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- PDB-3gjx: Crystal Structure of the Nuclear Export Complex CRM1-Snurportin1-... -

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Basic information

Entry
Database: PDB / ID: 3gjx
TitleCrystal Structure of the Nuclear Export Complex CRM1-Snurportin1-RanGTP
Components
  • Exportin-1
  • GTP-binding nuclear protein Ran
  • Snurportin-1
KeywordsPROTEIN TRANSPORT / Transport / Cytoplasm / Nucleus / RNA-binding / Acetylation / GTP-binding / Host-virus interaction / Nucleotide-binding / Phosphoprotein / Polymorphism / mRNA transport
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 / RNA import into nucleus / cellular response to salt / 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 / RNA import into nucleus / cellular response to salt / 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 / manchette / nuclear export signal receptor activity / regulation of centrosome duplication / 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 / Nuclear import of Rev protein / protein localization to nucleolus / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / GTP metabolic process / 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 / viral process / ribosomal large subunit export from nucleus / spermatid development / protein localization to nucleus / nuclear pore / sperm flagellum / mRNA export from nucleus / positive regulation of protein binding / Cajal body / ribosomal subunit export from nucleus / 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 / DNA-binding transcription factor binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cadherin binding / response to xenobiotic stimulus / protein heterodimerization activity / ribonucleoprotein complex / 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. / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / 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 / Alpha Horseshoe / 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 / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / Snurportin-1 / GTP-binding nuclear protein Ran / Exportin-1
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsMonecke, T. / Guettler, T. / Neumann, P. / Dickmanns, A. / Goerlich, D. / Ficner, R.
CitationJournal: Science / Year: 2009
Title: Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP.
Authors: Monecke, T. / Guttler, T. / Neumann, P. / Dickmanns, A. / Gorlich, D. / Ficner, R.
History
DepositionMar 9, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 26, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 10, 2021Group: Database references / Derived calculations / Category: database_2 / 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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)380,01513
Polymers378,8396
Non-polymers1,1767
Water17,276959
1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
A: Exportin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,9906
Polymers189,4193
Non-polymers5703
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9870 Å2
ΔGint-62 kcal/mol
Surface area65050 Å2
MethodPISA
2
E: Snurportin-1
F: GTP-binding nuclear protein Ran
D: Exportin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)190,0257
Polymers189,4193
Non-polymers6064
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10290 Å2
ΔGint-73 kcal/mol
Surface area63980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)72.173, 225.738, 163.451
Angle α, β, γ (deg.)90.00, 100.56, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 3 types, 6 molecules BECFAD

#1: Protein Snurportin-1 / RNA U transporter 1


Mass: 41610.945 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SNUPN, RNUT1, SPN1 / Production host: Escherichia coli (E. coli) / References: UniProt: O95149
#2: Protein GTP-binding nuclear protein Ran / RanGTP / GTPase Ran / Ras-related nuclear protein / Ras-like protein TC4 / Androgen receptor- ...RanGTP / GTPase Ran / Ras-related nuclear protein / Ras-like protein TC4 / Androgen receptor-associated protein 24


Mass: 24441.135 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Production host: Escherichia coli (E. coli) / References: UniProt: P62826
#3: Protein Exportin-1 / Crm1 / 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: Xpo1, Crm1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6P5F9

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Non-polymers , 5 types, 966 molecules

#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#5: 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
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 959 / 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: 2

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Sample preparation

Crystal
IDDensity Matthews (Å3/Da)Density % sol (%)
13.4664.4
2
Crystal grow
Temperature (K)Crystal-IDMethodpHDetails
2931vapor diffusion, sitting drop8PEG 1000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
2932vapor diffusion, sitting drop8PEG 1000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONBESSY 14.110.9
SYNCHROTRONBESSY 14.120.9
Detector
TypeIDDetectorDateDetails
MARMOSAIC 225 mm CCD1CCDDec 19, 2007mirrors
MARMOSAIC 225 mm CCD2CCDDec 20, 2007mirrors
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1GRAPHITESINGLE WAVELENGTHMx-ray1
2GRAPHITESINGLE WAVELENGTHMx-ray1
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.5→39.56 Å / Num. all: 176505 / Num. obs: 176505 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.9 % / Biso Wilson estimate: 38.453 Å2 / Rmerge(I) obs: 0.12 / Rsym value: 0.124 / Net I/σ(I): 10.7
Reflection shellResolution: 2.5→2.6 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.506 / Mean I/σ(I) obs: 2.9 / Num. measured obs: 75431 / Num. unique all: 19500 / Num. unique obs: 19500 / Rsym value: 0.5 / % possible all: 99.7

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACT3.006data extraction
MAR345dtbdata collection
XDSdata reduction
PHENIXrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→38.842 Å / Cor.coef. Fo:Fc: 0.831 / Cor.coef. Fo:Fc free: 0.811 / Occupancy max: 1 / Occupancy min: 1 / SU B: 12.389 / SU ML: 0 / Cross valid method: THROUGHOUT / σ(F): 1.36 / σ(I): 0 / ESU R: 0.416 / ESU R Free: 0.295 / Phase error: 27.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2808 8604 5 %RANDOM
Rwork0.2443 ---
all0.31 176504 --
obs0.2461 172082 97.36 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 0.8 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 74.356 Å2 / ksol: 0.371 e/Å3
Displacement parametersBiso max: 131.5 Å2 / Biso mean: 50.035 Å2 / Biso min: 12.34 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 2.5→38.842 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24252 0 69 959 25280
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00724872
X-RAY DIFFRACTIONf_angle_d1.07933732
X-RAY DIFFRACTIONf_dihedral_angle_d18.6259152
X-RAY DIFFRACTIONf_chiral_restr0.0843781
X-RAY DIFFRACTIONf_plane_restr0.0054303
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5-2.52840.32942790.2811528396
2.5284-2.55820.34612830.2721539096
2.5582-2.58930.30522840.2598539197
2.5893-2.62210.29722830.2542537497
2.6221-2.65660.32052900.2512550498
2.6566-2.6930.32672870.2537546698
2.693-2.73150.31582890.2663548098
2.7315-2.77220.31772910.2592553198
2.7722-2.81550.31232890.25548699
2.8155-2.86170.30122890.2496549698
2.8617-2.9110.2822900.2444551698
2.911-2.96390.30792880.2534546899
2.9639-3.02090.29032910.2456553998
3.0209-3.08250.32052880.2514545898
3.0825-3.14950.29422900.2455551798
3.1495-3.22280.2982870.2482545198
3.2228-3.30330.27422900.2383550898
3.3033-3.39260.27342880.2299547498
3.3926-3.49240.24212860.2252542698
3.4924-3.6050.2622900.2253551598
3.605-3.73370.27352850.2286542197
3.7337-3.88310.2552890.2215547897
3.8831-4.05970.2722860.2326545197
4.0597-4.27340.26912880.2321545897
4.2734-4.54080.25652860.2195543997
4.5408-4.89080.22972850.2179541397
4.8908-5.38180.27772850.2373541297
5.3818-6.15790.26272840.2576539596
6.1579-7.74820.27952830.2574539396
7.7482-38.8470.24382810.242534594
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)
10.0043-0.0671-0.0275-0.0776-0.041-0.0382-0.06960.03060.1128-0.01350.0072-0.0727-0.0407-0.12750.01640.0512-0.0184-0.01240.2612-0.09170.507254.4371-62.9557-2.968
20.34330.21340.14550.34520.04930.3676-0.03030.01780.45830.00010.06750.2077-0.0780.0530.01160.0780.0107-0.01330.1423-0.01290.52527.9503-61.8833-4.9291
30.0002-0.0031-0.0090.0074-0.0013-0.0028-0.0839-0.0714-0.0683-0.0005-0.0575-0.080.04990.0112-0.00030.4256-0.01960.0510.72250.03550.810127.1606-105.44625.435
40.02680.0185-0.0359-0.07840.04930.0621-0.04030.1174-0.4378-0.1203-0.12390.03130.2153-0.14420.0860.08960.0114-0.02220.1606-0.1060.635818.8146-150.5642-1.8724
50.5939-0.00920.32710.27610.1040.30540.0251-0.0138-0.57220.03130.10410.30510.03710.0474-0.15760.06140.01760.02340.1113-0.00390.6103-8.0332-151.9906-0.3197
60.08560.0199-0.3004-0.02160.0174-0.0406-0.05620.08380.0580.0241-0.024-0.0475-0.09040.00220.00650.7077-0.01120.08170.820.12580.4252-8.6453-109.7659-9.8881
7-0.0284-0.01490.12450.037-0.02270.15440.06650.25370.1564-0.21010.10820.0484-0.0299-0.08560.4981-0.089-0.027-0.36770.3034-0.0477-0.297841.4046-93.4266-46.0937
80.3671-0.1907-0.00610.57690.24360.21710.0584-0.29530.12740.2392-0.0022-0.21020.0367-0.0570.03050.11240.02480.06060.30780.0045-0.02155.4178-120.268640.6535
90.01040.0056-0.01790.0453-0.01940.0173-0.07130.0198-0.0179-0.00950.0489-0.08270.05440.06440.00950.6269-0.0928-0.0640.7535-0.1270.354160.218-132.5771-48.1303
100.0922-0.02310.03240.06430.09660.0708-0.05420.2145-0.0767-0.0275-0.0012-0.08590.4871-0.05790.04080.3291-0.04980.03330.4047-0.28070.33147.6864-130.65-47.2037
110.0264-0.02730.00670.0483-0.06550.1637-0.0155-0.0162-0.09440.01350.01870.03960.10390.3573-0.03140.25220.0630.13710.2001-0.24110.220844.4386-130.7432-33.7104
120.1820.0781-0.04930.21380.05580.0684-0.0250.0944-0.11860.03010.0040.1235-0.04940.0324-0.00890.0535-0.0001-0.03550.1043-0.06620.229935.0861-116.0507-19.0776
130.09380.1244-0.0454-0.04640.16630.09920.02750.0019-0.0813-0.0032-0.0118-0.00720.0265-0.006-0.01930.0861-0.0118-0.02990.0897-0.01190.31132.8794-94.1762-6.1132
140.16460.28630.06120.20790.07160.2872-0.11610.0990.220.0152-0.03490.06440.079-0.13270.10570.10120.00540.00780.15130.00410.355753.6883-77.6129-6.8861
15-0.04290.16420.02110.02460.08740.16230.06020.01110.067-0.06760.0943-0.233-0.14940.0157-0.11130.1116-0.03180.01630.24420.05840.325967.0589-71.7909-21.4635
16-0.0025-0.0066-0.02390.0064-0.0196-0.00080.05850.0094-0.03790.0226-0.0414-0.04990.068-0.10820.02420.0483-0.0998-0.0450.1912-0.0567-0.069765.8316-87.6037-29.229
170.00450.00290.00180.0111-0.00760.01040.0130.0189-0.10620.09740.00210.01910.04210.0875-0.03750.13920.0676-0.07680.3604-0.01330.222243.2923-87.272-25.0867
18-0.01060.0063-0.00980.0059-0.0013-0.01070.05980.1282-0.12070.09210.1243-0.1846-0.00340.1922-0.05340.0484-0.029-0.02210.2572-0.05440.205976.9157-82.3116-34.5282
190.03760.08840.01680.08890.06610.0133-0.05530.2512-0.0217-0.11310.0549-0.06790.04340.14440.01540.1666-0.049-0.0530.38270.00420.100775.2155-86.5276-41.6954
200.06510.02150.02960.00930.06840.0557-0.04810.3315-0.0544-0.04420.1698-0.0139-0.09110.1594-0.06050.3642-0.0978-0.02230.7460.04130.112272.7718-89.7944-58.357
210.1901-0.09920.06210.04260.0379-0.0089-0.01490.1233-0.14460.10010.11840.0212-0.10670.2331-0.03230.2235-0.0046-0.01350.8538-0.1120.018961.7865-106.8727-68.1924
220.06630.03230.00450.0657-0.014-0.01790.0784-0.1029-0.22420.05710.0493-0.13310.0763-0.02-0.03680.4277-0.0450.05320.7331-0.18530.178648.4234-107.6649-69.618
23-0.00520.01110.0192-0.0580.00310.07130.13120.00210.02230.0201-0.0956-0.01010.1256-0.09690.08030.30510.0197-0.0170.9612-0.2671-0.13841.8619-110.4952-72.7133
240.0472-0.00110.01050.00490.04130.06650.11080.03810.0187-0.0062-0.00540.0117-0.0265-0.07150.00090.4276-0.0155-0.28061.1868-0.21340.264625.7358-106.2048-67.3699
250.04210.0224-0.00130.0642-0.01070.06120.01170.124-0.0577-0.0751-0.0027-0.1596-0.01690.0809-0.00320.51790.0964-0.33880.7598-0.14250.541424.3947-81.212242.8573
260.90040.1449-0.66960.08230.05480.4569-0.3328-0.2445-0.01080.0941-0.12430.0282-0.1509-0.0305-0.05890.34770.0141-0.20790.4445-0.30880.370411.6369-83.167641.7825
270.11430.03160.07890.02230.1110.19390.044-0.04970.1578-0.0017-0.11810.1794-0.36520.19410.03440.288-0.0222-0.11460.2364-0.13220.39528.2773-82.896328.1685
280.0743-0.17410.1580.2422-0.03130.1743-0.042-0.10710.1215-0.02420.0719-0.0125-0.0533-0.012-0.0570.08340.0351-0.02910.1871-0.06920.345-1.1282-97.806513.8031
290.13560.00470.04630.01020.15210.10920.01190.04960.08620.04040.02970.0404-0.038-0.0648-0.03820.11420.02170.01360.1449-0.00540.3362-3.1955-119.62720.5046
300.1279-0.0842-0.06950.16450.09730.2247-0.0558-0.0087-0.15510.0444-0.06590.1927-0.0376-0.0120.10330.09890.0049-0.00320.13670.03310.305817.5852-136.27631.7365
310.0541-0.1790.03750.20670.20960.3810.0024-0.0913-0.02480.12410.1780.03460.14310.1645-0.01720.0580.07550.0130.19360.05680.237730.7909-142.229516.197
32-0.0156-0.01960.02680.0262-0.02520.02660.06610.11880.0134-0.0376-0.0245-0.1866-0.1152-0.0779-0.02310.0828-0.00550.05860.22280.01360.157929.7497-126.225823.8038
33-0.01710.0236-0.03580.0098-0.0079-0.0303-0.00590.002-0.0403-0.0087-0.13190.0078-0.2337-0.17210.03130.09360.0483-0.01310.5608-0.09490.43257.3518-126.567319.7191
340.07030.02590.0210.1586-0.0020.07750.0129-0.0523-0.0240.11910.1745-0.01860.12910.3311-0.05660.22930.1083-0.03340.1897-0.0570.167140.8328-131.511529.112
350.0218-0.13460.08680.24220.03590.12450.04840.1131-0.0614-0.03520.0389-0.233-0.09860.1565-0.00830.1040.077-0.05330.3602-0.02420.044439.1277-127.287436.2442
360.07970.0365-0.0523-0.0203-0.00910.13030.0558-0.0884-0.0010.16110.1585-0.16510.17140.1751-0.08710.33580.0615-0.06290.73110.08210.195236.72-124.04352.9186
370.35970.1464-0.02720.0469-0.01410.02770.0059-0.18420.21670.12040.00610.1040.0730.13060.02220.29610.05-0.05660.9192-0.10760.050125.6092-106.730762.8235
380.0330.00650.02430.0216-0.01840.01650.14830.0471-0.01210.04040.0641-0.00570.137-0.0951-0.03050.47820.1894-0.13330.8432-0.23140.158412.3823-106.137164.1913
390.10830.004-0.03530.10860.12720.097-0.1472-0.0119-0.0382-0.0475-0.04320.12110.0523-0.1668-0.11840.26210.07860.11940.9669-0.3284-0.25185.7673-103.299267.2551
400.055-0.0348-0.06860.0159-0.0657-0.03630.0989-0.02130.07170.0728-0.0959-0.03180.0010.00640.01080.34850.02220.06491.2759-0.05920.3554-10.1495-107.558862.0114
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 1028:1055
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 1028:1055
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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