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- PDB-6mgq: ERAP1 in the open conformation bound to 10mer phosphinic inhibito... -

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Basic information

Entry
Database: PDB / ID: 6mgq
TitleERAP1 in the open conformation bound to 10mer phosphinic inhibitor DG014
Components
  • Endoplasmic reticulum aminopeptidase 1ERAP1
  • Phosphinic inhibitor DG014
KeywordsHYDROLASE/INHIBITOR / Inhibitor / Aminopeptidase / Immune System / HYDROLASE / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


interleukin-1, type II receptor binding / interleukin-6 receptor binding / Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / metalloexopeptidase activity / antigen processing and presentation of peptide antigen via MHC class I / peptide catabolic process / regulation of innate immune response / fat cell differentiation / metalloaminopeptidase activity / membrane protein ectodomain proteolysis ...interleukin-1, type II receptor binding / interleukin-6 receptor binding / Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / metalloexopeptidase activity / antigen processing and presentation of peptide antigen via MHC class I / peptide catabolic process / regulation of innate immune response / fat cell differentiation / metalloaminopeptidase activity / membrane protein ectodomain proteolysis / aminopeptidase activity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide binding / response to bacterium / antigen processing and presentation of endogenous peptide antigen via MHC class I / regulation of blood pressure / positive regulation of angiogenesis / angiogenesis / endopeptidase activity / adaptive immune response / endoplasmic reticulum lumen / endoplasmic reticulum membrane / endoplasmic reticulum / proteolysis / extracellular space / extracellular exosome / zinc ion binding / extracellular region / membrane / cytosol / cytoplasm
Similarity search - Function
Zincin-like fold - #20 / Immunoglobulin-like - #1910 / Aminopeptidase N-type / ERAP1-like C-terminal domain / ERAP1-like C-terminal domain / Zincin-like fold / tricorn interacting facor f3 domain / Aminopeptidase N-like , N-terminal domain / Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase / Peptidase M1, membrane alanine aminopeptidase ...Zincin-like fold - #20 / Immunoglobulin-like - #1910 / Aminopeptidase N-type / ERAP1-like C-terminal domain / ERAP1-like C-terminal domain / Zincin-like fold / tricorn interacting facor f3 domain / Aminopeptidase N-like , N-terminal domain / Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase / Peptidase M1, membrane alanine aminopeptidase / Peptidase family M1 domain / Peptidase M1 N-terminal domain / Aminopeptidase N-like , N-terminal domain superfamliy / Neutral Protease Domain 2 / Neutral Protease; domain 2 / Peptidase M4/M1, CTD superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / Alpha Horseshoe / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Phosphinic inhibitor DG014 / Endoplasmic reticulum aminopeptidase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.92 Å
AuthorsStern, L.J. / Maben, Z.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)R01AI038996 United States
CitationJournal: Nat Commun / Year: 2021
Title: Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
Authors: Maben, Z. / Arya, R. / Georgiadis, D. / Stratikos, E. / Stern, L.J.
History
DepositionSep 14, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 18, 2019Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / 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_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / 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.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 / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.pdbx_value_order / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.0Jan 20, 2021Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Other / Refinement description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / atom_type / cell / chem_comp / entity / pdbx_branch_scheme / pdbx_entity_branch_descriptor / pdbx_entity_nonpoly / pdbx_entry_details / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / refine / refine_hist / refine_ls_restr / refine_ls_shell / reflns / reflns_shell / struct / struct_asym / struct_conn / symmetry
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.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _cell.volume / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _pdbx_branch_scheme.auth_asym_id / _pdbx_branch_scheme.auth_seq_num / _pdbx_entity_branch_descriptor.descriptor / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_mon_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.entity_id / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_refine_tls_group.selection_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine.ls_percent_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_hist.d_res_high / _refine_hist.number_atoms_solvent / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_protein / _refine_ls_restr.dev_ideal / _refine_ls_restr.number / _refine_ls_restr.type / _refine_ls_shell.percent_reflns_obs / _reflns.pdbx_CC_half / _reflns.pdbx_Rpim_I_all / _reflns.pdbx_Rrim_I_all / _struct.title / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_label_asym_id / _symmetry.space_group_name_Hall
Revision 3.1Jun 1, 2022Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 3.2Oct 11, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Endoplasmic reticulum aminopeptidase 1
B: Endoplasmic reticulum aminopeptidase 1
C: Endoplasmic reticulum aminopeptidase 1
D: Phosphinic inhibitor DG014
E: Phosphinic inhibitor DG014
F: Phosphinic inhibitor DG014
hetero molecules


Theoretical massNumber of molelcules
Total (without water)332,95818
Polymers329,5136
Non-polymers3,44512
Water64936
1
A: Endoplasmic reticulum aminopeptidase 1
D: Phosphinic inhibitor DG014
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,0946
Polymers109,8382
Non-polymers1,2574
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2880 Å2
ΔGint-24 kcal/mol
Surface area37160 Å2
MethodPISA
2
B: Endoplasmic reticulum aminopeptidase 1
E: Phosphinic inhibitor DG014
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,0946
Polymers109,8382
Non-polymers1,2574
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2700 Å2
ΔGint-24 kcal/mol
Surface area37020 Å2
MethodPISA
3
C: Endoplasmic reticulum aminopeptidase 1
F: Phosphinic inhibitor DG014
hetero molecules


Theoretical massNumber of molelcules
Total (without water)110,7706
Polymers109,8382
Non-polymers9324
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2410 Å2
ΔGint-27 kcal/mol
Surface area36700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.140, 234.700, 132.280
Angle α, β, γ (deg.)90.00, 93.12, 90.00
Int Tables number4
Space group name H-MP1211
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

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Protein / Protein/peptide , 2 types, 6 molecules ABCDEF

#1: Protein Endoplasmic reticulum aminopeptidase 1 / ERAP1 / ARTS-1 / Adipocyte-derived leucine aminopeptidase / A-LAP / Aminopeptidase PILS / Puromycin- ...ARTS-1 / Adipocyte-derived leucine aminopeptidase / A-LAP / Aminopeptidase PILS / Puromycin-insensitive leucyl-specific aminopeptidase / PILS-AP / Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator


Mass: 108557.305 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 / Production host: Trichoplusia ni (cabbage looper)
References: UniProt: Q9NZ08, Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases
#2: Protein/peptide Phosphinic inhibitor DG014


Type: Peptide-like / Class: Inhibitor / Mass: 1280.401 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: Phosphinic inhibitor DG014

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Sugars , 3 types, 6 molecules

#3: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE

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Non-polymers , 3 types, 42 molecules

#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#7: Chemical ChemComp-UNX / UNKNOWN ATOM OR ION


Mass: 18.015 Da / Num. of mol.: 3 / Source method: isolated from a natural source
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsUNX marks the site of electron density that might correspond to the C-terminus of the bound DG014 ...UNX marks the site of electron density that might correspond to the C-terminus of the bound DG014 ligand or to an unidentified buffer component.

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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: 2.66 Å3/Da / Density % sol: 58.55 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.6
Details: Final drop composition: 100mM Tris pH 8.60, 3.5% PEG 8000, 3% D-sorbitol, 5mg/mL ERAP1 preincubated with inhibitor

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 24, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.83→87.73 Å / Num. obs: 80216 / % possible obs: 99 % / Redundancy: 2.7 % / Biso Wilson estimate: 59.49 Å2 / Rmerge(I) obs: 0.182 / Net I/σ(I): 4.1
Reflection shellResolution: 2.92→2.99 Å / Redundancy: 2.4 % / Rmerge(I) obs: 1.919 / Mean I/σ(I) obs: 0.3 / % possible all: 98.9

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Processing

Software
NameVersionClassification
PHENIX1.14_3211refinement
MOSFLM7.2.1data reduction
PHASERphasing
STARANISO1.7.2data scaling
Aimless0.5.31data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3MDJ

3mdj


Resolution: 2.92→56.06 Å / SU ML: 0.403 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 29.776
RfactorNum. reflection% reflectionSelection details
Rfree0.256 2987 4.97 %Random selection
Rwork0.198 ---
obs0.201 60060 81.7 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 70.7 Å2
Refinement stepCycle: LAST / Resolution: 2.92→56.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20399 0 218 36 20653
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00521150
X-RAY DIFFRACTIONf_angle_d0.7828768
X-RAY DIFFRACTIONf_dihedral_angle_d16.7357587
X-RAY DIFFRACTIONf_chiral_restr0.0473267
X-RAY DIFFRACTIONf_plane_restr0.0073607
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.92-2.970.3564260.3138480X-RAY DIFFRACTION14
2.97-3.020.3172320.3158656X-RAY DIFFRACTION20
3.02-3.080.4158550.29371046X-RAY DIFFRACTION31
3.08-3.140.4332690.30541428X-RAY DIFFRACTION42
3.14-3.20.3659740.30311831X-RAY DIFFRACTION56
3.2-3.270.39771220.28722400X-RAY DIFFRACTION72
3.27-3.350.31421620.2762983X-RAY DIFFRACTION90
3.35-3.430.34221680.25533254X-RAY DIFFRACTION98
3.43-3.520.30751670.24693359X-RAY DIFFRACTION99
3.52-3.630.3541650.2323224X-RAY DIFFRACTION99
3.63-3.740.32771820.21893392X-RAY DIFFRACTION100
3.74-3.880.24411560.20133259X-RAY DIFFRACTION99
3.88-4.030.26791940.1983302X-RAY DIFFRACTION99
4.03-4.220.23911790.1773263X-RAY DIFFRACTION99
4.22-4.440.23511740.16053309X-RAY DIFFRACTION99
4.44-4.720.20151710.15343343X-RAY DIFFRACTION99
4.72-5.080.22111570.15373357X-RAY DIFFRACTION99
5.08-5.590.21122030.16633235X-RAY DIFFRACTION99
5.59-6.40.26361490.20123341X-RAY DIFFRACTION99
6.4-8.060.22511620.19653350X-RAY DIFFRACTION99
8.06-56.070.20742200.17393261X-RAY DIFFRACTION98
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)
12.8159-0.2867-0.56481.7045-0.3681.65650.0911-0.0605-0.3399-0.1776-0.0780.10790.1631-0.13350.00220.1488-0.0282-0.06830.16960.00620.272444.1273-11.334554.0514
20.47990.53-0.56941.7901-1.73772.9348-0.07150.2263-0.1405-0.42580.08420.14470.3207-0.28260.02890.24780.0094-0.02950.33-0.07150.295153.06469.810622.3015
31.5512-0.0150.15482.6173-0.23951.3991-0.30560.0221-1.057-0.41860.50860.84090.4415-0.55040.02071.2001-0.05230.07370.7589-0.06541.001448.9123-18.3477.4566
42.4277-0.322-0.12093.4684-0.37631.99590.1763-0.13790.32520.8713-0.08570.2218-0.616-0.01910.00470.8174-0.01250.04520.2158-0.04730.343755.637557.25486.3789
51.18031.13450.83973.6174-0.08562.2804-0.03380.00770.0530.2147-0.10940.4851-0.0462-0.2310.00110.3780.0735-0.00530.3308-0.09070.448353.162633.390379.2821
61.68220.27391.98193.38580.85243.1190.0396-0.28150.10720.5298-0.25920.57270.0214-0.118-0.01220.3188-0.0481-0.05390.3418-0.07140.332648.475813.352973.4184
71.648-0.34210.09350.7171-0.25851.47220.1428-0.82540.0671.1694-0.274-0.03910.93520.02790.0261.1028-0.1901-0.04010.6836-0.07710.345658.777411.1693102.45
80.42890.10080.66890.82770.22721.2499-0.3665-0.7690.8070.77160.01281.5576-0.0814-0.9392-0.03261.3559-0.21220.60971.536-0.42021.678941.28220.7496111.4277
93.56840.9363-0.02531.75140.22162.39690.21770.70070.3369-0.3505-0.02610.2131-0.1121-0.04960.06080.18860.10840.00230.480.10590.142348.532646.87015.3828
101.6873-0.5763-0.65471.33060.32372.47960.10160.16650.31490.0945-0.0701-0.3487-0.64770.416-0.06150.1053-0.02680.10820.46750.07630.256467.273356.881522.4299
111.50050.7416-0.6412.30511.61512.2799-0.2212-0.06960.16750.3216-0.08660.6299-0.1563-0.4221-0.03030.18740.0383-0.01480.3583-0.06670.313554.58252.801334.6623
122.28042.26730.40972.6210.64824.49020.09470.16790.03160.6529-0.1086-0.02680.3346-0.28230.01070.344-0.04190.01960.2059-0.06170.292758.107760.389454.6185
132.02330.7714-0.58392.2234-0.17422.4989-0.12780.7480.6126-0.35820.0136-0.6195-0.58660.4266-0.00460.5384-0.176-0.04290.61990.09340.666572.982585.403238.1457
141.0507-0.278-1.19381.39140.28451.268-0.30311.21650.7674-0.56250.03050.81-1.4319-0.89180.01421.0574-0.0441-0.43671.20150.26021.052955.627894.019433.2689
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 44 THROUGH 368 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 369 THROUGH 713 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 714 THROUGH 936 )
4X-RAY DIFFRACTION4CHAIN 'B' AND (RESID 45 THROUGH 368 )
5X-RAY DIFFRACTION5CHAIN 'B' AND (RESID 369 THROUGH 484 )
6X-RAY DIFFRACTION6CHAIN 'B' AND (RESID 485 THROUGH 615 )
7X-RAY DIFFRACTION7CHAIN 'B' AND (RESID 616 THROUGH 777 )
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESID 778 THROUGH 937 )
9X-RAY DIFFRACTION9CHAIN 'C' AND (RESID 44 THROUGH 254 )
10X-RAY DIFFRACTION10CHAIN 'C' AND (RESID 255 THROUGH 411 )
11X-RAY DIFFRACTION11CHAIN 'C' AND (RESID 412 THROUGH 483 )
12X-RAY DIFFRACTION12CHAIN 'C' AND (RESID 484 THROUGH 615 )
13X-RAY DIFFRACTION13CHAIN 'C' AND (RESID 616 THROUGH 794 )
14X-RAY DIFFRACTION14CHAIN 'C' AND (RESID 795 THROUGH 936 )

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