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

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Basic information

Entry
Database: PDB / ID: 3nbz
TitleCrystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal I)
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 / Heme signaling / HuR (ELAVL1) binds and stabilizes mRNA / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion ...Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Cyclin A/B1/B2 associated events during G2/M transition / Heme signaling / HuR (ELAVL1) binds and stabilizes mRNA / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / RHO GTPases Activate Formins / Separation of Sister Chromatids / RNA cap binding / regulation of centrosome duplication / RNA nuclear export complex / MAPK6/MAPK4 signaling / pre-miRNA export from nucleus / nuclear export signal receptor activity / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / manchette / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / NLS-dependent protein nuclear import complex / regulation of protein export from nucleus / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / GTP metabolic process / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / MicroRNA (miRNA) biogenesis / nuclear import signal receptor activity / DNA metabolic process / dynein intermediate chain binding / regulation of protein catabolic process / mitotic sister chromatid segregation / protein localization to nucleus / spermatid development / ribosomal large subunit export from nucleus / sperm flagellum / ribosomal small subunit export from nucleus / mRNA export from nucleus / ribosomal subunit export from nucleus / nuclear pore / Cajal body / centriole / protein export from nucleus / viral process / mitotic spindle organization / G protein activity / male germ cell nucleus / hippocampus development / Transcriptional regulation by small RNAs / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / recycling endosome / kinetochore / small GTPase binding / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / melanosome / positive regulation of protein binding / nuclear envelope / mitotic cell cycle / snRNP Assembly / midbody / actin cytoskeleton organization / nuclear membrane / DNA-binding transcription factor binding / ribonucleoprotein complex / cadherin binding / protein heterodimerization activity / protein domain specific binding / cell division / GTPase activity / chromatin binding / chromatin / nucleolus / GTP binding / negative regulation of transcription by RNA polymerase II / magnesium ion binding / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / DNA ligase/mRNA capping enzyme / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal ...Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / DNA ligase/mRNA capping enzyme / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / small GTPase Ran family profile. / Ran GTPase / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / 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 / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / 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: 2.8 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 1.2Jan 29, 2020Group: Advisory / Derived calculations
Category: pdbx_distant_solvent_atoms / pdbx_struct_assembly ...pdbx_distant_solvent_atoms / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop
Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details ..._pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list
Revision 1.3Oct 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_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.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_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Sep 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)371,12412
Polymers369,9836
Non-polymers1,1416
Water14,142785
1
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)185,5626
Polymers184,9923
Non-polymers5703
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Exportin-1
E: Snurportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)185,5626
Polymers184,9923
Non-polymers5703
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)72.660, 224.617, 164.021
Angle α, β, γ (deg.)90.00, 100.82, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111((chain A and (name CA or name N or name...
211((chain D and (name CA or name N or name...
112((chain B and (name CA or name N or name...
212((chain E and (name CA or name N or name...
113((chain C and (name CA or name N or name...
213((chain F and (name CA or name N or name...

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(0.999984, -0.000633, 0.005641), (-0.000632, -1, -0.000177), (0.005641, 0.000174, -0.999984)36.2896, -213.641998, -5.78234
2given(0.999937, 0.007463, 0.008403), (0.007396, -0.99994, 0.008026), (0.008462, -0.007963, -0.999932)37.4217, -213.585007, -6.78159
3given(0.999981, 0.001445, 0.005914), (0.001441, -0.999999, 0.000555), (0.005915, -0.000547, -0.999982)36.531101, -213.671005, -5.88281

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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) / 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 , 4 types, 791 molecules

#4: 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
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 785 / 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: 3.55 Å3/Da / Density % sol: 65.38 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: 0.1 M Tris/HCl, 16% (w/v) PEG 1000, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K

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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: 2.8 Å / Num. obs: 114008 / % possible obs: 90 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 40.773 Å2 / Rmerge F obs: 0.191 / Rmerge(I) obs: 0.128 / Rrim(I) all: 0.152 / Net I/σ(I): 7.05 / Num. measured all: 333225

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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: 2.8→38.897 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.44 / Isotropic thermal model: Isotropic / σ(F): 1.36 / Phase error: 28.18 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.285 5701 5 %
Rwork0.2262 --
obs0.2291 114001 90.1 %
all-120570 -
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.498 Å2 / ksol: 0.326 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--7.1092 Å2-0 Å2-1.5518 Å2
2---0.0046 Å20 Å2
3---4.4717 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.44 Å0.41 Å
Luzzati d res low-8 Å
Luzzati sigma a0.44 Å0.43 Å
Refinement stepCycle: LAST / Resolution: 2.8→38.897 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24291 0 68 785 25144
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00624905
X-RAY DIFFRACTIONf_angle_d0.93833758
X-RAY DIFFRACTIONf_dihedral_angle_d17.2739277
X-RAY DIFFRACTIONf_chiral_restr0.0663798
X-RAY DIFFRACTIONf_plane_restr0.0044291
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A7595X-RAY DIFFRACTIONPOSITIONAL
12D7595X-RAY DIFFRACTIONPOSITIONAL0.079
21B1938X-RAY DIFFRACTIONPOSITIONAL
22E1938X-RAY DIFFRACTIONPOSITIONAL0.08
31C1361X-RAY DIFFRACTIONPOSITIONAL
32F1361X-RAY DIFFRACTIONPOSITIONAL0.067
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.83180.34891930.28283656X-RAY DIFFRACTION92
2.8318-2.86510.33681960.27913734X-RAY DIFFRACTION93
2.8651-2.90010.36331990.27683779X-RAY DIFFRACTION93
2.9001-2.93680.34471920.27643652X-RAY DIFFRACTION93
2.9368-2.97540.37661970.26653730X-RAY DIFFRACTION93
2.9754-3.01610.32321950.25963705X-RAY DIFFRACTION93
3.0161-3.05920.33441940.24843697X-RAY DIFFRACTION93
3.0592-3.10490.33111940.24213681X-RAY DIFFRACTION92
3.1049-3.15340.28151970.22583733X-RAY DIFFRACTION92
3.1534-3.2050.30011910.22093643X-RAY DIFFRACTION92
3.205-3.26030.30981940.24113673X-RAY DIFFRACTION92
3.2603-3.31950.31921950.24413708X-RAY DIFFRACTION92
3.3195-3.38330.32221900.23033607X-RAY DIFFRACTION91
3.3833-3.45230.29491940.23563684X-RAY DIFFRACTION91
3.4523-3.52740.33911910.23123627X-RAY DIFFRACTION91
3.5274-3.60940.27851920.2123655X-RAY DIFFRACTION91
3.6094-3.69960.27121890.21333585X-RAY DIFFRACTION91
3.6996-3.79950.27631920.20633656X-RAY DIFFRACTION90
3.7995-3.91120.26241870.20793563X-RAY DIFFRACTION90
3.9112-4.03730.25381930.20123661X-RAY DIFFRACTION90
4.0373-4.18150.27591850.19713509X-RAY DIFFRACTION89
4.1815-4.34870.25151880.19753574X-RAY DIFFRACTION89
4.3487-4.54630.24711880.19513578X-RAY DIFFRACTION89
4.5463-4.78560.23911860.19453534X-RAY DIFFRACTION88
4.7856-5.08480.23261850.19553506X-RAY DIFFRACTION88
5.0848-5.47640.25141850.21123524X-RAY DIFFRACTION87
5.4764-6.02570.27771840.22143495X-RAY DIFFRACTION87
6.0257-6.89350.25451810.22313425X-RAY DIFFRACTION85
6.8935-8.66920.24221790.20723413X-RAY DIFFRACTION84
8.6692-38.90110.2371750.21863313X-RAY DIFFRACTION81
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)
10.3396-0.16630.07750.0883-0.07310.12230.042-0.0021-0.16760.0143-0.0506-0.04150.08740.07440.01870.0342-0.00360.00830.03370.03330.094355.5678-62.3601-2.0389
20.27670.01460.10.0121-0.03110.39740.0691-0.00530.2527-0.0619-0.02180.15220.12240.0369-0.04670.11420.00060.02820.0146-00.289928.0771-61.8677-4.9682
30.00380.0318-0.01240.4133-0.18040.07310.0245-0.0369-0.02920.0762-0.1965-0.15330.02570.05050.13860.0546-0.09560.00570.44760.0360.181729.4553-106.56575.711
41.0370.19590.22070.97110.33710.1929-0.14350.0737-0.25070.04690.14640.21960.06540.05710.01970.05250.024-0.04610.0934-0.1270.296119.2361-151.1986-3.248
50.3332-0.0213-0.03870.04580.14640.4438-0.0296-0.1438-0.44120.07370.08130.09880.03570.02-0.01860.1479-0.0221-0.0077-0.0351-0.06050.3453-8.1009-151.8853-0.6844
60.1160.1201-0.09840.1229-0.09940.088-0.3824-0.07690.1575-0.09280.0192-0.054-0.1823-0.00660.30870.73290.1825-0.19570.22450.05990.1339-6.7469-107.3255-11.1691
70.42250.0593-0.0870.16-0.02380.0042-0.0450.39940.0484-0.0592-0.00040.0009-0.0047-0.16010.03870.16710.038-0.00580.3341-0.02630.002642.3931-93.2666-46.4267
80.4077-0.03590.00960.2550.12930.08630.0162-0.16860.0461-0.1220.01360.10040.1212-0.21350.01630.0834-0.00990.03760.2215-0.0421-0.01725.7815-120.360740.6619
90.7090.5262-0.16090.3852-0.1210.0377-0.36510.2319-0.2344-0.21610.262-0.11620.0599-0.13090.13180.51350.03510.20870.5011-0.1560.346660.9123-132.3304-50.658
100.82120.16360.1711.24661.21021.1397-0.11910.3332-0.21550.06720.1371-0.10160.2310.0672-0.00790.1841-0.05240.11040.0978-0.31930.132648.8504-130.7732-47.3709
110.4118-0.59-0.28350.79420.40830.4168-0.1553-0.0218-0.09050.36110.18190.38550.10240.16950.0028-0.00560.22540.2684-0.2441-0.35060.012745.554-130.7277-33.8761
120.18550.040.00070.0120.17280.2712-0.1040.0315-0.1163-0.01850.2124-0.00360.0741-0.1172-0.02410.09450.0547-0.0047-0.0073-0.11940.106535.8765-116.1852-19.3458
130.10440.09070.03280.29780.19370.1397-0.026-0.0121-0.01230.01620.04570.0864-0.0247-0.007-0.01440.10290.0048-0.02440.0315-0.01170.079133.749-94.1067-6.1223
140.21480.1074-0.04350.013-0.04290.1252-0.0378-0.01280.0791-0.00890.03010.00380.04860.00330.01840.1327-0.0276-0.02690.08890.02570.152354.4831-77.299-7.1555
150.28790.04090.18450.58420.03890.2269-0.12030.2002-0.0175-0.03620.1922-0.0169-0.02520.0918-0.08520.0283-0.0292-0.02390.10490.00240.159167.9575-71.4532-21.5857
160.0814-0.1443-0.08860.30160.06650.2418-0.1256-0.02010.0550.10180.101-0.26350.1358-0.071-0.00030.0704-0.0409-0.05830.1669-0.07360.193266.8215-87.4908-29.2979
170.3891-0.5267-0.57960.93570.3171.70810.092-0.1040.20160.0765-0.1948-0.09320.1567-0.60080.08130.0622-0.0725-0.02170.3383-0.14610.117744.1598-87.0103-25.1014
181.9555-0.26040.05440.15480.31080.9537-0.12350.1361-0.17220.02890.0975-0.0007-0.12810.3695-0.00810.05140.0025-0.04080.2575-0.08540.141178.0117-82.1993-34.5909
190.9174-0.2775-0.10010.2196-0.00830.10620.27560.46470.0675-0.1517-0.0674-0.0426-0.0970.4015-0.14390.1565-0.08570.02180.4555-0.03340.075776.4508-86.501-41.8092
200.43420.05470.11081.51060.40530.0989-0.08960.41080.0515-0.07430.3288-0.15280.00670.2082-0.1680.0568-0.0217-0.03250.56080.02550.076874.0269-89.7444-58.5876
210.3630.1214-0.08020.2256-0.17860.1299-0.07960.4744-0.04660.0760.1341-0.0494-0.15690.1089-0.08760.04650.00060.02410.6186-0.1140.027962.9661-106.8273-68.503
220.2018-0.08850.12550.50540.16280.2888-0.0543-0.21990.0580.01970.2924-0.11910.0586-0.0624-0.16990.1004-0.06330.02630.9288-0.21360.099849.7669-107.8253-70.0057
230.00590.0006-0.00560.10270.29210.9160.22960.1194-0.01880.0648-0.1401-0.00630.0919-0.06180.04380.0613-0.10020.12680.643-0.4087-0.134143.19-110.8402-73.1155
240.88010.12490.05710.25380.13170.0579-0.25830.10020.0084-0.2210.08990.0677-0.2675-0.02170.16290.2005-0.0031-0.06141.0913-0.03560.117926.9904-106.3849-68.1487
250.20210.06970.15980.02790.05380.1264-0.1140.07980.02860.01060.05420.0204-0.06930.13310.04880.4094-0.0824-0.36890.4553-0.14830.570524.4161-81.18345.0657
261.7873-0.1889-0.23981.291.33171.3698-0.0062-0.41130.3048-0.37860.07730.1642-0.32990.04450.02150.24240.0362-0.11390.187-0.15580.292212.2726-82.878741.6398
270.23740.30420.21220.41780.35420.3319-0.1841-0.10850.0869-0.36650.11130.2595-0.09910.17160.05510.1205-0.1634-0.1458-0.1694-0.22520.1999.05-82.88628.1616
280.3827-0.0661-0.06630.06390.03980.1312-0.062-0.00950.3099-0.06480.0964-0.0569-0.0317-0.0245-0.01960.1072-0.0067-0.00930.0489-0.06680.165-0.5502-97.49813.567
290.2486-0.0732-0.12220.01660.00630.16460.02850.1036-0.0330.08780.03570.0838-0.022-0.06-0.03440.10910.0168-0.00220.0184-0.04060.1112-2.606-119.52590.3058
300.5327-0.09510.00520.314-0.22060.16330.09380.1095-0.13550.1549-0.10120.0492-0.0880.08660.00840.08710.02310.05020.0333-0.03120.098418.115-136.33681.4678
310.4684-0.3457-0.25610.50410.16410.45330.00420.1120.2699-0.08340.18750.0223-0.01790.34-0.1333-0.23580.17140.02360.06380.01270.165831.4879-142.228515.9469
320.31590.03180.1920.0630.00261.6540.097-0.15340.04040.0362-0.1305-0.0146-0.2872-0.34290.07450.12350.0001-0.04780.1022-0.0242-0.01630.3234-126.18423.648
330.8181-0.0448-0.09060.24320.42730.7903-0.09640.0607-0.1745-0.09140.0849-0.0005-0.13880.07810.00040.10480.01750.03660.1198-0.10180.14067.7564-126.327719.4528
340.076-0.2364-0.18980.86670.35211.0382-0.03780.10630.16270.034-0.06650.21110.110.43410.11760.00920.0411-0.020.2145-0.01950.179941.4814-131.475129.0118
351.3920.4018-0.30510.40020.27030.46230.2093-0.3558-0.07390.1479-0.0278-0.0696-0.02750.2438-0.16910.11960.06440.01190.31530.01770.060839.8468-127.18936.2139
360.4462-0.0613-0.07860.21250.18620.33790.2619-0.162-0.0469-0.07760.0035-0.06170.11370.1199-0.11780.09370.0455-0.01410.3208-0.0272-0.027437.3521-123.93152.9658
370.44390.0376-0.28120.0799-0.08120.2144-0.1883-0.6085-0.06220.1231-0.2352-0.10590.09370.3040.1230.1009-0.0262-0.0880.6396-0.1663-0.051326.238-106.840662.8424
380.303-0.0243-0.11960.11790.13180.18460.1032-0.30950.0436-0.0102-0.0245-0.0259-0.2937-0.2574-0.05440.17060.02150.00470.9896-0.14150.0513.0991-105.810264.3529
390.1265-0.0931-0.34020.12930.35371.10360.10390.0259-0.1028-0.0880.1777-0.1065-0.189-0.0773-0.14820.14320.2029-0.01650.6959-0.38080.05746.3655-102.85967.4322
400.9580.46170.01990.7014-0.0370.1373-0.318-0.131-0.107-0.13440.2843-0.0276-0.0121-0.32660.00040.11710.12220.04731.13640.08010.076-9.5856-107.462262.0962
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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