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- PDB-4wjv: Crystal structure of Rsa4 in complex with the Nsa2 binding peptide -

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Basic information

Entry
Database: PDB / ID: 4wjv
TitleCrystal structure of Rsa4 in complex with the Nsa2 binding peptide
Components
  • Maltose-binding periplasmic protein
  • Ribosome assembly protein 4
  • Ribosome biogenesis protein NSA2
KeywordsPROTEIN BINDING / ribosome biogenesis ribosome assembly
Function / homology
Function and homology information


protein-RNA complex remodeling / Antigen processing: Ubiquitination & Proteasome degradation / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / preribosome, large subunit precursor ...protein-RNA complex remodeling / Antigen processing: Ubiquitination & Proteasome degradation / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / preribosome, large subunit precursor / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA / ribosomal large subunit biogenesis / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / ribosomal large subunit assembly / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / nucleolus / membrane / nucleus
Similarity search - Function
NLE / NLE (NUC135) domain / Ribosomal biogenesis NSA2 family / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / YVTN repeat-like/Quinoprotein amine dehydrogenase / Bacterial extracellular solute-binding protein / 7 Propeller / Methylamine Dehydrogenase; Chain H ...NLE / NLE (NUC135) domain / Ribosomal biogenesis NSA2 family / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / YVTN repeat-like/Quinoprotein amine dehydrogenase / Bacterial extracellular solute-binding protein / 7 Propeller / Methylamine Dehydrogenase; Chain H / Bacterial extracellular solute-binding protein / Ribosomal protein S8e/ribosomal biogenesis NSA2 / Ribosomal protein S8e / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Mainly Beta
Similarity search - Domain/homology
alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Ribosome assembly protein 4 / Ribosome biogenesis protein NSA2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Escherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsHoldermann, I. / Paternoga, H. / Bassler, J. / Hurt, E. / Sinning, I.
CitationJournal: J.Cell Biol. / Year: 2014
Title: A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.
Authors: Baler, J. / Paternoga, H. / Holdermann, I. / Thoms, M. / Granneman, S. / Barrio-Garcia, C. / Nyarko, A. / Stier, G. / Clark, S.A. / Schraivogel, D. / Kallas, M. / Beckmann, R. / Tollervey, D. ...Authors: Baler, J. / Paternoga, H. / Holdermann, I. / Thoms, M. / Granneman, S. / Barrio-Garcia, C. / Nyarko, A. / Stier, G. / Clark, S.A. / Schraivogel, D. / Kallas, M. / Beckmann, R. / Tollervey, D. / Barbar, E. / Sinning, I. / Hurt, E.
History
DepositionOct 1, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Nov 19, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 3, 2014Group: Database references
Revision 1.2Dec 10, 2014Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_asym.entity_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _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: Ribosome assembly protein 4
B: Ribosome assembly protein 4
C: Ribosome assembly protein 4
D: Ribosome assembly protein 4
E: Maltose-binding periplasmic protein
F: Maltose-binding periplasmic protein
G: Maltose-binding periplasmic protein
H: Maltose-binding periplasmic protein
I: Ribosome biogenesis protein NSA2
J: Ribosome biogenesis protein NSA2
K: Ribosome biogenesis protein NSA2
L: Ribosome biogenesis protein NSA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)348,67826
Polymers346,34812
Non-polymers2,33014
Water0
1
A: Ribosome assembly protein 4
K: Ribosome biogenesis protein NSA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,2275
Polymers44,9392
Non-polymers2883
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Ribosome assembly protein 4
L: Ribosome biogenesis protein NSA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,1314
Polymers44,9392
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Ribosome assembly protein 4
I: Ribosome biogenesis protein NSA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,1314
Polymers44,9392
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Ribosome assembly protein 4
J: Ribosome biogenesis protein NSA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,2275
Polymers44,9392
Non-polymers2883
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Maltose-binding periplasmic protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9902
Polymers41,6481
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Maltose-binding periplasmic protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9902
Polymers41,6481
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Maltose-binding periplasmic protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9902
Polymers41,6481
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Maltose-binding periplasmic protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9902
Polymers41,6481
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)198.578, 96.493, 196.445
Angle α, β, γ (deg.)90.00, 115.45, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
Ribosome assembly protein 4


Mass: 42455.133 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: RSA4, YCR072C, YCR72C / Production host: Escherichia coli (E. coli) / References: UniProt: P25382
#2: Protein
Maltose-binding periplasmic protein / MBP / MMBP / Maltodextrin-binding protein


Mass: 41648.133 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Rsa4-interacting peptide of Nsa2 was fused C-terminally to carrier-protein MBP (mutated to reduce surface entropy) and co-crystallized with Rsa4. The linker (6 residues) between MBP and the ...Details: Rsa4-interacting peptide of Nsa2 was fused C-terminally to carrier-protein MBP (mutated to reduce surface entropy) and co-crystallized with Rsa4. The linker (6 residues) between MBP and the Nsa2 peptide is not visible in the electron density and was not built into the model.
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: malE, b4034, JW3994 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AEX9
#3: Protein/peptide
Ribosome biogenesis protein NSA2 / / NOP7-associated protein 2


Mass: 2483.665 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Rsa4-interacting peptide of Nsa2 was fused C-terminally to carrier-protein MBP (mutated to reduce surface entropy) and co-crystallized with Rsa4. The linker (6 residues) between MBP and the ...Details: Rsa4-interacting peptide of Nsa2 was fused C-terminally to carrier-protein MBP (mutated to reduce surface entropy) and co-crystallized with Rsa4. The linker (6 residues) between MBP and the Nsa2 peptide is not visible in the electron density and was not built into the model.
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: NSA2, YER126C, SYGP-ORF47 / Production host: Escherichia coli (E. coli) / References: UniProt: P40078
#4: Polysaccharide
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#5: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: SO4

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.39 Å3/Da / Density % sol: 48.44 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2M NH4SO4, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 1.3 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 7, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.3 Å / Relative weight: 1
ReflectionResolution: 3.2→48.985 Å / Num. obs: 55664 / % possible obs: 100 % / Redundancy: 11.4 % / Rmerge(I) obs: 0.168 / Net I/σ(I): 15.6
Reflection shellResolution: 3.2→3.3 Å / Redundancy: 11.5 % / Mean I/σ(I) obs: 3.1 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.4_1496)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4WJU and 4EDQ

4wju

4edq


Resolution: 3.2→48.985 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 23.55 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2438 2823 5.07 %
Rwork0.192 --
obs0.1946 55659 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.2→48.985 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23533 0 142 0 23675
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00324257
X-RAY DIFFRACTIONf_angle_d0.69632957
X-RAY DIFFRACTIONf_dihedral_angle_d12.1638721
X-RAY DIFFRACTIONf_chiral_restr0.0273615
X-RAY DIFFRACTIONf_plane_restr0.0034181
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.25520.37941360.28672660X-RAY DIFFRACTION100
3.2552-3.31440.29051410.27492617X-RAY DIFFRACTION100
3.3144-3.37810.29461240.24952611X-RAY DIFFRACTION100
3.3781-3.4470.27121340.24612679X-RAY DIFFRACTION100
3.447-3.5220.27941560.23692571X-RAY DIFFRACTION100
3.522-3.60390.30141420.23252595X-RAY DIFFRACTION100
3.6039-3.6940.27241520.2182643X-RAY DIFFRACTION100
3.694-3.79380.27011480.21722607X-RAY DIFFRACTION100
3.7938-3.90540.2791400.21572640X-RAY DIFFRACTION100
3.9054-4.03140.26511360.20112617X-RAY DIFFRACTION100
4.0314-4.17540.23951300.19252653X-RAY DIFFRACTION100
4.1754-4.34250.2211420.16652632X-RAY DIFFRACTION100
4.3425-4.540.20851360.16032645X-RAY DIFFRACTION100
4.54-4.77920.20921510.16072634X-RAY DIFFRACTION100
4.7792-5.07830.21341610.15532617X-RAY DIFFRACTION100
5.0783-5.46990.20441360.16822646X-RAY DIFFRACTION100
5.4699-6.01950.24831310.18692678X-RAY DIFFRACTION100
6.0195-6.88850.25891410.18492672X-RAY DIFFRACTION100
6.8885-8.67090.25341440.18082674X-RAY DIFFRACTION100
8.6709-48.99050.19191420.16322745X-RAY DIFFRACTION100
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)
10.15150.0545-0.17860.51140.49670.3485-0.10350.1289-0.1573-1.2304-0.0239-0.07590.382-0.1104-01.4505-0.21010.21970.6895-0.18430.969636.9576-5.185861.8896
20.8604-0.16920.02720.28330.25590.6815-0.0763-0.0461-0.1232-0.36760.2294-0.9102-0.08580.07130.15760.7993-0.10920.27560.5106-0.2271.077150.0286.014671.048
30.8098-1.0139-1.05861.59450.01451.9510.1398-0.0440.0705-0.54250.2005-0.2888-0.1092-0.18570.01410.7742-0.09010.0370.4645-0.05720.595131.447413.43775.6177
40.8261-0.16060.80852.2634-0.63531.2963-0.24280.064-0.08080.2624-0.0528-0.48970.43290.2472-0.10210.57490.0786-0.10180.73120.07450.606981.06134.71227.5143
50.18850.18910.31390.7579-0.08450.48780.06250.01110.06920.227-0.0303-0.2125-0.02140.1015-00.57330.0454-0.12780.74250.07640.484376.439521.192633.8827
60.95520.5480.50191.7409-0.95620.9888-0.00840.1838-0.11260.0329-0.0143-0.0264-0.10610.0121-00.42690.0308-0.0320.58490.07830.448868.632320.946217.0703
71.92431.296-1.15661.6845-0.46141.5931-0.10740.030.503-0.50570.0627-0.4719-0.06550.0692-0.0140.644-0.08690.09060.59990.12280.829441.5035-36.648263.7261
80.49550.4869-0.21621.4854-0.03090.8084-0.56360.2084-0.3948-0.7360.477-0.4427-0.044-0.0135-0.1560.7053-0.15680.25180.75340.03430.808941.4683-51.193758.0768
90.17830.167-0.11970.3984-0.2349-0.0102-0.09631.03960.3153-0.76740.4139-0.12670.1493-0.3860.00010.7618-0.1450.03130.75980.00920.569426.7886-55.460858.2141
101.5951.2123-0.2731.2795-1.00151.1562-0.045-0.15970.16570.1017-0.13970.01870.16740.1485-0.00010.4904-0.04420.03490.48630.05520.601329.0351-51.038276.5259
111.18240.94370.34892.5059-0.05811.00930.081-0.14220.22650.378-0.0155-0.3065-0.40670.036100.6219-0.0106-0.01950.69310.01030.560584.3967-29.402823.2603
120.37770.44670.6040.1111-0.03840.01230.1166-0.1218-0.26840.23220.0478-0.15760.1914-0.2308-00.63-0.0122-0.11710.63490.07240.535785.6318-46.699325.4978
130.74350.7880.31281.0728-0.73330.98120.0338-0.0280.16450.0563-0.110.0476-0.0289-0.2183-0.00010.41220.00190.02690.66150.09870.502370.1661-43.395815.8025
140.4001-0.10480.41621.1307-0.46070.6699-0.06740.14020.06780.57780.1471-0.194-0.17650.10510.00010.8081-0.02280.08410.42130.00790.557843.4609-15.720137.6169
150.04940.165-0.08110.12580.1830.04520.26180.0403-0.68430.4634-0.22490.3156-0.0091-0.0905-0.00020.8638-0.10260.15460.5412-0.00750.59234.9779-30.519931.1681
16-0.22550.37240.75070.4191-0.18740.8651-0.12410.0394-0.12490.3263-0.01720.3356-0.1287-0.2194-00.5375-0.00660.17930.5108-0.05510.526529.0652-6.4716.3929
170.07660.09390.21010.07720.15670.16530.20510.4199-0.5699-0.7108-0.30530.21070.11340.457-0.0010.4972-0.00170.06480.4253-0.0220.470942.4914-23.13677.0752
180.34290.32440.12470.5274-0.48350.37990.1996-0.27040.02230.2208-0.1007-0.0656-0.0783-0.1444-00.53990.01020.070.4786-0.05820.411734.41391.774311.861
190.4221-0.14930.27090.1335-0.18140.2491-0.0023-0.4845-0.02720.0619-0.26770.2912-0.5294-1.05330.04040.69750.08610.18810.5947-0.05370.527724.3074-1.230325.2508
200.6864-0.16-0.47270.81530.70690.50290.0301-0.1679-0.05260.1599-0.18340.10431.0224-0.2987-0.00020.6674-0.1150.11650.3828-0.010.476135.9259-19.882727.5355
210.17630.11890.25540.22560.20610.2201-0.4617-0.6452-0.16310.29320.45940.5408-0.1485-0.8076-0.01450.8176-0.00930.2670.6641-0.00470.674124.4197-18.495935.3168
220.371-0.42850.1050.674-0.09031.5015-0.0029-0.0351-0.20670.1508-0.07060.2294-0.0510.0324-00.5292-0.0260.03760.3878-0.03070.521740.2305-11.972513.1012
23-0.01460.2950.02950.638-0.21090.24240.04610.1542-0.0693-0.4794-0.048-0.10250.27640.5693-00.77320.0423-0.02980.92170.13610.56555.3118-13.385951.3583
240.7779-0.34170.11340.8097-0.86851.62960.04860.18320.1086-0.10460.01770.13060.01670.090400.54790.016-0.05670.45310.03250.4671-7.1169-18.343868.4509
250.15210.2333-0.09730.1759-0.07650.08650.12840.68820.1024-0.592-0.12280.62890.2277-0.22070.00010.89840.0173-0.10090.79940.20940.7917-13.6091-10.379252.155
260.0844-0.006-0.13340.1183-0.07950.0704-0.1702-0.18121.1687-0.2556-0.03410.59470.1055-0.16920.00020.80920.0163-0.06330.54110.06910.6753-11.7517-11.81568.7164
270.1472-0.0511-0.07360.02680.07420.3964-0.15270.690.02230.21520.2401-0.91630.39150.76960.01160.5447-0.14510.09070.47090.04440.52035.9897-19.5874.9448
280.2063-0.00850.17640.11530.14960.1924-0.169-0.1048-0.12790.23270.1905-0.51430.24850.6149-0.00010.53070.0186-0.05760.51090.01240.62197.3123-22.87183.8406
290.316-0.08380.1880.12270.10950.2320.4287-0.4676-0.4096-0.0971-0.3059-0.4250.85111.24430.90120.0068-0.28470.27481.3643-0.14790.777890.3352-7.932-15.6656
300.15260.04090.09220.13910.18120.3243-0.2139-0.0573-0.68440.48570.09210.1364-0.3350.6305-0.00020.59630.01040.06380.70510.06690.61678.8989-4.8309-5.4679
311.80881.27230.1841.60710.90161.2891-0.29970.369-0.0707-0.45760.2833-0.0684-0.28950.24810.00080.4846-0.06370.03220.5585-0.0130.387764.3333-11.5425-19.6199
320.3085-0.15150.19240.1213-0.08370.26560.24290.10480.2793-0.3107-0.3661-0.3287-0.08380.2690.09380.7137-0.54090.16991.3751-0.13410.765487.62531.2408-21.9909
330.02910.3310.1680.06260.20560.2959-0.07250.39340.0147-0.47520.1315-0.1472-0.25080.4092-0.0020.6997-0.24190.06830.89060.00190.478470.8124-3.553-27.3651
340.2877-0.13090.37540.1873-0.31070.54870.2326-0.4172-0.07230.8326-0.0725-0.45350.05980.0568-00.4222-0.0282-0.00890.4221-0.04120.505758.6648-13.8042-3.5484
350.26680.26370.48330.58870.64290.791-0.0660.053-0.2635-0.14920.445-0.58070.17610.24570.29910.47730.1679-0.12820.7989-0.29491.568840.5027-26.3391106.574
362.0386-0.28790.48120.83180.44351.13-0.0682-0.40550.06420.18320.2124-0.44660.1207-0.01520.0760.49050.1311-0.1830.4398-0.13330.711521.476-17.125111.24
371.24390.27430.02852.2456-0.07490.83950.135-0.2180.0603-0.21610.1835-0.6910.19750.11450.60550.35280.1225-0.14860.4171-0.13520.804321.6148-21.1986107.4382
380.00530.03410.00580.01470.0238-0.0013-0.2521-0.20480.41520.1284-0.12010.19010.20990.19270.00070.56380.00780.10240.47790.1811.185723.6414-33.789167.3518
390.01780.04270.0390.03650.0411-0.0027-0.30730.07820.5148-0.24740.1243-0.6016-0.4070.1606-0.00020.67490.0580.01340.61190.02120.813673.2413-25.40199.689
400.0150.00370.01260.02750.03670.02710.1208-0.29230.2986-0.50210.5254-0.46480.1318-0.1091-0.00010.8641-0.10210.15730.65240.10250.784532.018-5.109382.2975
410.035-0.06680.06120.0841-0.00620.0352-0.27190.0187-0.37890.4654-0.24320.2805-1.0468-0.2626-00.58740.1032-0.01030.57020.16340.770762.74623.390623.0691
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 138 through 223 )
2X-RAY DIFFRACTION2chain 'A' and (resid 224 through 364 )
3X-RAY DIFFRACTION3chain 'A' and (resid 365 through 515 )
4X-RAY DIFFRACTION4chain 'B' and (resid 138 through 286 )
5X-RAY DIFFRACTION5chain 'B' and (resid 287 through 386 )
6X-RAY DIFFRACTION6chain 'B' and (resid 387 through 515 )
7X-RAY DIFFRACTION7chain 'C' and (resid 138 through 299 )
8X-RAY DIFFRACTION8chain 'C' and (resid 300 through 364 )
9X-RAY DIFFRACTION9chain 'C' and (resid 365 through 410 )
10X-RAY DIFFRACTION10chain 'C' and (resid 411 through 515 )
11X-RAY DIFFRACTION11chain 'D' and (resid 138 through 328 )
12X-RAY DIFFRACTION12chain 'D' and (resid 329 through 386 )
13X-RAY DIFFRACTION13chain 'D' and (resid 387 through 515 )
14X-RAY DIFFRACTION14chain 'E' and (resid 12 through 83 )
15X-RAY DIFFRACTION15chain 'E' and (resid 84 through 106 )
16X-RAY DIFFRACTION16chain 'E' and (resid 107 through 174 )
17X-RAY DIFFRACTION17chain 'E' and (resid 175 through 195 )
18X-RAY DIFFRACTION18chain 'E' and (resid 196 through 228 )
19X-RAY DIFFRACTION19chain 'E' and (resid 229 through 255 )
20X-RAY DIFFRACTION20chain 'E' and (resid 256 through 292 )
21X-RAY DIFFRACTION21chain 'E' and (resid 293 through 324 )
22X-RAY DIFFRACTION22chain 'E' and (resid 325 through 380 )
23X-RAY DIFFRACTION23chain 'F' and (resid 13 through 83 )
24X-RAY DIFFRACTION24chain 'F' and (resid 84 through 292 )
25X-RAY DIFFRACTION25chain 'F' and (resid 293 through 324 )
26X-RAY DIFFRACTION26chain 'F' and (resid 325 through 343 )
27X-RAY DIFFRACTION27chain 'F' and (resid 344 through 361 )
28X-RAY DIFFRACTION28chain 'F' and (resid 362 through 380 )
29X-RAY DIFFRACTION29chain 'G' and (resid 12 through 52 )
30X-RAY DIFFRACTION30chain 'G' and (resid 53 through 83 )
31X-RAY DIFFRACTION31chain 'G' and (resid 84 through 282 )
32X-RAY DIFFRACTION32chain 'G' and (resid 283 through 304 )
33X-RAY DIFFRACTION33chain 'G' and (resid 305 through 343 )
34X-RAY DIFFRACTION34chain 'G' and (resid 344 through 380 )
35X-RAY DIFFRACTION35chain 'H' and (resid 12 through 106 )
36X-RAY DIFFRACTION36chain 'H' and (resid 107 through 304 )
37X-RAY DIFFRACTION37chain 'H' and (resid 305 through 380 )
38X-RAY DIFFRACTION38chain 'I' and (resid 85 through 95 )
39X-RAY DIFFRACTION39chain 'J' and (resid 85 through 95 )
40X-RAY DIFFRACTION40chain 'K' and (resid 85 through 96 )
41X-RAY DIFFRACTION41chain 'L' and (resid 85 through 95 )

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