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- PDB-5lhd: Structure of glycosylated human aminopeptidase N -

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Basic information

Entry
Database: PDB / ID: 5lhd
TitleStructure of glycosylated human aminopeptidase N
ComponentsAminopeptidase N
KeywordsHYDROLASE / Human aminopeptidase N / CD13 / metalloprotease
Function / homology
Function and homology information


membrane alanyl aminopeptidase / peptide catabolic process / metalloaminopeptidase activity / endoplasmic reticulum-Golgi intermediate compartment / Metabolism of Angiotensinogen to Angiotensins / aminopeptidase activity / secretory granule membrane / peptide binding / metallopeptidase activity / virus receptor activity ...membrane alanyl aminopeptidase / peptide catabolic process / metalloaminopeptidase activity / endoplasmic reticulum-Golgi intermediate compartment / Metabolism of Angiotensinogen to Angiotensins / aminopeptidase activity / secretory granule membrane / peptide binding / metallopeptidase activity / virus receptor activity / signaling receptor activity / angiogenesis / cell differentiation / external side of plasma membrane / lysosomal membrane / Neutrophil degranulation / proteolysis / extracellular space / extracellular exosome / zinc ion binding / plasma membrane / 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 ...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
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsRecacha, R. / Mudgal, G. / Santiago, C. / Casasnovas, J.M.
Funding support Spain, 1items
OrganizationGrant numberCountry
Spanish Ministry of ScienceBFU2011-23940 and BIO2014-52683-R Spain
CitationJournal: Sci Rep / Year: 2017
Title: Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.
Authors: Santiago, C. / Mudgal, G. / Reguera, J. / Recacha, R. / Albrecht, S. / Enjuanes, L. / Casasnovas, J.M.
History
DepositionJul 11, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 5, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 19, 2017Group: Database references
Revision 1.2Oct 16, 2019Group: Data collection / Category: reflns_shell
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_PDB_caveat / 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 / pdbx_validate_chiral / pdbx_validate_close_contact / 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 / _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] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_chiral.details / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _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.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aminopeptidase N
B: Aminopeptidase N
C: Aminopeptidase N
D: Aminopeptidase N
hetero molecules


Theoretical massNumber of molelcules
Total (without water)454,60689
Polymers431,8554
Non-polymers22,75185
Water11,980665
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A: Aminopeptidase N
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,37027
Polymers107,9641
Non-polymers5,40726
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Aminopeptidase N
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,93922
Polymers107,9641
Non-polymers4,97521
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Aminopeptidase N
hetero molecules


Theoretical massNumber of molelcules
Total (without water)114,98523
Polymers107,9641
Non-polymers7,02122
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Aminopeptidase N
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,31217
Polymers107,9641
Non-polymers5,34816
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)127.093, 168.856, 244.249
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Aminopeptidase N / hAPN / Alanyl aminopeptidase / Aminopeptidase M / AP-M / Microsomal aminopeptidase / Myeloid plasma ...hAPN / Alanyl aminopeptidase / Aminopeptidase M / AP-M / Microsomal aminopeptidase / Myeloid plasma membrane glycoprotein CD13 / gp150


Mass: 107963.734 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ANPEP, APN, CD13, PEPN / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P15144, membrane alanyl aminopeptidase

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Sugars , 8 types, 35 molecules

#2: Polysaccharide
beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-D-mannopyranose-(1-6)-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.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#3: Polysaccharide beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpb1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-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.: 12
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-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.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-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
DManpb1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-6)-[beta-D-mannopyranose-(1-3)]beta-D- ...beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-6)-[beta-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: 1072.964 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3DManpb1-6[DManpb1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2-2/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}}}}}}LINUCSPDB-CARE
#8: Polysaccharide beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)-beta-D- ...beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpb1-6]DManpb1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2-2/a4-b1_b4-c1_c6-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-D-Manp]{}}}}}}LINUCSPDB-CARE
#9: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 715 molecules

#10: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#11: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 46 / Source method: obtained synthetically / Formula: C2H6O2
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 665 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.91 Å3/Da / Density % sol: 57.66 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / Details: 50 mM Imidazol-HCl pH 8.0, 20% PEG6000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 7, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→20 Å / Num. obs: 160764 / % possible obs: 99.8 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 12.3

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Processing

Software
NameVersionClassification
PHENIX1.8_1069refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→19.973 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 0.8 / Phase error: 23.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2141 15393 5.02 %
Rwork0.1815 --
obs0.1831 306485 98.36 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.6→19.973 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29175 0 1491 665 31331
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00331497
X-RAY DIFFRACTIONf_angle_d0.77942928
X-RAY DIFFRACTIONf_dihedral_angle_d22.40911882
X-RAY DIFFRACTIONf_chiral_restr0.0544927
X-RAY DIFFRACTIONf_plane_restr0.0035348
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.62950.32315370.27619656X-RAY DIFFRACTION99
2.6295-2.66030.29435120.25879656X-RAY DIFFRACTION98
2.6603-2.69270.30394910.26249731X-RAY DIFFRACTION98
2.6927-2.72670.30234500.2659605X-RAY DIFFRACTION97
2.7267-2.76250.30624950.25299616X-RAY DIFFRACTION97
2.7625-2.80030.3075130.24629506X-RAY DIFFRACTION97
2.8003-2.84010.26924600.23679796X-RAY DIFFRACTION99
2.8401-2.88240.27125450.23229774X-RAY DIFFRACTION99
2.8824-2.92730.28924980.24119715X-RAY DIFFRACTION99
2.9273-2.97520.27244890.23139796X-RAY DIFFRACTION99
2.9752-3.02630.27275580.23059779X-RAY DIFFRACTION99
3.0263-3.08110.25814680.23229787X-RAY DIFFRACTION99
3.0811-3.14020.29954800.22099791X-RAY DIFFRACTION99
3.1402-3.2040.2585280.22259853X-RAY DIFFRACTION99
3.204-3.27340.25375470.22199632X-RAY DIFFRACTION99
3.2734-3.34920.25635760.21289751X-RAY DIFFRACTION99
3.3492-3.43250.23375190.20589791X-RAY DIFFRACTION99
3.4325-3.52490.235170.20339543X-RAY DIFFRACTION97
3.5249-3.6280.22314910.19389561X-RAY DIFFRACTION97
3.628-3.74440.2115370.17999610X-RAY DIFFRACTION98
3.7444-3.87720.21155510.18059713X-RAY DIFFRACTION99
3.8772-4.03130.20565670.16999752X-RAY DIFFRACTION99
4.0313-4.21310.16484870.14949806X-RAY DIFFRACTION99
4.2131-4.43290.17245650.13889748X-RAY DIFFRACTION99
4.4329-4.70730.16235060.12939785X-RAY DIFFRACTION99
4.7073-5.06520.17454580.149749X-RAY DIFFRACTION98
5.0652-5.5650.17114990.14919477X-RAY DIFFRACTION96
5.565-6.34750.21155000.16839844X-RAY DIFFRACTION100
6.3475-7.91360.18695220.16259763X-RAY DIFFRACTION99
7.9136-19.97350.1495270.13499506X-RAY DIFFRACTION97
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)
12.51570.79420.49052.37670.04781.7852-0.0424-0.05050.1492-0.03530.0070.4081-0.0207-0.33630.03660.26350.0213-0.01940.4402-0.02990.3309-32.565412.856146.696
21.0683-0.06880.24611.53550.50991.51040.1233-0.0844-0.14980.3178-0.0019-0.06380.5184-0.0051-0.11440.5347-0.062-0.09420.410.05410.3319-20.9096-20.407448.247
31.6756-0.05920.921.40090.32662.03590.2725-0.1404-0.34280.2292-0.0814-0.03430.7388-0.3023-0.18470.6723-0.1184-0.06850.3895-0.02170.4456-32.6333-37.185629.7349
43.2554-0.72210.34711.03710.47852.99720.2553-0.12040.6266-0.10870.0055-0.2236-0.46670.3317-0.24630.5546-0.12010.08230.4126-0.12290.4939-29.5375-18.301818.0252
50.5718-0.80850.33024.1410.60260.7210.1775-0.0171-0.2227-0.0922-0.21430.35820.2358-0.42020.02790.6014-0.10560.05110.7653-0.02040.5995-35.1418-11.173445.7165
62.47041.0635-0.53953.1129-0.84771.7277-0.02740.0981-0.1304-0.3525-0.109-0.28720.28150.1880.12930.39480.08-0.00390.42090.03530.241332.1661-13.253153.4347
70.8571-0.63040.29311.4391-0.45320.91830.0052-0.07520.14350.108-0.0435-0.0127-0.21420.04440.03770.4345-0.02420.02190.4482-0.02440.310619.361119.676255.2523
81.8341-0.8257-0.97420.70480.1151.67820.2499-0.08820.373-0.0436-0.0711-0.0983-0.41160.265-0.17750.5488-0.07780.03160.40130.05640.454430.376636.955136.744
93.301-0.86340.12780.93540.00072.53380.31630.001-0.6709-0.1173-0.03360.18950.516-0.1579-0.28240.5703-0.0576-0.09130.49840.13920.499228.70617.791124.8219
101.0935-1.16950.36933.5116-0.60471.3151-0.0638-0.03010.139-0.2363-0.0135-0.5922-0.08480.01080.13670.6781-0.19190.03130.8540.11060.559633.27827.215557.9443
112.274-0.80210.22532.3292-0.86882.12170.04980.0220.105-0.24760.018-0.3479-0.00280.4261-0.03920.3616-0.08630.09530.4882-0.0560.418755.2973-44.240837.987
121.31750.3251-0.02630.9298-0.12681.56870.02560.0257-0.1454-0.0770.0782-0.00230.0806-0.1702-0.10350.35120.0220.01570.35310.02680.295922.2902-55.619332.4922
131.12640.7748-0.62410.9969-0.12412.36230.0450.17710.0194-0.12090.06370.1574-0.1048-0.5523-0.11340.47450.011-0.07820.55710.03820.378113.3468-51.55546.7035
141.77650.8575-0.4382.58110.45342.50440.1311-0.072-0.24970.41310.0657-0.48420.53850.3493-0.18870.65080.0657-0.12280.4216-0.01910.389134.8386-57.58523.8022
152.53311.08170.84881.06090.58711.6679-0.21630.15170.1043-0.58570.08980.1997-0.065-0.06420.14080.88690.0081-0.00590.72660.06580.706125.0517-41.72125.9535
161.50540.44980.00682.038-0.17831.69540.0939-0.2065-0.08890.1297-0.0925-0.4677-0.18970.63710.01920.3385-0.1086-0.06870.68990.02270.452256.2408-40.888689.7669
171.0674-0.24390.03640.79550.08711.4180.0254-0.10080.0790.08470.02740.0451-0.2394-0.1559-0.0530.4079-0.0429-0.010.43460.00920.300923.2135-29.694996.5322
181.1046-0.79360.60580.9043-0.04662.4002-0.0126-0.2154-0.0620.0860.20440.19960.0564-0.6168-0.18230.421-0.00010.11650.57930.0350.355314.9903-33.8266122.5615
191.0667-0.59030.82373.4745-0.78512.55190.00860.02890.1831-0.4027-0.0612-0.6663-0.41130.3220.06310.5650.00910.16040.4964-0.0580.436536.0284-26.5666125.0947
201.9443-1.0493-0.52221.6770.70930.64980.0173-0.4675-0.04020.37750.17730.0692-0.02540.2177-0.17150.7791-0.0112-0.04270.99220.1080.552933.103-42.978398.0337
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resseq 63:286)
2X-RAY DIFFRACTION2(chain 'A' and resseq 287:652)
3X-RAY DIFFRACTION3(chain 'A' and resseq 653:802)
4X-RAY DIFFRACTION4(chain 'A' and resseq 803:967)
5X-RAY DIFFRACTION5(chain 'A' and resseq 1281:8181)
6X-RAY DIFFRACTION6(chain 'B' and resseq 64:286)
7X-RAY DIFFRACTION7(chain 'B' and resseq 287:652)
8X-RAY DIFFRACTION8(chain 'B' and resseq 653:802)
9X-RAY DIFFRACTION9(chain 'B' and resseq 803:967)
10X-RAY DIFFRACTION10(chain 'B' and resseq 1281:8181)
11X-RAY DIFFRACTION11(chain 'C' and resseq 63:286)
12X-RAY DIFFRACTION12(chain 'C' and resseq 287:652)
13X-RAY DIFFRACTION13(chain 'C' and resseq 653:802)
14X-RAY DIFFRACTION14(chain 'C' and resseq 803:967)
15X-RAY DIFFRACTION15(chain 'C' and resseq 1281:7356)
16X-RAY DIFFRACTION16(chain 'D' and resseq 64:286)
17X-RAY DIFFRACTION17(chain 'D' and resseq 287:652)
18X-RAY DIFFRACTION18(chain 'D' and resseq 653:802)
19X-RAY DIFFRACTION19(chain 'D' and resseq 803:967)
20X-RAY DIFFRACTION20(chain 'D' and resseq 1281:8181)

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