data_21075 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K724-D728) ; _BMRB_accession_number 21075 _BMRB_flat_file_name bmr21075.str _Entry_type original _Submission_date 2016-09-26 _Accession_date 2016-10-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Peptide contains a lactam bridge between the side-chains of K724 and D728' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wegener K. L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 21074 'Structure of the membrane proximal region of ITBG3 - residues 722-739' 21076 'NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K725-D729)' 21077 'NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K728-D732)' 21078 'NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K729-D733)' stop_ _Original_release_date 2016-10-12 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title ; The key position: influence of staple location on constrained peptide conformation and binding ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27722656 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Keeling K. L. . 2 Cho O. . . 3 Scanlon D. B. . 4 Booker G. W. . 5 Abell A. D. . 6 Wegener K. L. . stop_ _Journal_abbreviation 'Org. Biomol. Chem.' _Journal_name_full 'Organic and biomolecular chemistry' _Journal_volume . _Journal_issue . _Journal_ISSN 1477-0520 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name BLACA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BLACA $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 2356.640 _Mol_thiol_state 'not present' _Details 'Lactam bond between side-chains K724 and D728' ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence ; HDKKEFDKFEEERARAKW ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 722 HIS 2 723 ASP 3 724 LYS 4 725 LYS 5 726 GLU 6 727 PHE 7 728 ASP 8 729 LYS 9 730 PHE 10 731 GLU 11 732 GLU 12 733 GLU 13 734 ARG 14 735 ALA 15 736 ARG 16 737 ALA 17 738 LYS 18 739 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 $entity 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details '50mM potassium phosphate buffer pH6.1, 100mM NaCl,90% H2O, 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 5.5 mM 'natural abundance' DSS 100 uM 'natural abundance' 'potassium phosphate' 50 mM 'natural abundannce' NaCl 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address "Linge, O'Donoghue and Nilges" . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CCPNmr_Analysis _Saveframe_category software _Name CCPNmr_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample save_ save_High_resolution_1H_1D_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'High resolution 1H 1D' _Sample_label $sample save_ save_1H_1D_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ save_1H_1D_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ save_1H_1D_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ save_1H_1D_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ save_1H_1D_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ save_1H_1D_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 1D' _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '25 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details '15 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 288 . K stop_ save_ save_sample_conditions_3 _Saveframe_category sample_conditions _Details '20 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 293 . K stop_ save_ save_sample_conditions_4 _Saveframe_category sample_conditions _Details '30 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 303 . K stop_ save_ save_sample_conditions_5 _Saveframe_category sample_conditions _Details '35 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 308 . K stop_ save_ save_sample_conditions_6 _Saveframe_category sample_conditions _Details '40 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 313 . K stop_ save_ save_sample_conditions_7 _Saveframe_category sample_conditions _Details '45 degrees C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 318 . K 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 0.0 internal direct . . . 1.0 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CCPNmr_Analysis stop_ loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name BLACA _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 1 722 1 HIS HA H 4.182 0.01 1 2 722 1 HIS HB2 H 3.153 0.01 2 3 722 1 HIS HB3 H 3.099 0.01 2 4 723 2 ASP HA H 4.705 0.002 1 5 723 2 ASP HB2 H 2.786 0.004 2 6 723 2 ASP HB3 H 2.730 0.004 2 7 724 3 LYS H H 8.534 0.001 1 8 724 3 LYS HA H 4.161 0.002 1 9 724 3 LYS HB2 H 1.943 0.004 2 10 724 3 LYS HB3 H 1.811 0.002 2 11 724 3 LYS HD2 H 1.654 0.003 1 12 724 3 LYS HD3 H 1.654 0.003 1 13 724 3 LYS HE2 H 2.704 0.001 2 14 724 3 LYS HE3 H 3.707 0.002 2 15 724 3 LYS HG2 H 1.260 0.003 2 16 724 3 LYS HG3 H 1.499 0.003 2 17 724 3 LYS HZ H 8.157 0.004 1 18 725 4 LYS H H 8.241 0.002 1 19 725 4 LYS HA H 4.067 0.004 1 20 725 4 LYS HB2 H 1.872 0.004 2 21 725 4 LYS HB3 H 1.924 0.004 2 22 725 4 LYS HD2 H 1.733 0.01 1 23 725 4 LYS HD3 H 1.733 0.01 1 24 725 4 LYS HE2 H 3.025 0.001 1 25 725 4 LYS HE3 H 3.025 0.001 1 26 725 4 LYS HG2 H 1.539 0.003 2 27 725 4 LYS HG3 H 1.438 0.003 2 28 726 5 GLU H H 7.979 0.002 1 29 726 5 GLU HA H 4.059 0.005 1 30 726 5 GLU HB2 H 2.048 0.001 1 31 726 5 GLU HB3 H 2.048 0.001 1 32 726 5 GLU HG2 H 2.306 0.001 2 33 726 5 GLU HG3 H 2.234 0.003 2 34 727 6 PHE H H 8.418 0.004 1 35 727 6 PHE HA H 4.246 0.003 1 36 727 6 PHE HB2 H 3.055 0.003 1 37 727 6 PHE HB3 H 3.055 0.003 1 38 727 6 PHE HD1 H 7.224 0.004 1 39 727 6 PHE HD2 H 7.224 0.004 1 40 727 6 PHE HE1 H 7.338 0.01 1 41 727 6 PHE HE2 H 7.338 0.01 1 42 728 7 ASP H H 8.846 0.003 1 43 728 7 ASP HA H 4.568 0.004 1 44 728 7 ASP HB2 H 2.843 0.004 2 45 728 7 ASP HB3 H 2.745 0.002 2 46 729 8 LYS H H 7.713 0.002 1 47 729 8 LYS HA H 4.158 0.002 1 48 729 8 LYS HB2 H 1.855 0.004 1 49 729 8 LYS HB3 H 1.855 0.004 1 50 729 8 LYS HD2 H 1.652 0.004 1 51 729 8 LYS HD3 H 1.652 0.004 1 52 729 8 LYS HE2 H 2.916 0.01 1 53 729 8 LYS HE3 H 2.916 0.01 1 54 729 8 LYS HG2 H 1.449 0.001 2 55 729 8 LYS HG3 H 1.324 0.001 2 56 730 9 PHE H H 7.956 0.004 1 57 730 9 PHE HA H 4.432 0.002 1 58 730 9 PHE HB2 H 3.121 0.003 2 59 730 9 PHE HB3 H 3.187 0.003 2 60 730 9 PHE HD1 H 7.230 0.004 1 61 730 9 PHE HD2 H 7.230 0.004 1 62 730 9 PHE HE1 H 7.297 0.01 1 63 730 9 PHE HE2 H 7.297 0.01 1 64 731 10 GLU H H 8.236 0.003 1 65 731 10 GLU HA H 3.981 0.002 1 66 731 10 GLU HB2 H 1.974 0.004 1 67 731 10 GLU HB3 H 1.974 0.004 1 68 731 10 GLU HG2 H 2.119 0.004 2 69 731 10 GLU HG3 H 2.056 0.003 2 70 732 11 GLU H H 8.132 0.002 1 71 732 11 GLU HA H 4.077 0.002 1 72 732 11 GLU HB2 H 2.110 0.002 1 73 732 11 GLU HB3 H 2.109 0.002 1 74 732 11 GLU HG2 H 2.253 0.01 2 75 732 11 GLU HG3 H 2.375 0.002 2 76 733 12 GLU H H 8.120 0.005 1 77 733 12 GLU HA H 4.020 0.002 1 78 733 12 GLU HB2 H 2.041 0.002 2 79 733 12 GLU HB3 H 2.085 0.003 2 80 733 12 GLU HG2 H 2.254 0.001 2 81 733 12 GLU HG3 H 2.382 0.004 2 82 734 13 ARG H H 8.056 0.002 1 83 734 13 ARG HA H 4.004 0.004 1 84 734 13 ARG HB2 H 1.730 0.004 1 85 734 13 ARG HB3 H 1.730 0.004 1 86 734 13 ARG HD2 H 3.066 0.003 1 87 734 13 ARG HD3 H 3.066 0.003 1 88 734 13 ARG HE H 7.335 0.002 1 89 734 13 ARG HG2 H 1.567 0.001 2 90 734 13 ARG HG3 H 1.479 0.004 2 91 735 14 ALA H H 7.902 0.003 1 92 735 14 ALA HA H 4.151 0.003 1 93 735 14 ALA HB H 1.464 0.003 1 94 736 15 ARG H H 7.816 0.004 1 95 736 15 ARG HA H 4.028 0.001 1 96 736 15 ARG HB2 H 1.816 0.003 1 97 736 15 ARG HB3 H 1.816 0.003 1 98 736 15 ARG HD2 H 3.154 0.002 1 99 736 15 ARG HD3 H 3.154 0.002 1 100 736 15 ARG HG2 H 1.583 0.002 2 101 736 15 ARG HG3 H 1.693 0.001 2 102 737 16 ALA H H 7.818 0.004 1 103 737 16 ALA HA H 4.169 0.002 1 104 737 16 ALA HB H 1.346 0.001 1 105 738 17 LYS H H 7.822 0.003 1 106 738 17 LYS HA H 4.123 0.004 1 107 738 17 LYS HB2 H 1.621 0.004 1 108 738 17 LYS HB3 H 1.621 0.004 1 109 738 17 LYS HD2 H 1.527 0.003 1 110 738 17 LYS HD3 H 1.527 0.003 1 111 738 17 LYS HE2 H 2.842 0.01 1 112 738 17 LYS HE3 H 2.842 0.01 1 113 738 17 LYS HG2 H 1.213 0.01 2 114 738 17 LYS HG3 H 1.142 0.003 2 115 739 18 TRP H H 7.820 0.004 1 116 739 18 TRP HA H 4.677 0.003 1 117 739 18 TRP HB2 H 3.367 0.004 2 118 739 18 TRP HB3 H 3.237 0.001 2 119 739 18 TRP HD1 H 7.255 0.002 1 120 739 18 TRP HE1 H 10.159 0.001 1 121 739 18 TRP HE3 H 7.672 0.002 1 122 739 18 TRP HH2 H 7.232 0.003 1 123 739 18 TRP HZ2 H 7.489 0.002 1 124 739 18 TRP HZ3 H 7.150 0.005 1 stop_ save_