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- PDB-6cds: Human neurofibromin 2/merlin/schwannomin residues 1-339 in comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6cds | ||||||
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Title | Human neurofibromin 2/merlin/schwannomin residues 1-339 in complex with PIP2 | ||||||
![]() | Merlin | ||||||
![]() | SIGNALING PROTEIN / NEUROFIBROMIN 2 / SCHWANNOMIN / merlin / Tumor Suppressor protein | ||||||
Function / homology | ![]() regulation of hippo signaling / regulation of organelle assembly / regulation of gliogenesis / positive regulation of early endosome to late endosome transport / Schwann cell proliferation / osteoblast proliferation / negative regulation of tyrosine phosphorylation of STAT protein / negative regulation of Schwann cell proliferation / negative regulation of osteoblast proliferation / ectoderm development ...regulation of hippo signaling / regulation of organelle assembly / regulation of gliogenesis / positive regulation of early endosome to late endosome transport / Schwann cell proliferation / osteoblast proliferation / negative regulation of tyrosine phosphorylation of STAT protein / negative regulation of Schwann cell proliferation / negative regulation of osteoblast proliferation / ectoderm development / positive regulation of protein localization to early endosome / lens fiber cell differentiation / regulation of neural precursor cell proliferation / regulation of stem cell proliferation / negative regulation of receptor signaling pathway via JAK-STAT / cell-cell junction organization / regulation of protein localization to nucleus / filopodium membrane / negative regulation of MAPK cascade / negative regulation of cell-matrix adhesion / cortical actin cytoskeleton / negative regulation of cell-cell adhesion / odontogenesis of dentin-containing tooth / RHO GTPases activate PAKs / cleavage furrow / mesoderm formation / positive regulation of stress fiber assembly / negative regulation of cell migration / filopodium / hippocampus development / positive regulation of cell differentiation / adherens junction / regulation of protein stability / Regulation of actin dynamics for phagocytic cup formation / ruffle membrane / MAPK cascade / integrin binding / lamellipodium / apical part of cell / actin binding / regulation of cell shape / cell body / actin cytoskeleton organization / regulation of apoptotic process / early endosome / cytoskeleton / regulation of cell cycle / neuron projection / negative regulation of cell population proliferation / nucleolus / perinuclear region of cytoplasm / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chinthalapudi, K. / Sharff, A.J. / Bricogne, G. / Izard, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2. Authors: Chinthalapudi, K. / Mandati, V. / Zheng, J. / Sharff, A.J. / Bricogne, G. / Griffin, P.R. / Kissil, J. / Izard, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 297.8 KB | Display | ![]() |
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PDB format | ![]() | 241.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 935.7 KB | Display | ![]() |
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Full document | ![]() | 939.3 KB | Display | |
Data in XML | ![]() | 27.6 KB | Display | |
Data in CIF | ![]() | 38.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1isnS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 40179.520 Da / Num. of mol.: 2 / Mutation: G302E Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 229 molecules ![](data/chem/img/PIO.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.5 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100 mM HEPES (pH 7.5), 50 mM MgCl2(H2O)6, 35 % PEG 550 monomethyl ether |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Jun 14, 2015 Details: sagitally focusing 2nd crystal, Rosenbaum-Rock vertical focusing mirror |
Radiation | Monochromator: Si 111. Rosenbaum-Rock double-crystal monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.71→96.92 Å / Num. obs: 23131 / % possible obs: 99.3 % / Redundancy: 4.2 % / Biso Wilson estimate: 56.49 Å2 / CC1/2: 0.984 / Rpim(I) all: 0.119 / Net I/σ(I): 5.5 |
Reflection shell | Resolution: 2.71→2.84 Å / Redundancy: 3.6 % / Num. unique obs: 2952 / CC1/2: 0.31 / Rpim(I) all: 0.971 / % possible all: 95.4 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: 1isn Resolution: 2.62→48.3 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.88 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.367 Details: THE RESIDUE RANGES FOR EACH OF THE 8 TLS DOMAINS ARE AS FOLLOWS: TLS DOMAIN 1: A15 - A103 AND A804, A810, A813, A814, A820, A825, A829, A831, A832, A834, A835, A1004, A1005, A1017, A1020, ...Details: THE RESIDUE RANGES FOR EACH OF THE 8 TLS DOMAINS ARE AS FOLLOWS: TLS DOMAIN 1: A15 - A103 AND A804, A810, A813, A814, A820, A825, A829, A831, A832, A834, A835, A1004, A1005, A1017, A1020, A1023, A1027, A1032, A1038, A1039, A1042, A1050, A1053, A1058, A1060, A1062, A1067, A1068, A1071, A1072 TLS DOMAINS 2: A104 - A219 AND A656, A803, A806, A807, A809, A815, A816, A818, A821, A823, A830, A838, A839, A840, A1002, A1003, A1006, A1007, A1009, A1025, A1029, A1030, A1031, A1033, A1034, A1035, A1037, A1046, A1048, B1049, A1051, A1054, A1059, A1063 TLS DOMAIN 3: A220 - A290 AND A801, A805, A811, A812, A817, A822, A827, A833, A836, A837, A1010, A1011, A1013, A1021, A1024, A1026, A1028, A1040, A1041, A1047, A1052, A1055, A1057, A1061, A1064, A1065, A1066, A1070 TLS DOMAIN 4: A291 - A339 AND A500, A690, A802, A808, A819, A824, A826, A828, A1001, A1008, A1012, A1022, A1036, A1043, A1044, A1045, A1056, A1069 TLS DOMAIN 5: B15 - B103 AND A804, B810, B813, B814, B820, B825, B829, B831, B832, B834, B835, B1073, B1075, B1079, B1082, B1084, B1091, B1092, B1093, B1100, B1101, B1105, B1112, B1120, B1133, B1134, B1138 TLS DOMAIN 6: B104 - B219 AND B641, B803, B806, B807, B815, B816, B818, B821, B823, B830, B834, B838, B839, B1074, B1076, B1080, B1081, B1083, B1086, B1087, B1088, B1096, B1098, B1104, B1107, B1110, B1111, B1113, B1114, B1115, B1117, B1118, B1122, B1123, B1124, B1125, B1127, B1128, B1137, B1139, B1140 TLS DOMAIN 7: B220 - B290 AND B671, B700, B801, B805, B809, B811, B812, B817, B822, B827, B833, B836, B837, B8105, B1089, B1090, B1094, B9105, B1099, B1103, B1108, B1109, B1116, B1129, B1130, B1131, B1132, B1136, B1142, B1143 TLS DOMAIN 8: B291 - B339 AND B500, B802, B808, B819, B824, B826, B828, B1077, B1078, B1097, B1102, B1106, B1119, B1121, B1126, B1135, B1141
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Displacement parameters | Biso mean: 42.72 Å2
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Refine analyze | Luzzati coordinate error obs: 0.35 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 2.62→48.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.62→2.76 Å / Total num. of bins used: 10
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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