data_4261 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by NMR Spectroscopy ; _BMRB_accession_number 4261 _BMRB_flat_file_name bmr4261.str _Entry_type original _Submission_date 1998-10-29 _Accession_date 1998-10-29 _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 Hashimoto Yasuhiro . . 2 Toma Kazunori . . 3 Nishikido Joji . . 4 Yamamoto Keizo . . 5 Haneda Katuji . . 6 Inazu Toshiyuki . . 7 Valentine Kathleen . . 8 Opella Stanley J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 171 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-03 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4219 . 4260 . stop_ _Original_release_date 1999-12-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by NMR Spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99315214 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hashimoto Yasuhiro . . 2 Toma Kazunori . . 3 Nishikido Joji . . 4 Yamamoto Keizo . . 5 Haneda Katuji . . 6 Inazu Toshiyuki . . 7 Valentine Kathleen G. . 8 Opella Stanley J. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8377 _Page_last 8384 _Year 1999 _Details . loop_ _Keyword Calcium-regulator Hormone osteoporosis stop_ save_ ################################## # Molecular system description # ################################## save_system_CT _Saveframe_category molecular_system _Mol_system_name 'M6 eel calcitonin' _Abbreviation_common CT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'M6 eel calcitonin' $CT N-acetyl-D-glucosamine $entity_NAG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully oxidized' loop_ _Biological_function 'calcium-regulating hormone' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'M6 eel calcitonin' _Abbreviation_common CT _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details 'Asn3 is glycosylated' ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; CSNLSTCVLGKLSQELHKLQ TYPRTDVGAGTP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 CYS 2 2 SER 3 3 ASN 4 4 LEU 5 5 SER 6 6 THR 7 7 CYS 8 8 VAL 9 9 LEU 10 10 GLY 11 11 LYS 12 12 LEU 13 13 SER 14 14 GLN 15 15 GLU 16 16 LEU 17 17 HIS 18 18 LYS 19 19 LEU 20 20 GLN 21 21 THR 22 22 TYR 23 23 PRO 24 24 ARG 25 25 THR 26 26 ASP 27 27 VAL 28 28 GLY 29 29 ALA 30 30 GLY 31 31 THR 32 32 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 4219 "eel calcitonin" 100.00 32 100.00 100.00 1.44e-13 BMRB 4260 "GlcNAc eel calcitonin" 96.88 32 100.00 100.00 1.39e-12 PDB 1BKU "Effects Of Glycosylation On The Structure And Dynamics Of Eel Calcitonin, Nmr, 10 Structures" 100.00 33 100.00 100.00 1.45e-13 PDB 1BYV "Glycosylated Eel Calcitonin" 100.00 33 100.00 100.00 1.45e-13 PDB 1BZB "Glycosylated Eel Calcitonin" 100.00 33 100.00 100.00 1.45e-13 PRF 760596A calcitonin 100.00 32 100.00 100.00 1.44e-13 SP P01262 "RecName: Full=Calcitonin" 100.00 32 100.00 100.00 1.44e-13 stop_ save_ ############# # Ligands # ############# save_NAG _Saveframe_category ligand _Mol_type "non-polymer (D-SACCHARIDE)" _Name_common N-ACETYL-D-GLUCOSAMINE _BMRB_code NAG _PDB_code NAG _Molecular_mass 221.208 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? N2 N2 N . 0 . ? O1 O1 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? O7 O7 O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H83 H83 H . 0 . ? HN2 HN2 H . 0 . ? HO1 HO1 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 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 C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 N2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 N2 ? ? DOUB C7 O7 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C8 H83 ? ? SING N2 HN2 ? ? SING O1 HO1 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? stop_ _Mol_thiol_state 'not present' _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CT eel 7935 Eukaryota Metazoa Anguilla . 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 $CT 'chemically synthesized' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type micelles _Details ; Sodium dodecyl sulfate-d25 was used as micelles ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CT 1 mM . stop_ save_ ############################ # Computer software used # ############################ save_felix _Saveframe_category software _Name felix _Version 94 loop_ _Task assignment 'peak integration' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample save_ save_2D_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 4.5 0.2 n/a temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'M6 eel calcitonin' _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 CYS HA H 4.41 . 1 2 . 1 CYS HB2 H 3.65 . 1 3 . 1 CYS HB3 H 3.65 . 1 4 . 2 SER H H 8.52 . 1 5 . 2 SER HA H 4.56 . 1 6 . 2 SER HB2 H 3.94 . 2 7 . 2 SER HB3 H 3.82 . 2 8 . 3 ASN H H 7.77 . 1 9 . 3 ASN HA H 4.56 . 1 10 . 3 ASN HB2 H 3.19 . 1 11 . 3 ASN HB3 H 3.19 . 1 12 . 4 LEU H H 8.61 . 1 13 . 4 LEU HA H 4.04 . 1 14 . 4 LEU HB2 H 1.77 . 2 15 . 4 LEU HB3 H 1.73 . 2 16 . 4 LEU HG H 1.66 . 1 17 . 4 LEU HD1 H 0.93 . 1 18 . 4 LEU HD2 H 0.93 . 1 19 . 5 SER H H 8.46 . 1 20 . 5 SER HA H 3.94 . 1 21 . 5 SER HB2 H 4.08 . 1 22 . 5 SER HB3 H 4.08 . 1 23 . 6 THR H H 7.89 . 1 24 . 6 THR HA H 4.24 . 1 25 . 6 THR HB H 4.27 . 1 26 . 6 THR HG2 H 1.35 . 1 27 . 7 CYS H H 8.61 . 1 28 . 7 CYS HA H 4.70 . 1 29 . 7 CYS HB2 H 3.21 . 1 30 . 7 CYS HB3 H 3.21 . 1 31 . 8 VAL H H 8.55 . 1 32 . 8 VAL HA H 3.77 . 1 33 . 8 VAL HB H 2.21 . 1 34 . 8 VAL HG1 H 1.06 . 2 35 . 8 VAL HG2 H 0.93 . 2 36 . 9 LEU H H 8.27 . 1 37 . 9 LEU HA H 4.05 . 1 38 . 9 LEU HB2 H 1.92 . 2 39 . 9 LEU HB3 H 1.85 . 2 40 . 9 LEU HG H 1.63 . 1 41 . 9 LEU HD1 H 0.93 . 1 42 . 9 LEU HD2 H 0.93 . 1 43 . 10 GLY H H 8.14 . 1 44 . 10 GLY HA2 H 4.04 . 2 45 . 10 GLY HA3 H 3.91 . 2 46 . 11 LYS H H 7.65 . 1 47 . 11 LYS HA H 4.26 . 1 48 . 11 LYS HB2 H 2.03 . 2 49 . 11 LYS HB3 H 1.92 . 2 50 . 11 LYS HG2 H 1.57 . 2 51 . 11 LYS HG3 H 1.52 . 2 52 . 11 LYS HD2 H 1.77 . 1 53 . 11 LYS HD3 H 1.77 . 1 54 . 11 LYS HE2 H 2.99 . 1 55 . 11 LYS HE3 H 2.99 . 1 56 . 11 LYS HZ H 7.45 . 1 57 . 12 LEU H H 8.33 . 1 58 . 12 LEU HA H 4.03 . 1 59 . 12 LEU HB2 H 1.89 . 2 60 . 12 LEU HB3 H 1.85 . 2 61 . 12 LEU HG H 1.62 . 1 62 . 12 LEU HD1 H 0.88 . 1 63 . 12 LEU HD2 H 0.88 . 1 64 . 13 SER H H 8.49 . 1 65 . 13 SER HA H 4.03 . 1 66 . 13 SER HB2 H 4.03 . 1 67 . 13 SER HB3 H 4.03 . 1 68 . 14 GLN H H 7.85 . 1 69 . 14 GLN HA H 4.13 . 1 70 . 14 GLN HB2 H 2.33 . 2 71 . 14 GLN HB3 H 2.26 . 2 72 . 14 GLN HG2 H 2.58 . 2 73 . 14 GLN HG3 H 2.43 . 2 74 . 15 GLU H H 8.07 . 1 75 . 15 GLU HA H 4.33 . 1 76 . 15 GLU HB2 H 2.20 . 2 77 . 15 GLU HB3 H 2.13 . 2 78 . 15 GLU HG2 H 2.65 . 2 79 . 15 GLU HG3 H 2.35 . 2 80 . 16 LEU H H 8.46 . 1 81 . 16 LEU HA H 4.03 . 1 82 . 16 LEU HB2 H 1.71 . 1 83 . 16 LEU HB3 H 1.71 . 1 84 . 16 LEU HG H 1.67 . 1 85 . 16 LEU HD1 H 0.88 . 1 86 . 16 LEU HD2 H 0.88 . 1 87 . 17 HIS H H 8.01 . 1 88 . 17 HIS HA H 4.55 . 1 89 . 17 HIS HB2 H 3.37 . 2 90 . 17 HIS HB3 H 3.30 . 2 91 . 17 HIS HD1 H 8.56 . 2 92 . 17 HIS HE1 H 7.33 . 2 93 . 18 LYS H H 7.85 . 1 94 . 18 LYS HA H 4.12 . 1 95 . 18 LYS HB2 H 2.02 . 1 96 . 18 LYS HB3 H 2.02 . 1 97 . 18 LYS HG2 H 1.43 . 1 98 . 18 LYS HG3 H 1.43 . 1 99 . 18 LYS HD2 H 1.76 . 2 100 . 18 LYS HD3 H 1.67 . 2 101 . 18 LYS HE2 H 2.99 . 1 102 . 18 LYS HE3 H 2.99 . 1 103 . 18 LYS HZ H 7.36 . 1 104 . 19 LEU H H 7.91 . 1 105 . 19 LEU HA H 4.16 . 1 106 . 19 LEU HB2 H 1.91 . 1 107 . 19 LEU HB3 H 1.91 . 1 108 . 19 LEU HG H 1.67 . 1 109 . 19 LEU HD1 H 0.94 . 2 110 . 19 LEU HD2 H 0.88 . 2 111 . 20 GLN H H 8.94 . 1 112 . 20 GLN HA H 4.17 . 1 113 . 20 GLN HB2 H 2.17 . 1 114 . 20 GLN HB3 H 2.17 . 1 115 . 20 GLN HG2 H 2.53 . 2 116 . 20 GLN HG3 H 2.42 . 2 117 . 21 THR H H 7.55 . 1 118 . 21 THR HA H 4.25 . 1 119 . 21 THR HB H 4.18 . 1 120 . 21 THR HG2 H 1.11 . 1 121 . 22 TYR H H 7.65 . 1 122 . 22 TYR HA H 4.76 . 1 123 . 22 TYR HB2 H 3.09 . 2 124 . 22 TYR HB3 H 3.05 . 2 125 . 22 TYR HD1 H 7.14 . 1 126 . 22 TYR HD2 H 7.14 . 1 127 . 22 TYR HE1 H 6.77 . 1 128 . 22 TYR HE2 H 6.77 . 1 129 . 23 PRO HA H 4.43 . 1 130 . 23 PRO HB2 H 2.20 . 1 131 . 23 PRO HB3 H 2.20 . 1 132 . 23 PRO HG2 H 1.98 . 2 133 . 23 PRO HG3 H 1.94 . 2 134 . 23 PRO HD2 H 3.78 . 2 135 . 23 PRO HD3 H 3.40 . 2 136 . 24 ARG H H 8.10 . 1 137 . 24 ARG HA H 4.35 . 1 138 . 24 ARG HB2 H 1.95 . 2 139 . 24 ARG HB3 H 1.85 . 2 140 . 24 ARG HG2 H 1.74 . 2 141 . 24 ARG HG3 H 1.70 . 2 142 . 24 ARG HD2 H 3.23 . 1 143 . 24 ARG HD3 H 3.23 . 1 144 . 24 ARG HE H 7.20 . 2 145 . 25 THR H H 7.88 . 1 146 . 25 THR HA H 4.31 . 1 147 . 25 THR HB H 4.27 . 1 148 . 25 THR HG2 H 1.19 . 1 149 . 26 ASP H H 8.23 . 1 150 . 26 ASP HA H 4.78 . 1 151 . 26 ASP HB2 H 2.99 . 2 152 . 26 ASP HB3 H 2.86 . 2 153 . 27 VAL H H 7.87 . 1 154 . 27 VAL HA H 4.07 . 1 155 . 27 VAL HB H 2.14 . 1 156 . 27 VAL HG1 H 0.95 . 1 157 . 27 VAL HG2 H 0.95 . 1 158 . 28 GLY H H 8.30 . 1 159 . 28 GLY HA2 H 3.99 . 2 160 . 28 GLY HA3 H 3.92 . 2 161 . 29 ALA H H 7.97 . 1 162 . 29 ALA HA H 4.32 . 1 163 . 29 ALA HB H 1.39 . 1 164 . 30 GLY H H 8.23 . 1 165 . 30 GLY HA2 H 3.97 . 1 166 . 30 GLY HA3 H 3.97 . 1 167 . 31 THR H H 7.92 . 1 168 . 32 PRO HG2 H 1.97 . 1 169 . 32 PRO HG3 H 1.97 . 1 170 . 32 PRO HD2 H 3.81 . 2 171 . 32 PRO HD3 H 3.75 . 2 stop_ save_