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- PDB-6hv5: Yeast 20S proteasome with human beta2i (1-53) in complex with 4 -

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Basic information

Entry
Database: PDB / ID: 6hv5
TitleYeast 20S proteasome with human beta2i (1-53) in complex with 4
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


spermatoproteasome complex / Proteasome assembly / proteasome core complex / proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A ...spermatoproteasome complex / Proteasome assembly / proteasome core complex / proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / 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 / humoral immune response / endopeptidase activator activity / proteasome assembly / Ub-specific processing proteases / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / T cell proliferation / Neutrophil degranulation / proteasome complex / cell morphogenesis / peroxisome / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleoplasm / 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 B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-GQH / 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 ...Chem-GQH / 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 / Proteasome subunit beta type-10
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 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 10, 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 1.3Nov 6, 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-10,Proteasome subunit beta type-2
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-10,Proteasome subunit beta type-2
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)732,43042
Polymers729,70928
Non-polymers2,72014
Water4,468248
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)134.690, 300.440, 144.130
Angle α, β, γ (deg.)90.00, 112.59, 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(-0.999328, -0.00454, 0.03638), (-0.001707, -0.985466, -0.169865), (0.036623, -0.169813, 0.984796)66.90842, -288.9805, -25.65078

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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)
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)
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)
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)
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)
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)
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)
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-10,Proteasome subunit beta type-2 / Low molecular mass protein 10 / Macropain subunit MECl-1 / Multicatalytic endopeptidase complex ...Low molecular mass protein 10 / Macropain subunit MECl-1 / Multicatalytic endopeptidase complex subunit MECl-1 / Proteasome MECl-1 / Proteasome subunit beta-2i / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


Mass: 24443.674 Da / Num. of mol.: 2
Mutation: Chimera: 1-53 Homo sapiens,Chimera: 1-53 Homo sapiens
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Gene: PSMB10, LMP10, MECL1, PUP1, YOR157C / Production host: Saccharomyces cerevisiae S288C (yeast)
References: UniProt: P40306, UniProt: P25043, 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)
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)
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)
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)
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)
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)
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 4 types, 262 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-GQH / (2~{S})-~{N}-[(2~{S})-1-[[(2~{S})-1-[4-(aminomethyl)phenyl]-4-methylsulfonyl-butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]-2-[[(2~{S})-2-azido-3-phenyl-propanoyl]amino]-4-methyl-pentanamide


Mass: 613.771 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C30H43N7O5S
#18: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 248 / 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
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 205492 / % possible obs: 97.6 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 12.5
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 3.2 / % possible all: 99.3

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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: 3→15 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.943 / SU B: 40.341 / SU ML: 0.293 / Cross valid method: THROUGHOUT / ESU R Free: 0.319 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20401 10194 5 %RANDOM
Rwork0.17331 ---
obs0.17485 193694 96.91 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 78.206 Å2
Baniso -1Baniso -2Baniso -3
1-4.23 Å2-0 Å2-2.24 Å2
2---6.32 Å2-0 Å2
3---2.94 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49340 0 182 249 49771
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01950416
X-RAY DIFFRACTIONr_bond_other_d0.0020.0246982
X-RAY DIFFRACTIONr_angle_refined_deg1.1871.96768204
X-RAY DIFFRACTIONr_angle_other_deg0.9043.001109003
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.83656311
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.29224.4292251
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.817158742
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.56115282
X-RAY DIFFRACTIONr_chiral_restr0.070.27685
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0256277
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0210129
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_it2.6715.09125334
X-RAY DIFFRACTIONr_mcbond_other2.6715.09125333
X-RAY DIFFRACTIONr_mcangle_it3.6837.62631615
X-RAY DIFFRACTIONr_mcangle_other3.6837.62631616
X-RAY DIFFRACTIONr_scbond_it2.5085.4225082
X-RAY DIFFRACTIONr_scbond_other2.5085.41925082
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.1468.01136589
X-RAY DIFFRACTIONr_long_range_B_refined4.1658.6653130
X-RAY DIFFRACTIONr_long_range_B_other4.14458.6553102
X-RAY DIFFRACTIONr_rigid_bond_restr0.869397398
X-RAY DIFFRACTIONr_sphericity_free37.1815193
X-RAY DIFFRACTIONr_sphericity_bonded7.402596560
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1010A3063tight positional0.010.05
1111A3247tight positional0.030.05
1212A3389tight positional0.010.05
1313A3564tight positional0.010.05
1414A2919tight positional0.010.05
11A3765tight thermal4.750.5
22B3714tight thermal3.50.5
33C3685tight thermal9.230.5
44D3538tight thermal4.650.5
55E3459tight thermal5.580.5
66F3693tight thermal4.020.5
77G3724tight thermal30.5
88H3373tight thermal2.80.5
99I3091tight thermal2.240.5
1010J3063tight thermal2.620.5
1111K3247tight thermal2.470.5
1212L3389tight thermal2.350.5
1313M3564tight thermal2.220.5
1414N2919tight thermal2.450.5
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.337 740 -
Rwork0.323 14052 -
obs--99.36 %
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)
10.67-0.26090.36530.6362-0.01650.4451-0.09330.10650.00330.24410.0097-0.254-0.15140.00460.08360.375-0.0892-0.1180.1567-0.05460.412866.9389-91.667845.7056
20.26380.04240.31910.62030.29061.2119-0.11610.0467-0.0072-0.0931-0.0129-0.1707-0.22220.22250.1290.342-0.07950.04580.2230.05980.345259.4503-87.574816.1675
30.3960.26140.13960.5296-0.22760.7131-0.02150.00860.0518-0.1280.08270.0223-0.11490.1027-0.06120.4329-0.022-0.05540.19220.04810.263932.0766-87.29430.8754
40.4670.0812-0.15310.8113-0.1540.0839-0.0084-0.13740.0281-0.16450.00950.3642-0.00250.0556-0.00120.32620.1001-0.17150.15210.11710.48382.9465-89.912313.5841
50.23640.32630.22380.61040.14860.7379-0.0894-0.04460.07920.02490.02030.3579-0.2428-0.04910.06910.21470.16710.11190.1960.03060.7123-3.286-94.228445.5664
60.34840.21770.11810.4644-0.1850.28010.0409-0.08460.14460.1552-0.07620.2163-0.1077-0.04850.03530.49190.07910.15440.2202-0.13070.329515.361-94.815469.6858
70.21770.00450.03310.39510.21681.14960.04140.04540.07510.256-0.0563-0.1032-0.12870.01970.01490.5656-0.0522-0.10430.143-0.08920.225947.7654-93.204370.9022
80.1403-0.1849-0.13440.41450.24250.35270.05770.12320.08520.0513-0.0492-0.3372-0.14880.0173-0.00850.2846-0.0519-0.1650.2541-0.01420.474567.817-129.27347.1453
90.7112-0.2917-0.06732.03330.29490.08510.05480.0159-0.1041-0.1043-0.0335-0.3761-0.06480.0003-0.02130.1472-0.03130.09120.2578-0.00480.432168.4274-127.110720.6047
100.37110.01160.20441.3506-0.3240.28030.0172-0.05320.0547-0.32870.0556-0.01950.04210.0278-0.07280.3527-0.02070.05220.23030.00080.18744.6663-126.4251-0.7935
110.52350.6580.29371.13110.28560.6159-0.0141-0.04730.0503-0.18570.05420.3078-0.07710.0742-0.04010.25580.0374-0.19640.20940.0610.313610.8007-130.78342.5965
120.23930.17120.25110.98250.10550.3440.0759-0.07430.0303-0.0421-0.01180.45540.0003-0.091-0.06410.12910.0673-0.0220.23610.07980.5684-4.5192-134.282228.6522
130.32850.06860.10610.8251-0.06820.04690.059-0.0670.0670.2972-0.07920.18130.0074-0.00220.02020.3240.01840.14670.25090.00080.29237.9031-137.805360.4074
140.50180.3685-0.2981.136-0.10750.19230.08030.00860.02340.3213-0.0475-0.05720.0009-0.0028-0.03280.5221-0.012-0.10950.2092-0.04920.071840.0397-133.795870.8106
151.0111-0.3513-0.21150.82530.02940.2495-0.06910.0444-0.0160.16480.06140.17560.1999-0.05970.00760.3334-0.1008-0.1620.10440.0880.44272.2505-206.560936.7549
160.47660.55160.26940.80850.35470.618-0.0878-0.0930.0484-0.1160.02460.07160.0904-0.07780.06320.3236-0.0326-0.22140.1621-0.06010.37078.6346-205.37576.6859
170.67490.46880.04290.6414-0.06820.59020.14860.0154-0.0854-0.33430.01350.13330.11860.0937-0.16210.65210.0735-0.26470.0719-0.11530.31635.7554-203.1436-9.2846
180.6762-0.05040.310.91810.08390.1650.1366-0.1485-0.0111-0.4354-0.1433-0.33620.0354-0.09480.00660.41210.1440.14130.1737-0.08860.457265.1975-202.66592.9976
190.46380.57080.00140.8073-0.22210.93170.02450.0706-0.22370.02320.0803-0.44480.20550.0793-0.10480.15510.1333-0.16950.1368-0.12690.846672.444-203.727534.8045
200.5540.4067-0.01250.32160.09270.71290.1011-0.0695-0.28570.1336-0.0665-0.26990.0626-0.0033-0.03470.48460.0257-0.39440.0930.10170.507554.5944-207.350559.1886
210.0531-0.13260.16330.5282-0.33820.67160.04370.0058-0.05250.18570.02740.1310.09790.0249-0.07110.5383-0.0451-0.19420.10160.11550.297322.2709-209.463961.079
220.0669-0.09570.13210.3543-0.27040.30030.10480.0221-0.03420.0170.00430.30690.09260.0253-0.1090.2409-0.04210.0030.25180.09360.50931.6367-169.472845.2579
230.7883-0.54170.21261.5712-0.49820.1642-0.0182-0.03520.0606-0.0720.08750.32350.0163-0.0101-0.06940.1927-0.021-0.20750.20070.03570.44670.0483-167.311418.1643
240.36310.0493-0.12481.32030.05480.0513-0.0184-0.0298-0.0673-0.370.0383-0.0182-0.01420.019-0.01990.42990.0018-0.17790.1827-0.03790.165423.1918-164.2484-3.7721
250.38520.41720.13491.6087-0.09080.40530.00180.0572-0.0421-0.2350.0883-0.33130.0720.0735-0.090.26330.0610.14880.2711-0.08820.291857.1472-160.4774-0.7129
260.26660.0699-0.12031.2322-0.2830.37610.09140.0227-0.0545-0.0606-0.0899-0.53450.06010.0603-0.00160.09170.09930.0010.2481-0.06760.583973.2339-161.437325.0825
270.13410.15730.05151.32280.1430.06090.02080.0066-0.10560.3498-0.0263-0.3082-0.022-0.0580.00550.30340.0238-0.26630.19840.0080.34261.8328-163.432957.2865
280.32090.23980.01210.67570.14560.06910.13190.0685-0.02650.315-0.0762-0.04370.0238-0.0878-0.05570.4877-0.0179-0.07920.18410.08120.139830.0436-169.294767.8993
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 - 226
9X-RAY DIFFRACTION9I1 - 204
10X-RAY DIFFRACTION10J1 - 195
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 - 240
18X-RAY DIFFRACTION18R1 - 242
19X-RAY DIFFRACTION19S3 - 233
20X-RAY DIFFRACTION20T2 - 244
21X-RAY DIFFRACTION21U2 - 242
22X-RAY DIFFRACTION22V1 - 223
23X-RAY DIFFRACTION23W1 - 204
24X-RAY DIFFRACTION24X1 - 195
25X-RAY DIFFRACTION25Y1 - 212
26X-RAY DIFFRACTION26Z1 - 222
27X-RAY DIFFRACTION27a1 - 233
28X-RAY DIFFRACTION28b1 - 196

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