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- PDB-4xl1: Complex of Notch1 (EGF11-13) bound to Delta-like 4 (N-EGF1) -

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Basic information

Entry
Database: PDB / ID: 4xl1
TitleComplex of Notch1 (EGF11-13) bound to Delta-like 4 (N-EGF1)
Components
  • Delta-like protein
  • Neurogenic locus notch homolog protein 1
KeywordsPROTEIN BINDING / glycosylation / EGF domains / receptor-ligand complex
Function / homology
Function and homology information


Notch signaling involved in heart development / cardiac right ventricle formation / regulation of inner ear auditory receptor cell differentiation / negative regulation of inner ear auditory receptor cell differentiation / positive regulation of aorta morphogenesis / negative regulation of photoreceptor cell differentiation / apoptotic process involved in embryonic digit morphogenesis / venous blood vessel morphogenesis / regulation of somitogenesis / foregut morphogenesis ...Notch signaling involved in heart development / cardiac right ventricle formation / regulation of inner ear auditory receptor cell differentiation / negative regulation of inner ear auditory receptor cell differentiation / positive regulation of aorta morphogenesis / negative regulation of photoreceptor cell differentiation / apoptotic process involved in embryonic digit morphogenesis / venous blood vessel morphogenesis / regulation of somitogenesis / foregut morphogenesis / regulation of epithelial cell proliferation involved in prostate gland development / positive regulation of glial cell differentiation / auditory receptor cell fate commitment / secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development / CSL-Notch-Mastermind transcription factor complex / compartment pattern specification / endocardial cushion development / somatic stem cell division / coronary sinus valve morphogenesis / cardiac right atrium morphogenesis / growth involved in heart morphogenesis / regulation of cardioblast proliferation / mesenchymal cell development / cell differentiation in spinal cord / venous endothelial cell differentiation / arterial endothelial cell differentiation / collecting duct development / cell migration involved in endocardial cushion formation / negative regulation of pro-B cell differentiation / prostate gland epithelium morphogenesis / mitral valve formation / : / endocardium morphogenesis / distal tubule development / MAML1-RBP-Jkappa- ICN1 complex / cardiac chamber formation / cardiac atrium morphogenesis / endoderm development / pericardium morphogenesis / atrioventricular node development / cardiac ventricle morphogenesis / positive regulation of transcription of Notch receptor target / negative regulation of endothelial cell chemotaxis / cardiac septum morphogenesis / glomerular mesangial cell development / cellular response to tumor cell / positive regulation of smooth muscle cell differentiation / vasculogenesis involved in coronary vascular morphogenesis / negative regulation of extracellular matrix constituent secretion / regulation of extracellular matrix assembly / chemical synaptic transmission, postsynaptic / positive regulation of apoptotic process involved in morphogenesis / endocardial cell differentiation / left/right axis specification / epithelial to mesenchymal transition involved in endocardial cushion formation / positive regulation of endothelial cell differentiation / cardiac left ventricle morphogenesis / embryonic hindlimb morphogenesis / negative regulation of myotube differentiation / coronary vein morphogenesis / negative regulation of glial cell proliferation / cardiac vascular smooth muscle cell development / neuronal stem cell population maintenance / endocardium development / positive regulation of astrocyte differentiation / cardiac muscle cell myoblast differentiation / negative regulation of cell adhesion molecule production / negative regulation of stem cell differentiation / glial cell differentiation / tissue regeneration / T-helper 17 type immune response / skeletal muscle cell differentiation / negative regulation of calcium ion-dependent exocytosis / positive regulation of cardiac epithelial to mesenchymal transition / regulation of Notch signaling pathway / cardiac epithelial to mesenchymal transition / heart trabecula morphogenesis / embryonic limb morphogenesis / neuron fate commitment / negative regulation of oligodendrocyte differentiation / regulation of cell adhesion involved in heart morphogenesis / interleukin-17-mediated signaling pathway / negative regulation of catalytic activity / negative regulation of myoblast differentiation / cellular response to follicle-stimulating hormone stimulus / neural tube development / negative regulation of collagen biosynthetic process / negative regulation of cardiac muscle hypertrophy / luteolysis / determination of left/right symmetry / pulmonary valve morphogenesis / tube formation / cardiac muscle tissue morphogenesis / oligodendrocyte differentiation / atrioventricular valve morphogenesis / regulation of epithelial cell proliferation / cell fate specification / positive regulation of keratinocyte differentiation / inflammatory response to antigenic stimulus / ventricular trabecula myocardium morphogenesis
Similarity search - Function
Immunoglobulin-like - #3510 / : / Delta serrate ligand / N terminus of Notch ligand C2-like domain / Neurogenic locus notch homolog protein 1 / Notch, C-terminal / Domain of unknown function / Notch / Notch, NOD domain / Notch, NODP domain ...Immunoglobulin-like - #3510 / : / Delta serrate ligand / N terminus of Notch ligand C2-like domain / 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 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site / 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 1. / EGF-like domain signature 2. / EGF-like domain / Ankyrin repeat profile. / Ankyrin repeats (3 copies) / Ankyrin repeat region circular profile. / Ribbon / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
beta-D-glucopyranose / alpha-L-fucopyranose / NADH:ubiquinone oxidoreductase 17.2 kD subunit / Neurogenic locus notch homolog protein 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsLuca, V.C. / Jude, K.M. / Garcia, K.C.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM097015 United States
Howard Hughes Medical Institute (HHMI) United States
Ludwig Cancer Foundation 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 1.2Jul 15, 2015Group: Derived calculations
Revision 1.3Sep 20, 2017Group: Advisory / Author supporting evidence ...Advisory / Author supporting evidence / Derived calculations / Source and taxonomy
Category: entity_src_gen / pdbx_audit_support ...entity_src_gen / pdbx_audit_support / pdbx_struct_oper_list / pdbx_validate_close_contact
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Nov 20, 2019Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.value / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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
Revision 2.1Apr 2, 2025Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification

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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
D: Neurogenic locus notch homolog protein 1
E: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,36224
Polymers76,9784
Non-polymers3,38320
Water5,855325
1
A: Neurogenic locus notch homolog protein 1
B: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,18112
Polymers38,4892
Non-polymers1,69210
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4090 Å2
ΔGint1 kcal/mol
Surface area20430 Å2
MethodPISA
2
D: Neurogenic locus notch homolog protein 1
E: Delta-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,18112
Polymers38,4892
Non-polymers1,69210
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3970 Å2
ΔGint10 kcal/mol
Surface area20300 Å2
MethodPISA
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11580 Å2
ΔGint9 kcal/mol
Surface area37220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)77.809, 93.700, 99.126
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 2 types, 4 molecules ADBE

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


Mass: 12734.274 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Notch1 / Plasmid: pAcGp67A / Cell line (production host): Hi-Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q07008
#2: Protein Delta-like protein


Mass: 25754.836 Da / Num. of mol.: 2 / Mutation: G28S, F107L, L206P
Source method: isolated from a genetically manipulated source
Details: Methylated in vitro / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dll4, Dll4_predicted, rCG_26804 / Plasmid: pAcGp67A / Cell line (production host): Hi-Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: D3ZHH1

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Sugars , 4 types, 14 molecules

#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: Sugar
ChemComp-BGC / beta-D-glucopyranose / beta-D-glucose / D-glucose / glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
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 / alpha-L-fucose / 6-deoxy-alpha-L-galactopyranose / L-fucose / fucose


Type: L-saccharide, alpha linking / Mass: 164.156 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
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
#7: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4 / 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 , 2 types, 331 molecules

#6: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 325 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsThe C-terminus of Neurogenic locus notch homolog protein 1 is as follows: CQRLEVLFQ. The C-terminus ...The C-terminus of Neurogenic locus notch homolog protein 1 is as follows: CQRLEVLFQ. The C-terminus of Delta-like protein is: CNEAAAHHHHHHHH. These proteins were each treated with carboxypeptidase, so the tags may have been disorder or cleaved 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: 2.36 Å3/Da / Density % sol: 47.87 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 20% PEG 4000, 2.5% isopropanol, 1% n-dodecyl beta-D-maltoside

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0331 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jun 21, 2014
RadiationMonochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0331 Å / Relative weight: 1
ReflectionResolution: 2.29→50 Å / Num. obs: 32367 / % possible obs: 99.2 % / Redundancy: 6.34 % / Biso Wilson estimate: 39.83 Å2 / Rmerge(I) obs: 0.106 / Net I/σ(I): 12.15
Reflection shellResolution: 2.29→2.42 Å / Redundancy: 7.82 % / Rmerge(I) obs: 0.846 / Mean I/σ(I) obs: 1.78 / % possible all: 95.4

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.3 Å49.56 Å
Translation2.3 Å49.56 Å

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Processing

Software
NameVersionClassification
PHENIXDEV-1839refinement
XDS20140110data reduction
PHASER2.5.6phasing
PDB_EXTRACT3.15data extraction
XDS20140110data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→49.56 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.259 1591 4.95 %random selection
Rwork0.218 ---
obs0.22 32158 97.7 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 54.39 Å2
Refinement stepCycle: LAST / Resolution: 2.3→49.56 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5303 0 204 325 5832
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0215765
X-RAY DIFFRACTIONf_angle_d1.3547813
X-RAY DIFFRACTIONf_dihedral_angle_d13.7652104
X-RAY DIFFRACTIONf_chiral_restr0.056841
X-RAY DIFFRACTIONf_plane_restr0.0051024
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2989-2.37310.40071070.33132092X-RAY DIFFRACTION75
2.3731-2.45790.33391330.29852812X-RAY DIFFRACTION100
2.4579-2.55630.30871500.28172788X-RAY DIFFRACTION100
2.5563-2.67260.29551580.27422823X-RAY DIFFRACTION100
2.6726-2.81350.34171360.26052798X-RAY DIFFRACTION100
2.8135-2.98980.32011430.27292833X-RAY DIFFRACTION100
2.9898-3.22060.29321550.26012816X-RAY DIFFRACTION100
3.2206-3.54460.24721460.22432844X-RAY DIFFRACTION100
3.5446-4.05730.23461500.19042867X-RAY DIFFRACTION100
4.0573-5.11090.22581530.16512868X-RAY DIFFRACTION100
5.1109-49.57450.21211600.18853026X-RAY DIFFRACTION100
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)
10.0788-0.0383-0.00110.0568-0.03050.0169-0.10140.38470.0238-0.23560.26350.2104-0.699-0.0708-00.6184-0.01240.02780.47870.07720.420820.88132.5128-13.3376
20.023-0.0011-0.00790.07570.08110.0756-0.4184-0.52430.25710.28490.160.06990.0475-0.3118-00.5833-0.0257-0.06560.4757-0.05020.550527.237634.9217-8.7536
30.1058-0.0891-0.01540.0792-0.01730.033-0.3257-0.15750.03640.79180.31550.1539-0.05930.003-00.50130.01340.03280.34820.03170.499426.834720.0561-11.8616
40.01120.0282-0.020.0475-0.03330.01630.3714-0.0396-0.15650.1161-0.5076-0.17860.4473-0.229300.5225-0.0143-0.02370.36970.0110.502333.98361.0123-6.9892
50.02040.01690.01010.0414-0.00770.00890.28490.2707-0.49430.71010.04120.21380.1551-0.10750.00190.50690.0138-0.00570.34510.0580.375725.83444.5586-7.2553
60.04870.00490.00570.1046-0.07390.0443-0.2424-0.0570.0693-0.07330.0136-0.0994-0.5690.203800.5220.021-0.03520.3892-0.01210.439729.7076-7.78750.5468
70.15830.0402-0.05770.06620.04240.06360.08320.1642-0.4132-0.67090.29720.48440.5132-0.18770.00010.4933-0.0797-0.09420.47780.14070.629425.745-27.89417.504
80.6523-0.14740.4560.40760.23070.51450.0543-0.0539-0.0403-0.0460.03250.1369-0.0460.068200.32910.0013-0.02280.33090.03080.32839.5835-11.4964-21.5436
90.31990.14660.5220.18440.34320.7855-0.0014-0.10110.11460.0021-0.0090.012-0.2358-0.119100.27390.0132-0.01440.29990.0220.29717.1375-6.3034-21.8148
10-0.30290.127-0.20070.6055-0.36160.1365-0.04950.0567-0.0278-0.10130.1039-0.0298-0.06650.1344-00.3793-0.0612-0.00740.44970.03190.472325.856624.5381-28.2344
11222222-0.2323-0.81742.69352.93120.99561.8062-0.6277-2.5125-0.71371.15660.5042-0.02070.5518-0.1630.756743.00861.8945-28.546
120.3751-0.1715-0.38380.11530.10740.3806-0.0221-0.27590.00490.07420.00370.13180.0848-0.0289-00.4956-0.0738-0.03580.38120.04280.27748.2136-59.54427.1157
130.17170.1163-0.08010.15760.02810.1418-0.0539-0.26090.07170.07440.14370.0976-0.0803-0.245900.357-0.00450.06140.3176-0.00660.36625.2085-33.11580.183
140.3951-0.17170.01540.16190.04190.4326-0.1816-0.12970.27420.22230.09150.5411-0.5345-0.136300.7531-0.0097-0.05020.4306-0.04680.46018.9174-3.33133.7563
150.6275-0.3126-0.26810.4515-0.25010.58260.1185-0.21940.2649-0.38440.00390.03630.20880.31070.03390.2843-0.03690.06620.3203-0.06070.299527.7683-24.0687-23.3147
160.11850.04910.12720.01690.04610.10820.0982-0.46910.5278-0.06140.0133-0.5906-0.25450.1100.2973-0.05170.0380.3961-0.06770.385213.031-20.6436-9.6994
170.2612-0.04690.02250.0142-0.05950.338-0.1031-0.23510.31330.14710.2468-0.11280.63410.40220.00370.36430.05770.05630.4374-0.0150.278730.4226-31.1518-24.1311
180.21690.25410.27060.30580.35670.3877-0.1092-0.34450.08510.0650.20670.1505-0.01070.04520.0030.322-0.0375-0.00910.36010.00230.347120.6437-31.4455-14.9388
190.670.1369-0.21030.8170.16361.05380.0482-0.0791-0.0472-0.0190.0762-0.1105-0.0463-0.016-00.2048-0.0078-0.00390.2571-0.04180.283320.5785-30.276-20.1287
200.25820.14860.00070.29560.1740.11740.1520.0887-0.2866-0.4827-0.046-0.04550.22450.0659-00.45160.018-0.0330.4251-0.00670.4568.5979-60.8978-8.9584
210.08330.0503-0.14640.5715-0.14190.18-0.1611-0.08510.0704-0.2232-0.02110.8798-0.0559-0.08390.00010.7638-0.0167-0.03360.4075-0.02510.515-1.2394-79.9853-5.0134
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 414 THROUGH 427 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 428 THROUGH 439 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 440 THROUGH 454 )
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESID 455 THROUGH 465 )
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESID 466 THROUGH 477 )
6X-RAY DIFFRACTION6CHAIN 'A' AND (RESID 478 THROUGH 492 )
7X-RAY DIFFRACTION7CHAIN 'A' AND (RESID 493 THROUGH 528 )
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESID 26 THROUGH 76 )
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESID 77 THROUGH 148 )
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESID 149 THROUGH 253 )
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESID 254 THROUGH 254 )
12X-RAY DIFFRACTION12CHAIN 'D' AND (RESID 411 THROUGH 449 )
13X-RAY DIFFRACTION13CHAIN 'D' AND (RESID 450 THROUGH 477 )
14X-RAY DIFFRACTION14CHAIN 'D' AND (RESID 478 THROUGH 527 )
15X-RAY DIFFRACTION15CHAIN 'E' AND (RESID 25 THROUGH 62 )
16X-RAY DIFFRACTION16CHAIN 'E' AND (RESID 64 THROUGH 76 )
17X-RAY DIFFRACTION17CHAIN 'E' AND (RESID 77 THROUGH 95 )
18X-RAY DIFFRACTION18CHAIN 'E' AND (RESID 96 THROUGH 123 )
19X-RAY DIFFRACTION19CHAIN 'E' AND (RESID 124 THROUGH 185 )
20X-RAY DIFFRACTION20CHAIN 'E' AND (RESID 186 THROUGH 213 )
21X-RAY DIFFRACTION21CHAIN 'E' AND (RESID 214 THROUGH 253 )

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