data_16000 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the nucleocapsid-binding domain of the measles virus phosphoprotein ; _BMRB_accession_number 16000 _BMRB_flat_file_name bmr16000.str _Entry_type original _Submission_date 2008-10-23 _Accession_date 2008-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solution structure of the nucleocapsid-binding domain of the measles virus phosphoprotein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gely Stephane . . 2 Bourhis 'Jean Marie' . . 3 Longhi Sonia . . 4 Darbon Herve . . 5 Bernard Cedric . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 241 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-09-08 update BMRB 'complete entry citation' 2010-05-06 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20058326 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gely Stephane . . 2 Lowry David F. . 3 Bernard Cedric . . 4 Jensen Malene R. . 5 Blackledge Martin . . 6 Costanzo Stephanie . . 7 Bourhis Jean-Marie . . 8 Darbon Herve . . 9 Daughdrill Gary . . 10 Longhi Sonia . . stop_ _Journal_abbreviation 'J. Mol. Recognit.' _Journal_name_full 'Journal of molecular recognition : JMR' _Journal_volume 23 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 435 _Page_last 447 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name XD_domain _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label XD_domain $XD_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_XD_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common XD_domain _Molecular_mass 5169.205 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 44 _Mol_residue_sequence ; SVIRSIIKSSRLEEDRKRYL MTLLDDIKGANDLAKFHQML VKII ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 462 SER 2 463 VAL 3 464 ILE 4 465 ARG 5 466 SER 6 467 ILE 7 468 ILE 8 469 LYS 9 470 SER 10 471 SER 11 472 ARG 12 473 LEU 13 474 GLU 14 475 GLU 15 476 ASP 16 477 ARG 17 478 LYS 18 479 ARG 19 480 TYR 20 481 LEU 21 482 MET 22 483 THR 23 484 LEU 24 485 LEU 25 486 ASP 26 487 ASP 27 488 ILE 28 489 LYS 29 490 GLY 30 491 ALA 31 492 ASN 32 493 ASP 33 494 LEU 34 495 ALA 35 496 LYS 36 497 PHE 37 498 HIS 38 499 GLN 39 500 MET 40 501 LEU 41 502 VAL 42 503 LYS 43 504 ILE 44 505 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15993 XD 97.73 44 100.00 100.00 2.85e-20 BMRB 15994 XD 97.73 44 100.00 100.00 2.85e-20 PDB 1T6O "Nucleocapsid-Binding Domain Of The Measles Virus P Protein (Amino Acids 457-507) In Complex With Amino Acids 486-505 Of The Mea" 100.00 51 97.73 100.00 1.98e-20 PDB 2K9D "Solution Structure Of The Domain X Of Measle Phosphoprotein" 100.00 44 100.00 100.00 6.91e-21 DBJ BAA09955 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.23e-19 DBJ BAA09962 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.23e-19 DBJ BAA33868 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 4.62e-19 DBJ BAA33874 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 4.91e-19 DBJ BAA34978 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.64e-19 EMBL CAA34578 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.39e-19 EMBL CAA34585 "unnamed protein product [Measles virus]" 100.00 507 97.73 100.00 4.18e-19 EMBL CAA91364 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 2.25e-19 EMBL CAQ15998 "phosphoprotein [Measles virus MVi/Ibadan.NIE/8.98/9]" 100.00 507 97.73 100.00 3.75e-19 EMBL CAQ15999 "phosphoprotein [Measles virus MVi/Ibadan.NIE/9.98/5]" 100.00 507 97.73 100.00 4.49e-19 GB AAA46434 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 2.86e-19 GB AAA46435 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.39e-19 GB AAA46437 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 2.62e-19 GB AAA63284 "P protein [Measles virus]" 100.00 507 97.73 100.00 3.23e-19 GB AAA63285 "P protein [Measles virus]" 100.00 507 97.73 100.00 3.39e-19 REF NP_056919 "phosphoprotein [Measles virus]" 100.00 507 97.73 100.00 3.64e-19 SP P03422 "RecName: Full=Phosphoprotein; Short=Protein P" 100.00 507 97.73 100.00 2.62e-19 SP P35974 "RecName: Full=Phosphoprotein; Short=Protein P" 100.00 507 97.73 100.00 2.23e-19 SP Q9WMB4 "RecName: Full=Phosphoprotein; Short=Protein P" 100.00 507 97.73 100.00 3.64e-19 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $XD_domain Measles 11234 virus . Morbillivirus . stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $XD_domain 'recombinant technology' . Escherichia coli . PET41A(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $XD_domain 1.5 uM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $XD_domain 1.06 uM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'chemical shift assignment' refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water H 1 protons ppm 4.689 internal direct . . . 1.000000000 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name XD_domain _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 462 1 SER H H 8.474 . . 2 462 1 SER HA H 4.223 . . 3 462 1 SER HB2 H 3.997 . . 4 462 1 SER HB3 H 3.997 . . 5 463 2 VAL H H 7.605 . . 6 463 2 VAL HA H 3.822 . . 7 463 2 VAL HB H 2.254 . . 8 463 2 VAL HG1 H 1.146 . . 9 463 2 VAL HG2 H 1.009 . . 10 464 3 ILE H H 8.231 . . 11 464 3 ILE HA H 3.554 . . 12 464 3 ILE HB H 1.969 . . 13 464 3 ILE HD1 H 0.712 . . 14 464 3 ILE HG12 H 1.164 . . 15 464 3 ILE HG13 H 1.164 . . 16 465 4 ARG H H 8.643 . . 17 465 4 ARG HA H 3.812 . . 18 465 4 ARG HB2 H 1.986 . . 19 465 4 ARG HB3 H 1.986 . . 20 465 4 ARG HG2 H 1.695 . . 21 465 4 ARG HG3 H 1.695 . . 22 466 5 SER H H 7.859 . . 23 466 5 SER HA H 4.334 . . 24 466 5 SER HB2 H 4.167 . . 25 466 5 SER HB3 H 4.167 . . 26 467 6 ILE H H 8.270 . . 27 467 6 ILE HA H 3.818 . . 28 467 6 ILE HB H 2.257 . . 29 467 6 ILE HD1 H 0.932 . . 30 467 6 ILE HG12 H 2.192 . . 31 467 6 ILE HG13 H 2.192 . . 32 467 6 ILE HG2 H 1.164 . . 33 468 7 ILE H H 8.052 . . 34 468 7 ILE HA H 3.486 . . 35 468 7 ILE HB H 2.224 . . 36 468 7 ILE HD1 H 1.056 . . 37 468 7 ILE HG12 H 2.160 . . 38 468 7 ILE HG13 H 2.160 . . 39 468 7 ILE HG2 H 0.993 . . 40 469 8 LYS H H 8.602 . . 41 469 8 LYS HA H 4.034 . . 42 469 8 LYS HB2 H 2.025 . . 43 469 8 LYS HB3 H 2.025 . . 44 469 8 LYS HD2 H 1.755 . . 45 469 8 LYS HD3 H 1.755 . . 46 469 8 LYS HG2 H 1.488 . . 47 469 8 LYS HG3 H 1.488 . . 48 470 9 SER H H 8.201 . . 49 470 9 SER HA H 4.619 . . 50 470 9 SER HB2 H 4.001 . . 51 470 9 SER HB3 H 4.001 . . 52 471 10 SER H H 7.540 . . 53 471 10 SER HA H 4.536 . . 54 471 10 SER HB2 H 4.195 . . 55 471 10 SER HB3 H 4.195 . . 56 472 11 ARG H H 9.245 . . 57 472 11 ARG HA H 4.646 . . 58 472 11 ARG HB2 H 2.077 . . 59 472 11 ARG HB3 H 2.275 . . 60 472 11 ARG HG2 H 1.774 . . 61 472 11 ARG HG3 H 1.774 . . 62 473 12 LEU H H 6.980 . . 63 473 12 LEU HA H 3.959 . . 64 473 12 LEU HB2 H 1.557 . . 65 473 12 LEU HB3 H 1.690 . . 66 473 12 LEU HD1 H 0.778 . . 67 473 12 LEU HD2 H 0.709 . . 68 473 12 LEU HG H 1.389 . . 69 474 13 GLU H H 9.121 . . 70 474 13 GLU HA H 3.733 . . 71 474 13 GLU HB2 H 2.106 . . 72 474 13 GLU HB3 H 2.106 . . 73 474 13 GLU HG2 H 2.418 . . 74 474 13 GLU HG3 H 2.652 . . 75 475 14 GLU H H 9.127 . . 76 475 14 GLU HA H 4.296 . . 77 475 14 GLU HB2 H 2.210 . . 78 475 14 GLU HB3 H 2.210 . . 79 475 14 GLU HG2 H 2.520 . . 80 475 14 GLU HG3 H 2.520 . . 81 476 15 ASP H H 9.115 . . 82 476 15 ASP HA H 4.448 . . 83 476 15 ASP HB2 H 2.766 . . 84 476 15 ASP HB3 H 2.766 . . 85 477 16 ARG H H 7.386 . . 86 477 16 ARG HA H 4.372 . . 87 477 16 ARG HB2 H 1.825 . . 88 477 16 ARG HB3 H 1.915 . . 89 477 16 ARG HG2 H 1.496 . . 90 477 16 ARG HG3 H 1.496 . . 91 478 17 LYS H H 8.365 . . 92 478 17 LYS HA H 3.766 . . 93 478 17 LYS HB2 H 2.133 . . 94 478 17 LYS HB3 H 2.133 . . 95 478 17 LYS HD2 H 1.646 . . 96 478 17 LYS HD3 H 1.646 . . 97 478 17 LYS HG2 H 1.554 . . 98 478 17 LYS HG3 H 1.554 . . 99 479 18 ARG H H 8.139 . . 100 479 18 ARG HA H 4.073 . . 101 479 18 ARG HB2 H 1.934 . . 102 479 18 ARG HB3 H 2.055 . . 103 479 18 ARG HG2 H 1.718 . . 104 479 18 ARG HG3 H 1.718 . . 105 480 19 TYR H H 7.929 . . 106 480 19 TYR HA H 4.442 . . 107 480 19 TYR HB2 H 3.243 . . 108 480 19 TYR HB3 H 3.446 . . 109 480 19 TYR HD1 H 7.159 . . 110 480 19 TYR HD2 H 7.159 . . 111 480 19 TYR HE1 H 6.983 . . 112 480 19 TYR HE2 H 6.983 . . 113 481 20 LEU H H 8.595 . . 114 481 20 LEU HA H 4.066 . . 115 481 20 LEU HB2 H 2.200 . . 116 481 20 LEU HB3 H 2.200 . . 117 481 20 LEU HD1 H 0.925 . . 118 481 20 LEU HD2 H 0.880 . . 119 482 21 MET H H 8.609 . . 120 482 21 MET HA H 4.108 . . 121 482 21 MET HB2 H 1.599 . . 122 482 21 MET HB3 H 2.425 . . 123 482 21 MET HG2 H 2.695 . . 124 482 21 MET HG3 H 2.907 . . 125 483 22 THR H H 7.976 . . 126 483 22 THR HA H 4.402 . . 127 483 22 THR HB H 4.092 . . 128 483 22 THR HG2 H 1.361 . . 129 484 23 LEU H H 7.731 . . 130 484 23 LEU HA H 4.041 . . 131 484 23 LEU HB2 H 1.904 . . 132 484 23 LEU HB3 H 1.904 . . 133 484 23 LEU HD1 H 0.876 . . 134 484 23 LEU HG H 1.486 . . 135 485 24 LEU H H 7.937 . . 136 485 24 LEU HA H 3.353 . . 137 485 24 LEU HB2 H 2.041 . . 138 485 24 LEU HB3 H 2.041 . . 139 485 24 LEU HD1 H 1.032 . . 140 485 24 LEU HD2 H 0.706 . . 141 485 24 LEU HG H 1.263 . . 142 486 25 ASP H H 7.647 . . 143 486 25 ASP HA H 4.423 . . 144 486 25 ASP HB2 H 2.796 . . 145 486 25 ASP HB3 H 2.796 . . 146 487 26 ASP H H 7.404 . . 147 487 26 ASP HA H 4.424 . . 148 487 26 ASP HB2 H 2.850 . . 149 487 26 ASP HB3 H 2.664 . . 150 488 27 ILE H H 7.493 . . 151 488 27 ILE HA H 4.105 . . 152 488 27 ILE HB H 1.965 . . 153 488 27 ILE HD1 H 0.618 . . 154 488 27 ILE HG12 H 1.272 . . 155 488 27 ILE HG13 H 1.550 . . 156 488 27 ILE HG2 H 0.862 . . 157 489 28 LYS H H 9.161 . . 158 489 28 LYS HA H 4.583 . . 159 489 28 LYS HB2 H 1.868 . . 160 489 28 LYS HB3 H 1.955 . . 161 490 29 GLY H H 8.412 . . 162 490 29 GLY HA2 H 4.380 . . 163 492 31 ASN H H 8.269 . . 164 492 31 ASN HA H 4.388 . . 165 492 31 ASN HB2 H 2.822 . . 166 492 31 ASN HB3 H 2.708 . . 167 493 32 ASP H H 8.457 . . 168 493 32 ASP HA H 4.530 . . 169 493 32 ASP HB2 H 2.803 . . 170 493 32 ASP HB3 H 2.803 . . 171 494 33 LEU H H 8.311 . . 172 494 33 LEU HA H 3.975 . . 173 494 33 LEU HB2 H 1.762 . . 174 494 33 LEU HB3 H 1.762 . . 175 494 33 LEU HD1 H 0.866 . . 176 494 33 LEU HD2 H 0.927 . . 177 494 33 LEU HG H 1.855 . . 178 495 34 ALA H H 8.071 . . 179 495 34 ALA HA H 4.401 . . 180 495 34 ALA HB H 1.731 . . 181 496 35 LYS H H 7.979 . . 182 496 35 LYS HA H 4.214 . . 183 496 35 LYS HB2 H 2.111 . . 184 496 35 LYS HB3 H 2.111 . . 185 496 35 LYS HD2 H 1.836 . . 186 496 35 LYS HD3 H 1.856 . . 187 496 35 LYS HG2 H 1.701 . . 188 496 35 LYS HG3 H 1.701 . . 189 497 36 PHE H H 8.413 . . 190 497 36 PHE HA H 4.127 . . 191 497 36 PHE HB2 H 3.391 . . 192 497 36 PHE HB3 H 3.391 . . 193 497 36 PHE HD1 H 6.899 . . 194 497 36 PHE HD2 H 6.899 . . 195 497 36 PHE HE1 H 4.378 . . 196 497 36 PHE HE2 H 4.378 . . 197 498 37 HIS H H 8.920 . . 198 498 37 HIS HA H 4.216 . . 199 498 37 HIS HB2 H 3.182 . . 200 498 37 HIS HB3 H 3.635 . . 201 499 38 GLN H H 8.031 . . 202 499 38 GLN HA H 3.938 . . 203 499 38 GLN HB2 H 2.309 . . 204 499 38 GLN HB3 H 2.309 . . 205 499 38 GLN HG2 H 2.526 . . 206 499 38 GLN HG3 H 2.660 . . 207 500 39 MET H H 7.881 . . 208 500 39 MET HA H 4.115 . . 209 500 39 MET HB2 H 2.221 . . 210 500 39 MET HB3 H 2.221 . . 211 500 39 MET HG2 H 2.317 . . 212 500 39 MET HG3 H 2.317 . . 213 501 40 LEU H H 8.585 . . 214 501 40 LEU HA H 3.891 . . 215 501 40 LEU HB2 H 1.180 . . 216 501 40 LEU HB3 H 1.180 . . 217 502 41 VAL H H 8.233 . . 218 502 41 VAL HA H 3.631 . . 219 502 41 VAL HB H 2.131 . . 220 503 42 LYS H H 7.369 . . 221 503 42 LYS HA H 4.145 . . 222 503 42 LYS HB2 H 2.050 . . 223 503 42 LYS HB3 H 2.050 . . 224 503 42 LYS HD2 H 0.958 . . 225 503 42 LYS HD3 H 0.958 . . 226 503 42 LYS HG2 H 1.456 . . 227 503 42 LYS HG3 H 1.456 . . 228 504 43 ILE H H 8.096 . . 229 504 43 ILE HA H 3.903 . . 230 504 43 ILE HB H 2.164 . . 231 504 43 ILE HD1 H 0.943 . . 232 504 43 ILE HG12 H 1.872 . . 233 504 43 ILE HG13 H 1.304 . . 234 504 43 ILE HG2 H 1.033 . . 235 505 44 ILE H H 8.454 . . 236 505 44 ILE HA H 3.822 . . 237 505 44 ILE HB H 2.045 . . 238 505 44 ILE HD1 H 0.863 . . 239 505 44 ILE HG12 H 1.485 . . 240 505 44 ILE HG13 H 1.489 . . 241 505 44 ILE HG2 H 1.014 . . stop_ save_