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- PDB-4xtr: Structure of Get3 bound to the transmembrane domain of Pep12 -

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Basic information

Entry
Database: PDB / ID: 4xtr
TitleStructure of Get3 bound to the transmembrane domain of Pep12
Components
  • ATPase GET3
  • Antibody Heavy chain
  • Antibody Light chain
  • Pep12p
KeywordsHYDROLASE/TRANSPORT PROTEIN / membrane protein targeting complex / HYDROLASE-TRANSPORT PROTEIN complex
Function / homology
Function and homology information


GET complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / tail-anchored membrane protein insertion into ER membrane / Hydrolases; Acting on acid anhydrides / protein insertion into ER membrane / post-translational protein targeting to endoplasmic reticulum membrane / response to arsenic-containing substance / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / response to metal ion / protein folding chaperone ...GET complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / tail-anchored membrane protein insertion into ER membrane / Hydrolases; Acting on acid anhydrides / protein insertion into ER membrane / post-translational protein targeting to endoplasmic reticulum membrane / response to arsenic-containing substance / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / response to metal ion / protein folding chaperone / guanyl-nucleotide exchange factor activity / unfolded protein binding / response to heat / cellular response to oxidative stress / ribosome / endoplasmic reticulum membrane / endoplasmic reticulum / Golgi apparatus / ATP hydrolysis activity / ATP binding / metal ion binding / identical protein binding / cytosol
Similarity search - Function
Arsenical pump ATPase, ArsA/GET3, eukaryotic / Arsenical pump ATPase, ArsA/GET3 / Anion-transporting ATPase-like domain / Anion-transporting ATPase / 40S Ribosomal protein S10 / Plectin/S10, N-terminal / Plectin/S10 domain / Winged helix DNA-binding domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Winged helix-like DNA-binding domain superfamily ...Arsenical pump ATPase, ArsA/GET3, eukaryotic / Arsenical pump ATPase, ArsA/GET3 / Anion-transporting ATPase-like domain / Anion-transporting ATPase / 40S Ribosomal protein S10 / Plectin/S10, N-terminal / Plectin/S10 domain / Winged helix DNA-binding domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Winged helix-like DNA-binding domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / KLLA0B08173p / ATPase GET3
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsMateja, A. / Paduch, M. / Chang, H.-Y. / Szydlowska, A. / Kossiakoff, A.A. / Hegde, R.S. / Keenan, R.J.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM086487 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U01 GM094588 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U54 GM087519 United States
CitationJournal: Science / Year: 2015
Title: Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo.
Authors: Mateja, A. / Paduch, M. / Chang, H.Y. / Szydlowska, A. / Kossiakoff, A.A. / Hegde, R.S. / Keenan, R.J.
History
DepositionJan 23, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 18, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2017Group: Author supporting evidence / Derived calculations ...Author supporting evidence / Derived calculations / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_audit_support ...entity_src_gen / pdbx_audit_support / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Sep 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
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.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_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
Revision 1.4Oct 30, 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: ATPase GET3
B: ATPase GET3
C: Antibody Heavy chain
D: Antibody Light chain
E: Antibody Heavy chain
F: Antibody Light chain
G: Pep12p
hetero molecules


Theoretical massNumber of molelcules
Total (without water)181,80714
Polymers179,8247
Non-polymers1,9837
Water16,718928
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22920 Å2
ΔGint-212 kcal/mol
Surface area61770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.870, 112.030, 153.690
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Antibody , 2 types, 4 molecules CEDF

#2: Antibody Antibody Heavy chain


Mass: 24560.430 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens, synthetic construct
Description: Obtained by phage display from a library of human IgG antibody fragment, the CDRs are completely synthetic
Plasmid: RH2.2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)/pRIL
#3: Antibody Antibody Light chain


Mass: 23671.266 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens, synthetic construct
Description: Obtained by phage display from a library of human IgG antibody fragment, the CDRs are completely synthetic
Plasmid: RH2.2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)/pRIL

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Protein / Protein/peptide , 2 types, 3 molecules ABG

#1: Protein ATPase GET3 / Arsenical pump-driving ATPase / Arsenite-stimulated ATPase / Golgi to ER traffic protein 3 / Guided ...Arsenical pump-driving ATPase / Arsenite-stimulated ATPase / Golgi to ER traffic protein 3 / Guided entry of tail-anchored proteins 3


Mass: 39392.605 Da / Num. of mol.: 2 / Mutation: D57N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: GET3, ARR4, YDL100C, D2371 / Plasmid: pCDF1b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)/pRIL
References: UniProt: Q12154, Hydrolases; Acting on acid anhydrides
#4: Protein/peptide Pep12p


Mass: 4575.672 Da / Num. of mol.: 1 / Fragment: UNP residues 102-128
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: VIN 13 / Gene: VIN13_4407 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)/pRIL / References: UniProt: E7M086

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Non-polymers , 5 types, 935 molecules

#5: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: Mg
#7: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: Zn
#8: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 928 / 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

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Sample preparation

CrystalDensity Matthews: 2.67 Å3/Da / Density % sol: 53.9 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 2 mM ATP and 2 mM MgCl2 with 15% PEG 3350, 25 mM succinic acid pH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 10, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.05→53.95 Å / Num. obs: 109335 / % possible obs: 98 % / Redundancy: 3.8 % / Net I/σ(I): 11.7
Reflection shellResolution: 2.05→2.12 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 2.1 / % possible all: 90

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: dev_1839)refinement
Cootmodel building
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2woj and 3pgf

2woj

3pgf


Resolution: 2.05→53.95 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / Phase error: 23.23 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2161 5469 5 %
Rwork0.1872 103811 -
obs0.1886 109280 97.79 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 175.48 Å2 / Biso mean: 56.7877 Å2 / Biso min: 18.79 Å2
Refinement stepCycle: final / Resolution: 2.05→53.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11647 0 165 928 12740
Biso mean--37.52 48.95 -
Num. residues----1509
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00312069
X-RAY DIFFRACTIONf_angle_d0.76216378
X-RAY DIFFRACTIONf_chiral_restr0.0291856
X-RAY DIFFRACTIONf_plane_restr0.0032063
X-RAY DIFFRACTIONf_dihedral_angle_d13.334379
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.05-2.07340.33081470.2862883303082
2.0734-2.09780.31941810.27913162334391
2.0978-2.12330.29511660.26393347351396
2.1233-2.15020.28941940.24923383357797
2.1502-2.17850.29131650.2373472363799
2.1785-2.20840.27441810.23273445362698
2.2084-2.23990.25711930.2343493368699
2.2399-2.27330.25831680.22763469363799
2.2733-2.30890.26232020.219334673669100
2.3089-2.34670.26171940.217235043698100
2.3467-2.38720.25091990.217434723671100
2.3872-2.43060.23981810.20693505368699
2.4306-2.47740.24391760.20233443361998
2.4774-2.52790.24331750.204135233698100
2.5279-2.58290.25651920.20653482367499
2.5829-2.6430.23921570.199435553712100
2.643-2.70910.2341860.196335043690100
2.7091-2.78230.24841730.20613505367899
2.7823-2.86420.24361920.1993496368899
2.8642-2.95660.22951740.20393505367999
2.9566-3.06230.25551710.19583434360597
3.0623-3.18490.22521740.19873519369399
3.1849-3.32990.23441870.19673522370999
3.3299-3.50540.21652060.18783454366099
3.5054-3.7250.20012040.17653516372099
3.725-4.01250.17391610.16483490365197
4.0125-4.41620.18681810.14593551373299
4.4162-5.0550.16661860.13533540372698
5.055-6.36780.18771970.16863539373697
6.3678-61.5920.1852060.19223631383796
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)
12.769-0.7567-0.24692.57080.42211.21610.0608-0.10950.13070.1461-0.3739-0.62550.03120.21160.17130.2046-0.00560.00410.40480.22220.700350.7494-18.1404-19.4768
26.3232-1.0589-0.19454.95170.92973.7333-0.3644-0.5441-0.07060.677-0.0168-0.91360.35020.52010.29860.535-0.0051-0.13050.5420.06470.638448.051-13.4491-3.1934
33.5624-1.2506-1.67353.58290.82031.83590.1215-0.27250.16650.2741-0.1866-0.4879-0.25880.23070.18960.2965-0.0409-0.04760.4260.22570.599347.1143-10.2146-14.8124
43.2621-0.54611.7826.5139-1.06776.8632-0.0783-0.98010.87211.1374-0.10630.1742-1.5470.13850.2370.6602-0.1670.0230.8462-0.18370.887744.77862.29951.7369
51.1362-0.5719-1.41214.5774-1.4345.12370.0863-0.79090.49771.3904-0.5497-0.4679-0.88540.68780.47640.6827-0.2263-0.290.71660.05061.029853.405-0.3917-3.1184
62.60560.03310.0613.296-0.64092.18250.0140.27540.1309-0.3713-0.2399-0.010.08250.11820.23230.32520.05-0.00450.30870.12890.520938.4438-7.7017-30.2719
72.47462.20541.03926.5530.75992.11760.2350.279-0.1249-0.84620.13440.28840.4716-0.13380.16120.63850.0816-0.15030.43530.05920.496230.0787-10.806-41.1397
81.78210.16590.7711.9332-0.88262.1743-0.01370.552-0.079-0.8362-0.2203-0.51580.23720.23830.21490.49370.1430.13770.47460.16010.578645.2205-19.6182-37.406
92.0084-0.90450.27521.6857-0.38132.67530.1784-0.063-0.19120.0110.01810.2226-0.0643-0.0784-0.17730.22860.01840.010.26670.04250.359515.2077-14.5325-16.7345
103.0382-0.4678-0.29865.04432.04755.6024-0.0262-0.69310.92280.36420.0696-0.2577-1.28550.06-0.06790.6615-0.0339-0.03360.5718-0.1320.629229.17633.7114-2.2068
117.96360.4042-1.61721.61550.39292.1755-0.0426-0.50610.02750.27240.09850.2354-0.29390.126-0.05920.3442-0.0042-0.01960.39140.05640.272119.0444-9.2382-1.1873
122.1405-1.3008-1.48652.57850.21552.6617-0.1922-0.9951-0.04850.7910.3085-0.22170.04680.574-0.13180.43750.0211-0.05250.55660.04070.437424.0676-14.27012.8993
132.2526-0.1101-0.09472.3358-1.00272.8990.12850.0447-0.2942-0.2132-0.0591-0.07380.41060.2588-0.04560.30090.0469-0.05470.24860.02280.450925.9567-28.3847-17.5898
141.6803-0.179-0.64932.1846-1.9496.26440.32520.1585-0.4416-1.1526-0.25290.12140.03280.0221-0.17730.77870.1769-0.07770.334-0.05880.566329.7634-34.3712-32.0621
152.3712-0.3904-0.63871.31791.36431.66680.22050.3891-0.322-0.9492-0.05160.46370.2743-0.346-0.20.43310.0084-0.15440.2989-0.02650.414215.7406-23.1457-30.5912
162.62380.09411.34282.1421-0.61762.30450.09150.10920.2118-0.0312-0.049-0.0250.02690.1516-0.01950.24140.0283-0.02070.23290.00480.285745.8463-48.4673-7.0416
172.8257-0.32161.51732.39680.2292.40290.14261.072-0.472-0.36570.117-0.18160.42891.0171-0.26770.74510.1268-0.15490.7747-0.14170.459755.3409-81.6328-2.5923
183.11960.30940.14786.1823-0.21533.03010.33420.0585-0.70230.429-0.0407-0.25890.14680.8649-0.13310.76840.1952-0.09881.2168-0.23340.800263.1235-86.6133-0.0894
192.23540.1242-0.14565.74811.93224.01730.0829-0.11890.37440.7105-0.15140.31790.3803-0.25740.13390.3057-0.0064-0.06290.2868-0.00080.339525.5241-64.9915-10.0025
201.94560.88140.98343.23510.30211.74810.06140.05070.259-0.152-0.00180.50550.1017-0.0923-0.0410.2770.0092-0.06170.25020.03040.362228.549-57.1414-15.1457
210.94350.494-0.72383.341-0.46560.58060.4577-0.5218-0.46140.25780.2332-0.11760.628-0.05120.2080.7217-0.0478-0.39070.3570.1320.456731.6119-79.8893-10.74
221.409-0.62111.36431.1123-0.04341.61060.5301-1.0393-0.63820.06450.1420.17910.8556-0.7806-0.61230.7966-0.0812-0.29720.71590.14260.629344.32-84.86266.9754
233.4426-0.08441.83872.0401-0.4432.97440.10610.0243-0.30750.1294-0.32120.04110.18040.51320.4240.61350.0439-0.17680.47010.0020.427245.2528-82.36123.094
242.1603-0.5962.4310.616-0.74213.99760.3469-0.1627-0.39590.03950.18770.07320.8228-0.1536-0.06581.1559-0.4848-0.60081.15990.6960.802640.9419-92.78239.1
253.0787-1.2806-0.7365.180.30142.34680.24440.1797-0.01330.0865-0.37040.6345-0.2397-0.3970.02340.29170.0250.06220.27710.03970.245612.882720.9028-29.0548
262.2417-0.6146-0.42384.756-0.52821.5840.12220.0583-0.1307-0.0325-0.08350.3839-0.081-0.07340.04270.27580.014-0.0030.25810.0060.107819.734114.2138-31.0967
271.5536-0.0541-0.54263.25880.11080.92580.1688-0.1037-0.19560.6892-0.163-0.4966-0.00880.20110.07450.3999-0.0316-0.06160.28360.04990.160727.229614.876-23.6968
283.89931.06010.51818.0311.56363.35170.0704-0.0581-0.47810.7196-0.22480.3669-0.024-0.20910.05420.3354-0.01030.05540.28-0.00280.167816.037212.1857-23.2628
291.5475-1.6671-0.98982.9923-0.16231.95730.2393-0.0543-0.04240.5882-0.2733-0.1235-0.3049-0.1168-0.0690.37180.00760.02750.267-0.00530.107320.765823.7568-27.9401
304.557-4.172-0.85697.099-0.53280.98540.19380.0977-0.5262-0.4616-0.28030.1440.1765-0.05690.12840.33870.0794-0.02950.3030.00260.263824.36559.8775-37.5222
311.5364-1.44510.08642.8312-0.97650.59970.1368-0.05780.23870.59220.11850.3415-0.2069-0.1764-0.17870.48710.04430.13590.35580.02840.278111.361936.1721-27.5105
322.7251-0.98280.66352.43152.03953.9477-0.23740.08360.09360.108-0.08720.1473-0.06270.11150.20380.246-0.03320.06220.26320.07290.265410.429347.3161-44.7021
332.568-0.91661.39311.99911.0845.3747-0.3168-0.0287-0.07940.1455-0.13430.2984-0.1026-0.36280.33350.2202-0.02290.05990.28590.00230.30885.786547.3612-47.9392
344.1209-1.750.91071.61290.9226.9478-0.0709-0.29690.29430.2843-0.1710.7271-0.4247-0.48330.44710.31130.03770.0340.4721-0.06270.48531.361153.0231-44.1762
350.5070.48620.64882.397-1.79434.3180.33320.57760.2148-0.1758-0.488-0.5882-0.56910.3763-0.11020.60860.27610.22660.77620.330.43136.621726.0777-46.8103
361.3702-0.1963-1.32642.7138-0.56391.51210.91950.9188-0.2695-1.0758-0.999-1.51220.3580.52280.3970.62230.41070.35250.65890.1265-0.277733.016717.252-46.6909
371.6191-0.91410.73255.8063-1.30293.37030.2870.1435-0.02770.2576-0.6997-1.19560.0620.41530.42490.30320.0091-0.03450.38820.14690.328735.656915.2986-32.5197
380.6133-0.96210.7843.2551-2.03741.3494-0.22060.3963-0.205-0.0731-0.2123-0.13450.55660.78650.18050.47910.21540.18370.64080.21820.353128.855236.803-55.9244
393.19120.1031-1.02172.9951-0.22266.4734-0.2186-0.24130.29560.3318-0.01980.1292-0.69140.46060.28180.4045-0.0333-0.06460.34880.07340.321812.34258.1478-42.0327
401.6419-0.9592-0.83422.28091.55264.0847-0.323-0.2763-0.04450.20450.0122-0.3319-0.11981.47780.17240.3513-0.0523-0.00530.72450.20210.268724.533850.6505-46.903
411.39530.144-0.05322.54420.31613.4753-0.1055-0.2755-0.01020.1364-0.3927-0.14420.06130.9104-0.0060.2623-0.03910.00470.6880.20220.273723.732746.6171-46.4393
422.4121-0.4641-1.58813.72120.44024.2918-0.0314-0.30770.33440.15310.0593-0.1485-1.03041.1088-0.02720.5177-0.2447-0.06010.55480.13960.252222.453260.1487-44.0803
430.3190.20880.36660.61160.07570.73580.1605-0.21280.36730.0670.2803-0.5964-0.63980.5828-0.25131.3981-0.2267-0.18081.2658-0.19261.157938.2316-6.71244.4952
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 99 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 100 through 153 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 154 through 178 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 179 through 211 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 212 through 230 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 231 through 285 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 286 through 305 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 306 through 352 )A0
9X-RAY DIFFRACTION9chain 'B' and (resid 4 through 89 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 90 through 135 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 136 through 154 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 155 through 230 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 231 through 285 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 286 through 305 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 306 through 353 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 4 through 128 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 129 through 212 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 213 through 225 )C0
19X-RAY DIFFRACTION19chain 'D' and (resid 2 through 19 )D0
20X-RAY DIFFRACTION20chain 'D' and (resid 20 through 104 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 105 through 116 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 117 through 166 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 167 through 191 )D0
24X-RAY DIFFRACTION24chain 'D' and (resid 192 through 217 )D0
25X-RAY DIFFRACTION25chain 'E' and (resid 4 through 20 )E0
26X-RAY DIFFRACTION26chain 'E' and (resid 21 through 48 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 49 through 70 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 71 through 86 )E0
29X-RAY DIFFRACTION29chain 'E' and (resid 87 through 102 )E0
30X-RAY DIFFRACTION30chain 'E' and (resid 103 through 115 )E0
31X-RAY DIFFRACTION31chain 'E' and (resid 116 through 128 )E0
32X-RAY DIFFRACTION32chain 'E' and (resid 129 through 184 )E0
33X-RAY DIFFRACTION33chain 'E' and (resid 185 through 212 )E0
34X-RAY DIFFRACTION34chain 'E' and (resid 213 through 225 )E0
35X-RAY DIFFRACTION35chain 'F' and (resid 2 through 19 )F0
36X-RAY DIFFRACTION36chain 'F' and (resid 20 through 91 )F0
37X-RAY DIFFRACTION37chain 'F' and (resid 92 through 104 )F0
38X-RAY DIFFRACTION38chain 'F' and (resid 105 through 116 )F0
39X-RAY DIFFRACTION39chain 'F' and (resid 117 through 131 )F0
40X-RAY DIFFRACTION40chain 'F' and (resid 132 through 153 )F0
41X-RAY DIFFRACTION41chain 'F' and (resid 154 through 177 )F0
42X-RAY DIFFRACTION42chain 'F' and (resid 178 through 217 )F0
43X-RAY DIFFRACTION43chain 'G' and (resid 266 through 287 )G0

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