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- PDB-3kka: Co-crystal structure of the sam domains of EPHA1 AND EPHA2 -

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Basic information

Entry
Database: PDB / ID: 3kka
TitleCo-crystal structure of the sam domains of EPHA1 AND EPHA2
Components
  • EPHRIN TYPE-A RECEPTOR 1
  • EPHRIN TYPE-A RECEPTOR 2
KeywordsTRANSFERASE / ATP-BINDING / KINASE / NUCLEOTIDE-BINDING / RECEPTOR / TYROSINE-PROTEIN KINASE / STERILE ALPHA MOTIF / STRUCTURAL GENOMICS CONSORTIUM / SGC / GLYCOPROTEIN / MEMBRANE / PHOSPHOPROTEIN / POLYMORPHISM / TRANSMEMBRANE / Cataract
Function / homology
Function and homology information


POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / 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 ...POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / 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 / positive regulation of cell-matrix adhesion / RHOV GTPase cycle / regulation of GTPase activity / EPHA-mediated growth cone collapse / growth factor binding / regulation of cell adhesion mediated by integrin / lamellipodium membrane / RHOU GTPase cycle / fibronectin binding / 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 / positive regulation of stress fiber assembly / RAC1 GTPase cycle / transmembrane receptor protein tyrosine kinase activity / negative regulation of angiogenesis / negative regulation of cell migration / phosphatidylinositol 3-kinase/protein kinase B signal transduction / substrate adhesion-dependent cell spreading / 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 / negative regulation of protein kinase activity / receptor protein-tyrosine kinase / ruffle membrane / osteoblast differentiation / peptidyl-tyrosine phosphorylation / positive regulation of angiogenesis / intrinsic apoptotic signaling pathway in response to DNA damage / cell migration / lamellipodium / virus receptor activity / angiogenesis / protein autophosphorylation / cell surface receptor signaling pathway / receptor complex / cell adhesion / defense response to Gram-positive bacterium / protein kinase activity / positive regulation of cell migration / cadherin binding / inflammatory response / phosphorylation / focal adhesion / dendrite / positive regulation of cell population proliferation / protein kinase binding / cell surface / ATP binding / plasma membrane
Similarity search - Function
Ephrin type-A receptor 1, ligand binding domain / Transcription Factor, Ets-1 / Ephrin type-A receptor 2, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / 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 1, ligand binding domain / Transcription Factor, Ets-1 / Ephrin type-A receptor 2, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / 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) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / 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 / DNA polymerase; domain 1 / 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 / 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Ephrin type-A receptor 1 / Ephrin type-A receptor 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsWalker, J.R. / Yermekbayeva, L. / Butler-Cole, C. / Weigelt, J. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S. / Structural Genomics Consortium (SGC)
CitationJournal: To be Published
Title: Co-Crystal Structure of the SAM Domains of Human Ephrin Type-A Receptor 1 and Human Ephrin Type-A Receptor 2
Authors: Walker, J.R. / Yermekbayeva, L. / Butler-Cole, C. / Weigelt, J. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S.
History
DepositionNov 5, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: EPHRIN TYPE-A RECEPTOR 1
B: EPHRIN TYPE-A RECEPTOR 1
C: EPHRIN TYPE-A RECEPTOR 2
D: EPHRIN TYPE-A RECEPTOR 2
E: EPHRIN TYPE-A RECEPTOR 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,3466
Polymers49,3105
Non-polymers351
Water61334
1
A: EPHRIN TYPE-A RECEPTOR 1


Theoretical massNumber of molelcules
Total (without water)9,5601
Polymers9,5601
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: EPHRIN TYPE-A RECEPTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,5952
Polymers9,5601
Non-polymers351
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: EPHRIN TYPE-A RECEPTOR 2


Theoretical massNumber of molelcules
Total (without water)10,0631
Polymers10,0631
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: EPHRIN TYPE-A RECEPTOR 2


Theoretical massNumber of molelcules
Total (without water)10,0631
Polymers10,0631
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: EPHRIN TYPE-A RECEPTOR 2


Theoretical massNumber of molelcules
Total (without water)10,0631
Polymers10,0631
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)57.554, 56.071, 107.617
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein EPHRIN TYPE-A RECEPTOR 1 / TYROSINE-PROTEIN KINASE RECEPTOR EPH


Mass: 9559.910 Da / Num. of mol.: 2 / Fragment: SAM DOMAIN, UNP RESIDUES 911-974
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Gene: EPH, EPHA1, EPHT, EPHT1, MGC163163 / Plasmid: PET28-MHL / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P21709, receptor protein-tyrosine kinase
#2: Protein EPHRIN TYPE-A RECEPTOR 2 / TYROSINE-PROTEIN KINASE RECEPTOR ECK / EPITHELIAL CELL KINASE


Mass: 10063.460 Da / Num. of mol.: 3 / Fragment: SAM DOMAIN, UNP RESIDUES 903-971
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Gene: EPHA2 / Plasmid: PET28-MHL / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P29317, receptor protein-tyrosine kinase
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 34 / 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

Crystal growTemperature: 293.1 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 2.1 M AMMONIUM SULPHATE, 2% PEG 400, 0.1 M NA HEPES PH 7.2.PRIOR TO SETTING UP CRYSTALLIZATION PLATES, CHYMOTRYPSIN WAS ADDED TO THE PROTEIN SAMPLE TO A FINAL CONCENTRATION OF 0.57 ...Details: 2.1 M AMMONIUM SULPHATE, 2% PEG 400, 0.1 M NA HEPES PH 7.2.PRIOR TO SETTING UP CRYSTALLIZATION PLATES, CHYMOTRYPSIN WAS ADDED TO THE PROTEIN SAMPLE TO A FINAL CONCENTRATION OF 0.57 MICROMOLAR., VAPOR DIFFUSION, HANGING DROP, temperature 293.1K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97932 / Wavelength: 0.97932 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 14, 2009
RadiationMonochromator: DOUBLE CRYSTAL MONOCHOMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97932 Å / Relative weight: 1
ReflectionResolution: 2.4→33 Å / Num. all: 14362 / Num. obs: 14362 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.9 % / Rsym value: 0.106 / Net I/σ(I): 20.16304
Reflection shellResolution: 2.4→2.44 Å / Redundancy: 6.4 % / Mean I/σ(I) obs: 2.2083 / Num. unique all: 704 / Rsym value: 0.891 / % possible all: 100

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Processing

Software
NameVersionClassification
HKL-3000data collection
PHASERphasing
REFMAC5.5.0102refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3HIL

3hil


Resolution: 2.4→30.44 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.941 / SU B: 19.095 / SU ML: 0.199 / Cross valid method: THROUGHOUT / ESU R: 0.435 / ESU R Free: 0.25 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
RfactorNum. reflection% reflectionSelection details
Rfree0.23463 705 5 %RANDOM
Rwork0.19961 ---
obs0.2015 13463 99.93 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 54.789 Å2
Baniso -1Baniso -2Baniso -3
1-0.55 Å20 Å20 Å2
2--2.55 Å20 Å2
3----3.1 Å2
Refinement stepCycle: LAST / Resolution: 2.4→30.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2527 0 1 34 2562
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0222577
X-RAY DIFFRACTIONr_angle_refined_deg1.3921.9553482
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.5785317
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.75923.796108
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.2515464
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.3981514
X-RAY DIFFRACTIONr_chiral_restr0.0930.2396
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0211895
X-RAY DIFFRACTIONr_mcbond_it0.5611.51589
X-RAY DIFFRACTIONr_mcangle_it1.03822562
X-RAY DIFFRACTIONr_scbond_it1.7563988
X-RAY DIFFRACTIONr_scangle_it2.8174.5920
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.322 58 -
Rwork0.247 948 -
obs--99.6 %
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)
116.4253-2.4869-5.78610.52410.00868.0853-0.0518-0.10891.21730.070.0843-0.2362-0.51920.3854-0.03250.3326-0.0606-0.01490.42630.03470.36495.80046.8826-25.1736
215.34328.28443.499322.356312.96457.6647-0.26050.02040.2535-0.1440.17820.1513-0.11230.06540.08240.42510.12240.00230.30830.04140.17510.07795.7011-19.0493
326.029-2.77318.12218.6929-6.102522.6285-0.2347-0.13081.08930.44740.3530.8999-0.5815-0.7965-0.11820.20350.00850.08190.23390.02710.1809-5.88382.3769-21.2212
48.2769-5.70824.46525.5636-6.816110.995-0.2448-0.4776-0.060.25980.46410.1328-0.3184-0.5816-0.21930.3078-0.01790.0810.31650.01760.2254-5.5468-0.1871-13.1725
518.263618.7938-10.025820.1994-6.305424.53630.9391-0.5982.10651.0149-0.75692.3332-0.8182-0.071-0.18230.72620.0053-0.18770.2453-0.02530.44421.94720.1047-8.7584
627.7124-9.64547.34767.4158-0.029112.41050.1014-0.3430.8040.36170.2353-0.3631-1.00110.8215-0.33670.3718-0.1084-0.05950.1072-0.0180.25057.84894.1986-14.9107
75.06738.2117-2.00629.8622-6.12594.9156-0.2618-0.0624-0.12190.19960.0429-0.80920.0430.52810.21890.1809-0.0072-0.07260.26240.02670.1568.5813-5.1926-17.2613
810.3594-5.7424.92987.4681-1.86452.56680.09010.0883-0.02270.3362-0.0957-0.07060.04410.17960.00560.3895-0.131-0.05260.55140.05360.17073.7047-9.4223-10.9978
94.4347-2.22722.40531.8375-0.89757.6956-0.1028-0.0164-0.25030.08830.08110.27610.3681-0.47390.02170.2075-0.04570.00970.22530.03430.1817-3.269-9.5692-17.9242
1010.25511.6152-2.66255.43740.84326.0660.08030.2782-0.3378-0.3971-0.034-0.50640.25030.0465-0.04620.17-0.0108-0.010.19420.030.18824.6168-4.111-25.9629
117.3466-6.05487.62337.1467-2.172415.7703-0.144-0.6679-0.25030.17220.18750.356-0.0592-1.3814-0.04340.1086-0.01880.06770.48060.12020.2252-12.3941-0.6498-30.3665
126.90783.38784.639312.0676-2.60945.45390.0702-0.72990.18940.7123-0.04280.2204-0.235-0.7176-0.02750.22580.07180.00110.3420.06460.2042-6.8663.192-31.6881
133.5885-1.6653-0.5096.09115.786816.7686-0.0925-0.28110.5250.16630.2606-0.2766-1.1731-0.1432-0.16810.27660.02750.02450.2197-0.00320.2609-2.40066.8667-36.3007
140.4521-0.3856-2.219910.244-1.312711.97050.13380.13360.0277-0.19480.08350.3504-0.6191-0.7956-0.21720.21510.0236-0.01330.31970.06430.2474-8.79073.8666-44.1759
157.44780.7752-7.27290.92962.997423.7294-0.569-0.01050.1264-0.2885-0.36830.2671-0.4382-1.70560.93730.2077-0.0049-0.0820.59610.13840.2708-13.2154-2.1245-40.8306
1622.23655.1975-14.86085.7622-2.528610.1381-0.29050.9342-0.1334-0.06030.15010.33470.2766-0.67940.14040.5103-0.2093-0.24590.4770.11180.2659-9.9139-8.6264-38.1843
175.23327.4137-0.980313.5607-9.089919.74980.03030.124-0.1421-0.5431-0.0337-0.16511.43180.19850.00340.36560.1421-0.06180.4658-0.09280.2334-0.1017-6.9544-44.3482
184.1054-1.15572.4174.2899-1.56999.68650.0290.2036-0.1844-0.322-0.0889-0.234-0.03760.5290.060.18840.01730.02120.23130.03180.16292.6378-0.0196-43.1756
193.74692.4035-0.28679.38381.006115.16230.10970.2555-0.23460.0141-0.0489-0.19140.68750.2628-0.06090.15120.037-0.010.21240.03440.19372.1617-2.8047-35.3454
2010.10536.96020.655113.4016-9.328611.15420.55080.103-0.6568-0.08790.22650.1930.5697-0.176-0.77740.2946-0.0381-0.0160.2741-0.01540.283-3.7165-7.0821-30.2894
2161.249419.0652-14.688529.0613-4.30853.52570.05051.09390.30011.28160.0553-0.2328-0.0024-0.2585-0.10570.09510.11870.00950.68140.10390.2959-26.63473.8444-32.4002
223.7547-4.04221.967127.043115.18614.2439-0.21050.25070.4901-0.90240.1379-0.8451-1.00280.53350.07260.2166-0.1416-0.05940.56060.25190.3456-31.7439.4383-31.5527
232.61925.79480.663414.9642-0.10742.5036-0.1705-0.12380.4833-0.22860.03410.12760.305-0.02670.13640.28380.0652-0.26890.6821-0.11350.9379-30.62314.9509-24.2436
2414.4932-9.5469.275314.2753-1.469118.84250.37680.51990.8013-0.0431-0.5612-0.42130.25581.11260.18440.340.15270.00270.51760.08210.3622-27.9667-2.8743-24.4981
2521.3689-3.78674.701926.426520.223918.36260.1237-0.1821-2.013-1.03541.3686-1.0195-0.70191.4423-1.49230.38110.2590.09271.21540.26640.5663-24.5815-4.6186-32.8304
2638.2577-2.16-7.67611.08754.967422.8885-1.42332.9577-0.48010.15280.07780.28670.77740.38981.34550.59810.08750.05520.43850.07070.5703-33.0857-7.3672-34.3166
2717.084916.886313.521649.8507-2.389918.20270.85880.5999-0.8519-0.2342-0.383-1.23611.29110.988-0.47590.54160.22090.04440.39330.06870.3125-36.5533-6.2932-26.3446
289.6274.0399-6.40291.8486-3.54039.04070.1334-0.5357-0.273-0.0777-0.1621-0.09490.6504-0.1930.02870.22190.0138-0.05760.32320.08630.282-41.63342.0607-26.8834
2912.49098.12366.44216.71379.051619.8947-0.1507-0.92140.3084-0.0078-0.51210.35590.2666-0.00330.66270.20680.1276-0.01290.39480.05880.2639-39.75922.9693-35.2507
303.1898-1.4235-0.43430.6976-0.844419.83350.31190.3623-0.791-0.1205-0.10680.36710.03711.2396-0.20510.48640.21350.02420.8650.01730.6706-33.4098-1.1984-40.4952
313.95783.2779-2.00172.722-1.64921.0289-0.34790.3868-0.0401-0.34230.30860.0060.0887-0.22670.03930.52740.0842-0.12770.389-0.0470.3584-20.9399-13.8351-12.4298
329.82684.96-0.56310.2634-0.191322.8998-0.15560.46020.2638-0.2347-0.15411.0413-0.054-0.96060.30970.17680.025-0.0120.2344-0.00270.3106-24.1477-18.2357-5.699
336.06570.6610.825511.6032-0.38215.8659-0.08740.05570.16990.14650.00110.8063-0.3135-0.21450.08630.15150.01190.06090.1939-0.02250.2415-21.7541-12.98941.4693
343.5721.3836-0.375310.29553.25097.63950.12130.00810.3496-0.56470.0599-0.0652-0.37490.7024-0.18110.29480.00950.01250.24430.04020.2426-14.933-7.4572-2.4329
3532.9117-7.9337-5.67766.4522-5.71912.04810.01520.7032-0.63330.0433-0.30940.0373-0.10740.12640.29410.4906-0.13450.07930.2362-0.02530.1116-12.5733-11.3467-9.4797
369.9866-5.9242-8.47389.15057.885121.04610.0501-0.02190.11540.36040.0994-0.77870.24341.2323-0.14950.12560.0597-0.03050.4761-0.03170.4032-7.8894-17.3168-1.8824
376.52773.142-4.01799.69622.29914.6653-0.1488-0.864-0.22590.5397-0.0346-0.03980.38530.7450.18340.29680.0373-0.02820.42480.01750.2229-13.2071-16.78945.3836
384.38758.1957-3.853515.6099-5.579616.2218-0.0392-0.1673-0.38240.1466-0.1652-0.56010.50020.06870.20440.52190.22920.34370.31750.20960.3994-18.1114-24.80894.8144
397.4286-0.9578-5.96894.3797-1.069630.9709-0.03510.197-0.491-0.07-0.15550.23190.64520.20890.19070.19490.01370.03660.1599-0.01280.2311-15.8068-23.6161-6.0872
408.9379-11.9667-1.048317.5678-3.011920.54660.5980.35350.6957-1.007-0.5096-1.0762-0.22010.262-0.08840.2543-0.0928-0.01230.32240.02260.2522-10.1713-20.3657-14.728
412.9005-3.5743-1.07924.85790.277316.66320.6110.5005-0.2218-0.7931-0.15580.47250.7225-0.2301-0.45520.3186-0.00440.0190.67840.01480.3151-25.937-1.783-15.837
4210.7875-3.5295-0.43342.2089-4.106417.19250.46070.1591-0.5509-0.16430.06760.29470.0118-0.4604-0.52830.24720.0512-0.00770.2336-0.0120.1938-24.5052-1.9989-7.8664
435.04071.83411.360511.4874-4.77555.49410.44210.4101-0.04-0.125-0.04170.6223-0.2994-0.6552-0.40040.32320.13110.11580.3952-0.02960.2401-28.05533.7534-2.9534
4413.79933.305-7.21187.9784-0.12054.12830.18540.19311.1233-0.63560.21541.1656-0.2526-0.0595-0.40080.6130.2180.09850.32220.11220.4118-27.864711.061-7.6236
4523.540710.89714.415125.67210.926916.5742-0.31251.44210.6408-1.76950.57940.3537-2.365-0.0866-0.26690.47120.01280.16790.34220.03220.1602-22.95658.7792-15.2272
465.9909-6.43-3.39215.01260.928413.216-0.05480.3890.1840.0856-0.4338-0.1755-0.060.61770.48860.408-0.15160.18410.21650.12110.4949-16.060812.1138-7.363
4718.2983-8.67914.091916.243-16.960519.54010.4774-0.14740.09351.5047-0.14680.2565-2.14290.2084-0.33060.89620.05780.1510.114-0.09670.3667-21.390112.637-0.4761
481.27953.274-3.55829.1329-6.50420.71310.0261-0.15470.02380.109-0.0322-0.1074-0.31931.34070.00620.2872-0.05720.03010.4527-0.19590.414-17.11134.78242.5351
490.5709-0.4246-1.608810.6793-7.764112.32790.062-0.29280.270.49180.2044-0.8032-0.48260.8542-0.26650.3081-0.028-0.02380.3697-0.06960.3061-15.30081.2524-4.597
507.9132-6.45870.30766.182-4.658621.3691-0.33710.33720.62820.1694-0.2487-0.63190.4143-0.27440.58580.2685-0.00820.11240.43270.0160.2281-14.04591.6658-14.9247
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A911 - 916
2X-RAY DIFFRACTION2A917 - 921
3X-RAY DIFFRACTION3A922 - 926
4X-RAY DIFFRACTION4A927 - 932
5X-RAY DIFFRACTION5A933 - 938
6X-RAY DIFFRACTION6A939 - 943
7X-RAY DIFFRACTION7A944 - 951
8X-RAY DIFFRACTION8A952 - 956
9X-RAY DIFFRACTION9A957 - 967
10X-RAY DIFFRACTION10A968 - 974
11X-RAY DIFFRACTION11B912 - 919
12X-RAY DIFFRACTION12B920 - 925
13X-RAY DIFFRACTION13B926 - 930
14X-RAY DIFFRACTION14B931 - 936
15X-RAY DIFFRACTION15B937 - 942
16X-RAY DIFFRACTION16B943 - 948
17X-RAY DIFFRACTION17B949 - 954
18X-RAY DIFFRACTION18B955 - 963
19X-RAY DIFFRACTION19B964 - 968
20X-RAY DIFFRACTION20B969 - 974
21X-RAY DIFFRACTION21C907 - 912
22X-RAY DIFFRACTION22C913 - 917
23X-RAY DIFFRACTION23C918 - 922
24X-RAY DIFFRACTION24C923 - 928
25X-RAY DIFFRACTION25C929 - 933
26X-RAY DIFFRACTION26C934 - 941
27X-RAY DIFFRACTION27C942 - 947
28X-RAY DIFFRACTION28C948 - 954
29X-RAY DIFFRACTION29C955 - 959
30X-RAY DIFFRACTION30C960 - 965
31X-RAY DIFFRACTION31D903 - 910
32X-RAY DIFFRACTION32D911 - 918
33X-RAY DIFFRACTION33D919 - 925
34X-RAY DIFFRACTION34D926 - 932
35X-RAY DIFFRACTION35D933 - 937
36X-RAY DIFFRACTION36D938 - 942
37X-RAY DIFFRACTION37D943 - 950
38X-RAY DIFFRACTION38D951 - 956
39X-RAY DIFFRACTION39D957 - 965
40X-RAY DIFFRACTION40D966 - 970
41X-RAY DIFFRACTION41E903 - 910
42X-RAY DIFFRACTION42E911 - 917
43X-RAY DIFFRACTION43E918 - 923
44X-RAY DIFFRACTION44E924 - 929
45X-RAY DIFFRACTION45E930 - 937
46X-RAY DIFFRACTION46E938 - 945
47X-RAY DIFFRACTION47E946 - 950
48X-RAY DIFFRACTION48E951 - 956
49X-RAY DIFFRACTION49E957 - 961
50X-RAY DIFFRACTION50E962 - 968

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