data_6264 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of cryptdin-4, the most potent alpha-defensin from mouse Paneth cells ; _BMRB_accession_number 6264 _BMRB_flat_file_name bmr6264.str _Entry_type original _Submission_date 2004-07-16 _Accession_date 2004-07-16 _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 Jing W. . . 2 Hunter H. N. . 3 Tanabe H. . . 4 Ouellette A. J. . 5 Vogel H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 209 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-02-08 original author . stop_ _Original_release_date 2005-02-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of cryptdin-4, a mouse paneth cell alpha-defensin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15595831 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jing W. . . 2 Hunter H. N. . 3 Tanabe H. . . 4 Ouellette A. J. . 5 Vogel H. J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 15759 _Page_last 15766 _Year 2004 _Details . loop_ _Keyword 'beta hairpin' 'beta sheet' stop_ save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name Cryptdin-4 _Abbreviation_common Cryptdin-4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Cryptdin-4 $Cryptdin-4 stop_ _System_molecular_weight . _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cryptdin-4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Cryptdin-4 _Abbreviation_common Cryptdin-4 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; GLLCYCRKGHCKRGERVRGT CGIRFLYCCPRR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 LEU 3 LEU 4 CYS 5 TYR 6 CYS 7 ARG 8 LYS 9 GLY 10 HIS 11 CYS 12 LYS 13 ARG 14 GLY 15 GLU 16 ARG 17 VAL 18 ARG 19 GLY 20 THR 21 CYS 22 GLY 23 ILE 24 ARG 25 PHE 26 LEU 27 TYR 28 CYS 29 CYS 30 PRO 31 ARG 32 ARG 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 $Cryptdin-4 'house mouse' 10090 Eukaryota Metazoa Mus musculus 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 $Cryptdin-4 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) PET-28A 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 $Cryptdin-4 3.2 mg . stop_ save_ ############################ # Computer software used # ############################ save_NMRview _Saveframe_category software _Name NMRView _Version 4.1.3 loop_ _Task 'data analysis' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Task refinement stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Advance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 . 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_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_reference _Mol_system_component_name Cryptdin-4 _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 GLY HA3 H 3.848 . 1 2 . 1 GLY HA2 H 3.848 . 1 3 . 2 LEU H H 8.513 . 1 4 . 2 LEU HA H 4.360 . 1 5 . 2 LEU HB3 H 1.578 . 1 6 . 2 LEU HB2 H 1.578 . 1 7 . 2 LEU HG H 1.578 . 1 8 . 2 LEU HD1 H 0.901 . 1 9 . 2 LEU HD2 H 0.901 . 1 10 . 3 LEU H H 8.256 . 1 11 . 3 LEU HA H 4.272 . 1 12 . 3 LEU HB3 H 1.485 . 1 13 . 3 LEU HB2 H 1.485 . 1 14 . 3 LEU HG H 1.485 . 1 15 . 3 LEU HD1 H 0.854 . 1 16 . 3 LEU HD2 H 0.854 . 1 17 . 4 CYS H H 7.609 . 1 18 . 4 CYS HA H 5.017 . 1 19 . 4 CYS HB3 H 2.726 . 2 20 . 4 CYS HB2 H 1.669 . 2 21 . 4 CYS HG H 10.600 . 1 22 . 5 TYR H H 8.792 . 1 23 . 5 TYR HA H 4.589 . 1 24 . 5 TYR HB3 H 2.396 . 2 25 . 5 TYR HB2 H 2.935 . 2 26 . 5 TYR HD1 H 7.029 . 1 27 . 5 TYR HE1 H 6.711 . 1 28 . 5 TYR HE2 H 6.711 . 1 29 . 5 TYR HD2 H 7.029 . 1 30 . 6 CYS H H 9.142 . 1 31 . 6 CYS HA H 5.638 . 1 32 . 6 CYS HB3 H 2.935 . 2 33 . 6 CYS HB2 H 3.054 . 2 34 . 6 CYS HG H 10.700 . 1 35 . 7 ARG H H 9.901 . 1 36 . 7 ARG HA H 4.832 . 1 37 . 7 ARG HB3 H 1.742 . 2 38 . 7 ARG HB2 H 1.648 . 2 39 . 7 ARG HG3 H 1.415 . 1 40 . 7 ARG HG2 H 1.415 . 1 41 . 7 ARG HD3 H 3.222 . 1 42 . 7 ARG HD2 H 3.222 . 1 43 . 7 ARG HE H 9.619 . 1 44 . 7 ARG HH21 H 6.561 . 1 45 . 7 ARG HH22 H 6.561 . 1 46 . 7 ARG HH11 H 6.561 . 1 47 . 7 ARG HH12 H 6.561 . 1 48 . 8 LYS H H 8.679 . 1 49 . 8 LYS HA H 3.756 . 1 50 . 8 LYS HB3 H 1.556 . 1 51 . 8 LYS HB2 H 1.556 . 1 52 . 8 LYS HG3 H 0.982 . 1 53 . 8 LYS HG2 H 0.982 . 1 54 . 8 LYS HD3 H 1.252 . 1 55 . 8 LYS HD2 H 1.252 . 1 56 . 8 LYS HE3 H 2.851 . 1 57 . 8 LYS HE2 H 2.851 . 1 58 . 8 LYS HZ H 7.527 . 1 59 . 9 GLY H H 8.831 . 1 60 . 9 GLY HA3 H 4.243 . 2 61 . 9 GLY HA2 H 3.381 . 2 62 . 10 HIS H H 8.073 . 1 63 . 10 HIS HA H 4.637 . 1 64 . 10 HIS HB3 H 3.120 . 2 65 . 10 HIS HB2 H 3.379 . 2 66 . 10 HIS HD2 H 7.288 . 1 67 . 10 HIS HE1 H 8.586 . 1 68 . 11 CYS H H 8.882 . 1 69 . 11 CYS HA H 5.018 . 1 70 . 11 CYS HB3 H 3.728 . 2 71 . 11 CYS HB2 H 2.654 . 2 72 . 12 LYS H H 8.585 . 1 73 . 12 LYS HA H 4.384 . 1 74 . 12 LYS HB3 H 1.897 . 1 75 . 12 LYS HB2 H 1.897 . 1 76 . 12 LYS HG3 H 1.342 . 1 77 . 12 LYS HG2 H 1.342 . 1 78 . 12 LYS HD3 H 1.555 . 1 79 . 12 LYS HD2 H 1.555 . 1 80 . 12 LYS HE3 H 2.855 . 1 81 . 12 LYS HE2 H 2.855 . 1 82 . 13 ARG H H 8.510 . 1 83 . 13 ARG HA H 4.083 . 1 84 . 13 ARG HB3 H 1.837 . 2 85 . 13 ARG HB2 H 1.743 . 2 86 . 13 ARG HG3 H 1.579 . 1 87 . 13 ARG HG2 H 1.579 . 1 88 . 13 ARG HD3 H 3.218 . 1 89 . 13 ARG HD2 H 3.218 . 1 90 . 13 ARG HE H 7.183 . 1 91 . 14 GLY H H 8.914 . 1 92 . 14 GLY HA3 H 4.201 . 2 93 . 14 GLY HA2 H 3.799 . 2 94 . 15 GLU H H 7.812 . 1 95 . 15 GLU HA H 4.772 . 1 96 . 15 GLU HB3 H 1.599 . 2 97 . 15 GLU HB2 H 1.859 . 2 98 . 15 GLU HG3 H 2.057 . 2 99 . 15 GLU HG2 H 2.445 . 2 100 . 16 ARG H H 9.108 . 1 101 . 16 ARG HA H 4.727 . 1 102 . 16 ARG HB3 H 1.718 . 1 103 . 16 ARG HB2 H 1.718 . 1 104 . 16 ARG HG3 H 1.544 . 1 105 . 16 ARG HG2 H 1.544 . 1 106 . 16 ARG HD3 H 3.191 . 1 107 . 16 ARG HD2 H 3.191 . 1 108 . 16 ARG HE H 7.208 . 1 109 . 17 VAL H H 8.734 . 1 110 . 17 VAL HA H 4.291 . 1 111 . 17 VAL HB H 2.163 . 1 112 . 17 VAL HG2 H 1.134 . 2 113 . 17 VAL HG1 H 1.205 . 2 114 . 18 ARG H H 9.498 . 1 115 . 18 ARG HA H 4.758 . 1 116 . 18 ARG HB3 H 2.199 . 1 117 . 18 ARG HB2 H 2.199 . 1 118 . 18 ARG HG3 H 1.694 . 2 119 . 18 ARG HG2 H 1.621 . 2 120 . 18 ARG HD3 H 3.239 . 1 121 . 18 ARG HD2 H 3.239 . 1 122 . 18 ARG HE H 7.282 . 1 123 . 19 GLY H H 7.759 . 1 124 . 19 GLY HA3 H 4.524 . 2 125 . 19 GLY HA2 H 4.082 . 2 126 . 20 THR H H 8.573 . 1 127 . 20 THR HA H 5.087 . 1 128 . 20 THR HB H 4.466 . 1 129 . 20 THR HG2 H 1.228 . 1 130 . 21 CYS H H 8.100 . 1 131 . 21 CYS HA H 4.901 . 1 132 . 21 CYS HB3 H 3.217 . 2 133 . 21 CYS HB2 H 3.309 . 2 134 . 22 GLY H H 8.306 . 1 135 . 22 GLY HA3 H 3.989 . 2 136 . 22 GLY HA2 H 3.778 . 2 137 . 23 ILE H H 8.276 . 1 138 . 23 ILE HA H 4.058 . 1 139 . 23 ILE HB H 1.881 . 1 140 . 23 ILE HG13 H 1.484 . 1 141 . 23 ILE HG12 H 1.181 . 1 142 . 23 ILE HD1 H 0.922 . 1 143 . 23 ILE HG2 H 0.861 . 1 144 . 24 ARG H H 8.483 . 1 145 . 24 ARG HA H 4.015 . 1 146 . 24 ARG HB3 H 1.859 . 1 147 . 24 ARG HB2 H 1.859 . 1 148 . 24 ARG HG3 H 1.526 . 1 149 . 24 ARG HG2 H 1.526 . 1 150 . 24 ARG HD3 H 3.116 . 1 151 . 24 ARG HD2 H 3.116 . 1 152 . 24 ARG HE H 7.211 . 1 153 . 25 PHE H H 7.804 . 1 154 . 25 PHE HA H 5.098 . 1 155 . 25 PHE HB3 H 2.847 . 2 156 . 25 PHE HB2 H 3.029 . 2 157 . 25 PHE HD1 H 7.128 . 1 158 . 25 PHE HE1 H 7.349 . 1 159 . 25 PHE HZ H 7.247 . 1 160 . 25 PHE HE2 H 7.349 . 1 161 . 25 PHE HD2 H 7.128 . 1 162 . 26 LEU H H 9.336 . 1 163 . 26 LEU HA H 4.733 . 1 164 . 26 LEU HB3 H 1.645 . 1 165 . 26 LEU HB2 H 1.645 . 1 166 . 26 LEU HG H 1.391 . 1 167 . 26 LEU HD1 H 0.806 . 2 168 . 26 LEU HD2 H 0.853 . 2 169 . 27 TYR H H 8.412 . 1 170 . 27 TYR HA H 4.995 . 1 171 . 27 TYR HB3 H 2.749 . 2 172 . 27 TYR HB2 H 2.257 . 2 173 . 27 TYR HD1 H 6.900 . 1 174 . 27 TYR HE1 H 6.664 . 1 175 . 27 TYR HE2 H 6.664 . 1 176 . 27 TYR HD2 H 6.900 . 1 177 . 28 CYS H H 9.013 . 1 178 . 28 CYS HA H 5.090 . 1 179 . 28 CYS HB3 H 2.933 . 2 180 . 28 CYS HB2 H 3.192 . 2 181 . 29 CYS H H 9.089 . 1 182 . 29 CYS HA H 5.323 . 1 183 . 29 CYS HB3 H 3.098 . 2 184 . 29 CYS HB2 H 2.486 . 2 185 . 30 PRO HA H 4.646 . 1 186 . 30 PRO HB3 H 2.491 . 2 187 . 30 PRO HB2 H 2.037 . 2 188 . 30 PRO HG3 H 2.166 . 2 189 . 30 PRO HG2 H 2.257 . 2 190 . 30 PRO HD3 H 3.988 . 2 191 . 30 PRO HD2 H 3.738 . 2 192 . 31 ARG H H 8.446 . 1 193 . 31 ARG HA H 4.124 . 1 194 . 31 ARG HB3 H 1.810 . 2 195 . 31 ARG HB2 H 1.696 . 2 196 . 31 ARG HG3 H 1.578 . 1 197 . 31 ARG HG2 H 1.578 . 1 198 . 31 ARG HD3 H 3.169 . 1 199 . 31 ARG HD2 H 3.169 . 1 200 . 31 ARG HE H 7.213 . 1 201 . 32 ARG H H 7.893 . 1 202 . 32 ARG HA H 4.175 . 1 203 . 32 ARG HB3 H 1.829 . 2 204 . 32 ARG HB2 H 1.717 . 2 205 . 32 ARG HG3 H 1.578 . 1 206 . 32 ARG HG2 H 1.578 . 1 207 . 32 ARG HD3 H 3.173 . 1 208 . 32 ARG HD2 H 3.173 . 1 209 . 32 ARG HE H 7.213 . 1 stop_ save_