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- PDB-5nbn: Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80 -

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Basic information

Entry
Database: PDB / ID: 5nbn
TitleCrystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80
Components
  • Actin
  • Actin-like protein ARP8
  • Actin-related protein 4
  • Putative DNA helicase INO80
KeywordsHYDROLASE / Chromatin remodeling / Nanobody / INO80 / SWR1 / NuA4
Function / homology
Function and homology information


cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction / RHOB GTPase cycle / RHOA GTPase cycle / vacuole inheritance / ascospore wall assembly / actin cortical patch / mitotic recombination / regulation of TOR signaling / Swr1 complex ...cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction / RHOB GTPase cycle / RHOA GTPase cycle / vacuole inheritance / ascospore wall assembly / actin cortical patch / mitotic recombination / regulation of TOR signaling / Swr1 complex / kinetochore assembly / Ino80 complex / telomere maintenance via recombination / ATP-dependent chromatin remodeler activity / SWI/SNF complex / regulation of metabolic process / cellular response to stress / establishment of cell polarity / actin filament bundle / NuA4 histone acetyltransferase complex / protein secretion / chromosome, centromeric region / subtelomeric heterochromatin formation / actin filament / structural constituent of cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / endocytosis / double-strand break repair / actin cytoskeleton / chromatin organization / histone binding / transcription by RNA polymerase II / cytoskeleton / chromosome, telomeric region / chromatin remodeling / DNA repair / mRNA binding / DNA-templated transcription / DNA damage response / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Nucleotidyltransferase; domain 5 - #580 / DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / : / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / : / SNF2-like, N-terminal domain superfamily ...Nucleotidyltransferase; domain 5 - #580 / DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / : / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / ATPase, nucleotide binding domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Helicase conserved C-terminal domain / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Alpha-Beta Complex / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / LATRUNCULIN A / Chromatin-remodeling ATPase INO80 / Actin / Actin-related protein 4 / Actin-like protein ARP8
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 4 Å
AuthorsKnoll, K.R. / Eustermann, S. / Hopfner, K.P.
Funding support3items
OrganizationGrant numberCountry
German Research FoundationGRK1721
German Research FoundationGRK1721
European Research CouncilATMMACHINE
CitationJournal: Nat. Struct. Mol. Biol. / Year: 2018
Title: The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling.
Authors: Knoll, K.R. / Eustermann, S. / Niebauer, V. / Oberbeckmann, E. / Stoehr, G. / Schall, K. / Tosi, A. / Schwarz, M. / Buchfellner, A. / Korber, P. / Hopfner, K.P.
History
DepositionMar 2, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 22, 2018Provider: repository / Type: Initial release
Revision 1.1Sep 12, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Sep 19, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 17, 2024Group: Advisory / Data collection ...Advisory / 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 / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Actin-related protein 4
B: Actin-related protein 4
C: Actin
D: Actin
E: Actin-like protein ARP8
F: Actin-like protein ARP8
G: Putative DNA helicase INO80
H: Putative DNA helicase INO80
hetero molecules


Theoretical massNumber of molelcules
Total (without water)376,33518
Polymers373,3038
Non-polymers3,03210
Water00
1
A: Actin-related protein 4
D: Actin
F: Actin-like protein ARP8
H: Putative DNA helicase INO80
hetero molecules


Theoretical massNumber of molelcules
Total (without water)188,1679
Polymers186,6514
Non-polymers1,5165
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13250 Å2
ΔGint-84 kcal/mol
Surface area62490 Å2
MethodPISA
2
B: Actin-related protein 4
C: Actin
E: Actin-like protein ARP8
G: Putative DNA helicase INO80
hetero molecules


Theoretical massNumber of molelcules
Total (without water)188,1679
Polymers186,6514
Non-polymers1,5165
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13450 Å2
ΔGint-83 kcal/mol
Surface area62450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)172.294, 263.909, 241.402
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain F and (resseq 257:299 or resseq 301:302 or resseq...
21(chain E and (resseq 257:299 or resseq 301:302 or resseq...
12(chain A and (resseq 15:59 or resseq 61:171 or (resid...
22(chain B and (resseq 15:59 or resseq 61:171 or (resid...
13(chain C and ((resid 5 and (name N or name...
23(chain D and ((resid 5 and (name O or name...
14(chain H and (resseq 472 or resseq 474:481 or resseq 483:557))
24(chain G and (resseq 472 or resseq 474:481 or resseq 483:557))

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNLYSLYS(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 2994 - 46
121TRPTRPLEULEU(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF301 - 30248 - 49
131GLUGLUSERSER(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF305 - 30752 - 54
141LEULEUMETMET(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF315 - 33862 - 85
151TYRTYRTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF34087
161ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
171ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
181ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
191ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
1101ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
1111ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
1121ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
1131ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
1141ASNASNTYRTYR(chain F and (resseq 257:299 or resseq 301:302 or resseq...FF257 - 8814 - 628
211ASNASNLYSLYS(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 2994 - 46
221TRPTRPLEULEU(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE301 - 30248 - 49
231GLUGLUSERSER(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE305 - 30752 - 54
241LEULEUMETMET(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE315 - 33862 - 85
251TYRTYRTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE34087
261ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
271ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
281ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
291ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
2101ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
2111ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
2121ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
2131ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
2141ASNASNTYRTYR(chain E and (resseq 257:299 or resseq 301:302 or resseq...EE257 - 8814 - 628
112SERSERGLUGLU(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA15 - 5915 - 59
122SERSERVALVAL(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA61 - 17161 - 171
132ASPASPASPASP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA172172
142SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
152SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
162SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
172SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
182SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
192SERSERATPATP(chain A and (resseq 15:59 or resseq 61:171 or (resid...AA - J15 - 50215
212SERSERGLUGLU(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB15 - 5915 - 59
222SERSERVALVAL(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB61 - 17161 - 171
232ASPASPASPASP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB172172
242SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
252SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
262SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
272SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
282SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
292SERSERATPATP(chain B and (resseq 15:59 or resseq 61:171 or (resid...BB - L15 - 50215
113VALVALVALVAL(chain C and ((resid 5 and (name N or name...CC55
123VALVALCYSCYS(chain C and ((resid 5 and (name N or name...CC5 - 3745 - 374
133VALVALCYSCYS(chain C and ((resid 5 and (name N or name...CC5 - 3745 - 374
143VALVALCYSCYS(chain C and ((resid 5 and (name N or name...CC5 - 3745 - 374
153VALVALCYSCYS(chain C and ((resid 5 and (name N or name...CC5 - 3745 - 374
163VALVALCYSCYS(chain C and ((resid 5 and (name N or name...CC5 - 3745 - 374
213VALVALVALVAL(chain D and ((resid 5 and (name O or name...DD55
223VALVALCYSCYS(chain D and ((resid 5 and (name O or name...DD5 - 3745 - 374
233VALVALCYSCYS(chain D and ((resid 5 and (name O or name...DD5 - 3745 - 374
243VALVALCYSCYS(chain D and ((resid 5 and (name O or name...DD5 - 3745 - 374
253VALVALCYSCYS(chain D and ((resid 5 and (name O or name...DD5 - 3745 - 374
263VALVALCYSCYS(chain D and ((resid 5 and (name O or name...DD5 - 3745 - 374
114THRTHRTHRTHR(chain H and (resseq 472 or resseq 474:481 or resseq 483:557))HH47212
124THRTHRALAALA(chain H and (resseq 472 or resseq 474:481 or resseq 483:557))HH474 - 48114 - 21
134LYSLYSILEILE(chain H and (resseq 472 or resseq 474:481 or resseq 483:557))HH483 - 55723 - 97
214THRTHRTHRTHR(chain G and (resseq 472 or resseq 474:481 or resseq 483:557))GG47212
224THRTHRALAALA(chain G and (resseq 472 or resseq 474:481 or resseq 483:557))GG474 - 48114 - 21
234LYSLYSILEILE(chain G and (resseq 472 or resseq 474:481 or resseq 483:557))GG483 - 55723 - 97

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 4 types, 8 molecules ABCDEFGH

#1: Protein Actin-related protein 4 / Actin-like protein ARP4 / Actin-like protein 4


Mass: 54894.684 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Actin-related protein 4 (ATP bound)
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: ARP4, ACT3, YJL081C, J1012 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P80428
#2: Protein Actin


Mass: 41748.566 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Actin (ATP and Latrunculin A bound)
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: ACT1, ABY1, END7, YFL039C / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P60010
#3: Protein Actin-like protein ARP8


Mass: 71987.453 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: N-terminal truncated construct of Actin-related protein 8(residues 255-881) in a nucleotide free state.
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: ARP8, YOR141C, YOR3348C / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q12386
#4: Protein Putative DNA helicase INO80 / Inositol-requiring protein 80


Mass: 18020.693 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: HSA/DBINO domain of the Ino80 protein (residues 461-598) carrying a C-terminal StrepTag.
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: INO80, YGL150C, G1880 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P53115, DNA helicase

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Non-polymers , 3 types, 10 molecules

#5: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#6: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#7: Chemical ChemComp-LAR / LATRUNCULIN A / 4-(17-HYDROXY-5,12-DIMETHYL-3-OXO-2,16-DIOXABICYCLO[13.3.1]NONADECA-4,8,10-TRIEN-17-YL)-2-THIAZOLIDINONE


Mass: 421.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H31NO5S

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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: 3.68 Å3/Da / Density % sol: 66.54 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop
Details: 0.1 M sodium citrate tribasic dihydrate, 18% (w/v) polyethylene glycol 3,350, latrunculin A solved in DMSO molar ration 1:1.5 (protein : latrunculin A)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 29, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 4→49.43 Å / Num. obs: 46724 / % possible obs: 99.9 % / Redundancy: 9.6 % / Biso Wilson estimate: 114.95 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.289 / Rpim(I) all: 0.098 / Rrim(I) all: 0.306 / Net I/σ(I): 8.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsCC1/2Rpim(I) allRrim(I) all% possible all
4-4.14101.3452.30.6880.4451.418100
15.49-49.438.40.07126.40.9960.0250.07596.8

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation6.47 Å49.4 Å
Translation6.47 Å49.4 Å

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Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
XDSdata reduction
Aimless0.5.27data scaling
PHASER2.6.1phasing
PDB_EXTRACT3.22data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4AM6

4am6


Resolution: 4→49.399 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.54
RfactorNum. reflection% reflection
Rfree0.2422 2379 5.1 %
Rwork0.1927 --
obs0.1953 46675 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 282.05 Å2 / Biso mean: 121.6789 Å2 / Biso min: 34.6 Å2
Refinement stepCycle: final / Resolution: 4→49.399 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23029 0 186 0 23215
Biso mean--101.03 --
Num. residues----2898
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00223715
X-RAY DIFFRACTIONf_angle_d0.67532154
X-RAY DIFFRACTIONf_chiral_restr0.0633596
X-RAY DIFFRACTIONf_plane_restr0.0044105
X-RAY DIFFRACTIONf_dihedral_angle_d11.97714308
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11F5441X-RAY DIFFRACTION6.154TORSIONAL
12E5441X-RAY DIFFRACTION6.154TORSIONAL
21A3839X-RAY DIFFRACTION6.154TORSIONAL
22B3839X-RAY DIFFRACTION6.154TORSIONAL
31C3317X-RAY DIFFRACTION6.154TORSIONAL
32D3317X-RAY DIFFRACTION6.154TORSIONAL
41H842X-RAY DIFFRACTION6.154TORSIONAL
42G842X-RAY DIFFRACTION6.154TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 17

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
4.0001-4.08170.30761380.259725542692100
4.0817-4.17040.29911640.247825802744100
4.1704-4.26730.33391460.229525662712100
4.2673-4.3740.3071340.215625922726100
4.374-4.49220.2441140.207825952709100
4.4922-4.62430.25291260.196525992725100
4.6243-4.77340.2481300.190526042734100
4.7734-4.94390.24551490.186125522701100
4.9439-5.14160.24671550.19325752730100
5.1416-5.37530.23361320.190526122744100
5.3753-5.65840.27271460.21325882734100
5.6584-6.01230.26731610.198225832744100
6.0123-6.47560.23421230.193326242747100
6.4756-7.12550.2431310.191626402771100
7.1255-8.15260.22081310.170526312762100
8.1526-10.25630.1871660.139226482814100
10.2563-49.40260.21051330.19452753288699

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