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- PDB-3nc0: Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export... -

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Basic information

Entry
Database: PDB / ID: 3nc0
TitleCrystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II)
Components
  • Exportin-1
  • GTP-binding nuclear protein Ran
  • Snurportin-1
KeywordsGTP-binding protein/transport protein / protein transport / GTP-binding protein-transport protein complex
Function / homology
Function and homology information


Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Cyclin A/B1/B2 associated events during G2/M transition / HuR (ELAVL1) binds and stabilizes mRNA / Heme signaling / cellular response to triglyceride / cellular response to salt / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Transcriptional and post-translational regulation of MITF-M expression and activity ...Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Cyclin A/B1/B2 associated events during G2/M transition / HuR (ELAVL1) binds and stabilizes mRNA / Heme signaling / cellular response to triglyceride / cellular response to salt / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Transcriptional and post-translational regulation of MITF-M expression and activity / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / annulate lamellae / RHO GTPases Activate Formins / Separation of Sister Chromatids / regulation of proteasomal ubiquitin-dependent protein catabolic process / MAPK6/MAPK4 signaling / RNA cap binding / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / regulation of centrosome duplication / nuclear export signal receptor activity / manchette / cellular response to mineralocorticoid stimulus / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / NLS-dependent protein nuclear import complex / regulation of protein export from nucleus / Rev-mediated nuclear export of HIV RNA / protein localization to nucleolus / Nuclear import of Rev protein / NEP/NS2 Interacts with the Cellular Export Machinery / GTP metabolic process / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / MicroRNA (miRNA) biogenesis / DNA metabolic process / regulation of protein catabolic process / dynein intermediate chain binding / protein complex oligomerization / mitotic sister chromatid segregation / ribosomal large subunit export from nucleus / spermatid development / protein localization to nucleus / viral process / positive regulation of protein binding / sperm flagellum / nuclear pore / ribosomal subunit export from nucleus / mRNA export from nucleus / Cajal body / ribosomal small subunit export from nucleus / cytoskeleton organization / centriole / protein export from nucleus / mitotic spindle organization / male germ cell nucleus / hippocampus development / protein tetramerization / Transcriptional regulation by small RNAs / recycling endosome / kinetochore / positive regulation of protein import into nucleus / small GTPase binding / protein import into nucleus / GDP binding / melanosome / nuclear envelope / mitotic cell cycle / G protein activity / actin cytoskeleton organization / snRNP Assembly / midbody / nuclear membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / DNA-binding transcription factor binding / cadherin binding / response to xenobiotic stimulus / ribonucleoprotein complex / protein heterodimerization activity / protein domain specific binding / cell division / GTPase activity / chromatin binding / chromatin / GTP binding / protein-containing complex binding / nucleolus / magnesium ion binding / negative regulation of transcription by RNA polymerase II / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / nucleus / membrane / plasma membrane
Similarity search - Function
Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / Snurportin1, m3G cap-binding domain / DNA ligase/mRNA capping enzyme / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat ...Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / Snurportin1, m3G cap-binding domain / DNA ligase/mRNA capping enzyme / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / Ran GTPase / Small GTPase Ran-type domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / Importin-beta, N-terminal domain / Importin-alpha, importin-beta-binding domain / IBB domain profile. / D-amino Acid Aminotransferase; Chain A, domain 1 / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / Armadillo-type fold / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / PHENOL / DI(HYDROXYETHYL)ETHER / Snurportin-1 / GTP-binding nuclear protein Ran / Exportin-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.9 Å
AuthorsGuttler, T. / Madl, T. / Neumann, P. / Deichsel, D. / Corsini, L. / Monecke, T. / Ficner, R. / Sattler, M. / Gorlich, D.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Authors: Guttler, T. / Madl, T. / Neumann, P. / Deichsel, D. / Corsini, L. / Monecke, T. / Ficner, R. / Sattler, M. / Gorlich, D.
History
DepositionJun 4, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 27, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 6, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / 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_label_asym_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.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_label_asym_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 1.3Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
E: Snurportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)373,36733
Polymers369,9836
Non-polymers3,38327
Water11,331629
1
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)331,64429
Polymers328,5515
Non-polymers3,09324
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14470 Å2
ΔGint-23 kcal/mol
Surface area67850 Å2
MethodPISA
2
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
E: Snurportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)373,26132
Polymers369,9836
Non-polymers3,27726
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14600 Å2
ΔGint-21 kcal/mol
Surface area68120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.262, 225.895, 163.984
Angle α, β, γ (deg.)90.00, 100.75, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.999998, -0.00154, -0.001355), (-0.001541, -0.999999, -0.000523), (-0.001354, 0.000525, -0.999999)36.447399, -214.190002, -5.11945
2given(0.999997, 0.001843, 0.001709), (0.001838, -0.999994, 0.002936), (0.001714, -0.002932, -0.999994)36.899799, -214.149002, -5.64844
3given(0.999996, -0.002075, -0.002152), (-0.002076, -0.999998, -0.000646), (-0.002151, 0.00065, -0.999997)36.401901, -214.162994, -5.09039

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Components

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Protein , 3 types, 6 molecules ADBECF

#1: Protein Exportin-1 / Exp1 / Chromosome region maintenance 1 protein homolog


Mass: 123367.234 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Crm1, Xpo1, Xpo1 (GeneID: 103573) / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: Q6P5F9
#2: Protein Snurportin-1 / RNA U transporter 1


Mass: 41431.902 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: rev isolate D.ZA.85.R286 / Gene: SNUPN (GeneID: 10073), RNUT1, SNUPN, SPN1 / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: O95149
#3: Protein GTP-binding nuclear protein Ran / GTPase Ran / Ras-related nuclear protein / Ras-like protein TC4 / Androgen receptor-associated protein 24


Mass: 20192.484 Da / Num. of mol.: 2 / Mutation: Q69L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ARA24, OK/SW-cl.81, RAN, RAN (GeneID: 5901) / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: P62826

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Non-polymers , 6 types, 656 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical ChemComp-IPH / PHENOL


Mass: 94.111 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H6O
#7: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 629 / 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: 3.6 Å3/Da / Density % sol: 65.86 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: 0.1 M Tris/HCl, 16% (w/v) PEG 1000, 2 mM phenol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 10, 2009 / Details: mirrors
RadiationMonochromator: YALE MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionHighest resolution: 2.9 Å / Num. obs: 110353 / % possible obs: 95.4 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 37.846 Å2 / Rmerge F obs: 0.171 / Rmerge(I) obs: 0.143 / Rrim(I) all: 0.162 / Net I/σ(I): 8.97 / Num. measured all: 465206

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Processing

Software
NameVersionClassificationNB
XSCALEdata processing
PHENIX1.6.1_357refinement
PDB_EXTRACT3.1data extraction
MAR345dtbdata collection
XDSdata reduction
XSCALEdata scaling
CNSphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 3GJX

3gjx


Resolution: 2.9→39.046 Å / Occupancy max: 1 / Occupancy min: 0.5 / SU ML: 0.43 / Isotropic thermal model: Isotropic / σ(F): 1.36 / Phase error: 30.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2947 5516 5 %
Rwork0.2421 --
obs0.2448 110315 95.46 %
all-115337 -
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.078 Å2 / ksol: 0.307 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--7.9178 Å20 Å20.7153 Å2
2--0.7669 Å2-0 Å2
3----0.1102 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.43 Å0.39 Å
Luzzati d res low-8 Å
Luzzati sigma a0.43 Å0.4 Å
Refinement stepCycle: LAST / Resolution: 2.9→39.046 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24325 0 217 629 25171
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00325108
X-RAY DIFFRACTIONf_angle_d0.74733958
X-RAY DIFFRACTIONf_dihedral_angle_d16.1039373
X-RAY DIFFRACTIONf_chiral_restr0.0553805
X-RAY DIFFRACTIONf_plane_restr0.0034297
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9-2.93290.37781580.31122999X-RAY DIFFRACTION81
2.9329-2.96740.30851540.29942927X-RAY DIFFRACTION81
2.9674-3.00360.38431530.29132913X-RAY DIFFRACTION81
3.0036-3.04160.36771580.28683005X-RAY DIFFRACTION81
3.0416-3.08160.34911540.28122919X-RAY DIFFRACTION81
3.0816-3.12380.32341540.27092935X-RAY DIFFRACTION81
3.1238-3.16840.33231700.25383223X-RAY DIFFRACTION87
3.1684-3.21570.3151900.26193631X-RAY DIFFRACTION100
3.2157-3.26590.32831910.26823632X-RAY DIFFRACTION100
3.2659-3.31950.29811950.25693687X-RAY DIFFRACTION100
3.3195-3.37670.32331880.26543590X-RAY DIFFRACTION100
3.3767-3.4380.33481920.24363645X-RAY DIFFRACTION100
3.438-3.50410.30711960.23823712X-RAY DIFFRACTION100
3.5041-3.57560.28751890.22953595X-RAY DIFFRACTION100
3.5756-3.65330.30771940.23153687X-RAY DIFFRACTION100
3.6533-3.73820.29561900.22863599X-RAY DIFFRACTION100
3.7382-3.83160.30051930.23423679X-RAY DIFFRACTION100
3.8316-3.93510.28721910.22413622X-RAY DIFFRACTION100
3.9351-4.05080.2641940.21573681X-RAY DIFFRACTION100
4.0508-4.18140.25271890.21133608X-RAY DIFFRACTION100
4.1814-4.33070.22821940.21743698X-RAY DIFFRACTION100
4.3307-4.50380.28771910.2133613X-RAY DIFFRACTION100
4.5038-4.70850.2531910.20593634X-RAY DIFFRACTION100
4.7085-4.95620.30891920.21223660X-RAY DIFFRACTION100
4.9562-5.26610.27611930.22293656X-RAY DIFFRACTION99
5.2661-5.67150.28771930.24273658X-RAY DIFFRACTION99
5.6715-6.24020.32221910.25083627X-RAY DIFFRACTION99
6.2402-7.13840.28121920.24733647X-RAY DIFFRACTION99
7.1384-8.97560.24971920.22383654X-RAY DIFFRACTION99
8.9756-39.04990.23851940.23753663X-RAY DIFFRACTION98
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)
10.16650.0206-0.20950.3709-0.11250.2807-0.0588-0.09990.1056-0.0696-0.0679-0.02710.0128-0.05290.10970.02830.02030.01780.115-0.18370.324555.9182-62.6206-2.0221
20.12650.01160.01840.16530.04960.07150.01790.0540.244-0.0409-0.0308-0.05160.09370.04260.01420.0735-0.01380.0182-0.0283-0.03430.213628.3207-61.8094-4.907
30.00250.00350.00230.21410.14350.09670.04760.0115-0.00640.13570.0297-0.06280.0797-0.0609-0.06140.2767-0.010.12520.03270.070.263730.0275-107.29736.3774
40.0353-0.03980.01220.065-0.04880.0744-0.05630.00180.0580.1163-0.0539-0.075-0.0204-0.05630.09730.0892-0.0048-0.01610.0301-0.12820.272119.3422-151.7475-3.0815
50.20160.13190.02430.1610.04550.2250.0363-0.0165-0.28450.00640.0562-0.0717-0.01210.1067-0.04080.04910.00590.0096-0.0581-0.01290.208-8.2034-152.3845-0.2858
60.1078-0.0022-0.10150.09690.02650.1031-0.03340.01690.0279-0.02620.0226-0.0065-0.0564-0.05580.01250.4593-0.0734-0.07950.42480.07060.2619-6.2078-107.3603-11.264
70.2877-0.0105-0.1870.1225-0.01350.1181-0.010.2977-0.0112-0.1664-0.069-0.03480.11-0.14180.03390.13390.0337-0.03910.1677-0.0426-0.038142.5779-93.5153-46.0132
80.1072-0.00040.11950.06170.11640.28610.0944-0.18830.00260.0841-0.00840.01340.0916-0.1825-0.00240.04260.01630.1490.147-0.0014-0.19076.0033-120.698140.8344
90.0787-0.0079-0.03820.00340.00350.0185-0.0664-0.0664-0.03490.0220.01610.03450.0311-0.01530.04740.3195-0.01860.15250.3997-0.1390.435261.2542-132.7241-50.1627
100.1952-0.0264-0.04020.2548-0.02640.1313-0.10060.1089-0.0763-0.03920.00120.0030.1355-0.03970.07020.2442-0.02080.07230.3105-0.24890.24148.9261-131.0136-46.8894
110.00370.00830.00260.05970.02150.009-0.00940.0518-0.07210.1188-0.05880.07960.0433-0.01470.06240.18520.07760.08640.08-0.12390.221545.5787-131.0122-33.4139
120.1047-0.09280.04420.32950.17510.1539-0.03170.0911-0.14230.05110.2220.03630.06090.01-0.1028-0.030.17990.0938-0.2942-0.23210.003335.9774-116.4428-18.9085
130.07930.05750.0390.0280.0430.05480.025-0.0095-0.06690.08550.0845-0.02690.0035-0.0806-0.04790.086-0.0368-0.0157-0.1102-0.09580.089433.8887-94.2648-5.8282
140.2362-0.18360.12590.29870.11660.4684-0.1491-0.00970.16570.1969-0.0807-0.0120.0379-0.00320.19420.0748-0.0171-0.00360.0027-0.00760.127254.8133-77.4148-6.9545
150.16730.16490.06640.17490.03560.05970.02020.03850.0142-0.04540.05790.0152-0.0670.0052-0.0422-0.0467-0.1149-0.0357-0.0163-0.01520.111568.3872-71.604-21.3352
160.0026-0.002-0.00470.00130.00180.0068-0.0063-0.02260.00650.0507-0.0254-0.00960.0792-0.04590.02920.073-0.0719-0.0150.0743-0.0812-0.013667.1849-87.7623-28.9662
170.009-0.02570.03170.0889-0.08680.11620.0376-0.0395-0.0180.00360.0298-0.02120.0692-0.0724-0.06850.0826-0.11750.02170.2095-0.13110.252144.4581-87.3172-24.8263
180.15120.00090.03840.01490.0020.0773-0.01290.0423-0.0527-0.00580.0502-0.0445-0.03090.0689-0.04460.05120.01670.01680.2079-0.10630.136678.3881-82.4698-34.3069
190.1281-0.0161-0.04520.27780.16030.28890.00330.18580.0105-0.08340.1715-0.0944-0.02420.1317-0.1187-0.0061-0.076-0.04370.326-0.0617-0.032576.7837-86.8217-41.4991
200.38050.08550.1160.02620.07510.33660.07550.1587-0.017-0.01910.1541-0.0162-0.04770.2469-0.14310.1095-0.1257-0.00250.5095-0.01930.039974.2879-90.0443-58.1974
210.09040.06090.01960.336-0.10530.0609-0.00390.23-0.04850.06420.031-0.0305-0.04220.1397-0.02820.0805-0.0290.02550.787-0.21720.113763.1688-107.1689-68.1658
220.03550.00520.01720.12310.03660.01990.01410.0217-0.0081-0.01990.0792-0.062-0.01540.0561-0.0450.0648-0.16920.11080.4872-0.23690.080849.8607-108.0613-69.5662
230.0006-0.0028-0.00020.0039-0.00190.00730.07220.0310.04920.03-0.0015-0.02680.0430.0532-0.05350.4083-0.03770.06870.8259-0.41250.140143.4102-111.3248-72.5297
240.0830.01480.06260.10790.09560.1113-0.01880.053-0.0347-0.17510.07240.0567-0.1560.075-0.06310.19330.0815-0.03460.7655-0.11250.096127.1474-106.6947-67.6229
250.0060.0026-0.01070.0004-0.00310.03130.0216-0.05240.0010.0214-0.0217-0.00060.0159-0.02180.00010.2991-0.0162-0.17850.3758-0.17150.267624.6868-81.077944.965
260.13970.00980.02350.29330.13650.0624-0.0899-0.0660.0437-0.1731-0.03410.0851-0.1261-0.03580.09790.1132-0.0213-0.12870.0144-0.3110.172812.3921-83.222741.7231
270.00710.02530.01560.04270.03050.0334-0.03010.03680.0188-0.14670.00090.1364-0.08750.04740.03730.2712-0.1125-0.12660.0155-0.25990.18199.0457-83.196428.2339
280.0075-0.0316-0.0490.13890.12280.10070.0582-0.08190.0645-0.05470.0767-0.05880.0158-0.052-0.05350.03920.0229-0.0181-0.3104-0.2863-0.0912-0.6047-97.788913.7339
290.0699-0.0493-0.02920.0628-0.02470.0547-0.01170.0080.09070.13770.0863-0.1204-0.09160.025-0.0530.1308-0.01270.0147-0.0707-0.06210.1447-2.7491-119.9060.6258
300.1208-0.059-0.04550.27230.03950.21180.0037-0.0312-0.0497-0.1726-0.1060.0117-0.01640.03260.08490.08650.03070.0091-0.001-0.00960.111918.161-136.74381.724
310.078-0.0856-0.05370.14260.03530.06260.0260.04370.0148-0.0780.033-0.01010.07610.0969-0.0226-0.04440.14180.02290.0763-0.00340.064631.7463-142.619416.0938
320.20080.0066-0.07640.04730.06110.11710.0577-0.01270.0159-0.01050.054-0.0778-0.0323-0.0141-0.06980.1071-0.04180.00090.03290.010.082830.5783-126.489823.7431
330.00730.0136-0.00390.0295-0.01450.09530.02280.0358-0.0014-0.04420.0116-0.0195-0.0672-0.0885-0.03120.05780.07760.09380.1817-0.0460.10547.6948-127.078219.5913
340.05750.0155-0.02080.0815-0.00310.0995-0.008-0.04-0.002-0.012-0.04080.02190.04750.11830.01850.07390.1045-0.04250.2413-0.05570.066941.7816-131.80729.0648
350.1866-0.0093-0.02160.08770.10050.34490.0583-0.0591-0.04360.00710.00760.01110.0250.109-0.0504-0.00730.0440.010.1897-0.06020.030140.1828-127.4736.2835
360.3296-0.1855-0.00580.14670.11390.37190.0439-0.1845-0.0117-0.07490.21910.0340.10440.1322-0.17520.10660.0642-0.00650.51610.06420.047437.7148-124.217952.9738
370.0129-0.02040.01170.0091-0.0103-0.00060.0015-0.11760.02420.0601-0.06640.0299-0.060.01660.0470.10760.014-0.0220.7413-0.18130.064626.6383-107.063562.9413
380.0352-0.0244-0.04350.11230.01670.05780.029-0.0445-0.0138-0.02590.0621-0.0197-0.00370.0657-0.0630.1690.1628-0.11180.7809-0.26720.118913.3504-106.249564.4361
390.00450.0030.00650.0024-0.00360.1199-0.0017-0.0070.0101-0.01640.0327-0.01640.0307-0.08860.0050.15380.0880.02760.6732-0.31180.06866.8901-102.907767.7023
400.19880.28140.10410.4310.08490.2847-0.00170.00120.05970.022-0.06410.09820.1001-0.07930.06310.0456-0.01640.08020.68350.03940.0384-9.8989-107.932562.3534
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain B and resid 1:39
2X-RAY DIFFRACTION2chain B and resid 40:290
3X-RAY DIFFRACTION3chain B and resid 330:365
4X-RAY DIFFRACTION4chain E and resid 1:39
5X-RAY DIFFRACTION5chain E and resid 40:290
6X-RAY DIFFRACTION6chain E and resid 330:365
7X-RAY DIFFRACTION7chain C
8X-RAY DIFFRACTION8chain F
9X-RAY DIFFRACTION9chain A and resid 1028:1059
10X-RAY DIFFRACTION10chain A and resid 969:1027
11X-RAY DIFFRACTION11chain A and resid 908:963
12X-RAY DIFFRACTION12chain A and resid 767:907
13X-RAY DIFFRACTION13chain A and resid 627:766
14X-RAY DIFFRACTION14chain A and resid 533:626
15X-RAY DIFFRACTION15chain A and resid 468:532
16X-RAY DIFFRACTION16chain A and resid 449:467
17X-RAY DIFFRACTION17chain A and resid 425:448
18X-RAY DIFFRACTION18chain A and resid 402:424
19X-RAY DIFFRACTION19chain A and resid 311:401
20X-RAY DIFFRACTION20chain A and resid 240:310
21X-RAY DIFFRACTION21chain A and resid 145:239
22X-RAY DIFFRACTION22chain A and resid 120:144
23X-RAY DIFFRACTION23chain A and resid 67:119
24X-RAY DIFFRACTION24chain A and resid 4:66
25X-RAY DIFFRACTION25chain D and resid 1028:1059
26X-RAY DIFFRACTION26chain D and resid 969:1027
27X-RAY DIFFRACTION27chain D and resid 908:963
28X-RAY DIFFRACTION28chain D and resid 767:907
29X-RAY DIFFRACTION29chain D and resid 627:766
30X-RAY DIFFRACTION30chain D and resid 533:626
31X-RAY DIFFRACTION31chain D and resid 468:532
32X-RAY DIFFRACTION32chain D and resid 449:467
33X-RAY DIFFRACTION33chain D and resid 425:448
34X-RAY DIFFRACTION34chain D and resid 402:424
35X-RAY DIFFRACTION35chain D and resid 311:401
36X-RAY DIFFRACTION36chain D and resid 240:310
37X-RAY DIFFRACTION37chain D and resid 145:239
38X-RAY DIFFRACTION38chain D and resid 120:144
39X-RAY DIFFRACTION39chain D and resid 67:119
40X-RAY DIFFRACTION40chain D and resid 4:66

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