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- PDB-1wa5: Structure of the Cse1:Imp-alpha:RanGTP complex -

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Basic information

Entry
Database: PDB / ID: 1wa5
TitleStructure of the Cse1:Imp-alpha:RanGTP complex
Components
  • GTP-binding nuclear protein Ran
  • Importin alpha re-exporter
  • SRP1 isoform 1
KeywordsTRANSPORT PROTEIN / Cse1 / Importin-alpha / RanGTP / nuclear transport
Function / homology
Function and homology information


proteasome localization / RISC complex binding / pre-miRNA binding / pre-miRNA export from nucleus / import into nucleus / snRNA import into nucleus / nuclear export signal receptor activity / NLS-dependent protein nuclear import complex / NLS-bearing protein import into nucleus / nuclear localization sequence binding ...proteasome localization / RISC complex binding / pre-miRNA binding / pre-miRNA export from nucleus / import into nucleus / snRNA import into nucleus / nuclear export signal receptor activity / NLS-dependent protein nuclear import complex / NLS-bearing protein import into nucleus / nuclear localization sequence binding / RISC complex / GTP metabolic process / nuclear import signal receptor activity / protein targeting to membrane / mitotic sister chromatid segregation / ribosomal subunit export from nucleus / protein export from nucleus / positive regulation of protein export from nucleus / small GTPase binding / protein import into nucleus / disordered domain specific binding / melanosome / nuclear envelope / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cell division / GTPase activity / GTP binding / protein-containing complex binding / perinuclear region of cytoplasm / magnesium ion binding / protein-containing complex / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Exportin-2, C-terminal / CAS/CSE protein, C-terminus / Exportin-2, central domain / Cse1 / 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 ...Exportin-2, C-terminal / CAS/CSE protein, C-terminus / Exportin-2, central domain / Cse1 / 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 subunit alpha / Atypical Arm repeat / Importin-alpha, importin-beta-binding domain superfamily / Importin beta binding domain / Atypical Arm repeat / Importin-alpha, importin-beta-binding domain / IBB domain profile. / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / 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 / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / HLJ1_G0045170.mRNA.1.CDS.1 / Importin alpha re-exporter / GTP-binding nuclear protein Ran / Importin subunit alpha
Similarity search - Component
Biological speciesCanis lupus familiaris (dog)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsStewart, M.
Funding support1items
OrganizationGrant numberCountry
Human Frontier Science Program (HFSP)
CitationJournal: Nature / Year: 2004
Title: Structural basis for the assembly of a nuclear export complex.
Authors: Matsuura, Y. / Stewart, M.
History
DepositionOct 23, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 13, 2004Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Nov 4, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Experimental preparation / Other / Polymer sequence / Refinement description / Source and taxonomy / Structure summary / Version format compliance
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / atom_type / audit_author / audit_conform / citation / database_2 / database_PDB_matrix / diffrn / diffrn_radiation_wavelength / diffrn_source / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / exptl_crystal / exptl_crystal_grow / pdbx_audit_support / pdbx_database_related / pdbx_database_status / pdbx_distant_solvent_atoms / pdbx_entry_details / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_torsion / pdbx_xplor_file / refine / refine_hist / refine_ls_restr / refine_ls_shell / reflns / reflns_shell / software / struct / struct_conf / struct_conn / struct_keywords / struct_mon_prot_cis / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_sheet / struct_sheet_order / struct_sheet_range / struct_site / struct_site_gen
Item: _citation.journal_id_ISSN / _citation.page_last ..._citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _diffrn.ambient_temp / _diffrn.pdbx_serial_crystal_experiment / _diffrn_radiation_wavelength.wavelength / _diffrn_source.pdbx_wavelength / _diffrn_source.pdbx_wavelength_list / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_fragment / _entity.pdbx_number_of_molecules / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_poly_seq.mon_id / _entity_src_gen.gene_src_common_name / _entity_src_gen.gene_src_strain / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_seq_type / _exptl_crystal.density_Matthews / _exptl_crystal.density_percent_sol / _exptl_crystal_grow.method / _exptl_crystal_grow.pdbx_details / _exptl_crystal_grow.temp / _pdbx_database_status.SG_entry / _pdbx_database_status.status_code_sf / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.mon_id / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_struct_assembly.method_details / _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_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 / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.aniso_B[1][1] / _refine.aniso_B[1][2] / _refine.aniso_B[1][3] / _refine.aniso_B[2][2] / _refine.aniso_B[2][3] / _refine.aniso_B[3][3] / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_d_res_low / _refine.ls_number_reflns_R_free / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_R_free / _refine.ls_percent_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_R_Free_selection_details / _refine.pdbx_data_cutoff_high_absF / _refine.pdbx_ls_sigma_F / _refine.pdbx_overall_phase_error / _refine.pdbx_solvent_shrinkage_radii / _refine.pdbx_solvent_vdw_probe_radii / _refine.pdbx_starting_model / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine.solvent_model_param_bsol / _refine.solvent_model_param_ksol / _refine_hist.cycle_id / _refine_hist.d_res_low / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_protein / _refine_hist.pdbx_number_residues_total / _reflns.d_resolution_low / _reflns.observed_criterion_sigma_I / _reflns.pdbx_Rmerge_I_obs / _reflns.pdbx_netI_over_sigmaI / _reflns.pdbx_redundancy / _reflns_shell.Rmerge_I_obs / _reflns_shell.meanI_over_sigI_obs / _reflns_shell.number_unique_obs / _reflns_shell.pdbx_redundancy / _reflns_shell.percent_possible_all / _struct.pdbx_CASP_flag / _struct.pdbx_descriptor / _struct.title / _struct_conf.beg_auth_comp_id / _struct_conf.beg_auth_seq_id / _struct_conf.beg_label_comp_id / _struct_conf.beg_label_seq_id / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_class / _struct_conf.pdbx_PDB_helix_id / _struct_conf.pdbx_PDB_helix_length / _struct_conn.pdbx_dist_value / _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_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_keywords.pdbx_keywords / _struct_keywords.text / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession
Revision 2.1Dec 13, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: SRP1 isoform 1
C: Importin alpha re-exporter
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,2845
Polymers188,7363
Non-polymers5472
Water12,755708
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11130 Å2
ΔGint-30 kcal/mol
Surface area64070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)272.672, 72.261, 97.640
Angle α, β, γ (deg.)90.000, 92.570, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11C-1406-

HOH

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein GTP-binding nuclear protein Ran / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 20210.416 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canis lupus familiaris (dog) / Gene: RAN / Production host: Escherichia coli (E. coli) / References: UniProt: P62825
#2: Protein SRP1 isoform 1


Mass: 59072.531 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: SRP1, GI526_G0004888 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A6A5Q590, UniProt: Q02821*PLUS
#3: Protein Importin alpha re-exporter / Chromosome segregation protein CSE1


Mass: 109453.500 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: CSE1, YGL238W, HRC135 / Production host: Escherichia coli (E. coli) / References: UniProt: P33307

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Non-polymers , 3 types, 710 molecules

#4: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 1 / 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.: 1 / Source method: obtained synthetically / Formula: Mg
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 708 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.67 Å3/Da / Density % sol: 53.88 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.6
Details: 50mM TrisHCl, 200mM NaCl, 5mM Mg(OAc)2, .1mM GTP, 22% PEG3350 and 2% PEG400.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.0055 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: May 12, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0055 Å / Relative weight: 1
ReflectionResolution: 2→34.923 Å / Num. obs: 120581 / % possible obs: 94.3 % / Redundancy: 8.9 % / Rmerge(I) obs: 0.089 / Net I/σ(I): 5.5
Reflection shellResolution: 2→2.11 Å / Rmerge(I) obs: 1.8 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 16799

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Processing

Software
NameVersionClassification
PHENIX1.15.2_3472refinement
PDB_EXTRACT3.25data extraction
MOSFLMdata reduction
SCALAdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1EE4 + 1IBR

1ee4

1ibr


Resolution: 2→34.923 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 22.08 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2165 6086 5.05 %
Rwork0.1883 114465 -
obs0.1897 120551 93.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 215.48 Å2 / Biso mean: 52.499 Å2 / Biso min: 15.71 Å2
Refinement stepCycle: final / Resolution: 2→34.923 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12690 0 42 708 13440
Biso mean--26.33 42.93 -
Num. residues----1586
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2-2.02270.33871860.2994364290
2.0227-2.04650.29692110.2731358890
2.0465-2.07150.3091980.2604361489
2.0715-2.09770.30021970.2521364391
2.0977-2.12530.27742090.2429369891
2.1253-2.15440.27442190.228364892
2.1544-2.18520.26531710.2267375092
2.1852-2.21780.28781990.2344372292
2.2178-2.25240.35061800.3104374692
2.2524-2.28930.22712010.2146376493
2.2893-2.32880.27181920.2141382994
2.3288-2.37110.22351760.2009379594
2.3711-2.41670.21382150.1928384495
2.4167-2.46610.23842010.1935380194
2.4661-2.51970.22862070.1901386695
2.5197-2.57830.2272100.1979384595
2.5783-2.64270.23262020.1952386395
2.6427-2.71410.22892190.1919381895
2.7141-2.7940.2472380.1949384895
2.794-2.88410.23082130.1988386695
2.8841-2.98710.26882070.2048387596
2.9871-3.10670.211940.2389496
3.1067-3.2480.23682240.1923386396
3.248-3.41910.20852000.1944391996
3.4191-3.63310.20931980.1819394296
3.6331-3.91320.17931790.1629392596
3.9132-4.30640.18862060.1517391496
4.3064-4.92810.14782000.1373395196
4.9281-6.20320.18872250.1761396496
6.2032-34.9230.18492090.1737402895
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)
10.16130.0782-0.13450.29740.05450.1778-0.0930.19970.155-0.15080.1069-0.0502-0.04470.28230.00670.4409-0.1614-0.08290.56860.1170.340934.853844.2132-27.2488
20.1484-0.12730.13670.3091-0.18920.1803-0.0743-0.2756-0.0744-0.27190.24350.12950.2129-0.39160.14840.344-0.0714-0.04960.57430.18140.23221.420423.3405-4.6016
30.085-0.0238-0.05770.13790.03270.1055-0.04910.0552-0.14360.14350.0359-0.0412-0.0160.0689-0.01310.30720.02620.00350.41660.17890.296725.082313.152418.8421
40.09340.01760.07220.01380.03220.2512-0.0155-0.23010.4069-0.09050.0211-0.085-0.15930.2788-0.00040.2753-0.0780.00650.3787-0.05760.36368.131928.472233.0516
50.9010.43930.29980.34530.4440.9771-0.22621.16170.28170.06820.2952-0.17830.16770.91450.07940.22430.01070.13060.81820.02780.009457.272112.80216.5848
60.27590.0303-0.31750.3123-0.54260.5756-0.07630.211-0.1364-0.22060.0702-0.21770.35660.14440.0020.3945-0.0310.08010.3044-0.06190.318328.6405-14.469516.5287
70.3656-0.08740.18050.5025-0.10050.5832-0.0061-0.0157-0.00580.08850.04130.01890.02340.01060.06130.1736-0.00740.01750.10330.00880.251516.022410.959946.874
80.33390.2209-0.0250.2773-0.18350.24110.01770.16220.0441-0.09830.015-0.0909-0.04040.115100.26690.00270.01310.18850.0010.27689.709235.244333.7029
90.28250.20240.04850.18760.12470.127-0.05760.3929-0.1277-0.0958-0.0580.22150.03450.0373-0.01180.33470.0045-0.07010.38490.03660.2983-2.315534.881522.7858
100.01080.01540.00070.01010.00270.0042-0.0561-0.1869-0.0966-0.076-0.0536-0.0343-0.14550.224-0.0010.17290.01130.00520.31490.03790.279162.24436.083342.272
110.0326-0.0095-0.01770.0059-0.010.0049-0.0149-0.11960.0274-0.183-0.07020.0038-0.11490.0573-00.2442-0.00830.01150.21680.0140.242648.33710.280945.3636
120.1150.0897-0.06950.0392-0.04550.11410.0275-0.3863-0.00090.1866-0.10260.1052-0.1280.23600.2552-0.0010.0110.32280.02110.311654.8238.607247.044
130.00990.0098-0.00140.0151-0.0120.0054-0.01270.11270.039-0.00710.08290.0471-0.14280.098100.3043-0.08470.01630.2765-0.01580.283155.889721.751735.4422
140.05340.0562-0.04450.05180.00830.0722-0.00720.0917-0.2652-0.05860.1405-0.01220.00470.0107-00.1906-0.0247-0.02660.20390.00330.20651.500211.519230.2975
150.0158-0.01110.0151-0.00370.00360.01120.01270.0743-0.0656-0.22340.1076-0.1356-0.02020.14330.00010.2396-0.01170.02850.2431-0.03510.3255.6734.925731.605
160.0099-0.00920.01680.0244-0.01560.023-0.03310.1652-0.0009-0.06590.2860.101-0.0559-0.0713-00.2854-0.0512-0.04350.27960.0060.308436.10925.553932.3619
170.05730.02930.01220.03240.02420.0163-0.1003-0.0053-0.2021-0.30050.16770.05810.10860.1532-00.3769-0.035-0.00730.2705-0.04250.382646.75161.080634.8539
180.0013-0.00240.01580.02290.04130.1248-0.12770.0247-0.23340.0667-0.0481-0.02320.23890.0633-0.02890.25870.11090.0420.22360.01380.464757.5399-5.855939.3848
190.002-0.03730.0444-0.0216-0.04650.03110.13510.1376-0.08620.05320.0254-0.0698-0.00430.0413-00.5805-0.0511-0.06630.82040.13210.563241.183931.5375-6.3281
200.06480.0089-0.01930.0041-0.00440.0477-0.15940.3286-0.2447-0.60230.3517-0.14460.07910.3297-00.8335-0.0590.07610.80710.02530.786550.487848.2583-43.3922
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'B' and (resid 145 through 284 )B145 - 284
2X-RAY DIFFRACTION2chain 'B' and (resid 285 through 441 )B285 - 441
3X-RAY DIFFRACTION3chain 'B' and (resid 442 through 516 )B442 - 516
4X-RAY DIFFRACTION4chain 'C' and (resid 1 through 79 )C1 - 79
5X-RAY DIFFRACTION5chain 'C' and (resid 80 through 320 )C80 - 320
6X-RAY DIFFRACTION6chain 'C' and (resid 321 through 525 )C321 - 525
7X-RAY DIFFRACTION7chain 'C' and (resid 526 through 792 )C526 - 792
8X-RAY DIFFRACTION8chain 'C' and (resid 793 through 901 )C793 - 901
9X-RAY DIFFRACTION9chain 'C' and (resid 902 through 959 )C902 - 959
10X-RAY DIFFRACTION10chain 'A' and (resid 7 through 17 )A7 - 17
11X-RAY DIFFRACTION11chain 'A' and (resid 18 through 32 )A18 - 32
12X-RAY DIFFRACTION12chain 'A' and (resid 33 through 66 )A33 - 66
13X-RAY DIFFRACTION13chain 'A' and (resid 67 through 80 )A67 - 80
14X-RAY DIFFRACTION14chain 'A' and (resid 81 through 111 )A81 - 111
15X-RAY DIFFRACTION15chain 'A' and (resid 112 through 122 )A112 - 122
16X-RAY DIFFRACTION16chain 'A' and (resid 123 through 137 )A123 - 137
17X-RAY DIFFRACTION17chain 'A' and (resid 138 through 158 )A138 - 158
18X-RAY DIFFRACTION18chain 'A' and (resid 159 through 176 )A159 - 176
19X-RAY DIFFRACTION19chain 'B' and (resid 11 through 88 )B11 - 88
20X-RAY DIFFRACTION20chain 'B' and (resid 89 through 144 )B89 - 144

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