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- PDB-4int: Yeast 20S proteasome in complex with the vinyl sulfone LU122 -

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Basic information

Entry
Database: PDB / ID: 4int
TitleYeast 20S proteasome in complex with the vinyl sulfone LU122
Components(Proteasome component ...) x 14
KeywordsHYDROLASE/HYDROLASE INHIBITOR / UPS / drug discovery / irreversible inhibition / 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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / 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 ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / 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 / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
HMB-VAL-SER-PHE(4-NH2CH2)-METHYL VINYL SULFONE, BOUND FORM / Chem-1G5 / 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 ...HMB-VAL-SER-PHE(4-NH2CH2)-METHYL VINYL SULFONE, BOUND FORM / Chem-1G5 / 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: 2.9 Å
AuthorsGeurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E.M. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. ...Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E.M. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der Stelt, M. / Groll, M. / Overkleeft, H.S. / Kisselev, A.F.
CitationJournal: J.Med.Chem. / Year: 2013
Title: Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites.
Authors: Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der ...Authors: Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der Stelt, M. / Groll, M. / Overkleeft, H.S. / Kisselev, A.F.
History
DepositionJan 6, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 30, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 27, 2013Group: 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 / struct_conn / struct_ncs_dom_lim / 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.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 16, 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 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)730,84732
Polymers728,54028
Non-polymers2,3074
Water24,0501335
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area120880 Å2
ΔGint-360 kcal/mol
Surface area214980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)137.010, 299.510, 145.040
Angle α, β, γ (deg.)90.00, 113.24, 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
115K
215Y
116V
216H

NCS domain segments:

Component-ID: 1 / Refine code: 4

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11METMETLEULEUAA1 - 2501 - 250
21METMETLEULEUOO1 - 2501 - 250
12GLYGLYTHRTHRBB1 - 2442 - 245
22GLYGLYTHRTHRPP1 - 2442 - 245
13GLYGLYGLNGLNCC1 - 2413 - 243
23GLYGLYGLNGLNQQ1 - 2413 - 243
14ASPASPGLUGLUDD1 - 2429 - 250
24ASPASPGLUGLURR1 - 2429 - 250
15PHEPHEILEILEEE1 - 2332 - 234
25PHEPHEILEILESS1 - 2332 - 234
16GLYGLYASNASNFF1 - 2445 - 248
26GLYGLYASNASNTT1 - 2445 - 248
17ALAALAASPASPGG1 - 24310 - 252
27ALAALAASPASPUU1 - 24310 - 252
18THRTHRASPASPHH1 - 2221 - 222
28THRTHRASPASPVV1 - 2221 - 222
19SERSERASPASPII1 - 2042 - 205
29SERSERASPASPWW1 - 2042 - 205
110METMETGLNGLNJJ1 - 1981 - 198
210METMETGLNGLNXX1 - 1981 - 198
111THRTHRGLYGLYKK1 - 2121 - 212
211THRTHRGLYGLYYY1 - 2121 - 212
112GLNGLNASPASPLL1 - 2221 - 222
212GLNGLNASPASPZZ1 - 2221 - 222
113THRTHRILEILEMM1 - 2331 - 233
213THRTHRILEILEaAA1 - 2331 - 233
114THRTHRLEULEUNN1 - 1961 - 196
214THRTHRLEULEUbBA1 - 1961 - 196
1151G51G51G51G5KDA301
2151G51G51G51G5YFA301
1161G51G51G51G5VEA301
2161G51G51G51G5HCA301

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999715, 0.000111, 0.023869), (-0.00397, -0.986832, -0.161701), (0.023536, -0.16175, 0.986551)68.68169, -290.10629, -24.28515

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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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 2 types, 1339 molecules

#15: Chemical
ChemComp-1G5 / HMB-Val-Ser-Phe(4-NH2CH2)-methyl vinyl sulfone, bound form


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 576.705 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C28H40N4O7S
References: HMB-VAL-SER-PHE(4-NH2CH2)-METHYL VINYL SULFONE, BOUND FORM
#16: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1335 / 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: 3.75 Å3/Da / Density % sol: 67.23 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 mM magnesium acetate, 0.1 M MES, 12% 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: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 4, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→15 Å / Num. all: 236839 / Num. obs: 233547 / % possible obs: 98.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 16.88
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.483 / Mean I/σ(I) obs: 3.91 / % possible all: 99.5

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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: 2.9→15 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.928 / SU B: 29.185 / SU ML: 0.274 / Cross valid method: THROUGHOUT / ESU R: 1.115 / ESU R Free: 0.327 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.22997 11678 5 %RANDOM
Rwork0.22158 ---
obs0.222 221869 98.74 %-
all-221869 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 74.888 Å2
Baniso -1Baniso -2Baniso -3
1-3.78 Å20 Å2-2.03 Å2
2---8.83 Å20 Å2
3---3.45 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49538 0 160 1335 51033
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.0250618
X-RAY DIFFRACTIONr_angle_refined_deg0.8361.96668488
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.93956340
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.17624.4082264
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.255158780
X-RAY DIFFRACTIONr_dihedral_angle_4_deg10.36215288
X-RAY DIFFRACTIONr_chiral_restr0.0530.27698
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02138094
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1915MEDIUM POSITIONAL0.030.5
1A1915MEDIUM THERMAL0.962
2B1905MEDIUM POSITIONAL0.040.5
2B1905MEDIUM THERMAL0.872
3C1891MEDIUM POSITIONAL0.030.5
3C1891MEDIUM THERMAL1.282
4D1862MEDIUM POSITIONAL0.040.5
4D1862MEDIUM THERMAL0.752
5E1795MEDIUM POSITIONAL0.030.5
5E1795MEDIUM THERMAL0.722
6F1897MEDIUM POSITIONAL0.040.5
6F1897MEDIUM THERMAL0.872
7G1921MEDIUM POSITIONAL0.050.5
7G1921MEDIUM THERMAL0.752
8H1685MEDIUM POSITIONAL0.050.5
8H1685MEDIUM THERMAL0.622
9I1581MEDIUM POSITIONAL0.030.5
9I1581MEDIUM THERMAL0.782
10J1585MEDIUM POSITIONAL0.030.5
10J1585MEDIUM THERMAL0.882
11K1644MEDIUM POSITIONAL0.040.5
11K1644MEDIUM THERMAL0.82
12L1757MEDIUM POSITIONAL0.040.5
12L1757MEDIUM THERMAL0.862
13M1824MEDIUM POSITIONAL0.030.5
13M1824MEDIUM THERMAL0.432
14N1512MEDIUM POSITIONAL0.030.5
14N1512MEDIUM THERMAL0.562
15K40MEDIUM POSITIONAL0.650.5
15K40MEDIUM THERMAL0.512
16V40MEDIUM POSITIONAL0.290.5
16V40MEDIUM THERMAL1.32
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.351 830 -
Rwork0.341 15756 -
obs--99.54 %
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)
11.2331-0.06890.30380.8422-0.00530.75350.02710.0057-0.00880.1707-0.0152-0.2986-0.17390.0807-0.0120.3031-0.0997-0.07850.1834-0.01950.285467.615-92.425945.592
21.25550.139-0.2871.2684-0.16691.094-0.0228-0.10270.1054-0.0865-0.022-0.3575-0.19580.29030.04480.2147-0.08390.09140.2510.06750.190160.2283-88.40816.0096
30.73460.2597-0.23051.2559-0.20481.0383-0.01610.10810.1176-0.30650.10350.1199-0.05930.0974-0.08740.2683-0.00110.02450.17460.09550.119732.8004-87.71530.4254
40.84310.1191-0.16020.8440.03930.472-0.00790.00480.1664-0.19630.04110.4829-0.05110.0271-0.03330.19130.1111-0.03040.16010.13190.41834.1174-90.662213.8532
50.24720.17840.07380.2377-0.141.07180.0493-0.0070.15510.14660.01470.3223-0.2233-0.1559-0.0640.16780.11330.23330.2343-0.01130.6-2.2354-93.987945.1617
60.52710.12210.08150.4331-0.25790.79340.0529-0.18090.10140.2504-0.02640.2103-0.1046-0.0688-0.02640.49140.02890.27570.2587-0.09060.212416.1278-94.676969.2581
70.6650.2599-0.00620.7211-0.15060.60560.0699-0.1330.04750.4131-0.0404-0.1512-0.1847-0.0239-0.02960.619-0.0659-0.03450.2247-0.0720.140348.4128-93.439470.6298
80.1247-0.0287-0.08020.60040.16590.3570.06550.03170.03720.255-0.049-0.4497-0.04930.0364-0.01650.2618-0.0819-0.1640.23340.030.41568.0341-130.23848.3071
90.83340.4099-0.05071.9520.13930.87830.06560.0555-0.11970.0205-0.1024-0.4949-0.08130.04150.03680.0603-0.0260.080.2340.04530.33168.814-128.039820.7759
101.12130.31910.17661.7189-0.36110.1412-0.03990.12760.0127-0.40570.0459-0.07390.05310.0167-0.0060.28460.0160.11310.23110.00430.05245.3174-127.1449-1.1488
110.69370.36240.02641.19730.76930.9692-0.02190.10610.0844-0.33150.04430.3598-0.073-0.0331-0.02240.20840.0288-0.18880.20750.07010.289611.3629-131.25641.8672
120.7078-0.05980.33750.97230.16570.84550.1241-0.06880.03030.0473-0.02110.4914-0.045-0.0816-0.1030.06060.04190.07110.22080.07940.4555-3.9268-134.341728.413
130.4617-0.02010.1391.11080.03850.16740.0523-0.07140.03220.4373-0.02170.2284-0.0357-0.028-0.03060.3140.00430.22480.2410.0130.23918.1159-137.567760.2471
140.7990.2458-0.08750.81610.20490.53090.1129-0.07670.02450.334-0.0535-0.0829-0.02910.0178-0.05940.5334-0.074-0.01250.2482-0.0150.025440.1106-134.040570.6556
151.3173-0.1365-0.35581.24360.19770.46470.05810.0645-0.06640.0991-0.04710.39580.1308-0.0998-0.0110.1179-0.0979-0.09090.18070.07750.36051.9273-206.378336.947
160.57470.34070.26381.00160.23021.0537-0.0636-0.0605-0.0577-0.28440.02240.17560.0714-0.18870.04120.242-0.0476-0.17670.2072-0.06260.27088.6406-205.49876.9258
171.03840.12570.47590.9803-0.31060.85430.13190.1205-0.1436-0.75170.07180.16940.261-0.0143-0.20370.71750.0274-0.12730.1811-0.13710.255736.0681-203.8368-9.0746
181.0732-0.04980.38811.1674-0.16210.34570.02850.0542-0.084-0.4926-0.1334-0.34850.11320.06380.10490.34230.15320.23320.2191-0.06150.379264.906-203.04234.3707
191.19570.3475-0.02061.0256-0.45960.7420.10830.1543-0.26980.0247-0.0665-0.71220.14890.1905-0.04180.07180.1102-0.12230.2268-0.05790.740571.8259-204.623435.4793
200.61410.21120.0490.78070.44090.63430.1465-0.1866-0.27760.3177-0.0961-0.38760.11670.0205-0.05040.3182-0.0222-0.31570.16760.13650.405853.9095-207.86859.6107
210.57010.0805-0.10321.0772-0.14430.82890.0623-0.0758-0.10040.4205-0.00620.08190.03910.0056-0.0560.3517-0.0411-0.10270.14690.10030.189821.711-209.668461.3062
220.2122-0.0535-0.05060.5591-0.30090.34710.053-0.0264-0.09940.10520.05760.39960.0491-0.1061-0.11060.1662-0.03830.10490.23690.04830.37751.6217-169.529345.7207
230.9487-0.07710.01221.9139-0.37840.77790.07140.0290.0592-0.11650.07580.42810.0574-0.0126-0.14720.0781-0.0112-0.12850.19590.01990.34080.3622-167.25618.1109
240.97170.0355-0.23881.3296-0.06650.11860.01210.1034-0.1063-0.49990.03390.14970.09230.003-0.0460.36570.0131-0.11650.199-0.02650.10523.5216-164.5989-4.0347
251.08540.76480.0842.2695-0.520.67470.01570.106-0.0854-0.5228-0.0425-0.37780.07670.0440.02670.2590.06190.19130.2555-0.04350.190757.5526-161.0131-0.8689
260.538-0.3186-0.11791.4495-0.64480.7280.0640.00510.01370.032-0.1173-0.5483-0.01990.12180.05340.04950.0237-0.00290.2525-0.00510.531973.219-162.184525.5375
270.4146-0.2046-0.09711.01360.09150.26920.0282-0.0424-0.06440.4199-0.0205-0.3447-0.05510.0349-0.00760.2796-0.0572-0.22340.21370.04930.300361.7827-164.11457.5864
280.7178-0.17830.17431.73960.24540.59780.1093-0.0467-0.07860.4688-0.05680.044-0.0306-0.0711-0.05250.4319-0.08070.00260.2150.05310.039229.9964-169.345467.9182
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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