data_17888 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of the Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392 ; _BMRB_accession_number 17888 _BMRB_flat_file_name bmr17888.str _Entry_type original _Submission_date 2011-08-29 _Accession_date 2011-08-29 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Halskau Heli . . 2 Halskau Oyvind . Jr. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 193 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-17 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22573762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Havukainen Heli . . 2 Underhaug Jarl . . 3 Wolschin Florian . . 4 Amdam Gro V. . 5 Halskau Oyvind . Jr. stop_ _Journal_abbreviation 'J. Exp. Biol.' _Journal_volume 215 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1837 _Page_last 1846 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Polyserine Tract of Apis mellifera Vitellogenin' $Vg 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_Vg _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Vg _Molecular_mass 3986.349 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; EKLKQDILNLRTDISTSXSS ISSSEENDFWQPKPT ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 LYS 3 LEU 4 LYS 5 GLN 6 ASP 7 ILE 8 LEU 9 ASN 10 LEU 11 ARG 12 THR 13 ASP 14 ILE 15 SER 16 THR 17 SER 18 SEP 19 SER 20 SER 21 ILE 22 SER 23 SER 24 SER 25 GLU 26 GLU 27 ASN 28 ASP 29 PHE 30 TRP 31 GLN 32 PRO 33 LYS 34 PRO 35 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-23 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 PDB 2LIC "Nmr Structure Of The Polyserine Tract Of Apis Mellifera Vitellogenin, Residues 358-392" 100.00 35 100.00 100.00 1.77e-13 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOSERINE _BMRB_code SEP _PDB_code SEP _Standard_residue_derivative . _Molecular_mass 185.072 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? O O O . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? OG OG O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Vg 'honey bee' 7460 Eukaryota Metazoa Apis mellifera 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 $Vg 'chemical synthesis' . . . . . 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 $Vg 7.8 w/v [U-15N]-ILE 'sodium azide' 0.02 % 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' DSS 5 % '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 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AV600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 273 . K pH 6.7 . pH pressure 1 . atm 'ionic strength' 0.06 . M 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 DSS H 1 'methyl protons' ppm 0.00 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-15N HSQC' '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 'Polyserine Tract of Apis mellifera Vitellogenin' _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 1 1 GLU H H 8.430 0.002 . 2 1 1 GLU HA H 4.295 0.000 . 3 1 1 GLU HG2 H 2.248 0.001 . 4 1 1 GLU HG3 H 2.248 0.001 . 5 2 2 LYS H H 8.427 0.000 . 6 2 2 LYS HA H 4.348 0.001 . 7 2 2 LYS HB2 H 1.805 0.002 . 8 2 2 LYS HB3 H 1.805 0.002 . 9 2 2 LYS HG2 H 1.438 0.001 . 10 2 2 LYS HG3 H 1.438 0.001 . 11 2 2 LYS HD2 H 1.752 0.000 . 12 2 2 LYS HD3 H 1.752 0.000 . 13 2 2 LYS HE2 H 2.995 0.000 . 14 2 2 LYS HE3 H 2.995 0.000 . 15 3 3 LEU H H 8.487 0.001 . 16 3 3 LEU HA H 4.345 0.006 . 17 3 3 LEU HB2 H 1.563 0.002 . 18 3 3 LEU HB3 H 1.640 0.003 . 19 3 3 LEU HD1 H 0.931 0.003 . 20 3 3 LEU HD2 H 0.879 0.001 . 21 4 4 LYS H H 8.409 0.005 . 22 4 4 LYS HA H 4.270 0.002 . 23 4 4 LYS HB2 H 1.822 0.001 . 24 4 4 LYS HB3 H 1.822 0.001 . 25 4 4 LYS HG2 H 1.453 0.002 . 26 4 4 LYS HG3 H 1.407 0.003 . 27 4 4 LYS HD2 H 1.758 0.003 . 28 4 4 LYS HD3 H 1.758 0.003 . 29 4 4 LYS HE2 H 3.000 0.002 . 30 4 4 LYS HE3 H 3.000 0.002 . 31 5 5 GLN H H 8.428 0.002 . 32 5 5 GLN HA H 4.273 0.004 . 33 5 5 GLN HB2 H 2.332 0.004 . 34 5 5 GLN HB3 H 2.332 0.004 . 35 5 5 GLN HG2 H 2.067 0.007 . 36 5 5 GLN HE21 H 7.575 0.007 . 37 5 5 GLN HE22 H 6.884 0.005 . 38 6 6 ASP H H 8.417 0.002 . 39 6 6 ASP HA H 4.603 0.002 . 40 6 6 ASP HB2 H 2.696 0.001 . 41 6 6 ASP HB3 H 2.598 0.004 . 42 7 7 ILE H H 8.032 0.003 . 43 7 7 ILE HA H 4.128 0.001 . 44 7 7 ILE HB H 1.914 0.002 . 45 7 7 ILE HG12 H 1.447 0.002 . 46 7 7 ILE HG13 H 1.447 0.002 . 47 7 7 ILE HG2 H 1.182 0.000 . 48 7 7 ILE HD1 H 0.908 0.003 . 49 8 8 LEU H H 8.224 0.003 . 50 8 8 LEU HA H 4.298 0.002 . 51 8 8 LEU HB2 H 1.551 0.003 . 52 8 8 LEU HB3 H 1.670 0.002 . 53 8 8 LEU HD1 H 0.914 0.000 . 54 8 8 LEU HD2 H 0.865 0.000 . 55 9 9 ASN H H 8.295 0.003 . 56 9 9 ASN HA H 4.678 0.003 . 57 9 9 ASN HB2 H 2.840 0.003 . 58 9 9 ASN HB3 H 2.717 0.002 . 59 9 9 ASN HD21 H 7.657 0.002 . 60 9 9 ASN HD22 H 6.868 0.001 . 61 10 10 LEU H H 8.103 0.002 . 62 10 10 LEU HA H 4.330 0.001 . 63 10 10 LEU HB2 H 1.605 0.002 . 64 10 10 LEU HB3 H 1.651 0.000 . 65 10 10 LEU HD1 H 0.921 0.002 . 66 10 10 LEU HD2 H 0.859 0.001 . 67 11 11 ARG H H 8.324 0.004 . 68 11 11 ARG HA H 4.426 0.003 . 69 11 11 ARG HB2 H 1.914 0.001 . 70 11 11 ARG HB3 H 1.811 0.004 . 71 11 11 ARG HG2 H 1.672 0.005 . 72 11 11 ARG HG3 H 1.614 0.004 . 73 11 11 ARG HD2 H 3.204 0.001 . 74 11 11 ARG HD3 H 3.204 0.001 . 75 11 11 ARG HE H 7.491 0.001 . 76 12 12 THR H H 8.243 0.003 . 77 12 12 THR HA H 4.357 0.002 . 78 12 12 THR HB H 4.277 0.002 . 79 12 12 THR HG2 H 1.187 0.002 . 80 13 13 ASP H H 8.472 0.004 . 81 13 13 ASP HA H 4.649 0.001 . 82 13 13 ASP HB2 H 2.700 0.001 . 83 13 13 ASP HB3 H 2.655 0.001 . 84 14 14 ILE H H 7.967 0.003 . 85 14 14 ILE HA H 4.248 0.002 . 86 14 14 ILE HB H 1.909 0.001 . 87 14 14 ILE HG12 H 1.424 0.002 . 88 14 14 ILE HG13 H 1.424 0.002 . 89 14 14 ILE HG2 H 1.194 0.000 . 90 14 14 ILE HD1 H 0.903 0.003 . 91 15 15 SER H H 8.436 0.006 . 92 15 15 SER HA H 4.540 0.003 . 93 16 16 THR H H 8.218 0.003 . 94 16 16 THR HA H 4.467 0.002 . 95 16 16 THR HB H 4.346 0.002 . 96 16 16 THR HG2 H 1.208 0.002 . 97 17 17 SER H H 8.385 0.004 . 98 17 17 SER HA H 4.468 0.002 . 99 17 17 SER HB2 H 3.958 0.004 . 100 17 17 SER HB3 H 3.885 0.004 . 101 18 18 SEP H H 9.079 0.002 . 102 18 18 SEP HA H 4.506 0.001 . 103 18 18 SEP HB2 H 4.076 0.003 . 104 18 18 SEP HB3 H 4.132 0.002 . 105 19 19 SER H H 8.331 0.002 . 106 19 19 SER HA H 4.512 0.002 . 107 19 19 SER HB2 H 3.922 0.000 . 108 19 19 SER HB3 H 3.922 0.000 . 109 20 20 SER H H 8.186 0.009 . 110 20 20 SER HA H 4.469 0.002 . 111 20 20 SER HB2 H 3.889 0.002 . 112 20 20 SER HB3 H 3.889 0.002 . 113 21 21 ILE H H 8.081 0.004 . 114 21 21 ILE HA H 4.244 0.001 . 115 21 21 ILE HB H 1.894 0.004 . 116 21 21 ILE HG12 H 1.466 0.005 . 117 21 21 ILE HG13 H 1.466 0.005 . 118 21 21 ILE HG2 H 1.221 0.000 . 119 21 21 ILE HD1 H 0.915 0.000 . 120 22 22 SER H H 8.392 0.004 . 121 22 22 SER HA H 4.521 0.000 . 122 23 23 SER H H 8.413 0.002 . 123 23 23 SER HA H 4.528 0.001 . 124 26 26 GLU H H 8.336 0.003 . 125 26 26 GLU HA H 4.234 0.002 . 126 26 26 GLU HB2 H 2.047 0.004 . 127 26 26 GLU HB3 H 1.926 0.002 . 128 26 26 GLU HG2 H 2.243 0.002 . 129 26 26 GLU HG3 H 2.243 0.002 . 130 27 27 ASN H H 8.308 0.004 . 131 27 27 ASN HA H 4.665 0.002 . 132 27 27 ASN HB2 H 2.728 0.001 . 133 27 27 ASN HB3 H 2.696 0.000 . 134 27 27 ASN HD21 H 7.561 0.001 . 135 27 27 ASN HD22 H 6.898 0.002 . 136 28 28 ASP H H 8.271 0.002 . 137 28 28 ASP HA H 4.516 0.002 . 138 28 28 ASP HB2 H 2.542 0.002 . 139 28 28 ASP HB3 H 2.542 0.002 . 140 29 29 PHE H H 8.020 0.002 . 141 29 29 PHE HA H 4.491 0.002 . 142 29 29 PHE HB2 H 2.978 0.001 . 143 29 29 PHE HB3 H 2.978 0.001 . 144 29 29 PHE HD1 H 7.066 0.001 . 145 29 29 PHE HD2 H 7.066 0.001 . 146 29 29 PHE HE1 H 7.265 0.001 . 147 29 29 PHE HE2 H 7.265 0.001 . 148 30 30 TRP H H 7.926 0.002 . 149 30 30 TRP HA H 4.538 0.002 . 150 30 30 TRP HB2 H 3.224 0.003 . 151 30 30 TRP HB3 H 3.224 0.003 . 152 30 30 TRP HD1 H 7.240 0.001 . 153 30 30 TRP HE1 H 10.136 0.002 . 154 30 30 TRP HE3 H 7.554 0.001 . 155 30 30 TRP HZ2 H 7.489 0.001 . 156 30 30 TRP HZ3 H 7.140 0.001 . 157 30 30 TRP HH2 H 7.238 0.002 . 158 31 31 GLN H H 7.695 0.002 . 159 31 31 GLN HA H 4.421 0.002 . 160 31 31 GLN HB2 H 2.183 0.003 . 161 31 31 GLN HB3 H 2.183 0.003 . 162 31 31 GLN HG2 H 1.922 0.004 . 163 31 31 GLN HG3 H 1.744 0.004 . 164 31 31 GLN HE21 H 7.456 0.002 . 165 31 31 GLN HE22 H 6.834 0.001 . 166 32 32 PRO HA H 4.225 0.000 . 167 32 32 PRO HB2 H 2.240 0.002 . 168 32 32 PRO HB3 H 2.240 0.002 . 169 32 32 PRO HG2 H 1.941 0.002 . 170 32 32 PRO HG3 H 1.835 0.002 . 171 32 32 PRO HD2 H 3.521 0.003 . 172 32 32 PRO HD3 H 3.468 0.005 . 173 33 33 LYS H H 8.348 0.005 . 174 33 33 LYS HA H 4.570 0.002 . 175 33 33 LYS HB2 H 1.825 0.003 . 176 33 33 LYS HB3 H 1.825 0.003 . 177 33 33 LYS HG2 H 1.507 0.000 . 178 33 33 LYS HG3 H 1.482 0.000 . 179 33 33 LYS HD2 H 1.718 0.008 . 180 33 33 LYS HD3 H 1.718 0.008 . 181 33 33 LYS HE2 H 2.995 0.000 . 182 33 33 LYS HE3 H 2.995 0.000 . 183 34 34 PRO HA H 4.477 0.002 . 184 34 34 PRO HB2 H 2.303 0.003 . 185 34 34 PRO HB3 H 2.303 0.003 . 186 34 34 PRO HG2 H 2.041 0.005 . 187 34 34 PRO HG3 H 1.991 0.005 . 188 34 34 PRO HD2 H 3.807 0.002 . 189 34 34 PRO HD3 H 3.652 0.002 . 190 35 35 THR H H 7.823 0.003 . 191 35 35 THR HA H 4.232 0.003 . 192 35 35 THR HB H 4.123 0.002 . 193 35 35 THR HG2 H 1.189 0.001 . stop_ save_