data_4483 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Local interactions drive the formation of non-native structure in the denatured state of human alpha-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution ; _BMRB_accession_number 4483 _BMRB_flat_file_name bmr4483.str _Entry_type original _Submission_date 1999-02-27 _Accession_date 1999-12-06 _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 Demarest S. J. . 2 Hua Y. . . 3 Raleigh D. P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-04-15 update BMRB 'updating non-standard residue' 2008-07-10 update BMRB 'updating non-standard residue' 2008-03-24 update BMRB . 2000-06-29 original author . stop_ _Original_release_date 2015-04-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99282203 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Demarest S. J. . 2 Hua Y. . . 3 Raleigh D. P. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7380 _Page_last 7387 _Year 1999 _Details . loop_ _Keyword alpha-lactalbumin 'molten globule state' 'non-native interactions' 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_system_LCA _Saveframe_category molecular_system _Mol_system_name LCA _Abbreviation_common LCA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LCA $LCA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LCA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LCA _Name_variant C111A _Abbreviation_common LCA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 13 _Mol_residue_sequence ; XIDYWLAHKALAX ; loop_ _Residue_seq_code _Residue_label 1 ACE 2 ILE 3 ASP 4 TYR 5 TRP 6 LEU 7 ALA 8 HIS 9 LYS 10 ALA 11 LEU 12 ALA 13 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _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 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 12:20:53 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 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 N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LCA human 9606 Eukaryota Metazoa Homo sapiens 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 $LCA '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 $LCA . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_E.COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name E.COSY _Sample_label $sample_1 save_ save_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $sample_1 save_ save_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.8 . n/a pressure 1 . atm temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 na H 1 na 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label DQF-COSY E.COSY ROESY TOCSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name LCA _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 ACE H1 H 2.05 0.01 2 2 . 1 ACE H2 H 2.05 0.01 2 3 . 1 ACE H3 H 2.05 0.01 2 4 . 2 ILE H H 8.24 0.01 1 5 . 2 ILE HA H 4.04 0.01 1 6 . 2 ILE HB H 1.74 0.01 1 7 . 2 ILE HG12 H 1.17 0.01 1 8 . 2 ILE HG13 H 1.42 0.01 1 9 . 2 ILE HG2 H 0.77 0.01 1 10 . 2 ILE HD1 H 0.85 0.01 1 11 . 3 ASP H H 8.53 0.01 1 12 . 3 ASP HA H 4.52 0.01 1 13 . 3 ASP HB2 H 2.58 0.01 1 14 . 3 ASP HB3 H 2.68 0.01 1 15 . 4 TYR H H 8.18 0.01 1 16 . 4 TYR HA H 4.24 0.01 1 17 . 4 TYR HB2 H 2.83 0.01 1 18 . 4 TYR HB3 H 2.95 0.01 1 19 . 4 TYR HD1 H 6.83 0.01 1 20 . 4 TYR HD2 H 6.83 0.01 1 21 . 4 TYR HE1 H 6.60 0.01 1 22 . 4 TYR HE2 H 6.60 0.01 1 23 . 5 TRP H H 7.89 0.01 1 24 . 5 TRP HA H 4.53 0.01 1 25 . 5 TRP HB2 H 3.30 0.01 1 26 . 5 TRP HB3 H 3.56 0.01 1 27 . 5 TRP HD1 H 7.26 0.01 1 28 . 5 TRP HE1 H 10.30 0.01 1 29 . 5 TRP HE3 H 7.48 0.01 1 30 . 5 TRP HZ2 H 7.47 0.01 1 31 . 5 TRP HZ3 H 7.15 0.01 1 32 . 5 TRP HH2 H 7.24 0.01 1 33 . 6 LEU H H 7.65 0.01 1 34 . 6 LEU HA H 4.13 0.01 1 35 . 6 LEU HB2 H 1.51 0.01 1 36 . 6 LEU HB3 H 1.56 0.01 1 37 . 6 LEU HG H 1.45 0.01 1 38 . 6 LEU HD1 H 0.86 0.01 2 39 . 6 LEU HD2 H 0.91 0.01 2 40 . 7 ALA H H 7.84 0.01 1 41 . 7 ALA HA H 4.13 0.01 1 42 . 7 ALA HB H 1.27 0.01 1 43 . 8 HIS H H 8.11 0.01 1 44 . 8 HIS HA H 4.56 0.01 1 45 . 8 HIS HB2 H 2.94 0.01 1 46 . 8 HIS HB3 H 3.22 0.01 1 47 . 8 HIS HD2 H 7.13 0.01 1 48 . 8 HIS HE1 H 8.50 0.01 1 49 . 9 LYS H H 8.20 0.01 1 50 . 9 LYS HA H 4.20 0.01 1 51 . 9 LYS HB2 H 1.70 0.01 1 52 . 9 LYS HB3 H 1.74 0.01 1 53 . 9 LYS HG2 H 1.35 0.01 1 54 . 9 LYS HG3 H 1.35 0.01 1 55 . 9 LYS HD2 H 1.60 0.01 1 56 . 9 LYS HD3 H 1.60 0.01 1 57 . 9 LYS HE2 H 2.94 0.01 1 58 . 9 LYS HE3 H 2.94 0.01 1 59 . 9 LYS HZ H 7.58 0.01 2 60 . 10 ALA H H 8.39 0.01 1 61 . 10 ALA HA H 4.27 0.01 1 62 . 10 ALA HB H 1.38 0.01 1 63 . 11 LEU H H 8.26 0.01 1 64 . 11 LEU HA H 4.31 0.01 1 65 . 11 LEU HB2 H 1.56 0.01 1 66 . 11 LEU HB3 H 1.66 0.01 1 67 . 11 LEU HG H 1.60 0.01 1 68 . 11 LEU HD1 H 0.88 0.01 2 69 . 11 LEU HD2 H 0.93 0.01 2 70 . 12 ALA H H 8.27 0.01 1 71 . 12 ALA HA H 4.25 0.01 1 72 . 12 ALA HB H 1.39 0.01 1 73 . 13 NH2 HN1 H 7.10 0.01 1 74 . 13 NH2 HN2 H 7.54 0.01 1 stop_ save_