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- PDB-5lf0: Human 20S proteasome complex with Epoxomicin at 2.4 Angstrom -

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Basic information

Entry
Database: PDB / ID: 5lf0
TitleHuman 20S proteasome complex with Epoxomicin at 2.4 Angstrom
Components
  • (Proteasome subunit alpha type- ...) x 7
  • (Proteasome subunit beta type- ...) x 7
  • EPOXOMICIN (peptide inhibitor)
KeywordsHYDROLASE / Proteasome / Multicatalytic Proteinase / NTN-Hydrolase
Function / homology
Function and homology information


purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding / proteasome endopeptidase complex ...purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / negative regulation of inflammatory response to antigenic stimulus / : / sarcomere / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / ciliary basal body / proteolysis involved in protein catabolic process / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / 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 / lipopolysaccharide binding / Degradation of AXIN / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / Vif-mediated degradation of APOBEC3G / Autodegradation of the E3 ubiquitin ligase COP1 / 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 / P-body / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / response to virus / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / response to organic cyclic compound / 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 / nuclear matrix / 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 / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / peptidase activity / positive regulation of NF-kappaB transcription factor activity / ER-Phagosome pathway / regulation of inflammatory response / postsynapse / proteasome-mediated ubiquitin-dependent protein catabolic process / secretory granule lumen / endopeptidase activity / response to oxidative stress / ficolin-1-rich granule lumen / nuclear body / ribosome / Ub-specific processing proteases / cadherin binding / intracellular membrane-bounded organelle / centrosome / ubiquitin protein ligase binding / synapse / Neutrophil degranulation / mitochondrion / proteolysis / RNA binding
Similarity search - Function
Proteasome subunit alpha 1 / 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 subunit alpha 1 / 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
: / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 ...: / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-6 / Proteasome subunit beta type-7
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.41 Å
AuthorsSchrader, J. / Henneberg, F. / Mata, R. / Tittmann, K. / Schneider, T.R. / Stark, H. / Bourenkov, G. / Chari, A.
Funding support Germany, 3items
OrganizationGrant numberCountry
German Research FoundationCH1098/1-1 Germany
German Research FoundationSFB860-TP A5 Germany
Bundesministerium fuer Bildung und Forschung05K2013-624 Germany
CitationJournal: Science / Year: 2016
Title: The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design.
Authors: Schrader, J. / Henneberg, F. / Mata, R.A. / Tittmann, K. / Schneider, T.R. / Stark, H. / Bourenkov, G. / Chari, A.
History
DepositionJun 30, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 17, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 6, 2017Group: Author supporting evidence / Data collection / Category: diffrn_source / pdbx_audit_support
Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_audit_support.funding_organization
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Refinement description
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _chem_comp.type / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _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_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
Revision 2.1Jan 10, 2024Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 3.0Mar 6, 2024Group: Atomic model / Data collection / Derived calculations
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp_atom / chem_comp_bond / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2 / _pdbx_nonpoly_scheme.auth_mon_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.entity_id / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _struct_asym.entity_id / _struct_conn.pdbx_dist_value / _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_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-2
B: Proteasome subunit alpha type-4
C: Proteasome subunit alpha type-7
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-1
F: Proteasome subunit alpha type-3
G: Proteasome subunit alpha type-6
H: Proteasome subunit beta type-7
I: Proteasome subunit beta type-3
J: Proteasome subunit beta type-2
K: Proteasome subunit beta type-5
L: Proteasome subunit beta type-1
M: Proteasome subunit beta type-4
N: Proteasome subunit beta type-6
O: Proteasome subunit alpha type-2
P: Proteasome subunit alpha type-4
Q: Proteasome subunit alpha type-7
R: Proteasome subunit alpha type-5
S: Proteasome subunit alpha type-1
T: Proteasome subunit alpha type-3
U: Proteasome subunit alpha type-6
V: Proteasome subunit beta type-7
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-2
Y: Proteasome subunit beta type-5
Z: Proteasome subunit beta type-1
a: Proteasome subunit beta type-4
b: Proteasome subunit beta type-6
c: EPOXOMICIN (peptide inhibitor)
d: EPOXOMICIN (peptide inhibitor)
e: EPOXOMICIN (peptide inhibitor)
f: EPOXOMICIN (peptide inhibitor)
g: EPOXOMICIN (peptide inhibitor)
h: EPOXOMICIN (peptide inhibitor)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)726,915117
Polymers722,23734
Non-polymers4,67883
Water57,1623173
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area134310 Å2
ΔGint-1198 kcal/mol
Surface area207690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.070, 202.370, 314.790
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
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:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ARGARGILEILEAA3 - 2324 - 233
21ARGARGILEILEOO3 - 2324 - 233
12SERSERARGARGBB2 - 2492 - 249
22SERSERARGARGPP2 - 2492 - 249
13SERSERGLUGLUCC2 - 2372 - 237
23SERSERGLUGLUQQ2 - 2372 - 237
14ASPASPILEILEDD9 - 2419 - 241
24ASPASPILEILERR9 - 2419 - 241
15ASNASNLEULEUEE4 - 2364 - 236
25ASNASNLEULEUSS4 - 2364 - 236
16GLYGLYLEULEUFF6 - 2437 - 244
26GLYGLYLEULEUTT6 - 2437 - 244
17SERSERARGARGGG2 - 2452 - 245
27SERSERARGARGUU2 - 2452 - 245
18THRTHRGLUGLUHH1 - 2201 - 220
28THRTHRGLUGLUVV1 - 2201 - 220
19SERSERASPASPII1 - 2042 - 205
29SERSERASPASPWW1 - 2042 - 205
110METMETPHEPHEJJ1 - 1961 - 196
210METMETPHEPHEXX1 - 1961 - 196
111THRTHRTYRTYRKK1 - 1991 - 199
211THRTHRTYRTYRYY1 - 1991 - 199
112ARGARGASPASPLL1 - 2131 - 213
212ARGARGASPASPZZ1 - 2131 - 213
113THRTHRSERSERMM1 - 2161 - 216
213THRTHRSERSERaAA1 - 2161 - 216
114THRTHRTHRTHRNN1 - 2011 - 201
214THRTHRTHRTHRbBA1 - 2011 - 201

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 subunit alpha type- ... , 7 types, 14 molecules AOBPCQDRESFTGU

#1: Protein Proteasome subunit alpha type-2 / Macropain subunit C3 / Multicatalytic endopeptidase complex subunit C3 / Proteasome component C3


Mass: 25927.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P25787, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-4 / Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / ...Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / Proteasome subunit L


Mass: 29525.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P25789, proteasome endopeptidase complex
#3: Protein Proteasome subunit alpha type-7 / Proteasome subunit RC6-1 / Proteasome subunit XAPC7


Mass: 27986.941 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: O14818, proteasome endopeptidase complex
#4: Protein Proteasome subunit alpha type-5 / Macropain zeta chain / Multicatalytic endopeptidase complex zeta chain / Proteasome zeta chain


Mass: 26435.977 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P28066, proteasome endopeptidase complex
#5: Protein Proteasome subunit alpha type-1 / 30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex ...30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex subunit C2 / Proteasome component C2 / Proteasome nu chain


Mass: 29720.752 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P25786, proteasome endopeptidase complex
#6: Protein Proteasome subunit alpha type-3 / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8


Mass: 28469.252 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P25788, proteasome endopeptidase complex
#7: Protein Proteasome subunit alpha type-6 / 27 kDa prosomal protein / p27K / Macropain iota chain / Multicatalytic endopeptidase complex iota ...27 kDa prosomal protein / p27K / Macropain iota chain / Multicatalytic endopeptidase complex iota chain / Proteasome iota chain


Mass: 27739.760 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P60900, 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: 25321.980 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: Q99436, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / Proteasome chain 13 / Proteasome component C10-II / Proteasome theta chain


Mass: 22972.896 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P49720, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-2 / Macropain subunit C7-I / Multicatalytic endopeptidase complex subunit C7-I / Proteasome component C7-I


Mass: 22989.402 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P49721, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-5 / Macropain epsilon chain / Multicatalytic endopeptidase complex epsilon chain / Proteasome chain 6 / ...Macropain epsilon chain / Multicatalytic endopeptidase complex epsilon chain / Proteasome chain 6 / Proteasome epsilon chain / Proteasome subunit MB1 / Proteasome subunit X


Mass: 22484.369 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P28074, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-1 / Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / ...Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / Proteasome gamma chain


Mass: 23578.986 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P20618, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-4 / 26 kDa prosomal protein / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase complex ...26 kDa prosomal protein / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase complex beta chain / Proteasome beta chain / Proteasome chain 3 / HsN3


Mass: 24414.740 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P28070, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-6 / Macropain delta chain / Multicatalytic endopeptidase complex delta chain / Proteasome delta chain / ...Macropain delta chain / Multicatalytic endopeptidase complex delta chain / Proteasome delta chain / Proteasome subunit Y


Mass: 21921.836 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HELA
References: UniProt: P28072, proteasome endopeptidase complex

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Protein/peptide , 1 types, 6 molecules cdefgh

#15: Protein/peptide
EPOXOMICIN (peptide inhibitor)


Mass: 542.752 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 5 types, 3256 molecules

#16: Chemical...
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 58 / Source method: isolated from a natural source / Formula: Cl
#17: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: K
#18: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Mg
#19: Chemical
ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400


Mass: 238.278 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#20: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3173 / Source method: isolated from a natural source / Formula: H2O

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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: 2.54 Å3/Da / Density % sol: 51.65 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P14 (MX2) / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 20, 2015 / Details: CRL Transfocator
RadiationMonochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.41→170.23 Å / Num. obs: 262073 / % possible obs: 99.9 % / Redundancy: 9.6 % / Rmerge(I) obs: 0.17 / Net I/σ(I): 12.2
Reflection shellResolution: 2.41→2.5 Å / Mean I/σ(I) obs: 0.83 / % possible all: 99.6

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Processing

Software
NameVersionClassification
REFMAC5.8.0103refinement
PDB_EXTRACT3.2data extraction
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5LE5

5le5


Resolution: 2.41→170.23 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.938 / SU B: 23.631 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R: 0.428 / ESU R Free: 0.25 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.229 13832 5 %RANDOM
Rwork0.179 ---
obs0.182 262073 99.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 65.34 Å2
Baniso -1Baniso -2Baniso -3
1-0.7 Å20 Å20 Å2
2---0.76 Å20 Å2
3---0.06 Å2
Refinement stepCycle: LAST / Resolution: 2.41→170.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms47874 0 452 3173 51499
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01949444
X-RAY DIFFRACTIONr_bond_other_d0.0040.0247096
X-RAY DIFFRACTIONr_angle_refined_deg1.5221.97366978
X-RAY DIFFRACTIONr_angle_other_deg1.1773108076
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.96456301
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.81923.7052124
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.62158266
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.75315340
X-RAY DIFFRACTIONr_chiral_restr0.0880.27587
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0256226
X-RAY DIFFRACTIONr_gen_planes_other0.0040.0211206
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_it1.1783.54525031
X-RAY DIFFRACTIONr_mcbond_other1.1783.54525030
X-RAY DIFFRACTIONr_mcangle_it1.9965.31331271
X-RAY DIFFRACTIONr_mcangle_other1.9965.31331272
X-RAY DIFFRACTIONr_scbond_it1.4553.74424413
X-RAY DIFFRACTIONr_scbond_other1.4553.74424413
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.4475.53335668
X-RAY DIFFRACTIONr_long_range_B_refined7.01329.2756181
X-RAY DIFFRACTIONr_long_range_B_other7.01329.27156182
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A259660.07
12O259660.07
21B278860.08
22P278860.08
31C250860.1
32Q250860.1
41D262960.08
42R262960.08
51E274680.07
52S274680.07
61F280480.08
62T280480.08
71G264300.08
72U264300.08
81H253480.08
82V253480.08
91I255980.07
92W255980.07
101J245960.08
102X245960.08
111K234800.09
112Y234800.09
121L247100.06
122Z247100.06
131M250360.07
132a250360.07
141N236760.08
142b236760.08
LS refinement shellResolution: 2.41→2.47 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.363 997 -
Rwork0.353 18302 -
obs--95.09 %
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)
11.67530.49110.73112.12930.38752.3079-0.07640.07390.1172-0.187-0.0626-0.48610.11150.66710.1390.18080.13970.10180.34510.11180.17476.7426205.72091.1234
20.9404-0.010.18612.0044-0.22451.0794-0.06750.2182-0.1818-0.2339-0.0572-0.42260.44430.42040.12470.60970.19430.12840.25990.01570.138564.6909176.85710.0029
32.19890.05210.24183.1853-0.28931.44720.0165-0.0188-0.662-0.22020.0257-0.10880.5981-0.0442-0.04220.7203-0.0883-0.02490.20770.01040.214833.8127169.1653-3.9541
40.6804-0.3142-1.0211.6854-0.11622.414-0.0630.1381-0.2303-0.29560.0480.20050.4561-0.48780.0150.5302-0.1683-0.15470.39120.06280.220110.0897187.992-7.8384
52.5835-0.442-0.23931.0565-0.12832.0557-0.01160.2088-0.3347-0.12790.02260.29260.1964-0.5861-0.0110.1945-0.0602-0.05420.29530.02920.11779.831219.904-9
61.8014-0.74630.00942.37160.0640.97460.03610.15760.2452-0.1469-0.08330.1495-0.1636-0.13890.04720.14150.0138-0.02120.12980.05010.079132.394240.101-7.584
71.02980.3990.23342.9350.65591.5325-0.00760.21560.2379-0.3233-0.0626-0.2735-0.27320.35210.07010.13410.00420.05520.23850.13840.132764.017233.587-3.672
80.3718-0.1017-0.17551.7566-0.40341.0566-0.0173-0.0425-0.09620.0704-0.1586-0.22130.00810.4990.17580.0944-0.03180.01060.3720.10120.080171.352213.93239.439
90.79940.32210.5611.0686-0.98672.3789-0.0436-0.004-0.0354-0.0901-0.1955-0.17350.21250.53810.23910.21910.15910.08620.27880.09780.057966.571186.51839.549
101.40420.3396-0.16250.878-0.00963.1253-0.06690.0849-0.1147-0.2371-0.00880.14580.6458-0.06880.07570.46390.01390.02040.06460.02430.079639.129170.26536.27
111.1141-0.2537-0.63061.69040.30852.5926-0.00430.1463-0.1227-0.26710.06480.17730.461-0.5497-0.06050.3062-0.2168-0.10520.32650.14520.11128.034180.78332.228
121.19870.1983-0.26731.39270.14461.4805-0.00050.0304-0.0024-0.1120.13870.3624-0.0324-0.6235-0.13810.1183-0.0188-0.02230.48430.1940.1525-1.575210.26930.853
131.10260.25830.17561.23660.43522.2572-0.02060.00530.19130.12530.09660.1838-0.5334-0.3703-0.0760.27070.13530.07560.20290.08280.078116.302237.92133.116
141.7132-0.22080.15651.4149-0.16512.35320.0242-0.05170.12140.1214-0.0791-0.0291-0.53540.12160.05490.2933-0.0773-0.00160.09330.02330.019548.774241.43535.653
151.5479-0.09510.56422.0577-0.4961.926-0.0323-0.10960.35510.26390.0580.5867-0.5533-0.5897-0.02560.55390.32430.23370.6830.10220.3325-7.241225.984103.023
161.10590.47590.30841.81790.4151.5573-0.0056-0.24580.03740.28580.07410.517-0.113-0.808-0.06850.29480.07260.16870.74810.22930.2414-8.3567194.1928104.7678
173.2080.71490.12222.80380.39142.66690.1098-0.0972-0.73690.1853-0.00960.38570.6349-0.4686-0.10020.4441-0.0170.02040.41040.13170.31415.2599173.9302109.3716
181.06320.0716-0.48341.00050.14792.8606-0.0772-0.1743-0.25940.06120.03680.14440.29960.14380.04040.2747-0.0030.04170.33940.08550.101245.3622180.4972112.7604
192.4697-0.2013-0.10271.1218-0.05952.08-0.0675-0.3581-0.14110.3068-0.0236-0.1922-0.08140.57510.09110.453-0.1445-0.02880.4160.04190.049958.6017208.8297113.866
203.07140.7768-0.38582.14920.22830.58620.1648-0.46410.15030.1952-0.0974-0.3044-0.56030.3162-0.06740.9524-0.1729-0.00210.321-0.01830.072747.1779236.6674111.707
211.90920.4795-0.18341.6572-0.25381.0127-0.0093-0.24410.52960.32650.03610.1383-0.7009-0.1299-0.02680.99740.24870.15550.3784-0.04880.212516.6438244.0769107.4817
221.04930.69230.13351.4838-0.1490.9539-0.002-0.0771-0.0180.19240.13050.2914-0.3165-0.588-0.12840.36350.24720.16590.46720.12690.13181.6347229.681765.1496
230.4350.00570.54710.98010.47772.6955-0.0133-0.01010.08550.11040.16130.2899-0.1496-0.7983-0.1480.11540.02730.09550.64390.25460.2108-6.2296202.453165.1724
241.2066-0.1173-0.1871.12610.01642.2192-0.0411-0.0995-0.14280.04650.12360.00080.4395-0.2892-0.08240.265-0.1372-0.00420.27260.13370.104311.2566175.998868.5067
251.59390.48-0.78731.55540.15262.8567-0.0875-0.1883-0.1010.0757-0.0549-0.05870.52930.12260.14240.23330.0440.0270.15050.06780.03543.716172.272272.677
260.91190.1598-0.441.4029-0.13492.0913-0.0082-0.1228-0.02570.1609-0.1776-0.20750.07890.57220.18590.0935-0.00430.00190.3510.11380.061465.3256194.753473.8627
271.3792-0.0709-0.22171.1796-0.60042.19840.0228-0.11710.09810.2031-0.1143-0.1777-0.49980.39450.09160.3523-0.1608-0.03010.21970.02230.033560.6327227.460870.972
282.0388-0.06120.27791.4285-0.15972.27550.0126-0.03360.11750.29270.01020.0615-0.68880.0047-0.02280.63020.05070.06320.0963-0.01610.018932.8775244.527367.9061
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 232
2X-RAY DIFFRACTION2B2 - 249
3X-RAY DIFFRACTION3C2 - 238
4X-RAY DIFFRACTION4D9 - 241
5X-RAY DIFFRACTION5E4 - 237
6X-RAY DIFFRACTION6F6 - 244
7X-RAY DIFFRACTION7G2 - 245
8X-RAY DIFFRACTION8H1 - 220
9X-RAY DIFFRACTION8c1 - 5
10X-RAY DIFFRACTION9I1 - 204
11X-RAY DIFFRACTION10J1 - 196
12X-RAY DIFFRACTION11K1 - 200
13X-RAY DIFFRACTION11d1 - 5
14X-RAY DIFFRACTION12L1 - 213
15X-RAY DIFFRACTION13M1 - 216
16X-RAY DIFFRACTION14N1 - 202
17X-RAY DIFFRACTION14e1 - 5
18X-RAY DIFFRACTION15O3 - 232
19X-RAY DIFFRACTION16P2 - 249
20X-RAY DIFFRACTION17Q2 - 240
21X-RAY DIFFRACTION18R9 - 241
22X-RAY DIFFRACTION19S2 - 239
23X-RAY DIFFRACTION20T5 - 244
24X-RAY DIFFRACTION21U2 - 245
25X-RAY DIFFRACTION22V1 - 220
26X-RAY DIFFRACTION22f1 - 5
27X-RAY DIFFRACTION23W1 - 204
28X-RAY DIFFRACTION24X1 - 196
29X-RAY DIFFRACTION25Y1 - 201
30X-RAY DIFFRACTION25g1 - 5
31X-RAY DIFFRACTION26Z1 - 213
32X-RAY DIFFRACTION27a1 - 216
33X-RAY DIFFRACTION28b1 - 203
34X-RAY DIFFRACTION28h1 - 5

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