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- PDB-5dhf: Crystal Structure of hRio2 NES Peptide in complex with CRM1-Ran-RanBP1 -

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Basic information

Entry
Database: PDB / ID: 5dhf
TitleCrystal Structure of hRio2 NES Peptide in complex with CRM1-Ran-RanBP1
Components
  • Exportin-1
  • GTP-binding nuclear protein Ran
  • Ran-specific GTPase-activating protein 1
  • Serine/threonine-protein kinase RIO2
KeywordsTRANSPORT PROTEIN / Peptides / HEAT repeat / Nuclear Export signal / Exportin-1 / Nuclear Transport
Function / homology
Function and homology information


positive regulation of ribosomal small subunit export from nucleus / tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / Transcriptional and post-translational regulation of MITF-M expression and activity / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / nuclear export signal receptor activity / Regulation of cholesterol biosynthesis by SREBP (SREBF) ...positive regulation of ribosomal small subunit export from nucleus / tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / Transcriptional and post-translational regulation of MITF-M expression and activity / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / nuclear export signal receptor activity / Regulation of cholesterol biosynthesis by SREBP (SREBF) / positive regulation of rRNA processing / tRNA export from nucleus / SUMOylation of SUMOylation proteins / protein localization to kinetochore / SUMOylation of RNA binding proteins / protein localization to nucleolus / U4 snRNA binding / Rev-mediated nuclear export of HIV RNA / spindle pole body / Nuclear import of Rev protein / nuclear export / NEP/NS2 Interacts with the Cellular Export Machinery / GTP metabolic process / tRNA processing in the nucleus / RNA export from nucleus / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of chromatin organization proteins / regulation of mitotic metaphase/anaphase transition / nuclear import signal receptor activity / MicroRNA (miRNA) biogenesis / DNA metabolic process / preribosome, small subunit precursor / MAPK6/MAPK4 signaling / mitotic sister chromatid segregation / ribosomal large subunit export from nucleus / U5 snRNA binding / viral process / U2 snRNA binding / U6 snRNA binding / Major pathway of rRNA processing in the nucleolus and cytosol / nuclear pore / ribosomal subunit export from nucleus / mRNA export from nucleus / U1 snRNA binding / ribosomal small subunit export from nucleus / centriole / GTPase activator activity / protein export from nucleus / mitotic spindle organization / maturation of SSU-rRNA / Transcriptional regulation by small RNAs / recycling endosome / small GTPase binding / kinetochore / G1/S transition of mitotic cell cycle / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / positive regulation of protein binding / nuclear envelope / melanosome / mitotic cell cycle / G protein activity / ribosomal small subunit biogenesis / midbody / ubiquitin-dependent protein catabolic process / protein autophosphorylation / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / non-specific serine/threonine protein kinase / protein kinase activity / cadherin binding / protein heterodimerization activity / cell division / protein serine kinase activity / GTPase activity / chromatin binding / GTP binding / chromatin / nucleolus / perinuclear region of cytoplasm
Similarity search - Function
Serine/threonine-protein kinase Rio2 / RIO2 kinase winged helix domain, N-terminal / Rio2, N-terminal / RIO kinase, conserved site / RIO1/ZK632.3/MJ0444 family signature. / RIO kinase / RIO-like kinase / Ran-specific GTPase-activating protein 1, Ran-binding domain / : / RIO domain ...Serine/threonine-protein kinase Rio2 / RIO2 kinase winged helix domain, N-terminal / Rio2, N-terminal / RIO kinase, conserved site / RIO1/ZK632.3/MJ0444 family signature. / RIO kinase / RIO-like kinase / Ran-specific GTPase-activating protein 1, Ran-binding domain / : / RIO domain / 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 binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / Importin-beta, N-terminal domain / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / 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 / PH-like domain superfamily / Armadillo-type fold / Roll / Winged helix DNA-binding domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Winged helix-like DNA-binding domain superfamily / Protein kinase-like domain superfamily / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Exportin-1 / Ran-specific GTPase-activating protein 1 / GTP-binding nuclear protein Ran / Serine/threonine-protein kinase RIO2
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.285 Å
AuthorsFung, H.Y. / Chook, Y.M.
Funding support Hong Kong, United States, 6items
OrganizationGrant numberCountry
Croucher FoundationStudent Scholarship Hong Kong
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM069909 United States
Cancer Prevention and Research Institute of Texas (CPRIT)RP120352 United States
University of Texas SouthwesternEndowed Scholars Program United States
Welch FoundationI-1532 United States
Leukemia & Lymphoma SocietyScholar Award United States
CitationJournal: Elife / Year: 2015
Title: Structural determinants of nuclear export signal orientation in binding to exportin CRM1.
Authors: Fung, H.Y. / Fu, S.C. / Brautigam, C.A. / Chook, Y.M.
History
DepositionAug 30, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 16, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2015Group: Other
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Apr 24, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_conn_type
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id
Revision 1.7Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.8Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: Ran-specific GTPase-activating protein 1
C: Exportin-1
D: Serine/threonine-protein kinase RIO2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)164,04713
Polymers162,9954
Non-polymers1,0519
Water4,882271
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11660 Å2
ΔGint-122 kcal/mol
Surface area57440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.479, 106.479, 303.731
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 26758.564 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Plasmid: pET15 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62826
#2: Protein Ran-specific GTPase-activating protein 1 / Chromosome stability protein 20 / Perinuclear array-localized protein / Ran-binding protein 1 / RANBP1


Mass: 16521.867 Da / Num. of mol.: 1 / Fragment: RanDB1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: YRB1, CST20, HTN1, SFO1, YDR002W, YD8119.08 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P41920
#3: Protein Exportin-1 / Chromosome region maintenance protein 1 / Karyopherin-124


Mass: 117458.781 Da / Num. of mol.: 1 / Mutation: V441D,D536G,T539C,V540E,K541Q,Y1022C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: CRM1, KAP124, XPO1, YGR218W, G8514 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P30822

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Protein/peptide , 1 types, 1 molecules D

#4: Protein/peptide Serine/threonine-protein kinase RIO2


Mass: 2256.264 Da / Num. of mol.: 1 / Fragment: Nuclear Export Signal
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RIOK2 / Plasmid: pMal / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9BVS4*PLUS

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Non-polymers , 6 types, 280 molecules

#5: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 271 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.68 Å3/Da / Density % sol: 54.17 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.4
Details: 17% PEG3350, 100mM Bis-Tris pH6.4, 200mM NH4NO3, 10mM Spermine HCl

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 20, 2015
RadiationMonochromator: Rosenbaum-Rock high-resolution double-crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.28→50 Å / Num. obs: 79060 / % possible obs: 98.6 % / Redundancy: 7 % / Biso Wilson estimate: 28.29 Å2 / Rmerge(I) obs: 0.073 / Rpim(I) all: 0.028 / Rrim(I) all: 0.078 / Χ2: 0.889 / Net I/av σ(I): 24.316 / Net I/σ(I): 9 / Num. measured all: 552057
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.28-2.325.90.8939290.7010.3760.9720.88399.8
2.32-2.366.50.79439490.7430.320.8610.87899.7
2.36-2.417.10.73639170.8150.2820.7930.906100
2.41-2.467.10.61539310.8470.2340.6620.91499.7
2.46-2.517.10.51539230.880.1960.5540.93699.6
2.51-2.577.10.44339320.9050.1690.4770.92799.6
2.57-2.637.10.36439290.9340.1390.3920.92899.6
2.63-2.77.10.30439510.9510.1160.3270.91599.5
2.7-2.787.10.25239390.960.0950.2710.90599.4
2.78-2.877.10.19139460.9750.0720.2050.89298.8
2.87-2.987.10.15339380.9820.0580.1640.8899.3
2.98-3.097.10.11939370.9860.0450.1290.85999.2
3.09-3.247.20.09239490.9890.0350.0990.86398.5
3.24-3.417.10.06839440.9910.0260.0730.82999
3.41-3.627.10.05539610.9940.020.0590.82398.3
3.62-3.97.10.04639550.9940.0170.050.87698
3.9-4.297.10.04539380.9940.0170.0480.98497.3
4.29-4.917.10.04739670.9940.0170.0511.26397.2
4.91-6.196.90.03840070.9950.0140.0410.7996.2
6.19-506.60.02541180.9970.010.0270.5293.4

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Processing

Software
NameVersionClassification
PHENIXrefinement
SCALEPACKdata scaling
PDB_EXTRACT3.15data extraction
Cootmodel building
HKL-3000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4HB2

4hb2


Resolution: 2.285→45.718 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2185 2991 2.58 %
Rwork0.1781 113142 -
obs0.1791 116133 76.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 137.67 Å2 / Biso mean: 42.3238 Å2 / Biso min: 13.21 Å2
Refinement stepCycle: final / Resolution: 2.285→45.718 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10817 0 60 271 11148
Biso mean--44.07 33.4 -
Num. residues----1339
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00311231
X-RAY DIFFRACTIONf_angle_d0.61715204
X-RAY DIFFRACTIONf_chiral_restr0.0261729
X-RAY DIFFRACTIONf_plane_restr0.0021933
X-RAY DIFFRACTIONf_dihedral_angle_d12.5564202
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 21

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2849-2.32240.2734750.25812833290840
2.3224-2.36240.2598860.25413231331746
2.3624-2.40540.3076930.24733464355750
2.4054-2.45160.2675950.24453575367051
2.4516-2.50170.2801970.22973716381353
2.5017-2.55610.2614990.2333803390254
2.5561-2.61550.24741090.21394106421559
2.6155-2.68090.21121270.2224680480767
2.6809-2.75340.24621380.22285249538775
2.7534-2.83440.28021550.22775805596083
2.8344-2.92590.29131650.22146273643890
2.9259-3.03040.25651750.21386515669093
3.0304-3.15170.26581730.21036656682995
3.1517-3.29510.21911800.20276753693396
3.2951-3.46880.21861820.19246723690596
3.4688-3.6860.24441780.17346721689996
3.686-3.97050.21291780.15636704688296
3.9705-4.36980.16241720.13976635680795
4.3698-5.00140.1861690.1186648681795
5.0014-6.29860.15731740.15186587676194
6.2986-45.72730.18521710.14186465663692
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)
10.02640.00990.00550.0283-0.00690.0275-0.02520.0761-0.032-0.11090.0792-0.1793-0.05230.08740.0140.2054-0.05220.08230.3035-0.10870.33477.380745.789229.5403
20.0113-0.02440.00370.0609-0.02650.07250.06610.0363-0.04170.05610.0061-0.0216-0.070.09580.05370.1707-0.10010.04110.2528-0.11090.423411.663953.073837.9582
30.00120.00030.00120.0065-0.0050.0142-0.0180.0251-0.053-0.0083-0.0277-0.02320.01420.0104-0.03480.09870.0535-0.05470.3379-0.12850.553211.127232.548734.9079
40.10420.08460.01830.07680.04770.1449-0.0011-0.0150.05780.06320.0204-0.09230.00740.00170.10240.07650.0063-0.0630.1413-0.0970.26934.502342.656639.5989
50.03770.0352-0.04340.0356-0.04150.0503-0.04230.0339-0.0905-0.01710.003-0.13150.0755-0.008-0.02150.1220.0212-0.05120.1706-0.0620.3146-1.651434.199638.646
60.0080.00520.0040.003-0.00050.007-0.0108-0.0031-0.03440.0259-0.0098-0.01560.01130.003700.15590.0382-0.02950.1819-0.06320.2751.437643.502243.8832
70.0198-0.0093-0.01820.01880.01760.01940.06170.00010.0296-0.07560.03250.0114-0.0232-0.152900.16520.0052-0.01950.2349-0.02030.1997-8.271245.483534.4448
80.0123-0.04040.04820.159-0.14140.19720.00040.0795-0.00030.02760.13310.0419-0.18550.15370.04620.2872-0.08420.01870.2663-0.05060.20497.698862.829536.2836
90.00160.0017-0.00020.0013-0.00050.00310.0363-0.00730.0153-0.02450.0258-0.02570.0338-0.013900.5554-0.13420.12610.7396-0.150.516117.007961.68714.1962
100.0024-0.00110.00150.0010.00050.0022-0.0010.01420.00320.00660.0190.01780.01530.021400.3482-0.07410.11580.3854-0.10940.5541-1.678656.291511.9372
110.0050.007-0.00220.00730.00060.0061-0.01920.0151-0.00750.02850.02740.0227-0.01330.002-00.9076-0.160.07090.8855-0.03640.88163.347580.941546.2921
120.022-0.00010.02350.0005-0.00030.02520.06260.0464-0.0480.08720.03040.0165-0.02810.14140.00070.3971-0.11270.12930.3778-0.01290.46586.715863.215617.2505
130.01940.00090.00420.1075-0.03190.0135-0.1177-0.0066-0.06010.05-0.03110.0583-0.14640.1234-0.11290.6497-0.23220.18170.3558-0.01130.4696.407373.232924.8851
140.02580.05260.02640.18260.09680.0487-0.0732-0.0605-0.0832-0.0404-0.01590.0688-0.14450.2204-0.02470.4082-0.26410.09810.4879-0.03710.42059.775467.063214.1309
150.0282-0.019-0.01930.04150.0430.04550.00580.0385-0.0067-0.0563-0.05940.0709-0.10990.04370.00720.7571-0.2541-0.05460.35050.02340.46943.870577.999210.9198
160.0331-0.01220.03610.15970.05270.08890.0565-0.02390.00270.19930.1987-0.55150.11150.35991.36970.09170.2147-0.37610.3601-0.11130.797217.457624.893948.9624
170.0958-0.0485-0.00310.05170.030.0266-0.0543-0.13260.01620.4310.0398-0.17510.1471-0.0189-0.00010.40550.0441-0.07920.2472-0.02720.2608-7.432926.658660.9596
180.4160.0383-0.0790.68910.22890.47810.04390.05120.00610.06820.0206-0.0141-0.185-0.32380.06990.1720.04720.0170.2867-0.02540.111-26.54354.470248.5137
190.11440.0516-0.05240.39670.0920.30710.0476-0.04620.0693-0.12180.1145-0.0233-0.431-0.24340.60870.50870.26960.08670.46760.12660.1273-33.618562.73989.8308
200.2381-0.28590.10610.337-0.0680.1535-0.00670.1027-0.0376-0.07150.17540.0192-0.13040.01320.03240.20210.02740.02980.3046-0.03860.1974-15.938339.68120.8001
210.0537-0.07250.0570.096-0.06570.140.14-0.0007-0.3022-0.12370.04090.22360.2013-0.00660.00190.22990.0089-0.05010.2558-0.05790.3643-7.071410.470820.5151
220.00090.0015-0.00070.0017-0.00140.00060.01170.01630.0038-0.03710.0263-0.0133-0.01330.001700.88760.2898-0.02620.7951-0.02250.7342-39.75376.096928.1492
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 44 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 45 through 66 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 67 through 80 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 81 through 91 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 92 through 111 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 112 through 122 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 123 through 158 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 159 through 193 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 194 through 206 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 207 through 216 )A0
11X-RAY DIFFRACTION11chain 'B' and (resid 65 through 82 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 83 through 106 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 107 through 133 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 134 through 180 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 181 through 200 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 0 through 167 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 168 through 268 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 269 through 569 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 570 through 692 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 693 through 897 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 898 through 1052 )C0
22X-RAY DIFFRACTION22chain 'D' and (resid 391 through 403 )D0

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