data_2395 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy ; _BMRB_accession_number 2395 _BMRB_flat_file_name bmr2395.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Gooley Paul R. . 2 MacKenzie Neil E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 207 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Gooley, Paul R., MacKenzie, Neil E., "Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy," Biochemistry 27 (11), 4032-4040 (1988). ; _Citation_title ; Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gooley Paul R. . 2 MacKenzie Neil E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 27 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4032 _Page_last 4040 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_somatotropin _Saveframe_category molecular_system _Mol_system_name somatotropin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label somatotropin $somatotropin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_somatotropin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common somatotropin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXVFTNS LVFGTSDRVYEKLKDLEEGI LALMRELEDGTPR ; loop_ _Residue_seq_code _Residue_label 1 X 2 X 3 X 4 X 5 X 6 X 7 X 8 X 9 X 10 X 11 X 12 X 13 X 14 X 15 X 16 X 17 X 18 X 19 X 20 X 21 X 22 X 23 X 24 X 25 X 26 X 27 X 28 X 29 X 30 X 31 X 32 X 33 X 34 X 35 X 36 X 37 X 38 X 39 X 40 X 41 X 42 X 43 X 44 X 45 X 46 X 47 X 48 X 49 X 50 X 51 X 52 X 53 X 54 X 55 X 56 X 57 X 58 X 59 X 60 X 61 X 62 X 63 X 64 X 65 X 66 X 67 X 68 X 69 X 70 X 71 X 72 X 73 X 74 X 75 X 76 X 77 X 78 X 79 X 80 X 81 X 82 X 83 X 84 X 85 X 86 X 87 X 88 X 89 X 90 X 91 X 92 X 93 X 94 X 95 X 96 VAL 97 PHE 98 THR 99 ASN 100 SER 101 LEU 102 VAL 103 PHE 104 GLY 105 THR 106 SER 107 ASP 108 ARG 109 VAL 110 TYR 111 GLU 112 LYS 113 LEU 114 LYS 115 ASP 116 LEU 117 GLU 118 GLU 119 GLY 120 ILE 121 LEU 122 ALA 123 LEU 124 MET 125 ARG 126 GLU 127 LEU 128 GLU 129 ASP 130 GLY 131 THR 132 PRO 133 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2008-08-19 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $somatotropin . . . . . . 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 $somatotropin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.6 . na temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 TSP H . . ppm 0 . . . . . 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name somatotropin _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 . 96 VAL HA H 3.81 . 1 2 . 96 VAL HB H 2.21 . 1 3 . 96 VAL HG1 H 1.02 . 2 4 . 96 VAL HG2 H .99 . 2 5 . 97 PHE H H 8.53 . 1 6 . 97 PHE HA H 4.79 . 1 7 . 97 PHE HB2 H 3.19 . 2 8 . 97 PHE HB3 H 3.11 . 2 9 . 98 THR H H 7.86 . 1 10 . 98 THR HA H 4.27 . 1 11 . 98 THR HB H 4.2 . 1 12 . 98 THR HG2 H 1.15 . 1 13 . 99 ASN H H 8.08 . 1 14 . 99 ASN HA H 4.65 . 1 15 . 99 ASN HB2 H 2.86 . 2 16 . 99 ASN HB3 H 2.78 . 2 17 . 99 ASN HD21 H 7.44 . 2 18 . 99 ASN HD22 H 6.68 . 2 19 . 100 SER H H 8.12 . 1 20 . 100 SER HA H 4.37 . 1 21 . 100 SER HB2 H 3.95 . 2 22 . 100 SER HB3 H 3.89 . 2 23 . 101 LEU H H 7.98 . 1 24 . 101 LEU HA H 4.31 . 1 25 . 101 LEU HB2 H 1.71 . 2 26 . 101 LEU HB3 H 1.59 . 2 27 . 101 LEU HG H 1.64 . 1 28 . 101 LEU HD1 H .94 . 2 29 . 101 LEU HD2 H .88 . 2 30 . 102 VAL H H 7.62 . 1 31 . 102 VAL HA H 3.92 . 1 32 . 102 VAL HB H 1.96 . 1 33 . 102 VAL HG1 H .87 . 2 34 . 102 VAL HG2 H .76 . 2 35 . 103 PHE H H 7.86 . 1 36 . 103 PHE HA H 4.58 . 1 37 . 103 PHE HB2 H 3.22 . 2 38 . 103 PHE HB3 H 3.04 . 2 39 . 104 GLY H H 8.16 . 1 40 . 104 GLY HA2 H 4.01 . 1 41 . 104 GLY HA3 H 4.01 . 1 42 . 105 THR H H 7.94 . 1 43 . 105 THR HA H 4.28 . 1 44 . 105 THR HB H 4.32 . 1 45 . 105 THR HG2 H 1.26 . 1 46 . 106 SER H H 8.21 . 1 47 . 106 SER HA H 4.33 . 1 48 . 106 SER HB2 H 4.01 . 2 49 . 106 SER HB3 H 3.94 . 2 50 . 107 ASP H H 8.28 . 1 51 . 107 ASP HA H 4.61 . 1 52 . 107 ASP HB2 H 2.86 . 1 53 . 107 ASP HB3 H 2.86 . 1 54 . 108 ARG H H 7.96 . 1 55 . 108 ARG HA H 4.16 . 1 56 . 108 ARG HB2 H 1.95 . 1 57 . 108 ARG HB3 H 1.95 . 1 58 . 108 ARG HG2 H 1.82 . 2 59 . 108 ARG HG3 H 1.73 . 2 60 . 108 ARG HD2 H 3.25 . 1 61 . 108 ARG HD3 H 3.25 . 1 62 . 108 ARG HE H 7.22 . 1 63 . 109 VAL H H 7.83 . 1 64 . 109 VAL HA H 3.68 . 1 65 . 109 VAL HB H 2.12 . 1 66 . 109 VAL HG1 H 1.01 . 2 67 . 109 VAL HG2 H .89 . 2 68 . 110 TYR H H 7.89 . 1 69 . 110 TYR HA H 4.17 . 1 70 . 110 TYR HB2 H 3.13 . 1 71 . 110 TYR HB3 H 3.13 . 1 72 . 110 TYR HD1 H 6.82 . 1 73 . 110 TYR HD2 H 6.82 . 1 74 . 110 TYR HE1 H 7 . 1 75 . 110 TYR HE2 H 7 . 1 76 . 111 GLU H H 8.05 . 1 77 . 111 GLU HA H 3.92 . 1 78 . 111 GLU HB2 H 2.19 . 1 79 . 111 GLU HB3 H 2.19 . 1 80 . 111 GLU HG2 H 2.57 . 1 81 . 111 GLU HG3 H 2.57 . 1 82 . 112 LYS H H 7.73 . 1 83 . 112 LYS HA H 4.13 . 1 84 . 112 LYS HB2 H 2.06 . 2 85 . 112 LYS HB3 H 2.01 . 2 86 . 112 LYS HG2 H 1.65 . 2 87 . 112 LYS HG3 H 1.56 . 2 88 . 112 LYS HD2 H 1.76 . 1 89 . 112 LYS HD3 H 1.76 . 1 90 . 112 LYS HE2 H 2.99 . 1 91 . 112 LYS HE3 H 2.99 . 1 92 . 113 LEU H H 8.2 . 1 93 . 113 LEU HA H 4.1 . 1 94 . 113 LEU HB2 H 1.81 . 1 95 . 113 LEU HB3 H 1.81 . 1 96 . 113 LEU HD1 H .86 . 1 97 . 113 LEU HD2 H .86 . 1 98 . 114 LYS H H 8.22 . 1 99 . 114 LYS HA H 3.93 . 1 100 . 114 LYS HB2 H 1.82 . 2 101 . 114 LYS HB3 H 1.68 . 2 102 . 114 LYS HG2 H 1.4 . 1 103 . 114 LYS HG3 H 1.4 . 1 104 . 114 LYS HD2 H 1.7 . 1 105 . 114 LYS HD3 H 1.7 . 1 106 . 114 LYS HE2 H 2.96 . 1 107 . 114 LYS HE3 H 2.96 . 1 108 . 115 ASP H H 8.05 . 1 109 . 115 ASP HA H 4.44 . 1 110 . 115 ASP HB2 H 3.1 . 2 111 . 115 ASP HB3 H 2.85 . 2 112 . 116 LEU H H 8.16 . 1 113 . 116 LEU HA H 4.19 . 1 114 . 116 LEU HB2 H 1.84 . 1 115 . 116 LEU HB3 H 1.84 . 1 116 . 117 GLU H H 8.55 . 1 117 . 117 GLU HA H 4 . 1 118 . 117 GLU HB2 H 2.37 . 1 119 . 117 GLU HB3 H 2.37 . 1 120 . 117 GLU HG2 H 2.61 . 1 121 . 117 GLU HG3 H 2.61 . 1 122 . 118 GLU H H 8.43 . 1 123 . 118 GLU HA H 4.04 . 1 124 . 118 GLU HB2 H 2.29 . 2 125 . 118 GLU HB3 H 1.99 . 2 126 . 118 GLU HG2 H 2.73 . 2 127 . 118 GLU HG3 H 2.5 . 2 128 . 119 GLY H H 8.14 . 1 129 . 119 GLY HA2 H 3.89 . 2 130 . 119 GLY HA3 H 4.02 . 2 131 . 120 ILE H H 8.37 . 1 132 . 120 ILE HA H 3.8 . 1 133 . 120 ILE HB H 2.01 . 1 134 . 120 ILE HG12 H 1.75 . 2 135 . 120 ILE HG13 H 1.15 . 2 136 . 120 ILE HG2 H .95 . 1 137 . 120 ILE HD1 H .83 . 1 138 . 121 LEU H H 8.17 . 1 139 . 121 LEU HA H 4.1 . 1 140 . 121 LEU HB2 H 1.88 . 1 141 . 121 LEU HB3 H 1.88 . 1 142 . 122 ALA H H 7.98 . 1 143 . 122 ALA HA H 4.09 . 1 144 . 122 ALA HB H 1.57 . 1 145 . 123 LEU H H 7.93 . 1 146 . 123 LEU HA H 4.16 . 1 147 . 123 LEU HB2 H 1.84 . 1 148 . 123 LEU HB3 H 1.84 . 1 149 . 124 MET H H 8.64 . 1 150 . 124 MET HA H 4.07 . 1 151 . 124 MET HB2 H 2.28 . 2 152 . 124 MET HB3 H 2.09 . 2 153 . 124 MET HG2 H 2.77 . 2 154 . 124 MET HG3 H 2.47 . 2 155 . 124 MET HE H 1.97 . 1 156 . 125 ARG H H 8.14 . 1 157 . 125 ARG HA H 4.05 . 1 158 . 125 ARG HB2 H 2 . 1 159 . 125 ARG HB3 H 2 . 1 160 . 125 ARG HG2 H 1.85 . 2 161 . 125 ARG HG3 H 1.71 . 2 162 . 125 ARG HD2 H 3.23 . 1 163 . 125 ARG HD3 H 3.23 . 1 164 . 125 ARG HE H 7.19 . 1 165 . 126 GLU H H 7.96 . 1 166 . 126 GLU HA H 4.13 . 1 167 . 126 GLU HB2 H 2.35 . 2 168 . 126 GLU HB3 H 2.25 . 2 169 . 126 GLU HG2 H 2.6 . 2 170 . 126 GLU HG3 H 2.52 . 2 171 . 127 LEU H H 8.32 . 1 172 . 127 LEU HA H 4.17 . 1 173 . 127 LEU HB2 H 1.59 . 1 174 . 127 LEU HB3 H 1.59 . 1 175 . 128 GLU H H 8.13 . 1 176 . 128 GLU HA H 4.21 . 1 177 . 128 GLU HB2 H 2.18 . 1 178 . 128 GLU HB3 H 2.18 . 1 179 . 128 GLU HG2 H 2.63 . 2 180 . 128 GLU HG3 H 2.47 . 2 181 . 129 ASP H H 8.14 . 1 182 . 129 ASP HA H 4.77 . 1 183 . 129 ASP HB2 H 2.97 . 1 184 . 129 ASP HB3 H 2.97 . 1 185 . 130 GLY H H 8.04 . 1 186 . 130 GLY HA2 H 3.94 . 2 187 . 130 GLY HA3 H 4.11 . 2 188 . 131 THR H H 7.65 . 1 189 . 131 THR HA H 4.53 . 1 190 . 131 THR HB H 4.1 . 1 191 . 131 THR HG2 H 1.2 . 1 192 . 132 PRO HA H 4.46 . 1 193 . 132 PRO HB2 H 2.28 . 2 194 . 132 PRO HB3 H 1.98 . 2 195 . 132 PRO HG2 H 2.05 . 1 196 . 132 PRO HG3 H 2.05 . 1 197 . 132 PRO HD2 H 3.87 . 2 198 . 132 PRO HD3 H 3.71 . 2 199 . 133 ARG H H 7.92 . 1 200 . 133 ARG HA H 4.34 . 1 201 . 133 ARG HB2 H 1.94 . 2 202 . 133 ARG HB3 H 1.78 . 2 203 . 133 ARG HG2 H 1.68 . 1 204 . 133 ARG HG3 H 1.68 . 1 205 . 133 ARG HD2 H 3.24 . 1 206 . 133 ARG HD3 H 3.24 . 1 207 . 133 ARG HE H 7.14 . 1 stop_ save_