data_4643 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The solution structure of sheep myeloid antimicrobial peptide (smap29) and its relationship to biological function ; _BMRB_accession_number 4643 _BMRB_flat_file_name bmr4643.str _Entry_type original _Submission_date 2000-09-07 _Accession_date 2001-03-16 _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 Waring A. J. . 2 Sawai M. V. . 3 McCray P. B. . 4 Robertson A. D. . 5 Lehrer R. I. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 161 "coupling constants" 8 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-23 original author . stop_ _Original_release_date 2002-09-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'SMAP-29 has two LPS-binding sites and a central hinge' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21930705 _PubMed_ID 11856344 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tack B. F. . 2 Sawai M. V. . 3 Kearny W. R. . 4 Robertson A. D. . 5 Sherman M. A. . 6 Wang W. . . 7 Hong T. . . 8 Boo L. M. . 9 Wu H. . . 10 Waring A. J. . 11 Lehrer R. I. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 269 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1181 _Page_last 1189 _Year 2002 _Details . loop_ _Keyword 'random-ordered coil-loop' stop_ save_ ################################## # Molecular system description # ################################## save_system_SMAP _Saveframe_category molecular_system _Mol_system_name 'MYELOID ANTIMICROBIAL PEPTIDE' _Abbreviation_common 'MYELOID ANTIMICROBIAL PEPTIDE' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MYELOID ANTIMICROBIAL PEPTIDE' $SMAP 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_SMAP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MYELOID ANTIMICROBIAL PEPTIDE' _Abbreviation_common 'MYELOID ANTIMICROBIAL PEPTIDE' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 29 _Mol_residue_sequence ; RGLRRLGRKIAHGVKKYGPT VLRIIRIAG ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 GLY 3 LEU 4 ARG 5 ARG 6 LEU 7 GLY 8 ARG 9 LYS 10 ILE 11 ALA 12 HIS 13 GLY 14 VAL 15 LYS 16 LYS 17 TYR 18 GLY 19 PRO 20 THR 21 VAL 22 LEU 23 ARG 24 ILE 25 ILE 26 ARG 27 ILE 28 ALA 29 GLY 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 PDB 1FRY "The Solution Structure Of Sheep Myeloid Antimicrobial Peptide, Residues 1-29 (Smap29)" 96.55 29 100.00 100.00 2.79e-08 EMBL CAA63412 "cathelin-related prepropeptide [Ovis aries]" 100.00 160 100.00 100.00 1.68e-10 EMBL CAA63413 "cathelin-related prepropeptide [Ovis aries]" 100.00 160 100.00 100.00 3.22e-10 GB AAA85470 "SMAP-29 [Ovis aries]" 100.00 160 100.00 100.00 6.66e-10 GB AAB49715 "myeloid antimicrobial peptide precursor [Ovis aries]" 100.00 160 100.00 100.00 6.66e-10 REF NP_001009406 "cathelin-related peptide SC5 precursor [Ovis aries]" 100.00 160 100.00 100.00 3.22e-10 SP P49928 "RecName: Full=Cathelin-related peptide SC5; AltName: Full=Antibacterial peptide SMAP-29; AltName: Full=Myeloid antibacterial pe" 100.00 160 100.00 100.00 1.68e-10 SP P49929 "RecName: Full=Cathelin-related peptide SC5; AltName: Full=Antibacterial peptide SMAP-29; AltName: Full=Myeloid antibacterial pe" 100.00 160 100.00 100.00 3.22e-10 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SMAP sheep 9940 Eukaryota Metazoa Ovis aries 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 $SMAP . . . . . . 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 $SMAP 1 mM . 'phosphate buffer' 50 mM . H2O 60 % . trifluoroethanol 40 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details . save_ save_VNMR4.3b _Saveframe_category software _Name VNMR _Version 4.3b loop_ _Task collection stop_ _Details . save_ save_VNMR6.1b _Saveframe_category software _Name VNMR _Version 6.1b loop_ _Task 'data analysis' refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_TOCSY_3 _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 5.94 . pH temperature 298 . K 'ionic strength' 50 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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_citation_label _Correction_value_citation_label . H 1 . ppm . . . . . . $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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'MYELOID ANTIMICROBIAL PEPTIDE' _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 . 2 GLY H H 7.55 . 1 2 . 2 GLY HA2 H 3.62 . 2 3 . 2 GLY HA3 H 3.72 . 2 4 . 3 LEU H H 7.50 . 1 5 . 3 LEU HA H 3.96 . 1 6 . 3 LEU HB2 H 1.78 . 1 7 . 3 LEU HB3 H 1.78 . 1 8 . 3 LEU HG H 1.61 . 1 9 . 3 LEU HD1 H 0.83 . 2 10 . 3 LEU HD2 H 0.71 . 2 11 . 4 ARG H H 7.88 . 1 12 . 4 ARG HA H 4.00 . 1 13 . 4 ARG HB2 H 1.84 . 1 14 . 4 ARG HB3 H 1.84 . 1 15 . 4 ARG HD2 H 3.10 . 1 16 . 4 ARG HD3 H 3.10 . 1 17 . 5 ARG H H 8.59 . 1 18 . 5 ARG HA H 4.03 . 1 19 . 6 LEU H H 7.86 . 1 20 . 6 LEU HA H 4.09 . 1 21 . 6 LEU HB2 H 1.72 . 1 22 . 6 LEU HB3 H 1.72 . 1 23 . 6 LEU HG H 1.55 . 1 24 . 6 LEU HD1 H 0.84 . 2 25 . 6 LEU HD2 H 0.80 . 2 26 . 7 GLY H H 8.23 . 1 27 . 7 GLY HA2 H 3.67 . 2 28 . 7 GLY HA3 H 3.79 . 2 29 . 8 ARG H H 8.25 . 1 30 . 8 ARG HA H 3.85 . 1 31 . 9 LYS H H 7.82 . 1 32 . 9 LYS HA H 4.04 . 1 33 . 9 LYS HB2 H 1.95 . 1 34 . 9 LYS HB3 H 1.95 . 1 35 . 9 LYS HG2 H 1.38 . 1 36 . 9 LYS HG3 H 1.38 . 1 37 . 9 LYS HD2 H 1.61 . 1 38 . 9 LYS HD3 H 1.61 . 1 39 . 9 LYS HE2 H 2.88 . 1 40 . 9 LYS HE3 H 2.88 . 1 41 . 10 ILE H H 8.30 . 1 42 . 10 ILE HA H 3.65 . 1 43 . 10 ILE HB H 1.83 . 1 44 . 10 ILE HG2 H 0.76 . 1 45 . 10 ILE HG12 H 1.00 . 2 46 . 10 ILE HG13 H 1.66 . 2 47 . 10 ILE HD1 H 0.71 . 1 48 . 11 ALA H H 8.15 . 1 49 . 11 ALA HA H 3.92 . 1 50 . 11 ALA HB H 1.39 . 1 51 . 12 HIS H H 8.07 . 1 52 . 12 HIS HA H 4.20 . 1 53 . 12 HIS HB2 H 3.23 . 1 54 . 12 HIS HB3 H 3.23 . 1 55 . 12 HIS HD2 H 8.02 . 1 56 . 12 HIS HE1 H 7.04 . 1 57 . 13 GLY H H 8.24 . 1 58 . 13 GLY HA2 H 3.96 . 2 59 . 13 GLY HA3 H 4.38 . 2 60 . 14 VAL H H 8.63 . 1 61 . 14 VAL HA H 3.68 . 1 62 . 14 VAL HB H 2.04 . 1 63 . 14 VAL HG1 H 0.92 . 2 64 . 14 VAL HG2 H 0.76 . 2 65 . 15 LYS H H 7.84 . 1 66 . 15 LYS HA H 3.87 . 1 67 . 15 LYS HB2 H 1.80 . 1 68 . 15 LYS HB3 H 1.80 . 1 69 . 15 LYS HG2 H 1.30 . 2 70 . 15 LYS HG3 H 1.45 . 2 71 . 15 LYS HD2 H 1.59 . 1 72 . 15 LYS HD3 H 1.59 . 1 73 . 15 LYS HE2 H 2.85 . 1 74 . 15 LYS HE3 H 2.85 . 1 75 . 16 LYS H H 7.61 . 1 76 . 16 LYS HA H 3.86 . 1 77 . 16 LYS HB2 H 1.26 . 2 78 . 16 LYS HB3 H 1.12 . 2 79 . 16 LYS HG2 H 0.86 . 2 80 . 16 LYS HG3 H 0.44 . 2 81 . 16 LYS HD2 H 1.34 . 1 82 . 16 LYS HD3 H 1.34 . 1 83 . 16 LYS HE2 H 2.70 . 1 84 . 16 LYS HE3 H 2.70 . 1 85 . 17 TYR H H 8.47 . 1 86 . 17 TYR HA H 4.66 . 1 87 . 17 TYR HB2 H 3.15 . 2 88 . 17 TYR HB3 H 2.75 . 2 89 . 17 TYR HD1 H 7.13 . 1 90 . 17 TYR HD2 H 7.13 . 1 91 . 17 TYR HE1 H 6.75 . 1 92 . 17 TYR HE2 H 6.75 . 1 93 . 18 GLY H H 8.24 . 1 94 . 18 GLY HA2 H 3.92 . 2 95 . 18 GLY HA3 H 4.36 . 2 96 . 19 PRO HA H 4.19 . 1 97 . 19 PRO HB2 H 2.21 . 1 98 . 19 PRO HB3 H 2.21 . 1 99 . 19 PRO HG2 H 1.92 . 2 100 . 19 PRO HG3 H 1.98 . 2 101 . 19 PRO HD2 H 3.72 . 2 102 . 19 PRO HD3 H 3.55 . 2 103 . 20 THR H H 7.96 . 1 104 . 20 THR HA H 3.87 . 1 105 . 20 THR HB H 4.09 . 1 106 . 20 THR HG2 H 1.17 . 1 107 . 21 VAL H H 7.66 . 1 108 . 21 VAL HA H 3.68 . 1 109 . 21 VAL HB H 2.01 . 1 110 . 21 VAL HG1 H 0.93 . 2 111 . 21 VAL HG2 H 0.84 . 2 112 . 22 LEU H H 8.18 . 1 113 . 22 LEU HA H 4.20 . 1 114 . 22 LEU HB2 H 1.63 . 1 115 . 22 LEU HB3 H 1.63 . 1 116 . 22 LEU HG H 1.56 . 1 117 . 22 LEU HD1 H 0.83 . 2 118 . 22 LEU HD2 H 0.79 . 2 119 . 23 ARG H H 7.45 . 1 120 . 23 ARG HA H 4.00 . 1 121 . 23 ARG HB2 H 1.86 . 1 122 . 23 ARG HB3 H 1.86 . 1 123 . 23 ARG HG2 H 1.67 . 2 124 . 23 ARG HG3 H 1.57 . 2 125 . 23 ARG HD2 H 3.08 . 1 126 . 23 ARG HD3 H 3.08 . 1 127 . 24 ILE H H 7.70 . 1 128 . 24 ILE HA H 3.79 . 1 129 . 24 ILE HB H 1.84 . 1 130 . 24 ILE HG2 H 0.83 . 1 131 . 24 ILE HG12 H 1.18 . 2 132 . 24 ILE HG13 H 1.48 . 2 133 . 24 ILE HD1 H 0.65 . 1 134 . 25 ILE H H 7.48 . 1 135 . 25 ILE HA H 3.79 . 1 136 . 25 ILE HB H 1.87 . 1 137 . 25 ILE HG2 H 0.77 . 1 138 . 25 ILE HG12 H 1.09 . 2 139 . 25 ILE HG13 H 1.44 . 2 140 . 25 ILE HD1 H 0.66 . 1 141 . 26 ARG H H 7.59 . 1 142 . 26 ARG HA H 4.13 . 1 143 . 26 ARG HB2 H 1.82 . 1 144 . 26 ARG HB3 H 1.82 . 1 145 . 26 ARG HG2 H 1.60 . 2 146 . 26 ARG HG3 H 1.55 . 2 147 . 26 ARG HD2 H 3.09 . 1 148 . 26 ARG HD3 H 3.09 . 1 149 . 27 ILE H H 7.67 . 1 150 . 27 ILE HA H 3.99 . 1 151 . 27 ILE HB H 1.83 . 1 152 . 27 ILE HG2 H 0.81 . 1 153 . 27 ILE HG12 H 1.11 . 1 154 . 27 ILE HG13 H 1.11 . 1 155 . 27 ILE HD1 H 0.75 . 1 156 . 28 ALA H H 7.96 . 1 157 . 28 ALA HA H 4.29 . 1 158 . 28 ALA HB H 1.29 . 1 159 . 29 GLY H H 7.55 . 1 160 . 29 GLY HA2 H 3.65 . 2 161 . 29 GLY HA3 H 3.69 . 2 stop_ save_ ######################## # Coupling constants # ######################## save_JHNHA _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'MYELOID ANTIMICROBIAL PEPTIDE' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 6 LEU H 6 LEU HA 5.6 . . 1.0 2 3JHNHA 8 ARG H 8 ARG HA 9.1 . . 1.0 3 3JHNHA 9 LYS H 9 LYS HA 9.2 . . 1.0 4 3JHNHA 10 ILE H 10 ILE HA 8.5 . . 1.0 5 3JHNHA 11 ALA H 11 ALA HA 5.8 . . 1.0 6 3JHNHA 12 HIS H 12 HIS HA 3.4 . . 1.0 7 3JHNHA 15 LYS H 15 LYS HA 8.4 . . 1.0 8 3JHNHA 16 LYS H 16 LYS HA 8.3 . . 1.0 stop_ save_