data_3435 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton NMR Conformational Study of an Annexin I Fragment: Influence of a Phospholipidic Micellar Environment ; _BMRB_accession_number 3435 _BMRB_flat_file_name bmr3435.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Macquaire Francois . . 2 Baleux Francoise . . 3 Huynh-Dinh Tam . . 4 Rouge Dominique . . 5 Neumann Jean-Michel . . 6 Sanson Alain . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 2008-03-24 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Macquaire, Francois, Baleux, Francoise, Huynh-Dinh, Tam, Rouge, Dominique, Neumann, Jean-Michel, Sanson, Alain, "Proton NMR Conformational Study of an Annexin I Fragment: Influence of a Phospholipidic Micellar Environment," Biochem. J. 32 (28), 7244-7254 (1993). ; _Citation_title ; Proton NMR Conformational Study of an Annexin I Fragment: Influence of a Phospholipidic Micellar Environment ; _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 Macquaire Francois . . 2 Baleux Francoise . . 3 Huynh-Dinh Tam . . 4 Rouge Dominique . . 5 Neumann Jean-Michel . . 6 Sanson Alain . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 32 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7244 _Page_last 7254 _Year 1993 _Details . save_ ################################## # Molecular system description # ################################## save_system_annexin_I _Saveframe_category molecular_system _Mol_system_name 'annexin I' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'annexin I' $annexin_I stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_annexin_I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'annexin I' _Name_variant 'residues 1-32' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; XQWDADELRAAMKGLGTDED TLIEILASRTNK ; loop_ _Residue_seq_code _Residue_label 1 AYA 2 GLN 3 TRP 4 ASP 5 ALA 6 ASP 7 GLU 8 LEU 9 ARG 10 ALA 11 ALA 12 MET 13 LYS 14 GLY 15 LEU 16 GLY 17 THR 18 ASP 19 GLU 20 ASP 21 THR 22 LEU 23 ILE 24 GLU 25 ILE 26 LEU 27 ALA 28 SER 29 ARG 30 THR 31 ASN 32 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 3436 "annexin I" 96.88 32 100.00 100.00 6.44e-12 BMRB 3437 "annexin I" 96.88 32 100.00 100.00 6.44e-12 DBJ BAG59381 "unnamed protein product [Homo sapiens]" 59.38 172 100.00 100.00 1.41e-02 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_AYA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-ACETYLALANINE _BMRB_code AYA _PDB_code AYA _Standard_residue_derivative . _Molecular_mass 131.130 _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 . ? CM CM C . 0 . ? CT CT C . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HM1 HM1 H . 0 . ? HM2 HM2 H . 0 . ? HM3 HM3 H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? O O O . 0 . ? OT OT O . 0 . ? OXT OXT O . 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 CT ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB CT OT ? ? SING CT CM ? ? SING CM HM1 ? ? SING CM HM2 ? ? SING CM HM3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $annexin_I . . . . . . 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 $annexin_I '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 . _Model . _Field_strength . _Details . 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 6.4 . na temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details 'The chemical shift reference is not available at this time.' 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 . H 1 . ppm . . . . . . 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 'annexin I' _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 AYA H H 8.3 . 1 2 . 1 AYA HA H 4.22 . 1 3 . 1 AYA HB1 H 1.27 . 1 4 . 1 AYA HB2 H 1.27 . 1 5 . 1 AYA HB3 H 1.27 . 1 6 . 2 GLN H H 8.29 . 1 7 . 2 GLN HA H 4.29 . 1 8 . 2 GLN HB2 H 1.96 . 2 9 . 2 GLN HB3 H 1.86 . 2 10 . 2 GLN HG2 H 2.24 . 2 11 . 2 GLN HG3 H 2.17 . 2 12 . 2 GLN HE21 H 7.53 . 2 13 . 2 GLN HE22 H 6.86 . 2 14 . 3 TRP H H 8.14 . 1 15 . 3 TRP HA H 4.74 . 1 16 . 3 TRP HB2 H 3.32 . 2 17 . 3 TRP HB3 H 3.21 . 2 18 . 3 TRP HD1 H 7.27 . 1 19 . 3 TRP HE1 H 10.18 . 1 20 . 3 TRP HE3 H 7.61 . 1 21 . 3 TRP HZ2 H 7.48 . 1 22 . 3 TRP HZ3 H 7.12 . 1 23 . 3 TRP HH2 H 7.22 . 1 24 . 4 ASP H H 8.39 . 1 25 . 4 ASP HA H 4.61 . 1 26 . 4 ASP HB2 H 2.68 . 2 27 . 4 ASP HB3 H 2.64 . 2 28 . 5 ALA H H 8.35 . 1 29 . 5 ALA HA H 4.1 . 1 30 . 5 ALA HB H 1.46 . 1 31 . 6 ASP H H 8.36 . 1 32 . 6 ASP HA H 4.51 . 1 33 . 6 ASP HB2 H 2.76 . 2 34 . 6 ASP HB3 H 2.73 . 2 35 . 7 GLU H H 8.45 . 1 36 . 7 GLU HA H 4.12 . 1 37 . 7 GLU HB2 H 2.11 . 1 38 . 7 GLU HB3 H 2.11 . 1 39 . 7 GLU HG2 H 2.37 . 2 40 . 7 GLU HG3 H 2.26 . 2 41 . 8 LEU H H 8.18 . 1 42 . 8 LEU HA H 4.16 . 1 43 . 8 LEU HB2 H 1.73 . 2 44 . 8 LEU HB3 H 1.64 . 2 45 . 8 LEU HD1 H .83 . 1 46 . 8 LEU HD2 H .83 . 1 47 . 9 ARG H H 8.08 . 1 48 . 9 ARG HA H 4.08 . 1 49 . 9 ARG HB2 H 1.9 . 1 50 . 9 ARG HB3 H 1.9 . 1 51 . 9 ARG HG2 H 1.74 . 2 52 . 9 ARG HG3 H 1.62 . 2 53 . 9 ARG HD2 H 3.23 . 1 54 . 9 ARG HD3 H 3.23 . 1 55 . 10 ALA H H 8.04 . 1 56 . 10 ALA HA H 4.19 . 1 57 . 10 ALA HB H 1.48 . 1 58 . 11 ALA H H 8 . 1 59 . 11 ALA HA H 4.25 . 1 60 . 11 ALA HB H 1.46 . 1 61 . 12 MET H H 8.06 . 1 62 . 12 MET HA H 4.35 . 1 63 . 12 MET HB2 H 2.16 . 2 64 . 12 MET HB3 H 2.1 . 2 65 . 12 MET HG2 H 2.68 . 2 66 . 12 MET HG3 H 2.55 . 2 67 . 13 LYS H H 8.05 . 1 68 . 13 LYS HA H 4.28 . 1 69 . 13 LYS HB2 H 1.88 . 1 70 . 13 LYS HB3 H 1.88 . 1 71 . 13 LYS HG2 H 1.55 . 2 72 . 13 LYS HG3 H 1.49 . 2 73 . 13 LYS HD2 H 1.71 . 1 74 . 13 LYS HD3 H 1.71 . 1 75 . 13 LYS HE2 H 3.02 . 1 76 . 13 LYS HE3 H 3.02 . 1 77 . 14 GLY H H 8.44 . 1 78 . 14 GLY HA2 H 3.99 . 1 79 . 14 GLY HA3 H 3.99 . 1 80 . 15 LEU H H 8.1 . 1 81 . 15 LEU HA H 4.42 . 1 82 . 15 LEU HB2 H 1.77 . 2 83 . 15 LEU HB3 H 1.68 . 2 84 . 15 LEU HG H 1.65 . 1 85 . 15 LEU HD1 H .94 . 2 86 . 15 LEU HD2 H .9 . 2 87 . 16 GLY H H 8.5 . 1 88 . 16 GLY HA2 H 4.05 . 1 89 . 16 GLY HA3 H 4.05 . 1 90 . 17 THR H H 8.1 . 1 91 . 17 THR HA H 4.45 . 1 92 . 17 THR HB H 4.26 . 1 93 . 17 THR HG2 H 1.21 . 1 94 . 18 ASP H H 8.52 . 1 95 . 18 ASP HA H 4.65 . 1 96 . 18 ASP HB2 H 2.79 . 2 97 . 18 ASP HB3 H 2.75 . 2 98 . 19 GLU H H 8.57 . 1 99 . 19 GLU HA H 4.17 . 1 100 . 19 GLU HB2 H 2.1 . 2 101 . 19 GLU HB3 H 2 . 2 102 . 19 GLU HG2 H 2.3 . 1 103 . 19 GLU HG3 H 2.3 . 1 104 . 20 ASP H H 8.39 . 1 105 . 20 ASP HA H 4.57 . 1 106 . 20 ASP HB2 H 2.74 . 2 107 . 20 ASP HB3 H 2.71 . 2 108 . 21 THR H H 8.09 . 1 109 . 21 THR HA H 4.18 . 1 110 . 21 THR HB H 4.14 . 1 111 . 21 THR HG2 H 1.26 . 1 112 . 22 LEU H H 8.1 . 1 113 . 22 LEU HA H 4.22 . 1 114 . 22 LEU HB2 H 1.67 . 1 115 . 22 LEU HB3 H 1.67 . 1 116 . 22 LEU HD1 H .92 . 2 117 . 22 LEU HD2 H .88 . 2 118 . 23 ILE H H 8.06 . 1 119 . 23 ILE HA H 4.89 . 1 120 . 23 ILE HB H 1.94 . 1 121 . 23 ILE HG12 H 1.91 . 2 122 . 23 ILE HG13 H 1.25 . 2 123 . 23 ILE HG2 H .95 . 1 124 . 23 ILE HD1 H .9 . 1 125 . 24 GLU H H 8.12 . 1 126 . 24 GLU HA H 4.21 . 1 127 . 24 GLU HB2 H 2.08 . 1 128 . 24 GLU HB3 H 2.08 . 1 129 . 24 GLU HG2 H 2.33 . 2 130 . 24 GLU HG3 H 2.25 . 2 131 . 25 ILE H H 8.19 . 1 132 . 25 ILE HA H 3.97 . 1 133 . 25 ILE HB H 1.95 . 1 134 . 25 ILE HG12 H 1.65 . 2 135 . 25 ILE HG13 H 1.2 . 2 136 . 25 ILE HG2 H .9 . 1 137 . 25 ILE HD1 H .86 . 1 138 . 26 LEU H H 8.33 . 1 139 . 26 LEU HA H 4.2 . 1 140 . 26 LEU HB2 H 1.74 . 1 141 . 26 LEU HB3 H 1.74 . 1 142 . 26 LEU HG H 1.54 . 1 143 . 26 LEU HD1 H .84 . 1 144 . 26 LEU HD2 H .84 . 1 145 . 27 ALA H H 8.26 . 1 146 . 27 ALA HA H 4.29 . 1 147 . 27 ALA HB H 1.49 . 1 148 . 28 SER H H 8.05 . 1 149 . 28 SER HA H 4.44 . 1 150 . 28 SER HB2 H 2.99 . 1 151 . 28 SER HB3 H 2.99 . 1 152 . 29 ARG H H 8.08 . 1 153 . 29 ARG HA H 4.46 . 1 154 . 29 ARG HB2 H 1.99 . 2 155 . 29 ARG HB3 H 1.86 . 2 156 . 29 ARG HG2 H 1.75 . 2 157 . 29 ARG HG3 H 1.71 . 2 158 . 29 ARG HD2 H 3.2 . 1 159 . 29 ARG HD3 H 3.2 . 1 160 . 30 THR H H 8.14 . 1 161 . 30 THR HA H 4.27 . 1 162 . 30 THR HB H 4.38 . 1 163 . 30 THR HG2 H 1.26 . 1 164 . 31 ASN H H 8.46 . 1 165 . 31 ASN HA H 4.8 . 1 166 . 31 ASN HB2 H 2.89 . 2 167 . 31 ASN HB3 H 2.81 . 2 168 . 32 LYS H H 7.99 . 1 169 . 32 LYS HA H 4.18 . 1 170 . 32 LYS HB2 H 1.85 . 1 171 . 32 LYS HB3 H 1.85 . 1 172 . 32 LYS HG2 H 1.42 . 1 173 . 32 LYS HG3 H 1.42 . 1 174 . 32 LYS HD2 H 1.71 . 1 175 . 32 LYS HD3 H 1.71 . 1 176 . 32 LYS HE2 H 3.03 . 1 177 . 32 LYS HE3 H 3.03 . 1 stop_ save_