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- PDB-4xlw: Complex of Notch1 (EGF11-13) bound to Delta-like 4 (N-EGF2) -

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Basic information

Entry
Database: PDB / ID: 4xlw
TitleComplex of Notch1 (EGF11-13) bound to Delta-like 4 (N-EGF2)
Components
  • Delta-like protein
  • Neurogenic locus notch homolog protein 1
KeywordsPROTEIN BINDING / glycosylation / EGF domains / receptor-ligand complex
Function / homology
Function and homology information


ventral spinal cord interneuron fate commitment / regulation of neural retina development / Notch signaling involved in heart development / NOTCH3 Activation and Transmission of Signal to the Nucleus / regulation of cardioblast proliferation / blood vessel lumenization / regulation of inner ear auditory receptor cell differentiation / positive regulation of glial cell differentiation / venous blood vessel morphogenesis / dorsal aorta morphogenesis ...ventral spinal cord interneuron fate commitment / regulation of neural retina development / Notch signaling involved in heart development / NOTCH3 Activation and Transmission of Signal to the Nucleus / regulation of cardioblast proliferation / blood vessel lumenization / regulation of inner ear auditory receptor cell differentiation / positive regulation of glial cell differentiation / venous blood vessel morphogenesis / dorsal aorta morphogenesis / coronary sinus valve morphogenesis / cardiac right atrium morphogenesis / cardiac right ventricle formation / growth involved in heart morphogenesis / Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation / cell differentiation in spinal cord / retinal cone cell differentiation / venous endothelial cell differentiation / arterial endothelial cell differentiation / cardiac chamber formation / epithelial cell fate commitment / negative regulation of pro-B cell differentiation / negative regulation of inner ear auditory receptor cell differentiation / mitral valve formation / cell migration involved in endocardial cushion formation / glomerular mesangial cell development / negative regulation of photoreceptor cell differentiation / negative regulation of cell proliferation involved in heart valve morphogenesis / regulation of somitogenesis / inhibition of neuroepithelial cell differentiation / endocardium morphogenesis / atrioventricular node development / foregut morphogenesis / regulation of cell adhesion involved in heart morphogenesis / distal tubule development / MAML1-RBP-Jkappa- ICN1 complex / regulation of epithelial cell proliferation involved in prostate gland development / auditory receptor cell fate commitment / positive regulation of aorta morphogenesis / negative regulation of endothelial cell chemotaxis / neuroendocrine cell differentiation / collecting duct development / negative regulation of extracellular matrix constituent secretion / positive regulation of transcription of Notch receptor target / cellular response to oxygen-glucose deprivation / positive regulation of smooth muscle cell differentiation / cellular response to tumor cell / positive regulation of viral transcription / positive regulation of apoptotic process involved in morphogenesis / compartment pattern specification / vasculogenesis involved in coronary vascular morphogenesis / T-helper 17 type immune response / endocardial cushion development / epithelial to mesenchymal transition involved in endocardial cushion formation / regulation of extracellular matrix assembly / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / endocardial cell differentiation / cardiac ventricle morphogenesis / cardiac left ventricle morphogenesis / mesenchymal cell development / epidermal cell fate specification / regulation of Notch signaling pathway / negative regulation of collagen biosynthetic process / coronary vein morphogenesis / cardiac vascular smooth muscle cell development / negative regulation of myotube differentiation / somatic stem cell division / left/right axis specification / negative regulation of cell adhesion molecule production / negative regulation of cardiac muscle hypertrophy / secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development / positive regulation of endothelial cell differentiation / interleukin-17-mediated signaling pathway / apoptotic process involved in embryonic digit morphogenesis / endocardium development / glial cell differentiation / positive regulation of cardiac epithelial to mesenchymal transition / cardiac epithelial to mesenchymal transition / negative regulation of calcium ion-dependent exocytosis / neuron fate commitment / cardiac muscle cell myoblast differentiation / cellular response to follicle-stimulating hormone stimulus / pericardium morphogenesis / cardiac atrium morphogenesis / negative regulation of catalytic activity / cellular response to cholesterol / tissue regeneration / neuronal stem cell population maintenance / tube formation / positive regulation of astrocyte differentiation / negative regulation of oligodendrocyte differentiation / endoderm development / regulation of stem cell proliferation / pulmonary valve morphogenesis / calcium-ion regulated exocytosis / heart trabecula morphogenesis / negative regulation of biomineral tissue development / negative regulation of cell-cell adhesion mediated by cadherin / coronary artery morphogenesis / prostate gland epithelium morphogenesis
Similarity search - Function
Delta/Serrate/lag-2 (DSL) protein / Notch ligand, N-terminal domain / Delta serrate ligand / N terminus of Notch ligand C2-like domain / DSL domain profile. / delta serrate ligand / Neurogenic locus notch homolog protein 1 / Notch, C-terminal / Domain of unknown function / Notch ...Delta/Serrate/lag-2 (DSL) protein / Notch ligand, N-terminal domain / Delta serrate ligand / N terminus of Notch ligand C2-like domain / DSL domain profile. / delta serrate ligand / Neurogenic locus notch homolog protein 1 / Notch, C-terminal / Domain of unknown function / Notch / Notch, NOD domain / Notch, NODP domain / NOTCH protein / NOTCH protein / NOD / NODP / Notch-like domain superfamily / LNR (Lin-12/Notch) repeat profile. / LNR domain / Notch domain / Domain found in Notch and Lin-12 / EGF-like, conserved site / Human growth factor-like EGF / Calcium-binding EGF domain / Laminin / Laminin / EGF-type aspartate/asparagine hydroxylation site / EGF-like domain / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / Ankyrin repeat / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Ribbon / Mainly Beta
Similarity search - Domain/homology
beta-D-glucopyranose / alpha-L-fucopyranose / Delta-like protein 4 / Neurogenic locus notch homolog protein 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.39 Å
AuthorsLuca, V.C. / Jude, K.M. / Garcia, K.C.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)NIH-1RO1-GM097015 United States
CitationJournal: Science / Year: 2015
Title: Structural biology. Structural basis for Notch1 engagement of Delta-like 4.
Authors: Luca, V.C. / Jude, K.M. / Pierce, N.W. / Nachury, M.V. / Fischer, S. / Garcia, K.C.
History
DepositionJan 13, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 4, 2015Provider: repository / Type: Initial release
Revision 1.1Mar 11, 2015Group: Database references
Revision 1.2May 27, 2015Group: Refinement description
Revision 1.3Jun 10, 2015Group: Refinement description
Revision 1.4Sep 20, 2017Group: Author supporting evidence / Derived calculations / Source and taxonomy
Category: entity_src_gen / pdbx_audit_support / pdbx_struct_oper_list
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _pdbx_audit_support.funding_organization
Revision 1.6Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Neurogenic locus notch homolog protein 1
B: Delta-like protein
C: Neurogenic locus notch homolog protein 1
D: Delta-like protein
E: Neurogenic locus notch homolog protein 1
F: Delta-like protein
G: Neurogenic locus notch homolog protein 1
H: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)175,24640
Polymers170,7008
Non-polymers4,54732
Water0
1
A: Neurogenic locus notch homolog protein 1
B: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,72110
Polymers42,6752
Non-polymers1,0468
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3550 Å2
ΔGint5 kcal/mol
Surface area22280 Å2
MethodPISA
2
C: Neurogenic locus notch homolog protein 1
D: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,72110
Polymers42,6752
Non-polymers1,0468
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3620 Å2
ΔGint6 kcal/mol
Surface area22590 Å2
MethodPISA
3
E: Neurogenic locus notch homolog protein 1
F: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,90210
Polymers42,6752
Non-polymers1,2278
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3410 Å2
ΔGint3 kcal/mol
Surface area22360 Å2
MethodPISA
4
G: Neurogenic locus notch homolog protein 1
H: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,90210
Polymers42,6752
Non-polymers1,2278
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3490 Å2
ΔGint5 kcal/mol
Surface area22450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.560, 95.570, 122.900
Angle α, β, γ (deg.)90.00, 96.21, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A
211CHAIN C
311CHAIN E
411CHAIN G
112CHAIN B
212CHAIN D
312CHAIN F
412CHAIN H

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 8 molecules ACEGBDFH

#1: Protein
Neurogenic locus notch homolog protein 1 / Notch 1


Mass: 13524.217 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Notch1 / Plasmid: pAcGP67A / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q07008
#2: Protein
Delta-like protein


Mass: 29150.729 Da / Num. of mol.: 4 / Mutation: G28S, F107L, L206P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dll4, Dll4_predicted, rCG_26804 / Plasmid: pAcGP67A / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: D3ZHH1

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Sugars , 3 types, 22 molecules

#4: Sugar
ChemComp-BGC / beta-D-glucopyranose / Glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C6H12O6
IdentifierTypeProgram
DGlcpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-glucopyranoseCOMMON NAMEGMML 1.0
b-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Sugar
ChemComp-FUC / alpha-L-fucopyranose / Fucose


Type: L-saccharide, alpha linking / Mass: 164.156 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H12O5
IdentifierTypeProgram
LFucpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-L-fucopyranoseCOMMON NAMEGMML 1.0
a-L-FucpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
FucSNFG CARBOHYDRATE SYMBOLGMML 1.0
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


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

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Non-polymers , 1 types, 10 molecules

#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Ca

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Details

Sequence detailsDelta-like protein had C-terminal tag CDQAAAHHHHHHHH which is either disordered or cleaved after ...Delta-like protein had C-terminal tag CDQAAAHHHHHHHH which is either disordered or cleaved after treatment with carboxypeptidase prior to crystallization.

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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: 2.95 Å3/Da / Density % sol: 58.34 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.4 / Details: PEG 3350, MgSO4, Tris-HCl p, D-(+)-Galactose

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 0.999956 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 28, 2014
RadiationMonochromator: Double crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.999956 Å / Relative weight: 1
ReflectionResolution: 3.39→84.064 Å / Num. obs: 27009 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 87.04 Å2 / Rmerge(I) obs: 0.217 / Net I/σ(I): 6.12
Reflection shellResolution: 3.39→3.6 Å / Rmerge(I) obs: 1.22 / Mean I/σ(I) obs: 1.19 / % possible all: 96.6

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation3.99 Å47.83 Å
Translation3.99 Å47.83 Å

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Processing

Software
NameVersionClassification
PHENIXDEV-1839refinement
XDSdata reduction
PHASER2.5.6phasing
PDB_EXTRACT3.15data extraction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.39→84.06 Å / SU ML: 0.69 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 38.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.31 1330 4.95 %Random selection
Rwork0.257 ---
obs0.26 26865 98.8 %-
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 141.3 Å2
Refinement stepCycle: LAST / Resolution: 3.39→84.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11507 0 266 0 11773
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01212251
X-RAY DIFFRACTIONf_angle_d0.71916606
X-RAY DIFFRACTIONf_dihedral_angle_d13.2244448
X-RAY DIFFRACTIONf_chiral_restr0.0311746
X-RAY DIFFRACTIONf_plane_restr0.0032179
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDType
11A2189X-RAY DIFFRACTIONPOSITIONAL
12C2189X-RAY DIFFRACTIONPOSITIONAL
13E2189X-RAY DIFFRACTIONPOSITIONAL
14G2189X-RAY DIFFRACTIONPOSITIONAL
21B4803X-RAY DIFFRACTIONPOSITIONAL
22D4803X-RAY DIFFRACTIONPOSITIONAL
23F4803X-RAY DIFFRACTIONPOSITIONAL
24H4803X-RAY DIFFRACTIONPOSITIONAL
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3912-3.5270.4581370.39252706X-RAY DIFFRACTION95
3.527-3.68750.40031520.3552799X-RAY DIFFRACTION99
3.6875-3.88190.36041470.32782854X-RAY DIFFRACTION99
3.8819-4.12510.3111510.29582830X-RAY DIFFRACTION99
4.1251-4.44360.32521480.25612832X-RAY DIFFRACTION99
4.4436-4.89070.29381490.2132858X-RAY DIFFRACTION100
4.8907-5.59830.25971440.21482874X-RAY DIFFRACTION100
5.5983-7.05270.28441540.25082887X-RAY DIFFRACTION100
7.0527-84.08960.27741480.20962895X-RAY DIFFRACTION98
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)
18.8601-4.1919-3.22944.16953.39252.7089-0.1288-0.7765-0.59251.60570.45992.04240.66070.3016-0.32331.58510.36160.36771.09280.19141.9271-0.0596.324146.284
23.9586-5.1625-0.71056.78771.38728.4467-0.3604-0.12190.65581.56010.74612.49080.2261-0.1688-0.16161.04510.13910.23350.9191-0.20421.59345.635-0.221141.388
35.4027-1.4015-2.01078.29393.50124.1933-1.5332-0.43330.0712.86091.3051.48250.30970.40140.12672.00870.41750.01080.89590.21651.20495.2411.494146.382
46.4674-5.3389-0.93429.6537-0.54780.5798-0.4515-0.12520.28690.33160.8505-0.55110.21470.0105-0.42411.1420.2386-0.29550.95760.0111.063532.331-49.929138.165
52.01071.4061-1.53292.4839-0.22343.5998-0.322-0.22060.4895-2.15090.50790.71960.0181-0.041-0.15061.16570.1444-0.16180.85310.03460.644211.759-14.876185.281
65.1862-6.81223.28598.9693-4.40332.31621.0222-0.56180.2239-1.07780.11860.85310.75081.0762-1.16682.38120.14520.02421.05740.21812.10555.10528.735176.999
73.45730.6281-2.15952.64090.27754.9733-0.06180.56290.10120.3544-0.69761.5798-1.1424-0.3232-0.30420.1550.24550.36821.1617-0.23740.5321-6.0546.485204.815
84.4203-3.7299-1.12245.89123.51752.7381-0.0045-0.3307-0.57070.4470.4091.4050.67720.0685-0.280.66340.02330.25680.82770.08211.176-5.668-3.529205.101
97.327-2.07570.53238.8261.94463.4466-0.7784-0.55510.01450.08350.3008-1.2263-0.4998-0.02410.05060.488-0.00160.31610.8372-0.04460.3716-3.4030.391206.2
104.1481-2.8276-0.64634.94330.2469-0.0033-0.1203-0.1374-0.69670.64130.4410.75470.20850.1176-0.33021.50350.2365-0.22720.9590.03981.198824.075-51.679199.174
117.1839-0.76441.35939.0094-0.98962.34590.07690.01290.39661.49650.0712-0.5576-0.02280.6272-0.1911.40710.1975-0.431.0635-0.04181.137816.68323.645143.445
122.0359-0.87031.68262.9029-1.3993.2905-0.6103-0.38620.70931.7140.45721.4673-0.43490.27610.27311.50450.3402-0.30161.2306-0.1641.88042.90143.691145.31
135.1054-4.05140.72937.0629-4.13363.7999-0.6342-0.2074-0.17482.3101-0.1932.241-1.191-0.18590.79161.96920.4801-0.06041.2443-0.18662.5013-14.29278.526139.592
142.74040.83211.40572.9381-2.08063.11850.38851.2137-0.68350.0501-1.3036-2.06510.60390.08170.81761.54370.26680.20071.07820.08052.345-30.56598.871134.334
154.8989-3.363-0.17838.1741-4.29944.2019-0.39460.12240.09751.88350.43981.2027-0.61490.1751-0.06210.7501-0.0322-0.4560.866-0.14520.79929.56219.679209.386
168.2233-3.98891.12398.759-2.70088.25280.60110.23380.8743-0.2263-0.3039-0.2848-0.54170.1849-0.28780.69120.02050.16870.5829-0.07560.7049.64820.692204.096
176.95544.96010.86084.25612.26075.44380.7262-0.4368-0.03571.5997-0.12220.6193-0.2102-0.3283-0.71361.26280.1787-0.37380.94320.38351.36591.13530.642200.722
188.2926-3.83723.3326.4824-2.91673.2698-0.5411-0.30941.2949-0.11490.1456-0.1016-0.5167-0.33310.29961.05010.0103-0.21130.6592-0.05010.75385.12424.439206.107
191.82640.444-1.6345.5507-0.07671.39460.3854-0.0892-0.51141.22130.7330.4813-0.3473-0.1524-1.08621.61750.3984-0.11521.1023-0.15061.31-13.8462.947201.416
203.3366-1.75524.00255.2907-3.40355.3756-1.1276-0.52-0.44010.93391.13310.20820.1716-0.2982-0.01831.41170.23960.20970.87320.011.6536-31.89691.49198.024
211.9507-0.3949-0.99187.8534-1.5333.30370.53190.37080.947-2.4494-0.37020.09410.10180.2344-0.16451.40750.1639-0.26410.97790.26411.577418.692-13.084124.938
223.12062.98810.27963.08050.04810.0240.21830.56481.9312-1.1843-1.0106-0.8613-0.61970.97450.95242.49580.26390.21091.34050.46951.743713.39723.041117.053
232.17061.25040.41943.65310.66432.5760.73440.4805-0.1162-1.1133-0.94660.1498-0.350.00220.14461.47040.28-0.38291.05960.06942.8016-3.35841.661125.354
247.6003-2.4074-0.28077.24984.73773.3143-0.8954-0.44370.8662-1.72450.59821.4253-1.6943-1.08620.27621.64680.1584-0.06041.05640.15781.74932.971-1.863116.686
251.7838-2.42071.29734.38510.47074.8020.59950.38810.3116-1.5465-0.43030.5792-0.0790.1947-0.13450.87230.11920.02760.7657-0.14861.3345-10.03840.221185.614
268.0666-6.0816-1.25684.55350.94940.32430.3333-0.53070.1473-0.8721-0.0711-1.757-0.4796-1.3294-0.29421.93680.262-0.131.0696-0.13621.2744-3.037-3.079176.189
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN B AND RESID 26:95 )B26 - 95
2X-RAY DIFFRACTION2( CHAIN B AND RESID 96:123 )B96 - 123
3X-RAY DIFFRACTION3( CHAIN B AND RESID 124:185 )B124 - 185
4X-RAY DIFFRACTION4( CHAIN B AND RESID 186:284 )B186 - 284
5X-RAY DIFFRACTION5( CHAIN C AND RESID 482:482 )C482
6X-RAY DIFFRACTION6( CHAIN C AND RESID 493:530 )C493 - 530
7X-RAY DIFFRACTION7( CHAIN D AND RESID 26:76 )D26 - 76
8X-RAY DIFFRACTION8( CHAIN D AND RESID 77:117 )D77 - 117
9X-RAY DIFFRACTION9( CHAIN D AND RESID 118:185 )D118 - 185
10X-RAY DIFFRACTION10( CHAIN D AND RESID 186:283 )D186 - 283
11X-RAY DIFFRACTION11( CHAIN F AND RESID 26:148 )F26 - 148
12X-RAY DIFFRACTION12( CHAIN F AND RESID 149:213 )F149 - 213
13X-RAY DIFFRACTION13( CHAIN F AND RESID 214:255 )F214 - 255
14X-RAY DIFFRACTION14( CHAIN F AND RESID 256:283 )F256 - 283
15X-RAY DIFFRACTION15( CHAIN H AND RESID 26:48 )H26 - 48
16X-RAY DIFFRACTION16( CHAIN H AND RESID 49:95 )H49 - 95
17X-RAY DIFFRACTION17( CHAIN H AND RESID 96:117 )H96 - 117
18X-RAY DIFFRACTION18( CHAIN H AND RESID 118:185 )H118 - 185
19X-RAY DIFFRACTION19( CHAIN H AND RESID 186:234 )H186 - 234
20X-RAY DIFFRACTION20( CHAIN H AND RESID 236:283 )H236 - 283
21X-RAY DIFFRACTION21( CHAIN A AND RESID 414:492 )A414 - 492
22X-RAY DIFFRACTION22( CHAIN A AND RESID 493:526 )A493 - 526
23X-RAY DIFFRACTION23( CHAIN E AND RESID 414:492 )E414 - 492
24X-RAY DIFFRACTION24( CHAIN E AND RESID 493:530 )E493 - 530
25X-RAY DIFFRACTION25( CHAIN G AND RESID 414:492 )G414 - 492
26X-RAY DIFFRACTION26( CHAIN G AND RESID 493:530 )G493 - 530

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