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- PDB-3ice: Rho transcription termination factor bound to RNA and ADP-BeF3 -

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Basic information

Entry
Database: PDB / ID: 3ice
TitleRho transcription termination factor bound to RNA and ADP-BeF3
Components
  • 5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3'
  • Transcription termination factor rho
KeywordsTRANSCRIPTION REGULATOR/RNA / transcription / ATPase / hexamer / helicase / RNA / RecA / OB fold / motor / ATP-binding / Hydrolase / Nucleotide-binding / RNA-binding / Transcription regulation / Transcription termination / TRANSCRIPTION REGULATOR-RNA COMPLEX
Function / homology
Function and homology information


ATP-dependent activity, acting on RNA / DNA-templated transcription termination / helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / hydrolase activity / RNA binding / ATP binding / identical protein binding / membrane / cytosol
Similarity search - Function
Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / Cold shock domain ...Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / Cold shock domain / Cold shock protein domain / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / P-loop containing nucleotide triphosphate hydrolases / Nucleic acid-binding, OB-fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / SPERMIDINE / RNA / RNA (> 10) / Transcription termination factor Rho
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsThomsen, N.D. / Berger, J.M.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2009
Title: Running in reverse: the structural basis for translocation polarity in hexameric helicases.
Authors: Thomsen, N.D. / Berger, J.M.
History
DepositionJul 17, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 10, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 21, 2012Group: Database references / Refinement description
Revision 1.3Nov 1, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Sep 6, 2023Group: 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 / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / 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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr2_label_alt_id / _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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Nov 22, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.6Nov 27, 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: Transcription termination factor rho
B: Transcription termination factor rho
C: Transcription termination factor rho
D: Transcription termination factor rho
E: Transcription termination factor rho
F: Transcription termination factor rho
G: 5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)296,18727
Polymers292,7927
Non-polymers3,39620
Water1,51384
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)69.230, 127.030, 127.170
Angle α, β, γ (deg.)60.48, 90.26, 89.77
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42
13
23
33
43
53
63
14
24
34
44
54
64
15
25
35
45
55
65
16
26
36
46
56
66
17
27
37
47
57
18
28
38
48
58
68
19
29
39
49
59
69

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain B and resseq 2-9 and (backbone)
211chain C and resseq 2-9 and (backbone)
311chain D and resseq 2-9 and (backbone)
411chain E and resseq 2-9 and (backbone)
112chain B and resseq 15-20 and (backbone)
212chain C and resseq 15-20 and (backbone)
312chain D and resseq 15-20 and (backbone)
412chain E and resseq 15-20 and (backbone)
113chain B and resseq 33-40 and (backbone)
213chain A and resseq 33-40 and (backbone)
313chain C and resseq 33-40 and (backbone)
413chain D and resseq 33-40 and (backbone)
513chain E and resseq 33-40 and (backbone)
613chain F and resseq 33-40 and (backbone)
114chain B and resseq 49-104 and (backbone)
214chain A and resseq 49-104 and (backbone)
314chain C and resseq 49-104 and (backbone)
414chain D and resseq 49-104 and (backbone)
514chain E and resseq 49-104 and (backbone)
614chain F and resseq 49-104 and (backbone)
115chain B and resseq 113-120 and (backbone)
215chain A and resseq 113-120 and (backbone)
315chain C and resseq 113-120 and (backbone)
415chain D and resseq 113-120 and (backbone)
515chain E and resseq 113-120 and (backbone)
615chain F and resseq 113-120 and (backbone)
116chain B and resseq 156-274 and (backbone)
216chain A and resseq 156-274 and (backbone)
316chain C and resseq 156-274 and (backbone)
416chain D and resseq 156-274 and (backbone)
516chain E and resseq 156-274 and (backbone)
616chain F and resseq 156-274 and (backbone)
117chain B and resseq 297-322 and (backbone)
217chain C and resseq 297-322 and (backbone)
317chain D and resseq 297-322 and (backbone)
417chain E and resseq 297-322 and (backbone)
517chain F and resseq 297-322 and (backbone)
118chain B and resseq 351-394 and (backbone)
218chain A and resseq 351-394 and (backbone)
318chain C and resseq 351-394 and (backbone)
418chain D and resseq 351-394 and (backbone)
518chain E and resseq 351-394 and (backbone)
618chain F and resseq 351-394 and (backbone)
119chain B and resseq 1000-1001
219chain A and resseq 1000-1001
319chain C and resseq 1000-1001
419chain D and resseq 1000-1001
519chain E and resseq 1000-1001
619chain F and resseq 1000-1001

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9

NCS oper:
IDCodeMatrixVector
1given(0.993471, 0.111347, 0.024833), (-0.017305, 0.362243, -0.931923), (-0.112762, 0.925409, 0.361805)7.08517, -21.0284, -1.10112
2given(0.997647, 0.046073, -0.050768), (-0.013694, -0.591668, -0.806065), (-0.067175, 0.804864, -0.589645)4.00428, -21.072001, -14.9463
3given(0.999896, -0.013346, -0.005491), (-0.012526, -0.991556, 0.129074), (-0.007167, -0.128992, -0.99162)1.33739, -11.3373, -22.8664
4given(0.963795, 0.13974, 0.227094), (0.14387, 0.444537, -0.884131), (-0.2245, 0.884793, 0.408339)6.68755, -16.738501, -1.89937
5given(0.988851, 0.148274, -0.013762), (0.071464, -0.553604, -0.829708), (-0.130643, 0.819474, -0.558027)3.42587, -19.6502, -14.7597
6given(0.977869, -0.117818, -0.172889), (-0.114441, -0.992995, 0.029409), (-0.175143, -0.008972, -0.984502)11.0222, -8.3156, -26.3034
7given(0.999632, -0.00567, 0.026522), (-0.020429, 0.485803, 0.873829), (-0.017839, -0.87405, 0.485509)0.550473, 10.6996, -9.03291
8given(0.991815, -0.011303, 0.127186), (0.116215, 0.49255, -0.86249), (-0.052897, 0.870211, 0.489832)-0.401534, -14.3948, -4.4924
9given(0.99264, 0.109507, 0.05171), (0.10042, -0.505651, -0.856874), (-0.067686, 0.85576, -0.512926)0.555929, -18.1721, -17.223301
10given(0.997321, 0.067938, 0.027097), (0.067881, -0.997689, 0.003037), (0.027241, -0.00119, -0.999628)-2.83561, -8.80629, -28.5086
11given(0.980929, -0.059863, 0.184917), (-0.191085, -0.471082, 0.861144), (0.035561, -0.880056, -0.473537)8.67253, 6.0179, -21.808001
12given(0.999992, -0.003942, -1.0E-5), (0.001784, 0.450262, 0.892895), (-0.003516, -0.892888, 0.450266)-0.765939, 12.1003, -11.5296
13given(0.999953, 0.000481, -0.009721), (-0.008796, 0.472132, -0.881484), (0.004165, 0.881527, 0.472114)0.972871, -14.6957, -4.04677
14given(0.999624, 0.001256, -0.027376), (-0.022645, -0.524731, -0.850967), (-0.015434, 0.851267, -0.524505)2.46304, -17.767799, -17.528299
15given(0.998587, -0.037196, -0.037942), (-0.037664, -0.999222, -0.011716), (-0.037477, 0.013128, -0.999211)3.50874, -7.1934, -28.0396
16given(0.998798, -0.04886, -0.003814), (-0.023734, -0.550327, 0.834612), (-0.042878, -0.833518, -0.550825)2.95406, 7.53285, -24.903
17given(0.999095, -0.012719, -0.040598), (0.041306, 0.518489, 0.854086), (0.010186, -0.85499, 0.518545)-2.80297, 7.76505, -8.67032
18given(0.99974, 0.014751, 0.017404), (0.008442, 0.469524, -0.88288), (-0.021195, 0.882797, 0.469277)1.82716, -14.9146, -3.95992
19given(0.999564, 0.029529, 0.000479), (0.017472, -0.578197, -0.81571), (-0.02381, 0.815363, -0.57846)2.17674, -20.8193, -17.178699
20given(0.99825, -0.020949, -0.055298), (-0.01553, -0.995196, 0.096665), (-0.057058, -0.095637, -0.99378)3.48365, -10.9876, -26.005699
21given(0.99584, -0.071535, -0.056441), (0.002125, -0.601008, 0.79924), (-0.091095, -0.796035, -0.598356)3.09434, 9.61602, -26.977301
22given(0.999908, 0.013439, 0.001859), (-0.008196, 0.489186, 0.872141), (0.010811, -0.872076, 0.489251)-1.04481, 10.4803, -9.92678
23given(0.999964, 0.006931, 0.004832), (0.000709, 0.501025, -0.865433), (-0.008419, 0.865405, 0.501002)1.50265, -13.2883, -4.09106
24given(0.999461, 0.009472, -0.031433), (-0.022718, -0.491644, -0.8705), (-0.023699, 0.870745, -0.491164)2.79187, -16.847401, -17.622999
25given(0.997628, -0.042066, -0.054482), (-0.042614, -0.999052, -0.00893), (-0.054055, 0.01123, -0.998475)4.10174, -7.71168, -27.774599
26given(0.99658, 0.009967, 0.082035), (-0.066243, -0.497134, 0.865142), (0.049405, -0.867617, -0.494773)1.62848, 5.15789, -21.8571
27given(0.999135, 0.03483, -0.022714), (-0.037037, 0.497107, -0.866899), (-0.018903, 0.86699, 0.497967)1.95147, -14.0359, -4.18594
28given(0.998372, 0.01063, -0.056031), (-0.043119, -0.50233, -0.8636), (-0.037326, 0.86461, -0.501054)3.03213, -17.589199, -17.8584
29given(0.995338, -0.063192, -0.072868), (-0.063253, -0.997996, 0.001483), (-0.072816, 0.003133, -0.99734)4.46161, -8.28937, -27.944901
30given(0.995192, 0.00215, 0.09792), (-0.083505, -0.503848, 0.859747), (0.051186, -0.86379, -0.501246)1.90891, 4.87602, -22.0301
31given(0.999851, 0.016708, 0.004372), (-0.012131, 0.499252, 0.866372), (0.012293, -0.866296, 0.49938)-0.879003, 10.1836, -9.52773
32given(0.999996, -0.001897, 0.002127), (0.002795, 0.506416, -0.862285), (0.000559, 0.862287, 0.506419)1.07976, -13.0237, -3.90909
33given(0.999975, 0.000975, 0.006973), (0.006587, -0.479292, -0.877631), (0.002486, 0.877655, -0.479287)2.12912, -15.6396, -16.822001
34given(0.998337, -0.026943, -0.050958), (-0.028853, -0.998894, -0.037138), (-0.049901, 0.038547, -0.99801)3.95729, -6.99498, -27.7607
35given(0.995392, -0.005348, 0.095744), (-0.085173, -0.508035, 0.857115), (0.044057, -0.86132, -0.506149)2.04738, 4.51701, -22.243299
36given(0.999087, -0.037206, 0.020986), (0.000836, 0.508223, 0.861225), (-0.042709, -0.860421, 0.50779)-0.209063, 9.96452, -10.4047
37given(0.999972, -0.006209, 0.004264), (0.006669, 0.466597, -0.884445), (0.003501, 0.884448, 0.466625)0.815778, -14.0572, -3.36282
38given(0.998119, -0.045333, -0.041273), (-0.05811, -0.485025, -0.872567), (0.019537, 0.873325, -0.486747)2.54962, -17.4776, -16.563801
39given(0.997881, -0.064915, -0.004431), (-0.065022, -0.997398, -0.031122), (-0.002399, 0.031344, -0.999506)4.31692, -8.11391, -26.801001
40given(0.998696, -0.021984, 0.046075), (-0.050968, -0.480701, 0.875402), (0.002904, -0.876609, -0.481195)1.00022, 5.33656, -22.4666

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Components

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Protein / RNA chain , 2 types, 7 molecules ABCDEFG

#1: Protein
Transcription termination factor rho / ATP-dependent helicase rho


Mass: 48193.773 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Gene: b3783, JW3756, nitA, psuA, rho, rnsC, sbaA, tsu / Plasmid: pET24b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) pLysS
References: UniProt: P0AG30, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#2: RNA chain 5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3'


Mass: 3629.032 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: RNA is commerically synthesized

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Non-polymers , 5 types, 104 molecules

#3: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: BeF3
#6: Chemical ChemComp-SPD / SPERMIDINE / N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE / PA(34)


Mass: 145.246 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H19N3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 84 / 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: 3.34 Å3/Da / Density % sol: 63.22 %
Crystal growTemperature: 291 K / pH: 7.9
Details: 2.5% MPD, 50mM HEPES, 5mM Tris-HCL, 160mM sodium chloride, 1.25mM magnesium chloride, 5mM spermidine-HCL, 0.5mM TCEP, 1.25mM ADP-BeF3,, pH 7.9, MICROBATCH, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 14, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11 Å / Relative weight: 1
ReflectionResolution: 2.8→41.9 Å / Num. obs: 87864 / % possible obs: 94.6 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 49.7 Å2 / Rmerge(I) obs: 0.079 / Net I/σ(I): 15.5
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.342 / Mean I/σ(I) obs: 3.8 / % possible all: 66.6

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1PVO AND UNPUBLISHED STRUCTURE

1pvo


Resolution: 2.8→41.88 Å / Occupancy max: 1 / Occupancy min: 0.4 / SU ML: 0.56 / Isotropic thermal model: isotropic+TLS(domains) / Phase error: 31.08 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.295 4440 5.05 %
Rwork0.27 --
obs0.271 87859 94.7 %
all-87859 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 20 Å2 / ksol: 0.25 e/Å3
Displacement parametersBiso mean: 70.48 Å2
Baniso -1Baniso -2Baniso -3
1--14.943 Å20.718 Å2-0.036 Å2
2--5.974 Å21.368 Å2
3---8.087 Å2
Refinement stepCycle: LAST / Resolution: 2.8→41.88 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19120 121 212 84 19537
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01319772
X-RAY DIFFRACTIONf_angle_d0.9726678
X-RAY DIFFRACTIONf_dihedral_angle_d19.5477624
X-RAY DIFFRACTIONf_chiral_restr0.0653037
X-RAY DIFFRACTIONf_plane_restr0.0063427
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11B32X-RAY DIFFRACTIONPOSITIONAL
12C32X-RAY DIFFRACTIONPOSITIONAL0.211
13D32X-RAY DIFFRACTIONPOSITIONAL0.234
14E32X-RAY DIFFRACTIONPOSITIONAL0.194
21B24X-RAY DIFFRACTIONPOSITIONAL
22C24X-RAY DIFFRACTIONPOSITIONAL0.4
23D24X-RAY DIFFRACTIONPOSITIONAL0.27
24E24X-RAY DIFFRACTIONPOSITIONAL0.321
31B32X-RAY DIFFRACTIONPOSITIONAL
32A32X-RAY DIFFRACTIONPOSITIONAL0.291
33C32X-RAY DIFFRACTIONPOSITIONAL0.21
34D32X-RAY DIFFRACTIONPOSITIONAL0.267
35E32X-RAY DIFFRACTIONPOSITIONAL0.285
36F32X-RAY DIFFRACTIONPOSITIONAL0.264
41B224X-RAY DIFFRACTIONPOSITIONAL
42A224X-RAY DIFFRACTIONPOSITIONAL0.323
43C224X-RAY DIFFRACTIONPOSITIONAL0.285
44D224X-RAY DIFFRACTIONPOSITIONAL0.331
45E224X-RAY DIFFRACTIONPOSITIONAL0.336
46F224X-RAY DIFFRACTIONPOSITIONAL0.473
51B32X-RAY DIFFRACTIONPOSITIONAL
52A32X-RAY DIFFRACTIONPOSITIONAL0.438
53C32X-RAY DIFFRACTIONPOSITIONAL0.283
54D32X-RAY DIFFRACTIONPOSITIONAL0.374
55E32X-RAY DIFFRACTIONPOSITIONAL0.319
56F32X-RAY DIFFRACTIONPOSITIONAL0.38
61B476X-RAY DIFFRACTIONPOSITIONAL
62A476X-RAY DIFFRACTIONPOSITIONAL0.304
63C476X-RAY DIFFRACTIONPOSITIONAL0.308
64D476X-RAY DIFFRACTIONPOSITIONAL0.318
65E476X-RAY DIFFRACTIONPOSITIONAL0.385
66F476X-RAY DIFFRACTIONPOSITIONAL0.471
71B104X-RAY DIFFRACTIONPOSITIONAL
72C104X-RAY DIFFRACTIONPOSITIONAL0.289
73D104X-RAY DIFFRACTIONPOSITIONAL0.272
74E104X-RAY DIFFRACTIONPOSITIONAL0.26
75F104X-RAY DIFFRACTIONPOSITIONAL0.291
81B176X-RAY DIFFRACTIONPOSITIONAL
82A176X-RAY DIFFRACTIONPOSITIONAL0.292
83C176X-RAY DIFFRACTIONPOSITIONAL0.245
84D176X-RAY DIFFRACTIONPOSITIONAL0.293
85E176X-RAY DIFFRACTIONPOSITIONAL0.444
86F176X-RAY DIFFRACTIONPOSITIONAL0.392
91B28X-RAY DIFFRACTIONPOSITIONAL
92A28X-RAY DIFFRACTIONPOSITIONAL0.128
93C28X-RAY DIFFRACTIONPOSITIONAL0.214
94D28X-RAY DIFFRACTIONPOSITIONAL0.315
95E28X-RAY DIFFRACTIONPOSITIONAL0.389
96F28X-RAY DIFFRACTIONPOSITIONAL0.419
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.8320.302900.2941781X-RAY DIFFRACTION60
2.832-2.8650.3571090.3251925X-RAY DIFFRACTION66
2.865-2.90.381220.3312198X-RAY DIFFRACTION73
2.9-2.9370.351370.3252299X-RAY DIFFRACTION82
2.937-2.9750.3661600.3372714X-RAY DIFFRACTION92
2.975-3.0160.4351530.3392912X-RAY DIFFRACTION97
3.016-3.0590.361460.3362829X-RAY DIFFRACTION99
3.059-3.1050.3641490.3272942X-RAY DIFFRACTION98
3.105-3.1530.371720.3252868X-RAY DIFFRACTION97
3.153-3.2050.3381560.2992866X-RAY DIFFRACTION99
3.205-3.260.341650.2982849X-RAY DIFFRACTION98
3.26-3.3190.321500.2852891X-RAY DIFFRACTION98
3.319-3.3830.2991600.2932899X-RAY DIFFRACTION99
3.383-3.4520.31490.2782916X-RAY DIFFRACTION97
3.452-3.5270.2791580.2722894X-RAY DIFFRACTION99
3.527-3.6090.2741570.2752884X-RAY DIFFRACTION98
3.609-3.70.341460.2652866X-RAY DIFFRACTION98
3.7-3.80.2891570.2672932X-RAY DIFFRACTION99
3.8-3.9110.3021390.2772901X-RAY DIFFRACTION98
3.911-4.0370.2831640.2672879X-RAY DIFFRACTION99
4.037-4.1820.2771510.2532919X-RAY DIFFRACTION99
4.182-4.3490.2781560.2552905X-RAY DIFFRACTION98
4.349-4.5470.2511400.2462943X-RAY DIFFRACTION100
4.547-4.7860.2681570.2412867X-RAY DIFFRACTION99
4.786-5.0850.3081520.2472930X-RAY DIFFRACTION99
5.085-5.4770.2851370.2542911X-RAY DIFFRACTION99
5.477-6.0270.2851650.2562941X-RAY DIFFRACTION99
6.027-6.8960.2931420.2532935X-RAY DIFFRACTION99
6.896-8.6750.1881440.222932X-RAY DIFFRACTION99
8.675-41.8830.2351570.2022891X-RAY DIFFRACTION99
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)
10.0656-0.06670.02330.01850.07220.04710.18610.48670.0567-0.11350.1213-0.07390.0334-0.0965-00.34860.04040.0620.74160.17810.51777.556118.9874-58.1574
20.6479-0.1287-0.02330.52420.2160.3560.0560.23860.19820.1109-0.02470.0207-0.0332-0.011800.26340.01730.05620.17140.11180.2796-20.950614.1083-39.8907
30.00530.00280.00780.0085-0.0043-0.008-0.09760.09570.0749-0.0220.01220.0010.1473-0.0122-00.93540.1775-0.09670.905-0.46431.16331.2741-48.1589-53.9518
40.91150.714-0.11620.1826-0.25930.3310.16080.4948-0.67890.0188-0.1501-0.0642-0.09030.2963-0.13280.24460.18380.00920.454-0.38240.37997.5074-29.5926-54.8355
51.1576-0.2048-0.0870.3904-0.62740.66280.03810.3375-0.39310.07690.12150.1121-0.0881-0.13661.72990.16390.007-0.06870.0531-0.13330.0283-22.1194-17.2277-41.9136
60.3151-0.1149-0.30160.1282-0.11211.20250.0214-0.2267-0.28170.09110.21250.03460.10470.55060.04540.19390.1131-0.03920.22440.09340.60855.7375-53.4919-6.6094
71.6074-0.17020.55710.14770.10821.355-0.0732-0.3668-0.6959-0.04960.16860.142-0.1445-0.29330.11850.166-0.0368-0.03080.04150.04810.3744-23.1427-34.8545-15.6843
8-0.0073-0.0311-0.01450.00670.02230.0081-0.0128-0.04220.06090.1793-0.0467-0.00570.1532-0.081300.67150.2106-0.09350.91340.09790.410.983-15.86945.8428
90.12730.0546-0.0069-0.02270.10750.08160.1755-0.2723-0.0853-0.0194-0.1395-0.1964-0.10820.18930.00070.2251-0.051-0.01460.69730.17470.23816.0972-25.138129.8989
100.6749-0.21510.10671.3950.44470.59510.0016-0.5013-0.2408-0.1152-0.04750.3545-0.1223-0.1769-0.03810.15580.03740.03170.50750.07730.119-24.2868-21.297512.8926
110.2554-0.0711-0.43590.8477-0.22830.4550.1526-0.26350.3382-0.186-0.17770.22420.0334-0.0164-00.36520.04320.02690.5359-0.22950.5067-16.003914.791618.9462
120.05580.04080.0093-0.0155-0.00580.00220.12870.1330.13980.2636-0.149-0.05370.19540.147400.92370.05410.00970.61670.08471.43766.392345.9306-15.9524
130.13280.0763-0.04830.027-0.16450.3457-0.1163-0.10010.14510.2254-0.0776-0.25580.1299-0.1452-00.7795-0.0745-0.08620.45040.01760.6644-23.058128.4556-11.2572
140.0010.0038-0.0049-0.0016-0.0061-0.00280.0575-0.02530.23620.0020.0041-0.0238-0.08730.10300.7120.1115-0.03141.05720.04490.4161-7.5518-3.5337-13.4371
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 1-130A1 - 130
2X-RAY DIFFRACTION2chain A and resseq 131-1002A131 - 1002
3X-RAY DIFFRACTION3chain B and resseq 1-21B1 - 21
4X-RAY DIFFRACTION4chain B and resseq 30-131B30 - 131
5X-RAY DIFFRACTION5chain b and resseq 132-1002B132 - 1002
6X-RAY DIFFRACTION6chain C and resseq 1-130C1 - 130
7X-RAY DIFFRACTION7chain D and resseq 131-1002C131 - 1002
8X-RAY DIFFRACTION8chain D and resseq 1-23D1 - 23
9X-RAY DIFFRACTION9chain D and resseq 29-130D29 - 130
10X-RAY DIFFRACTION10chain D and resseq 131-1002D131 - 1002
11X-RAY DIFFRACTION11chain EE0
12X-RAY DIFFRACTION12chain F and resseq 1-129F1 - 129
13X-RAY DIFFRACTION13chain F and resseq 130-1002F130 - 1002
14X-RAY DIFFRACTION14chain GG0

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