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- PDB-6huu: Yeast 20S proteasome with human beta2c (S171G) in complex with 29 -

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Basic information

Entry
Database: PDB / ID: 6huu
TitleYeast 20S proteasome with human beta2c (S171G) in complex with 29
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE / Proteasome / Mutant / Inhibitor / Binding Analysis
Function / homology
Function and homology information


Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / 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 ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / 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 / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / 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 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / Asymmetric localization of PCP proteins / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / Degradation of AXIN / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / G2/M Checkpoints / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / The role of GTSE1 in G2/M progression after G2 checkpoint / UCH proteinases / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / peroxisome / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / ER-Phagosome pathway / secretory granule lumen / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / ficolin-1-rich granule lumen / nuclear body / Ub-specific processing proteases / mRNA binding / Neutrophil degranulation / endoplasmic reticulum membrane / mitochondrion / extracellular region / nucleoplasm / 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
Chem-GTW / 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-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 ...Chem-GTW / 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-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 / Proteasome subunit beta type-7
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHuber, E.M. / Groll, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationGR1861/10-1 Germany
CitationJournal: J.Med.Chem. / Year: 2019
Title: Structure-Based Design of Inhibitors Selective for Human Proteasome beta 2c or beta 2i Subunits.
Authors: Xin, B.T. / Huber, E.M. / de Bruin, G. / Heinemeyer, W. / Maurits, E. / Espinal, C. / Du, Y. / Janssens, M. / Weyburne, E.S. / Kisselev, A.F. / Florea, B.I. / Driessen, C. / van der Marel, G. ...Authors: Xin, B.T. / Huber, E.M. / de Bruin, G. / Heinemeyer, W. / Maurits, E. / Espinal, C. / Du, Y. / Janssens, M. / Weyburne, E.S. / Kisselev, A.F. / Florea, B.I. / Driessen, C. / van der Marel, G.A. / Groll, M. / Overkleeft, H.S.
History
DepositionOct 9, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 30, 2019Provider: repository / Type: Initial release
Revision 1.1Apr 24, 2019Group: Data collection / Database references
Category: citation / citation_author ...citation / citation_author / database_PDB_rev / database_PDB_rev_record / pdbx_database_proc / pdbx_seq_map_depositor_info
Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.name / _pdbx_seq_map_depositor_info.one_letter_code / _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.2Jan 24, 2024Group: 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_conn_type
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-2
B: Proteasome subunit alpha type-3
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-6
F: Probable proteasome subunit alpha type-7
G: Proteasome subunit alpha type-1
H: Proteasome subunit beta type-7
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-7
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-4
Y: Proteasome subunit beta type-5
Z: Proteasome subunit beta type-6
a: Proteasome subunit beta type-7
b: Proteasome subunit beta type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)734,45544
Polymers731,40628
Non-polymers3,04916
Water7,764431
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)134.670, 299.610, 143.620
Angle α, β, γ (deg.)90.00, 112.36, 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

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A1 - 300
2111O1 - 300
1121B1 - 300
2121P1 - 300
1131C1 - 300
2131Q1 - 300
1141D1 - 300
2141R1 - 300
1151E1 - 300
2151S1 - 300
1161F1 - 300
2161T1 - 300
1171G1 - 300
2171U1 - 300
1181H1 - 300
2181V1 - 300
1191I1 - 300
2191W1 - 300
11101J1 - 300
21101X1 - 300
11111K1 - 300
21111Y1 - 300
11121L1 - 300
21121Z1 - 300
11131M1 - 300
21131a1 - 300
11141N1 - 300
21141b1 - 300

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

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999606, 0.000124, 0.028061), (-0.004824, -0.985863, -0.167486), (0.027643, -0.167555, 0.985475)67.76776, -288.33615, -25.66959
3given(1), (1), (1)
4given(-0.999671, 0.005135, 0.025112), (-0.009054, -0.987316, -0.158512), (0.02398, -0.158687, 0.987038)68.82191, -288.87827, -23.80901
5given(1), (1), (1)
6given(-0.999831, -0.002215, 0.018252), (-0.000804, -0.986506, -0.163723), (0.018369, -0.16371, 0.986337)67.44286, -288.94788, -24.68738
7given(1), (1), (1)
8given(-0.999854, 0.00312, 0.016795), (-0.005774, -0.987037, -0.160392), (0.016076, -0.160466, 0.98691)68.56395, -288.7124, -23.93738
9given(1), (1), (1)
10given(-0.999657, -0.005442, 0.025627), (0.001034, -0.985622, -0.168964), (0.026178, -0.168879, 0.985289)66.7001, -288.43463, -26.08385
11given(1), (1), (1)
12given(-0.999651, -0.010827, 0.024079), (0.006629, -0.985758, -0.168041), (0.025555, -0.167823, 0.985486)65.74009, -288.51624, -25.75245
13given(1), (1), (1)
14given(-0.999624, -0.006262, 0.026706), (0.00139, -0.983911, -0.178655), (0.027395, -0.17855, 0.983549)66.55291, -287.42569, -27.85279
15given(1), (1), (1)
16given(-0.999742, 0.000478, 0.022715), (-0.004174, -0.986626, -0.162946), (0.022333, -0.162999, 0.986373)67.97312, -288.64935, -24.62455
17given(1), (1), (1)
18given(-0.999689, -0.001299, 0.024885), (-0.002835, -0.986227, -0.165375), (0.024757, -0.165394, 0.985917)67.63288, -288.67938, -24.96662
19given(1), (1), (1)
20given(-0.999703, -0.002903, 0.024187), (-0.001211, -0.98572, -0.168391), (0.02433, -0.168371, 0.985423)67.3623, -288.78647, -25.46762
21given(1), (1), (1)
22given(-0.999689, -0.00197, 0.024869), (-0.002072, -0.986872, -0.161492), (0.024861, -0.161493, 0.986561)67.53335, -288.94238, -24.41753
23given(1), (1), (1)
24given(-0.999748, -0.000911, 0.022409), (-0.002826, -0.986091, -0.16618), (0.022249, -0.166202, 0.985841)67.72897, -288.54916, -25.00414
25given(1), (1), (1)
26given(-0.999709, -0.002133, 0.024033), (-0.00188, -0.98617, -0.165729), (0.024054, -0.165726, 0.985878)67.4656, -288.39316, -25.00444
27given(1), (1), (1)
28given(-0.999613, -0.002624, 0.027681), (-0.001946, -0.986494, -0.163787), (0.027737, -0.163778, 0.986107)67.1525, -288.51773, -24.82865

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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 (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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Protein , 1 types, 2 molecules FT

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


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

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

#8: Protein Proteasome subunit beta type-7 / Macropain chain Z / Multicatalytic endopeptidase complex chain Z / Proteasome subunit Z


Mass: 25291.953 Da / Num. of mol.: 2 / Mutation: S171G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB7, Z / Production host: Saccharomyces cerevisiae (brewer's yeast) / Strain (production host): ATCC204508/S288C
References: UniProt: Q99436, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit PUP3 / Proteasome component PUP3


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


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


Mass: 23325.248 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (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 (strain ATCC 204508 / S288c) (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: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-1 / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component ...Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component PRE3 / Proteinase YSCE subunit PRE3


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

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Non-polymers , 5 types, 447 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-GTW / ~{N}-[(2~{S})-1-[[(2~{S})-1-[[(2~{S})-1-[4-(aminomethyl)phenyl]-4-methylsulfonyl-butan-2-yl]amino]-3-cyclohexyl-1-oxidanylidene-propan-2-yl]amino]-4-methyl-1-oxidanylidene-pentan-2-yl]-2-methyl-1,3-thiazole-5-carboxamide


Mass: 647.892 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C32H49N5O5S2
#18: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 431 / 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: 3.67 Å3/Da / Density % sol: 66.52 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 / Details: 20 mM MgAC2, 13% MPD, 0.1 M MES / PH range: 6.8

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 20, 2016
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→50 Å / Num. obs: 255383 / % possible obs: 99.1 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 11.4
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.585 / % possible all: 99.4

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
REFMACphasing
REFMAC5.8.0158refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5CZ4

5cz4


Resolution: 2.8→15 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.934 / SU B: 35.811 / SU ML: 0.278 / Cross valid method: THROUGHOUT / ESU R Free: 0.285 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22086 12770 5 %RANDOM
Rwork0.19438 ---
obs0.1957 242613 99.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 77.253 Å2
Baniso -1Baniso -2Baniso -3
1-1.86 Å20 Å2-0.52 Å2
2---4.97 Å2-0 Å2
3---2.64 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms48944 0 196 433 49573
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01950022
X-RAY DIFFRACTIONr_bond_other_d0.0020.0246704
X-RAY DIFFRACTIONr_angle_refined_deg1.2111.96867662
X-RAY DIFFRACTIONr_angle_other_deg0.9453.002108360
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.97356260
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.07924.3582226
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.006158684
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.64915290
X-RAY DIFFRACTIONr_chiral_restr0.0730.27628
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0255736
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0210030
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_it2.5133.91425136
X-RAY DIFFRACTIONr_mcbond_other2.5133.91425135
X-RAY DIFFRACTIONr_mcangle_it3.3215.85531364
X-RAY DIFFRACTIONr_mcangle_other3.3215.85531365
X-RAY DIFFRACTIONr_scbond_it2.4424.29724886
X-RAY DIFFRACTIONr_scbond_other2.4394.29624878
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.9456.29236286
X-RAY DIFFRACTIONr_long_range_B_refined3.89745.31952909
X-RAY DIFFRACTIONr_long_range_B_other3.86545.29352864
X-RAY DIFFRACTIONr_rigid_bond_restr0.814396726
X-RAY DIFFRACTIONr_sphericity_free36.6775316
X-RAY DIFFRACTIONr_sphericity_bonded6.425595961
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1010A3063tight positional0.010.05
1111A3256tight positional0.010.05
1212A3389tight positional0.010.05
1313A3419tight positional0.010.05
1414A2919tight positional0.010.05
11A3622tight thermal6.440.5
22B3714tight thermal4.450.5
33C3685tight thermal11.040.5
44D3538tight thermal6.30.5
55E3459tight thermal8.030.5
66F3693tight thermal6.080.5
77G3724tight thermal4.050.5
88H3340tight thermal4.690.5
99I3091tight thermal2.390.5
1010J3063tight thermal2.860.5
1111K3256tight thermal2.710.5
1212L3389tight thermal2.30.5
1313M3419tight thermal2.610.5
1414N2919tight thermal2.350.5
LS refinement shellResolution: 2.8→2.872 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.38 944 -
Rwork0.363 17923 -
obs--99.45 %
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)
10.99110.19880.31010.69280.00480.1078-0.00520.0437-0.09130.3655-0.0206-0.3142-0.080.00720.02580.7948-0.0913-0.20720.2802-0.04830.408366.585-90.544145.1811
20.1957-0.068-0.04480.15460.31130.7421-0.0597-0.04450.00960.02930.048-0.0459-0.08040.17840.01170.6766-0.0846-0.03950.31130.07140.335259.6002-87.663915.949
30.33160.3409-0.00070.3538-0.00380.0365-0.05780.06390.0771-0.03740.06980.09780.02770.0873-0.0120.7413-0.0017-0.11140.28370.09780.249632.2398-87.28280.6758
40.65070.0779-0.26740.1088-0.08640.2578-0.00810.0054-0.0132-0.02320.04370.2157-0.06170.0922-0.03560.67510.1148-0.19530.19290.12390.53673.2305-89.789613.3212
50.4628-0.06020.1510.05160.0110.1607-0.0474-0.0183-0.04740.0677-0.01580.1654-0.11890.0440.06320.71020.06760.11660.2224-0.03250.6819-3.009-93.782145.3764
60.36310.1548-0.06290.1248-0.10130.19240.1187-0.09580.05420.2101-0.10250.0616-0.05680.0586-0.01621.0237-0.04540.12830.2518-0.10530.294115.6702-94.278269.4182
70.18460.0766-0.20050.5683-0.41860.5310.15670.02-0.01920.4544-0.1683-0.1402-0.17530.09990.01161.1324-0.1801-0.18880.2606-0.05830.224447.9975-92.890570.5431
80.0513-0.04050.02670.32810.05510.22020.08140.07750.00970.2037-0.0751-0.2857-0.0579-0.0664-0.00630.7288-0.053-0.25770.3263-0.00920.469467.4025-129.755448.4502
90.268-0.04580.12830.9648-0.00910.1390.0489-0.0109-0.0698-0.0473-0.0665-0.2927-0.1029-0.01230.01770.5763-0.0281-0.02150.32640.00610.483268.2244-127.029820.8102
100.18460.32620.08870.94440.06620.0874-0.0073-0.0498-0.0076-0.16890.0597-0.01550.0131-0.0127-0.05240.7330.0105-0.03310.34540.00650.207744.6446-126.49-0.7113
110.29260.3238-0.07040.85830.04410.08740.0299-0.0334-0.02690.0190.02120.09910.09030.0735-0.0510.54690.0233-0.24630.25020.03920.277310.8743-130.68532.7051
120.08550.08660.10850.89890.06690.22640.089-0.02740.02150.0336-0.05550.2827-0.00080.0564-0.03360.55970.0431-0.06250.29190.05480.5738-4.5094-133.944728.6043
130.2031-0.20240.03260.60070.00640.02050.09410.02680.07430.2975-0.09650.09610.01860.03070.00240.8075-0.0570.09120.3411-0.0030.34357.5155-135.442560.1002
140.58120.0658-0.39390.9740.18740.33190.11960.04070.07540.3754-0.0436-0.0544-0.00940.014-0.0760.9882-0.0752-0.16210.3095-0.0230.169239.8562-133.343570.8569
150.5214-0.0718-0.05920.06020.06220.1101-0.03250.01540.03130.07220.04260.04850.1318-0.0252-0.01010.5921-0.0927-0.22560.14330.10120.47442.196-206.867536.6542
160.0974-0.00890.13920.3095-0.22020.3404-0.1016-0.0471-0.0021-0.16810.0844-0.0335-0.0082-0.11750.01720.6367-0.0284-0.26780.2185-0.08960.39378.3493-205.01357.105
170.50320.21150.24420.16860.07080.16760.07850.0043-0.0642-0.19230.02180.08140.03440.0499-0.10030.89380.0635-0.26920.0984-0.1410.309135.4957-203.017-8.6529
180.12-0.10330.0720.1976-0.07790.04660.0441-0.08030.1207-0.2461-0.0937-0.21670.0859-0.03540.04960.71460.1950.06390.2293-0.06740.472564.771-202.52553.7686
190.01230.00060.00230.2387-0.24910.31810.06280.0191-0.01960.0346-0.0422-0.1188-0.0034-0.0156-0.02050.45440.1238-0.21960.1743-0.06330.692271.7591-203.539635.7343
200.6505-0.13680.1330.0396-0.03820.08010.13510.0678-0.11980.0505-0.0598-0.0312-0.0705-0.039-0.07530.7545-0.0069-0.44550.09420.11560.41353.7864-206.903759.9558
210.21-0.30350.02480.5202-0.05460.5446-0.02080.0016-0.05940.24070.07720.0935-0.0110.001-0.05640.8082-0.0279-0.23420.12220.11810.317321.5277-208.861261.521
220.0805-0.12540.09490.3401-0.20240.1490.09330.0504-0.03820.059-0.00120.2177-0.0220.0921-0.09210.649-0.0624-0.06510.27040.09560.4771.5426-168.677246.1645
230.5549-0.1116-0.24571.1042-0.29760.23630.0162-0.02160.0146-0.1230.06470.13950.02990.0485-0.08090.5618-0.0167-0.25680.26220.02020.43890.0863-166.991218.4113
240.22290.2488-0.04510.6633-0.08640.01670.0135-0.0576-0.0859-0.21390.02590.05940.02550.02-0.03930.75330.0406-0.23320.2709-0.04840.244523.1104-164.0789-3.4804
250.10780.25860.00250.66270.00360.00080.0308-0.0582-0.0324-0.0091-0.0493-0.1203-0.0066-0.00940.01850.58880.06220.01340.2868-0.04710.291156.9845-160.4503-0.2047
260.0986-0.2322-0.04490.94520.01270.18650.07980.0022-0.01190.0302-0.0988-0.3247-0.0122-0.02590.0190.51240.0642-0.10940.3276-0.0230.561572.9735-161.300525.5511
270.0919-0.2246-0.02830.69830.0250.0296-0.00980.0504-0.00780.2577-0.0243-0.1817-0.0599-0.07930.03410.7533-0.0101-0.3530.29760.0450.421461.7083-164.810657.1231
280.55170.08580.17490.6896-0.10730.09570.09470.0080.01160.3194-0.0702-0.0413-0.0567-0.0321-0.02440.8881-0.0625-0.11240.25130.07560.204829.6496-168.674768.1862
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION2B1 - 244
3X-RAY DIFFRACTION3C1 - 240
4X-RAY DIFFRACTION4D1 - 242
5X-RAY DIFFRACTION5E3 - 233
6X-RAY DIFFRACTION6F2 - 244
7X-RAY DIFFRACTION7G2 - 242
8X-RAY DIFFRACTION8H1 - 219
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
11X-RAY DIFFRACTION11K1 - 212
12X-RAY DIFFRACTION12L1 - 222
13X-RAY DIFFRACTION13M1 - 224
14X-RAY DIFFRACTION14N1 - 196
15X-RAY DIFFRACTION15O1 - 250
16X-RAY DIFFRACTION16P1 - 244
17X-RAY DIFFRACTION17Q1 - 240
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S3 - 233
20X-RAY DIFFRACTION20T2 - 244
21X-RAY DIFFRACTION21U2 - 242
22X-RAY DIFFRACTION22V1 - 219
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 224
28X-RAY DIFFRACTION28b1 - 196

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