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- PDB-4iem: Human apurinic/apyrimidinic endonuclease (APE1) with product DNA ... -

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Basic information

Entry
Database: PDB / ID: 4iem
TitleHuman apurinic/apyrimidinic endonuclease (APE1) with product DNA and Mg2+
Components
  • DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
  • DNA (5'-D(*GP*CP*TP*AP*C)-3')
  • DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
  • DNA-(apurinic or apyrimidinic site) lyaseDNA-(apurinic or apyrimidinic site) lyase
KeywordsHYDROLASE / LYASE/DNA / metalloprotein / DNA damage / DNA repair / base excision repair / protein-DNA / REF1 / nuclease / LYASE-DNA complex
Function / homology
Function and homology information


Resolution of Abasic Sites (AP sites) / class II DNA-(apurinic or apyrimidinic site) endonuclease activity / phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands / telomere maintenance via base-excision repair / site-specific endodeoxyribonuclease activity, specific for altered base / DNA-(abasic site) binding / double-stranded DNA exodeoxyribonuclease activity / double-stranded telomeric DNA binding / exodeoxyribonuclease III / double-stranded DNA 3'-5' DNA exonuclease activity ...Resolution of Abasic Sites (AP sites) / class II DNA-(apurinic or apyrimidinic site) endonuclease activity / phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands / telomere maintenance via base-excision repair / site-specific endodeoxyribonuclease activity, specific for altered base / DNA-(abasic site) binding / double-stranded DNA exodeoxyribonuclease activity / double-stranded telomeric DNA binding / exodeoxyribonuclease III / double-stranded DNA 3'-5' DNA exonuclease activity / phosphodiesterase I activity / Displacement of DNA glycosylase by APEX1 / 3'-5'-DNA exonuclease activity / phosphoric diester hydrolase activity / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / uracil DNA N-glycosylase activity / DNA demethylation / DNA catabolic process / Resolution of AP sites via the multiple-nucleotide patch replacement pathway / Abasic sugar-phosphate removal via the single-nucleotide replacement pathway / PCNA-Dependent Long Patch Base Excision Repair / POLB-Dependent Long Patch Base Excision Repair / base-excision repair, gap-filling / DNA-(apurinic or apyrimidinic site) endonuclease activity / 3'-5' exonuclease activity / regulation of mRNA stability / telomere maintenance / cell redox homeostasis / DNA endonuclease activity / base-excision repair / chromatin DNA binding / transcription corepressor activity / RNA-DNA hybrid ribonuclease activity / endonuclease activity / regulation of apoptotic process / DNA recombination / damaged DNA binding / chromosome, telomeric region / transcription coactivator activity / oxidoreductase activity / ribosome / nuclear speck / DNA repair / centrosome / nucleolus / perinuclear region of cytoplasm / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / RNA binding / nucleoplasm / metal ion binding / nucleus / cytoplasm
Similarity search - Function
AP endonucleases family 1 signature 2. / AP endonuclease 1, conserved site / AP endonucleases family 1 signature 3. / AP endonuclease 1, binding site / AP endonucleases family 1 signature 1. / AP endonuclease 1 / AP endonucleases family 1 profile. / Deoxyribonuclease I; Chain A / Endonuclease/exonuclease/phosphatase / Endonuclease/exonuclease/phosphatase ...AP endonucleases family 1 signature 2. / AP endonuclease 1, conserved site / AP endonucleases family 1 signature 3. / AP endonuclease 1, binding site / AP endonucleases family 1 signature 1. / AP endonuclease 1 / AP endonucleases family 1 profile. / Deoxyribonuclease I; Chain A / Endonuclease/exonuclease/phosphatase / Endonuclease/exonuclease/phosphatase / Endonuclease/Exonuclease/phosphatase family / Endonuclease/exonuclease/phosphatase superfamily / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
DNA / DNA (> 10) / DNA repair nuclease/redox regulator APEX1
Similarity search - Component
Biological speciesHomo sapiens (human)
Synthetic DNA (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3936 Å
AuthorsTsutakawa, S.E. / Mol, C.D. / Arvai, A.S. / Tainer, J.A.
CitationJournal: J.Biol.Chem. / Year: 2013
Title: Conserved Structural Chemistry for Incision Activity in Structurally Non-homologous Apurinic/Apyrimidinic Endonuclease APE1 and Endonuclease IV DNA Repair Enzymes.
Authors: Tsutakawa, S.E. / Shin, D.S. / Mol, C.D. / Izumi, T. / Arvai, A.S. / Mantha, A.K. / Szczesny, B. / Ivanov, I.N. / Hosfield, D.J. / Maiti, B. / Pique, M.E. / Frankel, K.A. / Hitomi, K. / ...Authors: Tsutakawa, S.E. / Shin, D.S. / Mol, C.D. / Izumi, T. / Arvai, A.S. / Mantha, A.K. / Szczesny, B. / Ivanov, I.N. / Hosfield, D.J. / Maiti, B. / Pique, M.E. / Frankel, K.A. / Hitomi, K. / Cunningham, R.P. / Mitra, S. / Tainer, J.A.
History
DepositionDec 13, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 13, 2013Group: Database references / Derived calculations / Other
Revision 1.2Apr 10, 2013Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
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_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_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA-(apurinic or apyrimidinic site) lyase
E: DNA (5'-D(*GP*CP*TP*AP*C)-3')
F: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
G: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
B: DNA-(apurinic or apyrimidinic site) lyase
H: DNA (5'-D(*GP*CP*TP*AP*C)-3')
I: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
J: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
C: DNA-(apurinic or apyrimidinic site) lyase
K: DNA (5'-D(*GP*CP*TP*AP*C)-3')
L: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
M: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
D: DNA-(apurinic or apyrimidinic site) lyase
N: DNA (5'-D(*GP*CP*TP*AP*C)-3')
O: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
P: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,49632
Polymers168,11916
Non-polymers37716
Water4,900272
1
A: DNA-(apurinic or apyrimidinic site) lyase
E: DNA (5'-D(*GP*CP*TP*AP*C)-3')
F: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
G: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,19511
Polymers42,0304
Non-polymers1657
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4790 Å2
ΔGint-75 kcal/mol
Surface area14070 Å2
MethodPISA
2
B: DNA-(apurinic or apyrimidinic site) lyase
H: DNA (5'-D(*GP*CP*TP*AP*C)-3')
I: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
J: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,1238
Polymers42,0304
Non-polymers934
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4450 Å2
ΔGint-51 kcal/mol
Surface area13660 Å2
MethodPISA
3
C: DNA-(apurinic or apyrimidinic site) lyase
K: DNA (5'-D(*GP*CP*TP*AP*C)-3')
L: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
M: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,0786
Polymers42,0304
Non-polymers492
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4430 Å2
ΔGint-49 kcal/mol
Surface area14150 Å2
MethodPISA
4
D: DNA-(apurinic or apyrimidinic site) lyase
N: DNA (5'-D(*GP*CP*TP*AP*C)-3')
O: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')
P: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,1007
Polymers42,0304
Non-polymers703
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4370 Å2
ΔGint-55 kcal/mol
Surface area13630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.639, 74.090, 112.138
Angle α, β, γ (deg.)90.00, 111.98, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A and (resseq 44:110 or resseq 113:318 ) and (not element H)
21chain B and (resseq 44:110 or resseq 113:318 ) and (not element H)
31chain C and (resseq 44:110 or resseq 113:318 ) and (not element H)
41chain D and (resseq 44:110 or resseq 113:318 ) and (not element H)
12chain G and (resseq 513:522 ) and (not element H)
22chain J and (resseq 513:522 ) and (not element H)
32chain M and (resseq 513:522 ) and (not element H)
42chain P and (resseq 513:522 ) and (not element H)

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain 'A' and (resseq 44:110 or resseq 113:318 ) and (not element H)A44 - 110
121chain 'A' and (resseq 44:110 or resseq 113:318 ) and (not element H)A113 - 318
211chain 'B' and (resseq 44:110 or resseq 113:318 ) and (not element H)B44 - 110
221chain 'B' and (resseq 44:110 or resseq 113:318 ) and (not element H)B113 - 318
311chain 'C' and (resseq 44:110 or resseq 113:318 ) and (not element H)C44 - 110
321chain 'C' and (resseq 44:110 or resseq 113:318 ) and (not element H)C113 - 318
411chain 'D' and (resseq 44:110 or resseq 113:318 ) and (not element H)D44 - 110
421chain 'D' and (resseq 44:110 or resseq 113:318 ) and (not element H)D113 - 318
112chain 'G' and (resseq 513:522 ) and (not element H)G0
212chain 'J' and (resseq 513:522 ) and (not element H)J0
312chain 'M' and (resseq 513:522 ) and (not element H)M0
412chain 'P' and (resseq 513:522 ) and (not element H)P0

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(-0.581627, -0.731172, -0.356507), (-0.667779, 0.178901, 0.722541), (-0.464522, 0.658317, -0.592315)53.399399, -6.19556, 33.681198
2given(0.89414, 0.444622, 0.053154), (-0.444112, 0.865349, 0.232241), (0.057262, -0.231262, 0.971205)-57.404999, -24.688101, 0.042935
3given(-0.798439, -0.580856, -0.158435), (-0.532119, 0.557681, 0.637057), (-0.281682, 0.592957, -0.754359)117.220001, -5.88341, 24.749599
4given(-0.581135, -0.727055, -0.365613), (-0.680993, 0.188478, 0.707619), (-0.445568, 0.660202, -0.60465)53.544498, -5.39382, 33.378502
5given(0.889803, 0.453482, 0.051039), (-0.452596, 0.862652, 0.225806), (0.05837, -0.224023, 0.972834)-57.595402, -23.887501, -0.295164
6given(-0.798711, -0.580556, -0.158163), (-0.533259, 0.561187, 0.633012), (-0.27874, 0.589935, -0.757813)117.259003, -5.82706, 24.8011
7given(-0.549254, -0.759527, -0.348481), (-0.68903, 0.175673, 0.70312), (-0.472819, 0.626305, -0.619826)52.460899, -4.46962, 35.905499
8given(0.910785, 0.411567, 0.03291), (-0.40728, 0.882488, 0.235241), (0.067775, -0.227658, 0.97138)-56.409801, -26.816999, -0.359558
9given(-0.789146, -0.597013, -0.144306), (-0.548883, 0.580038, 0.6019), (-0.275639, 0.554194, -0.785425)116.920998, -4.34031, 27.8734
10given(-0.593273, -0.733033, -0.332699), (-0.655148, 0.199514, 0.72868), (-0.467769, 0.650274, -0.598612)53.018299, -7.43813, 34.388
11given(0.875337, 0.481549, 0.043544), (-0.476317, 0.843325, 0.24885), (0.083112, -0.238568, 0.967563)-58.132198, -22.2873, -0.464967
12given(-0.803601, -0.581267, -0.127887), (-0.519189, 0.579585, 0.628112), (-0.290979, 0.571149, -0.767542)116.573997, -8.06579, 27.690701
13given(-0.572453, -0.734266, -0.364897), (-0.66609, 0.156934, 0.729175), (-0.478144, 0.660473, -0.578925)53.269901, -5.83705, 33.828701
14given(0.87678, 0.478297, 0.04989), (-0.477268, 0.852767, 0.212139), (0.058921, -0.20981, 0.975965)-57.882198, -22.3561, -0.89294
15given(-0.783895, -0.595282, -0.176489), (-0.544635, 0.522764, 0.655813), (-0.298132, 0.610211, -0.734003)117.120003, -2.90258, 24.9592

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
DNA-(apurinic or apyrimidinic site) lyase / DNA-(apurinic or apyrimidinic site) lyase / APEX nuclease / APEN / Apurinic-apyrimidinic endonuclease 1 / AP endonuclease 1 / APE-1 / REF-1 / ...APEX nuclease / APEN / Apurinic-apyrimidinic endonuclease 1 / AP endonuclease 1 / APE-1 / REF-1 / Redox factor-1 / DNA-(apurinic or apyrimidinic site) lyase / mitochondrial


Mass: 35475.293 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APE, APE1, APEX, APEX1, APX, HAP1, REF1 / Production host: Escherichia coli (E. coli)
References: UniProt: P27695, Hydrolases; Acting on ester bonds, DNA-(apurinic or apyrimidinic site) lyase

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DNA chain , 3 types, 12 molecules EHKNFILOGJMP

#2: DNA chain
DNA (5'-D(*GP*CP*TP*AP*C)-3')


Mass: 1480.012 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: DNA oligonucleotide synthesis / Source: (synth.) Synthetic DNA (others)
#3: DNA chain
DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3')


Mass: 1700.131 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: DNA oligonucleotide synthesis / Source: (synth.) Synthetic DNA (others)
#4: DNA chain
DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3')


Mass: 3374.210 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: DNA oligonucleotide synthesis / Source: (synth.) Synthetic DNA (others)

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Non-polymers , 3 types, 288 molecules

#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Na
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 272 / 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: 2.4 Å3/Da / Density % sol: 48.7 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 50 mM MES pH 6.0, 200 mM LiSO4, and 25% mPEG 2K, vapor diffusion, hanging drop, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.97956 Å
DetectorDate: Jul 1, 2001
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97956 Å / Relative weight: 1
ReflectionRedundancy: 3.1 % / Number: 177329 / Rmerge(I) obs: 0.064 / Χ2: 1.08 / D res high: 2.4 Å / D res low: 30 Å / Num. obs: 56733 / % possible obs: 90.2
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
5.163098.710.0350.9683.1
4.15.1696.710.0460.9933
3.584.19110.0541.0353
3.263.5887.510.0671.1323.1
3.023.2687.110.0931.1293.1
2.853.0286.910.1361.1473.2
2.72.8587.210.1851.1383.2
2.592.78810.2381.1493.2
2.492.5989.110.3131.0983.2
2.42.4989.810.4021.0623.2
ReflectionResolution: 2.3926→30 Å / Num. obs: 56727 / % possible obs: 90.05 %

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
AMoREphasing
PHENIX1.8_1069refinement
PDB_EXTRACT3.11data extraction
DENZOdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3936→29.643 Å / Occupancy max: 1 / Occupancy min: 0.32 / SU ML: 0.32 / σ(F): 1.34 / Phase error: 27.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2462 2868 5.06 %
Rwork0.2079 --
obs0.2099 56705 90.01 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 54.8586 Å2
Refinement stepCycle: LAST / Resolution: 2.3936→29.643 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8809 1697 16 272 10794
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01711009
X-RAY DIFFRACTIONf_angle_d0.91815283
X-RAY DIFFRACTIONf_dihedral_angle_d19.5124209
X-RAY DIFFRACTIONf_chiral_restr0.0471622
X-RAY DIFFRACTIONf_plane_restr0.0031681
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2154X-RAY DIFFRACTIONPOSITIONAL0.978
12B2154X-RAY DIFFRACTIONPOSITIONAL0.978
13C2170X-RAY DIFFRACTIONPOSITIONAL0.768
14D2170X-RAY DIFFRACTIONPOSITIONAL0.846
21G208X-RAY DIFFRACTIONPOSITIONAL0.242
22J208X-RAY DIFFRACTIONPOSITIONAL0.242
23M208X-RAY DIFFRACTIONPOSITIONAL0.186
24P208X-RAY DIFFRACTIONPOSITIONAL0.301
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3936-2.43480.37561320.28542555X-RAY DIFFRACTION86
2.4348-2.47910.34321550.27242630X-RAY DIFFRACTION89
2.4791-2.52670.33471290.27722658X-RAY DIFFRACTION89
2.5267-2.57830.34051400.26982638X-RAY DIFFRACTION89
2.5783-2.63430.32281650.2592607X-RAY DIFFRACTION88
2.6343-2.69550.29421340.25322620X-RAY DIFFRACTION88
2.6955-2.76290.34141500.26172577X-RAY DIFFRACTION87
2.7629-2.83760.27811250.2542616X-RAY DIFFRACTION87
2.8376-2.9210.31641380.25562575X-RAY DIFFRACTION87
2.921-3.01520.34181380.25272576X-RAY DIFFRACTION87
3.0152-3.12280.29391470.24632626X-RAY DIFFRACTION87
3.1228-3.24770.25141210.23392585X-RAY DIFFRACTION87
3.2477-3.39530.27811340.22062617X-RAY DIFFRACTION87
3.3953-3.57410.24631420.2072620X-RAY DIFFRACTION88
3.5741-3.79760.23651510.19762676X-RAY DIFFRACTION90
3.7976-4.09010.22911430.18862770X-RAY DIFFRACTION92
4.0901-4.50040.19711470.17562852X-RAY DIFFRACTION95
4.5004-5.14870.20311540.17592974X-RAY DIFFRACTION98
5.1487-6.47560.21611660.18353001X-RAY DIFFRACTION99
6.4756-29.64510.17411570.16783064X-RAY DIFFRACTION98
Refinement TLS params.Method: refined / Origin x: 45.2061 Å / Origin y: 29.162 Å / Origin z: 22.322 Å
111213212223313233
T0.3301 Å20.0128 Å20.0212 Å2-0.3413 Å2-0.0252 Å2--0.2634 Å2
L0.9093 °20.8234 °20.0257 °2-0.9301 °20.1705 °2--0.1084 °2
S0.2309 Å °-0.3189 Å °0.0861 Å °0.2853 Å °-0.2003 Å °0.088 Å °0.0803 Å °0.0545 Å °-0.0321 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA41 - 318
2X-RAY DIFFRACTION1allA401 - 596
3X-RAY DIFFRACTION1allE501 - 505
4X-RAY DIFFRACTION1allF506 - 511
5X-RAY DIFFRACTION1allG512 - 522
6X-RAY DIFFRACTION1allB44 - 318
7X-RAY DIFFRACTION1allB401 - 531
8X-RAY DIFFRACTION1allH501 - 505
9X-RAY DIFFRACTION1allI506 - 510
10X-RAY DIFFRACTION1allJ512 - 522
11X-RAY DIFFRACTION1allC41 - 318
12X-RAY DIFFRACTION1allK - C401 - 772
13X-RAY DIFFRACTION1allK501 - 505
14X-RAY DIFFRACTION1allL506 - 511
15X-RAY DIFFRACTION1allM512 - 522
16X-RAY DIFFRACTION1allD43 - 318
17X-RAY DIFFRACTION1allD401 - 558
18X-RAY DIFFRACTION1allN501 - 505
19X-RAY DIFFRACTION1allO506 - 511
20X-RAY DIFFRACTION1allP512 - 522

+
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