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- PDB-6nk0: EphA2 LBD in complex with bA-WLA-Yam peptide -

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Basic information

Entry
Database: PDB / ID: 6nk0
TitleEphA2 LBD in complex with bA-WLA-Yam peptide
Components
  • Ephrin type-A receptor 2
  • bA-WLA-Yam
KeywordsTRANSFERASE / protein-peptide interaction / kinase / ephrin / eph receptor / drug development / SIGNALING PROTEIN
Function / homology
Function and homology information


notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / axial mesoderm formation / pericyte cell differentiation / cAMP metabolic process / positive regulation of bicellular tight junction assembly / regulation of blood vessel endothelial cell migration ...notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / axial mesoderm formation / pericyte cell differentiation / cAMP metabolic process / positive regulation of bicellular tight junction assembly / regulation of blood vessel endothelial cell migration / leading edge membrane / negative regulation of chemokine production / post-anal tail morphogenesis / bone remodeling / transmembrane-ephrin receptor activity / response to growth factor / tight junction / activation of GTPase activity / regulation of lamellipodium assembly / branching involved in mammary gland duct morphogenesis / EPH-Ephrin signaling / neural tube development / RND1 GTPase cycle / RND2 GTPase cycle / RND3 GTPase cycle / mammary gland epithelial cell proliferation / RHOV GTPase cycle / EPHA-mediated growth cone collapse / growth factor binding / regulation of cell adhesion mediated by integrin / lamellipodium membrane / RHOU GTPase cycle / RHOG GTPase cycle / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / RAC2 GTPase cycle / RAC3 GTPase cycle / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / vasculogenesis / regulation of angiogenesis / keratinocyte differentiation / RAC1 GTPase cycle / transmembrane receptor protein tyrosine kinase activity / negative regulation of angiogenesis / phosphatidylinositol 3-kinase/protein kinase B signal transduction / regulation of ERK1 and ERK2 cascade / osteoclast differentiation / cell chemotaxis / skeletal system development / molecular function activator activity / protein localization to plasma membrane / cell motility / positive regulation of protein localization to plasma membrane / axon guidance / receptor protein-tyrosine kinase / ruffle membrane / osteoblast differentiation / intrinsic apoptotic signaling pathway in response to DNA damage / cell migration / lamellipodium / virus receptor activity / receptor complex / cell adhesion / defense response to Gram-positive bacterium / positive regulation of cell migration / cadherin binding / inflammatory response / phosphorylation / focal adhesion / dendrite / cell surface / ATP binding / plasma membrane
Similarity search - Function
Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. ...Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. / Ephrin receptor ligand binding domain / Putative ephrin-receptor like / SAM domain (Sterile alpha motif) / Galactose-binding domain-like / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Jelly Rolls / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich / Mainly Beta
Similarity search - Domain/homology
6-AMINOHEXANOIC ACID / DI(HYDROXYETHYL)ETHER / Ephrin type-A receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.53 Å
AuthorsLechtenberg, B.C. / Pasquale, E.B.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)R01NS087070 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)P30CA030199 United States
CitationJournal: J.Biol.Chem. / Year: 2019
Title: Engineering nanomolar peptide ligands that differentially modulate EphA2 receptor signaling.
Authors: Gomez-Soler, M. / Petersen Gehring, M. / Lechtenberg, B.C. / Zapata-Mercado, E. / Hristova, K. / Pasquale, E.B.
History
DepositionJan 4, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 1, 2019Provider: repository / Type: Initial release
Revision 1.1May 8, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jun 12, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Apr 13, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / database_2 / entity / entity_src_gen / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_residues / pdbx_validate_rmsd_angle / struct_asym / struct_conn / struct_ref_seq / 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.group_PDB / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.pdbx_formal_charge / _atom_site.type_symbol / _atom_site_anisotrop.id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_gen.gene_src_common_name / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_site_gen.label_asym_id
Revision 2.1Oct 11, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 3.0Nov 15, 2023Group: Atomic model / Data collection / Category: atom_site / chem_comp_atom / chem_comp_bond
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_atom_id / _atom_site.label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ephrin type-A receptor 2
B: Ephrin type-A receptor 2
C: bA-WLA-Yam
D: bA-WLA-Yam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,87511
Polymers45,2374
Non-polymers6387
Water7,116395
1
A: Ephrin type-A receptor 2
C: bA-WLA-Yam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,9966
Polymers22,6192
Non-polymers3774
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2540 Å2
ΔGint-6 kcal/mol
Surface area10070 Å2
MethodPISA
2
B: Ephrin type-A receptor 2
D: bA-WLA-Yam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,8795
Polymers22,6192
Non-polymers2603
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2150 Å2
ΔGint-9 kcal/mol
Surface area10540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.798, 78.060, 58.340
Angle α, β, γ (deg.)90.000, 98.770, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain 'A' and (resid 27 through 54 or resid 56...A27 - 37
121(chain 'A' and (resid 27 through 54 or resid 56...A43 - 54
131(chain 'A' and (resid 27 through 54 or resid 56...A56 - 58
141(chain 'A' and (resid 27 through 54 or resid 56...A60
151(chain 'A' and (resid 27 through 54 or resid 56...A63 - 67
161(chain 'A' and (resid 27 through 54 or resid 56...A69 - 125
171(chain 'A' and (resid 27 through 54 or resid 56...A127 - 152
181(chain 'A' and (resid 27 through 54 or resid 56...A154 - 156
191(chain 'A' and (resid 27 through 54 or resid 56...A158 - 169
1101(chain 'A' and (resid 27 through 54 or resid 56...A171 - 188
1111(chain 'A' and (resid 27 through 54 or resid 56...A190 - 194
1121(chain 'A' and (resid 27 through 54 or resid 56...A196 - 207
1131(chain 'A' and (resid 27 through 54 or resid 56...A301
1141(chain 'A' and (resid 27 through 54 or resid 56...A601
2151(chain 'B' and (resid 27 through 39 or resid 43...B27 - 37
211(chain 'B' and (resid 27 through 39 or resid 43...B43 - 54
221(chain 'B' and (resid 27 through 39 or resid 43...B56 - 58
231(chain 'B' and (resid 27 through 39 or resid 43...B60
241(chain 'B' and (resid 27 through 39 or resid 43...B63 - 67
251(chain 'B' and (resid 27 through 39 or resid 43...B69 - 125
261(chain 'B' and (resid 27 through 39 or resid 43...B127 - 152
271(chain 'B' and (resid 27 through 39 or resid 43...B154 - 156
281(chain 'B' and (resid 27 through 39 or resid 43...B158 - 169
291(chain 'B' and (resid 27 through 39 or resid 43...B171 - 188
2101(chain 'B' and (resid 27 through 39 or resid 43...B190 - 194
2111(chain 'B' and (resid 27 through 39 or resid 43...B196 - 207
2121(chain 'B' and (resid 27 through 39 or resid 43...B301
2131(chain 'B' and (resid 27 through 39 or resid 43...B501
112chain 'C'C1 - 11
212chain 'D'D1 - 11

NCS ensembles :
ID
1
2

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Components

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Protein / Protein/peptide , 2 types, 4 molecules ABCD

#1: Protein Ephrin type-A receptor 2 / Epithelial cell kinase / Tyrosine-protein kinase receptor ECK


Mass: 21339.113 Da / Num. of mol.: 2 / Fragment: Ephrin type-A receptor 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EPHA2, ECK / Production host: Escherichia coli (E. coli)
References: UniProt: P29317, receptor protein-tyrosine kinase
#2: Protein/peptide bA-WLA-Yam


Mass: 1279.420 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 5 types, 402 molecules

#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-ACA / 6-AMINOHEXANOIC ACID / AMINOCAPROIC ACID


Type: peptide linking / Mass: 131.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO2 / Comment: inhibitor*YM
#5: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 395 / 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: 2.33 Å3/Da / Density % sol: 47.17 % / Mosaicity: 0.21 °
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 0.09M BIS-TRIS pH5.5, 22.5% w/v PEG 3,350, 3% w/v 6-aminohexanoic acid

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-E SUPERBRIGHT / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS HTC / Detector: IMAGE PLATE / Date: Aug 14, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.53→28.83 Å / Num. obs: 61846 / % possible obs: 98.2 % / Redundancy: 3.6 % / Biso Wilson estimate: 16 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.04 / Rpim(I) all: 0.024 / Rrim(I) all: 0.047 / Net I/σ(I): 17.3
Reflection shellResolution: 1.53→1.55 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.463 / Num. unique obs: 2631 / CC1/2: 0.753 / Rpim(I) all: 0.344 / Rrim(I) all: 0.581 / % possible all: 85

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Processing

Software
NameVersionClassification
PHENIX1.14rc2-3191refinement
XDSJan 26, 2018data reduction
Aimless0.7.2data scaling
PDB_EXTRACT3.24data extraction
PHASER2.8.2phasing
CrystalCleardata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3HEI

3hei


Resolution: 1.53→28.83 Å / SU ML: 0.1549 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 17.265
RfactorNum. reflection% reflection
Rfree0.1771 3088 5 %
Rwork0.1512 --
obs0.1525 61808 98.05 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 24.6 Å2
Refinement stepCycle: LAST / Resolution: 1.53→28.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3087 0 44 395 3526
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01253327
X-RAY DIFFRACTIONf_angle_d1.31864515
X-RAY DIFFRACTIONf_chiral_restr0.161460
X-RAY DIFFRACTIONf_plane_restr0.0098583
X-RAY DIFFRACTIONf_dihedral_angle_d11.70781943
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.53-1.550.25351060.2712269X-RAY DIFFRACTION83.57
1.55-1.570.20531320.21122661X-RAY DIFFRACTION96.91
1.57-1.60.21961360.18782659X-RAY DIFFRACTION98.31
1.6-1.630.21951530.19052611X-RAY DIFFRACTION97.53
1.63-1.660.23051490.18962652X-RAY DIFFRACTION98.38
1.66-1.70.19861560.17952646X-RAY DIFFRACTION98.63
1.7-1.730.20051480.16992704X-RAY DIFFRACTION98.79
1.73-1.770.20221370.16932666X-RAY DIFFRACTION98.49
1.77-1.820.2211380.16342720X-RAY DIFFRACTION99.2
1.82-1.870.21941370.16232691X-RAY DIFFRACTION99.12
1.87-1.920.20471400.1642677X-RAY DIFFRACTION99.26
1.92-1.980.19091390.15052689X-RAY DIFFRACTION99.12
1.98-2.050.14561520.14162692X-RAY DIFFRACTION99.27
2.05-2.140.1651450.13882692X-RAY DIFFRACTION99.23
2.14-2.230.15231450.13772719X-RAY DIFFRACTION99.03
2.23-2.350.16851450.14022666X-RAY DIFFRACTION99.05
2.35-2.50.181320.15092715X-RAY DIFFRACTION99.13
2.5-2.690.17611500.14872683X-RAY DIFFRACTION98.75
2.69-2.960.18391460.14762693X-RAY DIFFRACTION98.68
2.96-3.390.15811200.14052737X-RAY DIFFRACTION98.82
3.39-4.270.1461240.132735X-RAY DIFFRACTION98.82
4.27-28.830.17781580.1542743X-RAY DIFFRACTION98.94
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)
12.94483066194-1.302466915872.230241327153.63322703106-1.348088186362.56014112878-0.0210270643695-0.151267497558-0.466912211725-0.0244838211244-0.050736156477-0.1101314198360.651038165457-0.231853126211-0.03558456761490.172387487283-0.01898574739490.03217113950390.1363698369920.0294110300770.187307811595-37.0262261824.23226928948-14.4871589591
26.310844414560.7592691301690.1366548126927.358873200080.7524087197925.235036954210.02172887621440.3846964102840.379398086754-0.219451860326-0.04615758112430.579717221452-0.339052167569-0.715214093229-0.2508259484520.1176838240740.0347765805812-0.01999248364340.1793786994850.008506702200430.181224354349-41.253071048915.9244825735-30.9046746078
31.59888812936-0.1024979258720.2206615238342.551264823641.155949928061.619517706550.06722607601050.134054127249-0.0682619252705-0.0607978536222-0.1075588948410.1289625968890.0738691403577-0.05034266355310.02529133391070.1062862220670.00551938701446-0.01148266864590.0857360148517-0.003277542002040.123126856926-39.04285491066.00421915892-33.5519499408
41.33083063626-0.413848155517-0.7696843264160.9706672103520.7648240343941.809300620330.04546969619240.006281039748610.0921115137067-0.06661657143390.0467422663307-0.028683933824-0.08783004237930.0573389319714-0.116823790020.0804863722029-0.01060883604690.0005141890584010.07778599402530.01006889703160.119733877311-31.751388691313.8352221682-24.5125659754
52.491777002071.06986055148-0.4553595653732.305075423512.703353272394.855328538390.03803448315590.08938145202060.395978212821-0.1136542695660.0805804970627-0.116609347485-0.1898962540850.0534653634024-0.01615887053040.0978760735009-0.0219392219210.01030622011670.08008651356810.02488552865830.143552941487-27.684702595120.0399224253-23.9302155435
60.814016126436-0.297781159818-0.2105329728951.434370508381.897647657733.271153985450.00233490168864-0.0150626939629-0.03521881486060.07442990047810.124315060946-0.07917634296030.1896867113810.170318850844-0.1565676722350.120173057802-0.01074947416390.01227845309130.08669956314150.00164386398080.145616244899-27.67870184193.71387783119-28.3986102829
71.31214909946-0.26381202546-0.9544725811471.307703063010.2546326259063.1564420389-0.0806066714956-0.246646963528-0.03578466273230.1935793912230.06610646136050.007399220482510.1542864125960.1502960008420.03562777072720.1043373857340.008039933718570.00242656736290.1350548132960.004168856103410.141257910258-33.2124682119.81937772804-15.6736537779
82.28780523322-0.411325540431-1.702144283082.084641938330.2700563211956.196435065280.1994784028780.22957409318-0.41126821622-0.225907948886-0.0472357482952-0.0414458382310.7116218110830.230040508691-0.1823042550310.2053196067930.00862603232742-0.01956622697740.11483473437-0.03403725261320.186374546552-5.918799771936.38188031451-15.433019031
94.93784076575-2.52341391228-2.912512982173.53362341083-1.307300130985.21046703220.0524299742027-0.5152975178290.2587078446870.228514680.0259828971376-0.298015926018-0.1980992604580.315998144329-0.1652004565120.14095019656-0.0460075801076-0.02298934839550.212772520595-0.02262535091630.169309012222-1.5001737460515.98417626770.24382549919
101.659723988150.1312400995330.4177151235621.03939258255-0.8660398758132.298027942420.0506437796129-0.217910022002-0.1141367472120.04821888861050.0247238788890.01352786861040.163872401562-0.0927876248677-0.0525980607980.0969267916438-0.002254056457010.00115604645340.1105868119690.01141734885770.114419515383-7.94157181299.40402855881-1.60759719954
110.652316279885-0.115195218141.044190269354.60900824088-2.934803835183.32165083284-0.0571874323714-1.078933083520.1213634378810.7482063849760.4514089968190.359129415405-0.887438887705-0.694030911687-0.3692460088450.2887212296320.05198243047880.05895332855560.6611714581460.09637023466830.222762158769-18.33982081810.189225986714.6039808882
123.349786375381.18345779568-1.732209446251.35757270069-1.894545421642.888074956490.236507286668-0.236185610760.2729286259260.25262411338-0.01111020093950.171512070422-0.337655698878-0.0398342952838-0.1674506046930.154711083659-0.001500412833310.02054306767970.128737403306-0.01648678412730.155976684884-11.953584508521.8268068823-7.08999052499
131.025588254890.144505957420.2849359830681.3396891517-1.097306474712.308414437030.0689008008568-0.260225570812-0.1872280965760.00105923473560.1240310947050.1483387151690.252958087871-0.25487537744-0.1456530366480.118789819127-0.0140504537682-0.0025070326080.1695861939220.06345243214680.183323266487-14.03499060047.45804506797-2.1663652233
141.141490544690.1490723683871.78758784580.02232877881750.2828525813762.97310947487-0.02655766330530.349021887658-0.0143644142716-0.0596648205581-0.0325477354359-0.06522467840470.367294088776-0.0151776045436-0.01086554075710.165477269976-0.02982684223850.003313105161080.2783748383780.01591556997540.131807705993-12.58071320386.99113217124-22.5316274163
156.683922010040.3797147008842.403054144015.7886228079-1.651912009322.18011793727-0.07280083134150.0706161773105-0.09102595865940.182037655165-0.01645191489850.2438262099830.0939071253531-0.08703791878880.09217811481020.106624984591-0.00230328368913-0.008972800404440.0890637684595-0.0362946189330.110476592395-39.44615049072.35367966049-38.2589558386
164.767143125510.500009038322-2.089459786430.885099940062-0.4153027524691.541467919030.0793696441036-0.26380294366-0.0215510127978-0.104964510145-0.0215335445919-0.0706184953060.208592158970.228040128978-0.06797857787890.173834848464-0.00210984103332-0.03145481390010.2351649284380.05206561732160.167721128315-2.993122116573.047940673198.29378412504
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 27 through 36 )
2X-RAY DIFFRACTION2chain 'A' and (resid 37 through 52 )
3X-RAY DIFFRACTION3chain 'A' and (resid 53 through 82 )
4X-RAY DIFFRACTION4chain 'A' and (resid 83 through 135 )
5X-RAY DIFFRACTION5chain 'A' and (resid 136 through 146 )
6X-RAY DIFFRACTION6chain 'A' and (resid 147 through 176 )
7X-RAY DIFFRACTION7chain 'A' and (resid 177 through 207 )
8X-RAY DIFFRACTION8chain 'B' and (resid 27 through 36 )
9X-RAY DIFFRACTION9chain 'B' and (resid 37 through 52 )
10X-RAY DIFFRACTION10chain 'B' and (resid 53 through 107 )
11X-RAY DIFFRACTION11chain 'B' and (resid 108 through 117 )
12X-RAY DIFFRACTION12chain 'B' and (resid 118 through 146 )
13X-RAY DIFFRACTION13chain 'B' and (resid 147 through 188 )
14X-RAY DIFFRACTION14chain 'B' and (resid 189 through 207 )
15X-RAY DIFFRACTION15chain 'C' and (resid 2 through 11 )
16X-RAY DIFFRACTION16chain 'D' and (resid 2 through 11 )

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