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- PDB-4xhq: Re-refinement the crystal structure of Dscam1 isoform 1.34, N-ter... -

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Basic information

Entry
Database: PDB / ID: 4xhq
TitleRe-refinement the crystal structure of Dscam1 isoform 1.34, N-terminal four Ig domains
ComponentsDscam
KeywordsCELL ADHESION / Ig fold
Function / homology
Function and homology information


DSCAM interactions / mushroom body development / detection of mechanical stimulus involved in sensory perception of touch / detection of molecule of bacterial origin / central nervous system morphogenesis / ventral cord development / dendrite self-avoidance / cell-cell adhesion mediator activity / axon extension involved in axon guidance / axon guidance receptor activity ...DSCAM interactions / mushroom body development / detection of mechanical stimulus involved in sensory perception of touch / detection of molecule of bacterial origin / central nervous system morphogenesis / ventral cord development / dendrite self-avoidance / cell-cell adhesion mediator activity / axon extension involved in axon guidance / axon guidance receptor activity / peripheral nervous system development / axonal fasciculation / regulation of dendrite morphogenesis / regulation of axonogenesis / homophilic cell adhesion via plasma membrane adhesion molecules / neuron development / phagocytosis / antigen binding / axon guidance / perikaryon / neuron projection / axon / neuronal cell body / dendrite / protein homodimerization activity / extracellular region / identical protein binding / plasma membrane
Similarity search - Function
Down syndrome cell adhesion molecule, C-terminal / Down syndrome cell adhesion molecule C terminal / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. ...Down syndrome cell adhesion molecule, C-terminal / Down syndrome cell adhesion molecule C terminal / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Cell adhesion molecule Dscam1
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / Resolution: 1.948 Å
AuthorsChen, Q. / Yu, Y.
CitationJournal: NATURE / Year: 2007
Title: Structural Basis of Dscam Isoform Specificity
Authors: Meijers, R. / Puettmann-Holgado, R. / Skiniotis, G. / Liu, J.-H. / Walz, T. / Wang, J.-H. / Schmucker, D.
History
DepositionJan 6, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Oct 12, 2016Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...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_struct_oper_list / pdbx_struct_special_symmetry / struct_asym / struct_conn / 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_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _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_struct_oper_list.symmetry_operation / _pdbx_struct_special_symmetry.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_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Remark 0THIS ENTRY 4XHQ REFLECTS AN ALTERNATIVE MODELING OF THE STRUCTURAL DATA IN R2V5MSF ORIGINAL DATA ...THIS ENTRY 4XHQ REFLECTS AN ALTERNATIVE MODELING OF THE STRUCTURAL DATA IN R2V5MSF ORIGINAL DATA DETERMINED BY AUTHOR: R.MEIJERS,R.PUETTMANN-HOLGADO,G.SKINIOTIS,J.-H.LIU,T.WALZ, D.SCHMUCKER,J.-H.WANG

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Dscam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,08016
Polymers42,8811
Non-polymers2,20015
Water6,900383
1
A: Dscam
hetero molecules

A: Dscam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,16032
Polymers85,7612
Non-polymers4,39930
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_755-x+2,y,-z1
Buried area11870 Å2
ΔGint-137 kcal/mol
Surface area37300 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.172, 99.172, 163.991
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number93
Space group name H-MP4222
Components on special symmetry positions
IDModelComponents
11A-420-

SO4

21A-882-

HOH

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Dscam /


Mass: 42880.582 Da / Num. of mol.: 1 / Fragment: UNP residues 36-423
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: Dscam1, Dscam, CG17800 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9NBA1

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Sugars , 2 types, 2 molecules

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


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE

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Non-polymers , 5 types, 396 molecules

#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#6: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#7: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 383 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 4.7 Å3/Da / Density % sol: 73.84 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 2V5M.
Crystal growDetails: 1.5 M AMMONIUM SULPHATE, 0.1 M HEPES PH 7.5

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.4_1496)refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementResolution: 1.948→19.834 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.5 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2332 3003 5.04 %
Rwork0.2031 --
obs0.2047 59545 98.58 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.948→19.834 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3014 0 136 383 3533
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0183218
X-RAY DIFFRACTIONf_angle_d1.664359
X-RAY DIFFRACTIONf_dihedral_angle_d13.7871210
X-RAY DIFFRACTIONf_chiral_restr0.094508
X-RAY DIFFRACTIONf_plane_restr0.008551
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9482-1.98010.36681110.30532445X-RAY DIFFRACTION91
1.9801-2.01420.33251240.28522577X-RAY DIFFRACTION96
2.0142-2.05080.31831630.2732576X-RAY DIFFRACTION98
2.0508-2.09020.29461350.2642672X-RAY DIFFRACTION98
2.0902-2.13280.26561360.2522644X-RAY DIFFRACTION99
2.1328-2.17910.30021270.24912676X-RAY DIFFRACTION99
2.1791-2.22980.28381580.24582638X-RAY DIFFRACTION99
2.2298-2.28550.27521570.25142663X-RAY DIFFRACTION99
2.2855-2.34720.3191390.23952674X-RAY DIFFRACTION99
2.3472-2.41610.291300.24742702X-RAY DIFFRACTION99
2.4161-2.49390.27111320.25032685X-RAY DIFFRACTION99
2.4939-2.58290.29061510.24462675X-RAY DIFFRACTION99
2.5829-2.68610.29751310.24462724X-RAY DIFFRACTION99
2.6861-2.8080.27141410.23182716X-RAY DIFFRACTION99
2.808-2.95560.23931600.22222700X-RAY DIFFRACTION99
2.9556-3.14010.25491250.2122739X-RAY DIFFRACTION100
3.1401-3.38140.23181590.2022713X-RAY DIFFRACTION100
3.3814-3.71970.20761480.18272764X-RAY DIFFRACTION100
3.7197-4.25330.19731560.16232770X-RAY DIFFRACTION100
4.2533-5.34140.16641700.14822795X-RAY DIFFRACTION100
5.3414-19.83540.22071500.19052994X-RAY DIFFRACTION100

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