30240.46240.18410.3060.52170.0140.8115-2.672-94.707545.5895
62.13850.90480.63261.13080.3052.209-0.0253-0.39410.33490.6306-0.02180.3412-0.2959-0.52120.04710.79990.09590.40230.5018-0.11760.35915.797-95.495169.6596
71.53070.2108-0.37281.85880.51681.69470.0211-0.31370.08570.7044-0.0742-0.274-0.29880.07490.05310.8271-0.0766-0.06270.288-0.0960.27548.1191-94.020670.8908
80.7772-0.2798-0.36521.20880.29950.3690.09490.1070.01460.4588-0.0196-0.7329-0.04080.1679-0.07530.37-0.0884-0.23190.33630.01270.585767.5907-130.861448.0176
90.9073-0.4005-0.25292.51120.20161.95620.09530.19510.00770.1787-0.089-0.9405-0.01080.1443-0.00630.1351-0.00070.06980.35620.00620.607468.5374-128.463620.6467
102.7566-0.35751.19263.7349-0.39761.5046-0.0560.2335-0.0425-1.00610.06280.1117-0.0520.0989-0.00680.46630.0010.1350.34830.00820.158145.0164-127.3773-1.1629
111.17770.77180.2032.28411.06661.6796-0.04250.21320.006-0.71110.0940.5435-0.0717-0.029-0.05150.37760.048-0.23470.29730.08690.350711.1383-131.79522.322
120.69650.4319-0.32261.67930.59050.8156-0.0835-0.17310.2217-0.3166-0.01790.7625-0.1601-0.15060.10140.15480.04460.0370.40480.11710.7039-4.0727-134.950628.5947
131.6856-0.98630.68582.6242-0.8061.61070.1348-0.15330.03940.92090.02490.35810.0005-0.2102-0.15980.5687-0.04910.2970.34830.00110.33687.9251-138.479360.2863
141.96150.0794-0.55572.3812-0.04040.99970.0891-0.22460.12250.766-0.0097-0.1523-0.052-0.0543-0.07940.6485-0.0635-0.06930.296-0.02280.081740.1003-134.923670.4241
152.1998-0.5105-0.63652.82810.47341.6535-0.0638-0.1678-0.20340.29430.0350.57490.2475-0.27160.02880.363-0.0977-0.13470.33380.10230.52951.8499-207.334336.5809
161.95590.99920.5152.84150.36022.3446-0.13650.006-0.1512-0.17380.1220.40260.1086-0.38530.01450.5037-0.0468-0.17080.3125-0.06830.42588.5554-206.16196.5233
171.59320.22460.2871.8255-0.08362.40510.11390.5488-0.4168-0.86390.1270.27010.5531-0.2092-0.24090.88950.0376-0.11680.457-0.20910.607435.936-204.2045-9.5034
182.19550.39571.23013.56010.27561.67370.15260.0294-0.108-0.6387-0.1104-0.17010.31610.0392-0.04210.38430.1240.32830.4999-0.08760.62964.8155-203.41663.9559
190.95770.22670.20911.6031-0.99111.6561-0.01880.2479-0.3994-0.05410.0666-0.81440.34980.4399-0.04780.36280.1421-0.10640.4978-0.12181.066271.8031-205.305235.1552
201.89650.48380.34691.47710.24982.02520.1728-0.2196-0.45290.38960.0004-0.63090.23590.2855-0.17320.61960.029-0.37310.27810.13710.649753.8405-208.714259.3186
211.3725-0.11640.16482.5705-0.39381.74330.0013-0.234-0.18020.56190.02830.21380.1701-0.0401-0.02970.5856-0.0514-0.17580.21470.11320.40821.7378-210.658760.9095
221.143-0.03451.21561.3644-0.72011.69320.2131-0.1754-0.0934-0.03610.0740.62870.288-0.2944-0.28710.1584-0.02530.16460.45050.07120.59561.7049-170.250445.4708
231.4147-0.11040.94333.4802-0.37411.78580.0046-0.0296-0.0501-0.33210.15430.76450.1586-0.1425-0.15890.0747-0.0088-0.05740.31760.03250.42160.1211-167.850717.9417
242.0977-0.7003-0.61652.8208-0.06650.5220.00310.2392-0.0186-0.63780.04070.1578-0.09950.0377-0.04370.5235-0.0071-0.11710.3384-0.03610.151423.2982-165.0075-4.2866
251.55970.994-0.17343.4143-0.05450.64230.04090.26940.0247-0.79350.1211-0.33980.18840.231-0.1620.42190.10040.22630.457-0.0770.354557.2627-161.3277-0.8197
260.6117-0.1138-0.07052.065-0.36321.48750.05160.1813-0.06660.2346-0.0314-0.95230.08540.2722-0.02020.11380.0556-0.00570.4116-0.03770.758372.9254-162.743125.2432
271.26610.030.14451.43740.62271.12540.0257-0.0946-0.11830.6872-0.0288-0.5580.04170.12390.00310.4462-0.021-0.2940.24820.06610.402161.544-164.728857.3947
281.77390.19280.24981.97540.45051.0830.1395-0.1602-0.11290.8868-0.0604-0.04740.1488-0.1639-0.07910.5535-0.06450.01030.30570.07190.145229.6758-170.106567.4461
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 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 DIFFRACTION15O2 - 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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