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- PDB-3hei: Ligand Recognition by A-Class Eph Receptors: Crystal Structures o... -

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Basic information

Entry
Database: PDB / ID: 3hei
TitleLigand Recognition by A-Class Eph Receptors: Crystal Structures of the EphA2 Ligand-Binding Domain and the EphA2/ephrin-A1 Complex
Components
  • Ephrin type-A receptor 2
  • Ephrin-A1Ephrin A1
KeywordsTRANSFERASE/SIGNALING PROTEIN / Eph receptor tyrosine kinase / ephrin / Cell membrane / Disulfide bond / Glycoprotein / GPI-anchor / Lipoprotein / Membrane / ATP-binding / Kinase / Nucleotide-binding / Phosphoprotein / Receptor / Transferase / Transmembrane / Tyrosine-protein kinase / TRANSFERASE-SIGNALING PROTEIN COMPLEX
Function / homology
Function and homology information


endocardial cushion to mesenchymal transition involved in heart valve formation / negative regulation of proteolysis involved in protein catabolic process / negative regulation of dendritic spine morphogenesis / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / notochord cell development / mitral valve morphogenesis / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis ...endocardial cushion to mesenchymal transition involved in heart valve formation / negative regulation of proteolysis involved in protein catabolic process / negative regulation of dendritic spine morphogenesis / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / notochord cell development / mitral valve morphogenesis / 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 / negative regulation of epithelial to mesenchymal transition / negative regulation of chemokine production / ephrin receptor activity / leading edge membrane / bone remodeling / post-anal tail morphogenesis / response to growth factor / activation of GTPase activity / aortic valve morphogenesis / regulation of lamellipodium assembly / negative regulation of thymocyte apoptotic process / tight junction / 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 / regulation of axonogenesis / positive regulation of amyloid-beta formation / EPHA-mediated growth cone collapse / negative regulation of MAPK cascade / growth factor binding / regulation of cell adhesion mediated by integrin / lamellipodium membrane / RHOU GTPase cycle / RHOG GTPase cycle / EPH-ephrin mediated repulsion of cells / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / RAC3 GTPase cycle / RAC2 GTPase cycle / ephrin receptor signaling pathway / positive regulation of protein tyrosine kinase activity / vasculogenesis / regulation of angiogenesis / side of membrane / regulation of peptidyl-tyrosine phosphorylation / keratinocyte differentiation / RAC1 GTPase cycle / transmembrane receptor protein tyrosine kinase activity / ephrin receptor binding / cell chemotaxis / negative regulation of angiogenesis / substrate adhesion-dependent cell spreading / osteoclast differentiation / regulation of ERK1 and ERK2 cascade / phosphatidylinositol 3-kinase/protein kinase B signal transduction / skeletal system development / molecular function activator activity / cell motility / axon guidance / protein localization to plasma membrane / positive regulation of protein localization to plasma membrane / receptor protein-tyrosine kinase / neuron differentiation / ruffle membrane / osteoblast differentiation / cell surface receptor protein tyrosine kinase signaling pathway / intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of peptidyl-tyrosine phosphorylation / cell migration / virus receptor activity / cell-cell signaling / lamellipodium / angiogenesis / positive regulation of MAPK cascade / protein stabilization / receptor complex / cell adhesion / positive regulation of cell migration / defense response to Gram-positive bacterium / cadherin binding / inflammatory response / positive regulation of protein phosphorylation / phosphorylation / signaling receptor binding / focal adhesion / negative regulation of transcription by RNA polymerase II / cell surface / extracellular region / ATP binding / plasma membrane
Similarity search - Function
Ephrin-A ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) domain profile. / Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain ...Ephrin-A ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) 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 / Cupredoxins - blue copper proteins / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Cupredoxin / 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 / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Ephrin-A1 / Ephrin type-A receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsHimanen, J.P. / Goldgur, Y. / Miao, H. / Myshkin, E. / Guo, H. / Buck, M. / Nguyen, M. / Rajashankar, K.R. / Wang, B. / Nikolov, D.B.
CitationJournal: Embo Rep. / Year: 2009
Title: Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex.
Authors: Himanen, J.P. / Goldgur, Y. / Miao, H. / Myshkin, E. / Guo, H. / Buck, M. / Nguyen, M. / Rajashankar, K.R. / Wang, B. / Nikolov, D.B.
History
DepositionMay 8, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 30, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Revision 1.3Mar 31, 2021Group: Database references / Source and taxonomy / Category: entity_src_gen / struct_ref_seq_dif
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain / _struct_ref_seq_dif.details

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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-A1
C: Ephrin type-A receptor 2
D: Ephrin-A1
E: Ephrin type-A receptor 2
F: Ephrin-A1
G: Ephrin type-A receptor 2
H: Ephrin-A1
I: Ephrin type-A receptor 2
J: Ephrin-A1
K: Ephrin type-A receptor 2
L: Ephrin-A1
M: Ephrin type-A receptor 2
N: Ephrin-A1
O: Ephrin type-A receptor 2
P: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)286,38716
Polymers286,38716
Non-polymers00
Water49,6492756
1
A: Ephrin type-A receptor 2
B: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2150 Å2
ΔGint-11 kcal/mol
Surface area15360 Å2
MethodPISA
2
C: Ephrin type-A receptor 2
D: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2090 Å2
ΔGint-11 kcal/mol
Surface area15360 Å2
MethodPISA
3
E: Ephrin type-A receptor 2
F: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2170 Å2
ΔGint-11 kcal/mol
Surface area15350 Å2
MethodPISA
4
G: Ephrin type-A receptor 2
H: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2120 Å2
ΔGint-10 kcal/mol
Surface area15380 Å2
MethodPISA
5
I: Ephrin type-A receptor 2
J: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2150 Å2
ΔGint-12 kcal/mol
Surface area15370 Å2
MethodPISA
6
K: Ephrin type-A receptor 2
L: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2180 Å2
ΔGint-10 kcal/mol
Surface area15270 Å2
MethodPISA
7
M: Ephrin type-A receptor 2
N: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2090 Å2
ΔGint-12 kcal/mol
Surface area15400 Å2
MethodPISA
8
O: Ephrin type-A receptor 2
P: Ephrin-A1


Theoretical massNumber of molelcules
Total (without water)35,7982
Polymers35,7982
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2170 Å2
ΔGint-11 kcal/mol
Surface area15320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.483, 102.108, 135.255
Angle α, β, γ (deg.)84.25, 79.77, 73.94
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
51I
61K
71M
81O
12B
22D
32F
42H
52J
62L
72N
82P

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 174
2114C1 - 174
3114E1 - 174
4114G1 - 174
5114I1 - 174
6114K1 - 174
7114M1 - 174
8114O1 - 174
1122B18 - 149
2122D18 - 149
3122F18 - 149
4122H18 - 149
5122J18 - 149
6122L18 - 149
7122N18 - 149
8122P18 - 149

NCS ensembles :
ID
1
2

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Components

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


Mass: 19913.592 Da / Num. of mol.: 8 / Fragment: UNP residues 28-201
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EPHA2, ECK / Plasmid: pBabe / Cell (production host): human embryonic kidney (HEK) cells / Cell line (production host): HEK293 / Organ (production host): kidney / Production host: HOMO SAPIENS (human)
References: UniProt: P29317, receptor protein-tyrosine kinase
#2: Protein
Ephrin-A1 / Ephrin A1 / EPH-related receptor tyrosine kinase ligand 1 / LERK-1 / Immediate early response protein B61 / ...EPH-related receptor tyrosine kinase ligand 1 / LERK-1 / Immediate early response protein B61 / Tumor necrosis factor / alpha-induced protein 4


Mass: 15884.819 Da / Num. of mol.: 8 / Fragment: UNP residues 18-147
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EFNA1, EPLG1, LERK1, TNFAIP4 / Plasmid: pBabe / Cell (production host): human embryonic kidney (HEK) cells / Cell line (production host): HEK293 / Organ (production host): kidney / Production host: HOMO SAPIENS (human) / References: UniProt: P20827
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2756 / 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: 2.67 Å3/Da / Density % sol: 53.89 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 20% PEG 8,000, 100 mM Tris, pH 8.5, vapor diffusion, hanging drop, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 2, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 192014 / % possible obs: 96.1 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 18.214
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2-2.072.20.273191.2
2.07-2.152.20.227193.2
2.15-2.252.20.184194.4
2.25-2.372.20.153195
2.37-2.522.20.124195.8
2.52-2.712.30.103196.7
2.71-2.992.30.078197.6
2.99-3.422.30.061198.5
3.42-4.312.30.046198.9
4.31-502.30.045199.2

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Phasing

PhasingMethod: molecular replacement
Phasing MRR rigid body: 0.391 / Cor.coef. Fo:Fc: 0.609 / Cor.coef. Io to Ic: 0.607

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMAC5.2.0019refinement
PDB_EXTRACT3.005data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→50 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.92 / Occupancy max: 1 / Occupancy min: 1 / SU B: 8.925 / SU ML: 0.114 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.178 / ESU R Free: 0.17 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23299 9696 5 %RANDOM
Rwork0.1718 ---
obs0.1749 182318 96.02 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 10.358 Å2
Baniso -1Baniso -2Baniso -3
1--1.88 Å20.01 Å2-0.84 Å2
2--0.68 Å20.04 Å2
3---1.48 Å2
Refinement stepCycle: LAST / Resolution: 2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20152 0 0 2756 22908
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0260.02220728
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.0491.93428080
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.5752432
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.18723.8691096
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.129153488
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.5415128
X-RAY DIFFRACTIONr_chiral_restr0.1820.22904
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.02116080
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2630.29798
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3140.213685
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2360.22997
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.3560.2222
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2540.2136
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.2761.512192
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.225219712
X-RAY DIFFRACTIONr_scbond_it3.36338536
X-RAY DIFFRACTIONr_scangle_it5.1444.58368
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1395MEDIUM POSITIONAL0.340.5
1C1395MEDIUM POSITIONAL0.360.5
1E1395MEDIUM POSITIONAL0.360.5
1G1395MEDIUM POSITIONAL0.360.5
1I1395MEDIUM POSITIONAL0.370.5
1K1395MEDIUM POSITIONAL0.40.5
1M1395MEDIUM POSITIONAL0.310.5
1O1395MEDIUM POSITIONAL0.320.5
1A1395MEDIUM THERMAL2.652
1C1395MEDIUM THERMAL2.832
1E1395MEDIUM THERMAL1.152
1G1395MEDIUM THERMAL1.532
1I1395MEDIUM THERMAL1.952
1K1395MEDIUM THERMAL1.272
1M1395MEDIUM THERMAL1.862
1O1395MEDIUM THERMAL2.262
2B528TIGHT POSITIONAL0.090.05
2D528TIGHT POSITIONAL0.080.05
2F528TIGHT POSITIONAL0.10.05
2H528TIGHT POSITIONAL0.110.05
2J528TIGHT POSITIONAL0.070.05
2L528TIGHT POSITIONAL0.070.05
2N528TIGHT POSITIONAL0.080.05
2P528TIGHT POSITIONAL0.070.05
2B591MEDIUM POSITIONAL0.390.5
2D591MEDIUM POSITIONAL0.380.5
2F591MEDIUM POSITIONAL0.430.5
2H591MEDIUM POSITIONAL0.40.5
2J591MEDIUM POSITIONAL0.340.5
2L591MEDIUM POSITIONAL0.420.5
2N591MEDIUM POSITIONAL0.420.5
2P591MEDIUM POSITIONAL0.380.5
2B528TIGHT THERMAL0.340.5
2D528TIGHT THERMAL0.230.5
2F528TIGHT THERMAL0.30.5
2H528TIGHT THERMAL0.370.5
2J528TIGHT THERMAL0.260.5
2L528TIGHT THERMAL0.250.5
2N528TIGHT THERMAL0.260.5
2P528TIGHT THERMAL0.280.5
2B591MEDIUM THERMAL1.552
2D591MEDIUM THERMAL1.272
2F591MEDIUM THERMAL1.542
2H591MEDIUM THERMAL1.682
2J591MEDIUM THERMAL1.252
2L591MEDIUM THERMAL1.192
2N591MEDIUM THERMAL1.382
2P591MEDIUM THERMAL1.242
LS refinement shellResolution: 2→2.051 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.251 699 -
Rwork0.181 12598 -
obs--90.4 %
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)
11.46930.1397-0.12161.1651-0.40981.2472-0.00890.04910.12170.05280.02040.0039-0.0273-0.0374-0.01150.2097-0.00230.0330.0469-0.0150.02354.9648.994-7.161
21.2391-0.2858-0.23541.64340.23361.2982-0.0341-0.0446-0.05790.1194-0.00390.0920.0782-0.14090.03810.2557-0.01450.04440.0407-0.00780.014-6.412-11.1349.132
31.0452-0.0072-0.10640.9426-0.04111.2891-0.0374-0.02620.0011-0.0822-0.0282-0.04660.01370.03860.06560.21190.00630.04140.0386-0.00640.03256.28818.091118.739
41.059-0.0894-0.68861.4742-0.13182.1425-0.05040.0455-0.0376-0.106-0.0749-0.00560.03720.08790.12530.30620.02820.04330.0691-0.00330.015868.0678.83994.747
51.843-0.6236-0.62191.69090.73861.7788-0.022-0.0789-0.01550.050.06470.09040.0822-0.0604-0.04270.25240.00090.0370.06660.00480.015535.44554.32432.866
60.7792-0.0858-0.13892.0333-0.69971.72660.013-0.0028-0.03740.0533-0.0182-0.16410.12060.13990.00520.25850.03230.01330.0647-0.03380.040855.35443.14116.216
70.9319-0.0248-0.19242.0430.58491.8140.00140.0769-0.0459-0.1537-0.07420.086-0.0054-0.07540.07280.25630.02730.01910.0571-0.03370.026944.97450.215112.309
81.98380.02320.23541.05350.4471.04440.01620.00130.0507-0.0152-0.04210.02430.02820.02750.02580.24150.01320.04270.0309-0.00480.010956.31166.783132.204
93.9058-2.50581.48753.2444-1.32532.8793-0.0910.21120.37230.0479-0.1051-0.4613-0.08520.34570.19610.29240.01410.03820.1331-0.01440.087266.36268.14495.191
101.33090.11620.0443.17080.68491.95990.04070.01160.0043-0.014-0.06860.1143-0.0363-0.21630.0280.33780.07820.05580.1247-0.01070.018441.3877.6786.023
111.2224-0.304-0.02211.9696-0.14262.6039-0.0544-0.02010.0983-0.0520.0582-0.0537-0.05920.105-0.00370.26790.02420.04420.0556-0.01860.026661.00173.30839.737
121.2364-0.3627-0.76181.2806-0.28032.6755-0.0783-0.035-0.03720.0286-0.0187-0.03180.1570.04240.0970.370.07520.0420.1071-0.01910.017256.90959.08763.824
131.961-1.50241.28563.4167-1.33943.6674-0.3743-0.11110.35250.3840.0775-0.5609-0.3182-0.00380.29680.38670.0523-0.09510.0359-0.05830.161423.5498.04945.253
141.99920.23380.7662.274-0.08251.3413-0.05760.01140.08280.0759-0.0174-0.1096-0.0547-0.00920.0750.34360.02580.01160.0305-0.01980.02973.90414.98926.142
151.5571.12070.36744.43261.58883.35610.0324-0.1013-0.0211-0.0448-0.0690.38930.3187-0.32040.03660.4268-0.0078-0.00820.1302-0.00250.05354.96211.03263.17
162.2741-0.75690.46582.8456-0.69552.27420.01970.02120.0620.0042-0.0881-0.1162-0.23160.14070.06840.42780.01430.04730.07720.00080.013470.52232.81472.255
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 174
2X-RAY DIFFRACTION2B18 - 149
3X-RAY DIFFRACTION3C1 - 174
4X-RAY DIFFRACTION4D18 - 149
5X-RAY DIFFRACTION5E1 - 174
6X-RAY DIFFRACTION6F18 - 149
7X-RAY DIFFRACTION7G1 - 174
8X-RAY DIFFRACTION8H18 - 149
9X-RAY DIFFRACTION9I1 - 174
10X-RAY DIFFRACTION10J18 - 149
11X-RAY DIFFRACTION11K1 - 174
12X-RAY DIFFRACTION12L18 - 149
13X-RAY DIFFRACTION13M1 - 174
14X-RAY DIFFRACTION14N18 - 149
15X-RAY DIFFRACTION15O1 - 174
16X-RAY DIFFRACTION16P18 - 149

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