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- PDB-6nk1: EphA2 LBD in complex with bA-WLA-YRPKbio peptide -

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Basic information

Entry
Database: PDB / ID: 6nk1
TitleEphA2 LBD in complex with bA-WLA-YRPKbio peptide
Components
  • Ephrin type-A receptor 2
  • bA-WLA-YRPKbio
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 / regulation of blood vessel endothelial cell migration / leading edge membrane ...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 / regulation of blood vessel endothelial cell migration / leading edge membrane / negative regulation of chemokine production / post-anal tail morphogenesis / response to growth factor / bone remodeling / positive regulation of bicellular tight junction assembly / activation of GTPase activity / regulation of lamellipodium assembly / branching involved in mammary gland duct morphogenesis / EPH-Ephrin signaling / tight junction / RND1 GTPase cycle / RND2 GTPase cycle / neural tube development / 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 / regulation of angiogenesis / regulation of ERK1 and ERK2 cascade / vasculogenesis / keratinocyte differentiation / transmembrane receptor protein tyrosine kinase activity / RAC1 GTPase cycle / osteoclast differentiation / cell surface receptor protein tyrosine kinase signaling pathway / negative regulation of angiogenesis / molecular function activator activity / protein localization to plasma membrane / skeletal system development / cell chemotaxis / positive regulation of protein localization to plasma membrane / cell motility / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / ruffle membrane / intrinsic apoptotic signaling pathway in response to DNA damage / neuron differentiation / osteoblast differentiation / cell migration / lamellipodium / virus receptor activity / angiogenesis / receptor complex / defense response to Gram-positive bacterium / cell adhesion / positive regulation of cell migration / cadherin binding / inflammatory response / focal adhesion / 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. ...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 / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / 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
ACETATE ION / Ephrin type-A receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.55 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 1.4Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.5Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)46,2187
Polymers46,0084
Non-polymers2103
Water7,404411
1
A: Ephrin type-A receptor 2
C: bA-WLA-YRPKbio


Theoretical massNumber of molelcules
Total (without water)23,0042
Polymers23,0042
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1720 Å2
ΔGint-13 kcal/mol
Surface area10640 Å2
MethodPISA
2
B: Ephrin type-A receptor 2
D: bA-WLA-YRPKbio
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,2145
Polymers23,0042
Non-polymers2103
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2500 Å2
ΔGint-14 kcal/mol
Surface area9460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)44.684, 48.137, 50.211
Angle α, β, γ (deg.)99.391, 96.791, 90.197
Int Tables number1
Space group name H-MP1
Space group name HallP1
Symmetry operation#1: x,y,z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLYGLYGLYGLY(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA277
121TRPTRPTRPTRP(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA5232
131GLNGLNGLNGLN(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA5636
141VALVALVALVAL(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA6949
151ILEILEILEILE(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA9474
161CYSCYSCYSCYS(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA11595
171LEULEULEULEU(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA138118
181VALVALVALVAL(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA170150
191ALAALAALAALA(CHAIN A AND (RESID 27 THROUGH 46 OR RESID 52...AA190170
211GLYGLYGLYGLY(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB277
221TRPTRPTRPTRP(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB5232
231GLNGLNGLNGLN(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB5636
241VALVALVALVAL(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB6949
251ILEILEILEILE(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB9474
261CYSCYSCYSCYS(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB11595
271LEULEULEULEU(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB138118
281VALVALVALVAL(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB170150
291ALAALAALAALA(CHAIN B AND (RESID 27 THROUGH 46 OR RESID 52...BB190170
112BALBALBALBAL(CHAIN C AND (RESID 1 THROUGH 8 OR RESID 10 THROUGH 14))CC11
122PROPROPROPRO(CHAIN C AND (RESID 1 THROUGH 8 OR RESID 10 THROUGH 14))CC1010
212BALBALBALBAL(CHAIN D AND (RESID 1 THROUGH 8 OR RESID 10 THROUGH 14))DD11
222PROPROPROPRO(CHAIN D AND (RESID 1 THROUGH 8 OR RESID 10 THROUGH 14))DD1010

NCS ensembles :
ID
1
2

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Components

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


Mass: 21339.113 Da / Num. of mol.: 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-YRPKbio


Mass: 1664.900 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: Biotin linked to Lys 14 side-chain / Source: (synth.) synthetic construct (others)
#3: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 411 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.28 Å3/Da / Density % sol: 45.98 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.5
Details: 0.09 M Sodium-Acetate pH 4.5, 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: Oct 1, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.55→27.6 Å / Num. obs: 52329 / % possible obs: 87.9 % / Redundancy: 2 % / Biso Wilson estimate: 15.91 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.021 / Rpim(I) all: 0.021 / Rrim(I) all: 0.03 / Net I/σ(I): 12.3 / Num. measured all: 104127
Reflection shellResolution: 1.55→1.58 Å / Redundancy: 2 % / Rmerge(I) obs: 0.108 / Mean I/σ(I) obs: 4.4 / Num. unique obs: 2440 / CC1/2: 0.976 / Rpim(I) all: 0.108 / Rrim(I) all: 0.152 / % possible all: 83.4

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation3.96 Å32.78 Å
Translation3.96 Å32.78 Å

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Processing

Software
NameVersionClassificationNB
PHENIXrefinement
XDSdata reduction
Aimless0.7.3data scaling
PHASER2.8.2phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6NJZ

6njz


Resolution: 1.55→27.6 Å / SU ML: 0.1033 / Cross valid method: FREE R-VALUE / σ(F): 2.03 / Phase error: 16.9784
RfactorNum. reflection% reflection
Rfree0.1686 2722 5.2 %
Rwork0.1457 --
obs0.1469 52324 87.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 24.67 Å2
Refinement stepCycle: LAST / Resolution: 1.55→27.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3098 0 14 411 3523
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00843376
X-RAY DIFFRACTIONf_angle_d1.03074597
X-RAY DIFFRACTIONf_chiral_restr0.0612470
X-RAY DIFFRACTIONf_plane_restr0.0078601
X-RAY DIFFRACTIONf_dihedral_angle_d10.02531988
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.55-1.580.21381230.19342496X-RAY DIFFRACTION83.83
1.58-1.610.16941390.17452559X-RAY DIFFRACTION85.65
1.61-1.640.19581150.17062578X-RAY DIFFRACTION86.76
1.64-1.680.1851380.17362597X-RAY DIFFRACTION86.94
1.68-1.720.18881290.17022615X-RAY DIFFRACTION87.11
1.72-1.760.18331470.16332584X-RAY DIFFRACTION88.15
1.76-1.810.16761440.15952649X-RAY DIFFRACTION88.08
1.81-1.860.19211250.16182647X-RAY DIFFRACTION88.2
1.86-1.920.17721320.15472620X-RAY DIFFRACTION88.55
1.92-1.990.16241300.15222596X-RAY DIFFRACTION87.65
1.99-2.070.17941530.14522576X-RAY DIFFRACTION87.27
2.07-2.160.15881560.1432606X-RAY DIFFRACTION88.24
2.16-2.280.17561660.14112604X-RAY DIFFRACTION88.19
2.28-2.420.17481700.14792562X-RAY DIFFRACTION87.06
2.42-2.60.17451600.14182587X-RAY DIFFRACTION88.36
2.6-2.870.16461250.13982634X-RAY DIFFRACTION87.78
2.87-3.280.16311760.14182615X-RAY DIFFRACTION89.25
3.28-4.130.14371650.13072679X-RAY DIFFRACTION90.92
4.13-27.610.17731290.14042798X-RAY DIFFRACTION93.34
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)
13.196678160020.0226912877679-0.6982005758154.45554162831-0.5228179239253.541479066950.00319772760567-0.00810366666442-0.215873616051-0.05395782812750.07205923210420.4107400025670.00986230933257-0.423431926788-0.09592683871380.105435823519-0.0117319261821-0.007511170970640.117292015389-0.02566332003320.152848509801-19.5745193755-43.76440225817.94419386777
21.939394776670.697713541136-1.270984715864.222871024920.3945939021554.00511654567-0.0437633754982-0.331741091652-0.3004626290730.481180867531-0.0816039057380.1647087281420.367241825326-0.143296719328-0.1229694252550.187638393764-0.01959993613730.0252910022980.1370160411880.03300233225580.137973428395-17.1933380036-46.403646952721.9779150733
31.89705736741-0.418953097996-0.5359084450542.51414733631-0.4021924081492.411003326870.00380081860048-0.1268859262680.0514037975873-0.0160774949942-0.0571962293131-0.04888602029310.0002458721451040.226326256070.1952627476910.079251488107-0.0316696388424-0.01108697022250.0711405307139-0.003644628244140.101056053486-9.00142076876-37.99632556312.3225618279
41.3623453542-0.153016327796-0.2635318905831.28592509070.366233549421.77614075515-0.0204036898083-0.308477966710.1215172646540.2510309347210.02555645725810.0480966212473-0.2335433261270.07836498056130.02403028536870.210046596613-0.002060705549030.01113667199980.136525416666-0.02064828496980.0989255014036-13.0262159658-32.038569107423.5903732225
51.41010062801-0.2833830799052.0429627690.176160243104-0.1657065944883.417938719020.3283108165540.2137311155010.0222320926568-0.216614787757-0.167827681997-0.299754485402-0.2425297678810.4166502566960.07253997849930.1777947435270.02148066229330.04672067805610.1578623621920.01780667191310.257970406408-0.576916815848-44.87677562586.39500825249
65.57237561693-1.75904920013-1.962776032683.690581910510.8342175208723.078234048950.103367867878-0.1996461802830.263676096284-0.0529302056069-0.00366785748911-0.381426013601-0.4134836705690.253148676174-0.0538048226290.197474150543-0.0627440696677-0.002717117810580.1170200046040.01060048780350.145149849661-4.9273732813-31.755720074313.0290655339
71.96059928135-0.0613950994643-1.205996399421.68898682234-0.001442804551184.76321980895-0.0597564557334-0.1255917148790.03905800747430.253548193298-0.02868489366060.222890134839-0.114077522466-0.276786987937-0.0004371010184610.1893504415660.01604720927160.02852107706140.130813226389-0.02999641463310.152805887408-20.2670345881-32.148558807618.562625083
81.95870617125-0.21262360357-0.6083914422021.427228341380.2906308202833.468612635270.0264809928237-0.2144321110660.07415963406380.08739171783320.0379174559067-0.107508477413-0.3020007095730.3280586169490.01828990593180.148599795874-0.02439772751620.0009698444644550.0995283360390.00422007426920.118772761932-8.92246372435-36.84569593615.8477525667
92.333454546720.096488940329-0.05651981784440.9998512505750.1915686073940.1357716162830.02691804244560.3237203783510.0935156254397-0.106352020260.03389611895590.324514248081-0.288855881029-0.3764705030680.1555163285230.1868080610270.0469531655401-0.008244120278870.183748673262-0.004602184810390.177308141971-25.2176659071-34.59013562194.32812260541
106.012744579780.3024341491710.8430132312443.71074916503-2.550135883667.78866905710.08585693880020.2298244649340.327923301201-0.2764673962880.0364789735174-0.308850882255-0.141109229971-0.187874987237-0.1028212328510.09443473270810.03385569456220.04207895767290.07262154379960.04649736599120.2175138800572.45200523772-52.2536184281-2.05742767999
116.614876537930.580719045071-0.1927664427112.685638953150.5427862252871.498674511280.0342489283439-0.3214192538910.2054943027750.178978359375-0.0677565864575-0.219741423655-0.1369413719110.09061135318530.002484563936780.103572877812-0.00736199044237-0.03768548557030.115100342225-0.01543499104950.1409347216328.27193963168-57.858026961810.9917543194
125.98993478618-2.989949717651.703243556654.27799160386-1.581385055962.8117698409-0.132976667955-0.52050212285-0.3075450915020.2302250327080.155925404130.01566680083450.123002779943-0.05659990576180.06730523663380.10329196296-0.00450245048432-0.008990387044450.1412307411420.0100015591550.1194830696631.92797437703-68.635990405914.1140241565
132.08922146128-0.2871378945030.2576018584442.782660292482.568662861323.89437705619-0.1399779998220.9345989100740.552168689366-0.546970474803-0.1075037013580.215281862505-0.430635856775-0.1049533388870.1006049037650.185335140248-0.0176610187492-0.04691732322660.369530850550.08934715728670.157129742781-9.71314083393-55.2245689297-6.7945339906
142.83406765584-0.6139215780080.1966140370421.12527596201-0.07882343147890.753717397418-0.04263332231330.0407372468949-0.2556272092650.018425530817-0.004244865072990.01117051125540.08689140583930.05999773776160.04138530445730.0928346396237-0.0009974372984940.00824876922830.0892309972644-0.00461377367620.1203458329724.58943561409-70.42664451794.10521841527
153.028754311680.4633762230.803532079351.672825808381.731935024064.02383232432-0.100236711803-0.265859677405-0.03244124902020.1958830789430.1301049472090.298716935909-0.131551514454-0.308040345130.076300854710.106687941014-0.00130633020306-0.01430447927190.117237667748-0.02914114929210.201031759279-13.045005054-55.10071983918.44083252037
164.43120012701-0.238838086519-0.05132105379661.865540170570.1637292292311.047360132820.00280931114420.0846799581493-0.2605572868460.0582689685115-0.09982985399690.2388444151070.00859049396346-0.1378098191880.1529475791480.0864653849831-0.02798533396870.004637780515360.0879012527842-0.001230924386770.15483217147-8.35424863531-68.30512035934.01172943621
173.799338142530.1065208613280.3368348437131.170716916620.216919565621.06484731058-0.06507534974350.1664791857950.1153146793170.01629317439310.00260057957251-0.1233123056730.07141258980390.2996905744890.00664353410280.0986949854834-0.003068176540010.01087513849990.1498891201390.004976551093560.18237841955619.4122113651-69.51772812642.81727892285
184.44392089421-0.8541523278170.2827108121611.161896478340.2222019262371.09357953343-0.2010496542450.715355456599-0.2619943173540.0139303081516-0.03601817084940.232976475364-0.0949094480252-0.237200673771-0.04244274395380.121753540093-0.00741744157547-0.02145320436720.2493710588-0.01821204749090.119005165405-5.90248455186-63.395997661-6.78041160232
193.95431699138-1.138133151850.2736720486771.1952832028-0.4926375347220.943304329973-0.0351720010055-0.0325400615802-0.0241462066506-0.06380527918850.0348173532650.007969053232420.0344659684546-0.07842561929190.05405287660940.0878221917943-0.01360824688140.0004034683674780.0887671546538-0.009119733352760.122688782547-2.07372744506-64.64329717265.37519800967
203.7013444359-1.109886631432.724737741112.29936040043-0.9259458774613.99997497415-0.1153510757670.6149956818110.299088401872-0.2646980287890.030877125169-0.115469676041-0.194375106943-0.06941658167390.117679350610.10461161763-0.005262224043650.005590756724640.2676444577620.05615934468960.1221930477831.89348984216-58.927214584-6.05038086393
211.025237120750.9956238010540.9770365502862.815916127592.752276250782.9014349028-0.0750003004087-0.177137107396-0.4003246485830.569292675015-0.02648740660080.2442605813060.6923408512770.0111275387177-0.2510419974690.398431893969-0.01574135450230.09369556500040.2218218109330.0373950601870.213624614184-19.2333699787-48.384018519226.1083876197
220.5876027113311.233310854560.1382377669317.060187274081.85369048781.338977257540.12628766047-0.3472573174020.3320436842160.297179530712-0.1301277086840.124492280859-0.3716058384570.1451127697180.02073943496660.170004515034-0.0222794985276-0.02304210866830.222897804622-0.03418383183810.24557595634913.6809589764-57.442314634712.1297727281
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 27 through 43 )
2X-RAY DIFFRACTION2chain 'A' and (resid 44 through 69 )
3X-RAY DIFFRACTION3chain 'A' and (resid 70 through 93 )
4X-RAY DIFFRACTION4chain 'A' and (resid 94 through 126 )
5X-RAY DIFFRACTION5chain 'A' and (resid 127 through 135 )
6X-RAY DIFFRACTION6chain 'A' and (resid 136 through 146 )
7X-RAY DIFFRACTION7chain 'A' and (resid 147 through 176 )
8X-RAY DIFFRACTION8chain 'A' and (resid 177 through 188 )
9X-RAY DIFFRACTION9chain 'A' and (resid 189 through 207 )
10X-RAY DIFFRACTION10chain 'B' and (resid 27 through 43 )
11X-RAY DIFFRACTION11chain 'B' and (resid 44 through 69 )
12X-RAY DIFFRACTION12chain 'B' and (resid 70 through 82 )
13X-RAY DIFFRACTION13chain 'B' and (resid 83 through 93 )
14X-RAY DIFFRACTION14chain 'B' and (resid 94 through 126 )
15X-RAY DIFFRACTION15chain 'B' and (resid 127 through 135 )
16X-RAY DIFFRACTION16chain 'B' and (resid 136 through 146 )
17X-RAY DIFFRACTION17chain 'B' and (resid 147 through 163 )
18X-RAY DIFFRACTION18chain 'B' and (resid 164 through 176 )
19X-RAY DIFFRACTION19chain 'B' and (resid 177 through 188 )
20X-RAY DIFFRACTION20chain 'B' and (resid 189 through 200 )
21X-RAY DIFFRACTION21chain 'C' and (resid 2 through 14 )
22X-RAY DIFFRACTION22chain 'D' and (resid 2 through 14 )

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