data_4112 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H Assignment and Secondary Structure of the Bacteriocin AS-48 Cyclic Peptide. ; _BMRB_accession_number 4112 _BMRB_flat_file_name bmr4112.str _Entry_type original _Submission_date 1998-02-24 _Accession_date 1998-02-24 _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 Langdon Grant M. . 2 Bruix Marta . . 3 Galvez Antonio . . 4 Valdivia Eva . . 5 Maqueda Mercedes . . 6 Rico Manuel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 397 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-02 original author . stop_ _Original_release_date 1999-02-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Langdon, G.M., Bruix, M., Galvez, A., Valdivia, E., Maqueda, M., and Rico, M., "Sequence-specific 1H Assignment and Secondary Structure of the Bacteriocin AS-48 Cyclic Peptide," J. Biomol. NMR 12, 173-175 (1998). ; _Citation_title ; Sequence-specific 1H Assignment and Secondary Structure of the Bacteriocin AS-48 Cyclic Peptide. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98399494 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Langdon Grant M. . 2 Bruix Marta . . 3 Galvez Antonio . . 4 Valdivia Eva . . 5 Maqueda Mercedes . . 6 Rico Manuel . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 173 _Page_last 175 _Year 1998 _Details . loop_ _Keyword 'Bacteriocin AS-48' 'cyclic protein' 'NMR assignments' 'secondary structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_bacteriocin_cAS48 _Saveframe_category molecular_system _Mol_system_name bacteriocin_cas48 _Abbreviation_common cAS48 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label bacteriocin_cAS48 $bacteriocin_cAS48 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bacteriocin_cAS48 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Bacteriocin AS-48' _Abbreviation_common cAS48 _Molecular_mass 7149 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 70 _Mol_residue_sequence ; MAKEFGIPAAVAGTVLNVVE AGGWVTTIVSILTAVGSGGL SLLAAAGRESIKAYLKKEIK KKGKRAVIAW ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 GLU 5 PHE 6 GLY 7 ILE 8 PRO 9 ALA 10 ALA 11 VAL 12 ALA 13 GLY 14 THR 15 VAL 16 LEU 17 ASN 18 VAL 19 VAL 20 GLU 21 ALA 22 GLY 23 GLY 24 TRP 25 VAL 26 THR 27 THR 28 ILE 29 VAL 30 SER 31 ILE 32 LEU 33 THR 34 ALA 35 VAL 36 GLY 37 SER 38 GLY 39 GLY 40 LEU 41 SER 42 LEU 43 LEU 44 ALA 45 ALA 46 ALA 47 GLY 48 ARG 49 GLU 50 SER 51 ILE 52 LYS 53 ALA 54 TYR 55 LEU 56 LYS 57 LYS 58 GLU 59 ILE 60 LYS 61 LYS 62 LYS 63 GLY 64 LYS 65 ARG 66 ALA 67 VAL 68 ILE 69 ALA 70 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 1E68 "Solution Structure Of Bacteriocin As-48" 98.57 70 100.00 100.00 1.65e-36 PDB 1O82 "X-Ray Structure Of Bacteriocin As-48 At Ph 4.5. Sulphate Bound Form" 100.00 70 100.00 100.00 1.53e-37 PDB 1O83 "Crystal Structure Of Bacteriocin As-48 At Ph 7.5, Phosphate Bound. Crystal Form I" 100.00 70 100.00 100.00 1.53e-37 PDB 1O84 "Crystal Structure Of Bacteriocin As-48. N-Decyl-Beta-D- Maltoside Bound" 100.00 70 100.00 100.00 1.53e-37 PDB 4RGD "The Structure A As-48 G13k/l40k Mutant" 100.00 70 97.14 97.14 1.38e-27 DBJ BAA24805 "bacA [Enterococcus faecalis]" 100.00 105 98.57 98.57 9.94e-37 EMBL CAA56076 "peptide antibiotic AS-48 [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 EMBL CAA72917 "AS-48 protein [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 GB AGQ55496 "enterocin proprotein [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 GB AHL69645 "AS-48A [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 GB AKU62176 "BacA (plasmid) [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 GB EOJ79470 "circularin A/uberolysin family circular bacteriocin [Enterococcus faecalis EnGen0369]" 100.00 105 100.00 100.00 6.67e-38 REF WP_010824081 "circularin A/uberolysin family circular bacteriocin [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 REF WP_032489109 "hypothetical protein [Enterococcus faecalis]" 100.00 105 98.57 98.57 9.94e-37 REF YP_009074455 "peptide antibiotic AS-48 [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 REF YP_009075264 "bacA [Enterococcus faecalis]" 100.00 105 98.57 98.57 9.94e-37 REF YP_009091579 "AS-48A [Enterococcus faecalis]" 100.00 105 100.00 100.00 6.67e-38 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Subvariant _Plasmid _Details $bacteriocin_cAS48 enterococcus 1351 Eubacteria . Enterococcus faecalis S-48 liquefaciens pMB2 ; TREMBL: Q47765 tr|Q47765|Q47765 PEPTIDE ANTIBIOTIC AS-48 - ENTEROCOCCUS FAECALIS (STREPTOCOCCUS FAECALIS). ; 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 $bacteriocin_cAS48 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $bacteriocin_cAS48 1.5 mM . NaCl 0.1 M . stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.01 M pH 3.0 0.05 n/a temperature 298 0.05 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details ; Methods of reference follow the guidelines suggested in "Wishart, D.S. and Sykes, B.D. Methods in Enzymology 239:363-385 Chemical shifts as tool for structure determination (1994) ; 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 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 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_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name bacteriocin_cAS48 _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 MET H H 9.00 0.01 1 2 . 1 MET HA H 3.63 0.01 1 3 . 1 MET HB2 H 2.32 0.01 1 4 . 1 MET HB3 H 1.98 0.01 1 5 . 1 MET HG2 H 3.28 0.01 2 6 . 1 MET HG3 H 2.26 0.01 2 7 . 1 MET HE H 1.96 0.01 1 8 . 2 ALA H H 7.87 0.01 1 9 . 2 ALA HA H 4.46 0.01 1 10 . 2 ALA HB H 1.52 0.01 1 11 . 3 LYS H H 8.36 0.01 1 12 . 3 LYS HA H 3.99 0.01 1 13 . 3 LYS HB2 H 1.95 0.01 1 14 . 3 LYS HB3 H 1.82 0.01 1 15 . 3 LYS HG2 H 1.41 0.01 1 16 . 3 LYS HG3 H 1.41 0.01 1 17 . 3 LYS HD2 H 1.70 0.01 1 18 . 3 LYS HD3 H 1.70 0.01 1 19 . 3 LYS HE2 H 2.97 0.01 1 20 . 3 LYS HE3 H 2.97 0.01 1 21 . 4 GLU H H 8.70 0.01 1 22 . 4 GLU HA H 3.90 0.01 1 23 . 4 GLU HB2 H 0.99 0.01 1 24 . 4 GLU HB3 H 0.71 0.01 1 25 . 4 GLU HG2 H 1.70 0.01 2 26 . 4 GLU HG3 H 1.45 0.01 2 27 . 5 PHE H H 6.40 0.01 1 28 . 5 PHE HA H 3.49 0.01 1 29 . 5 PHE HB2 H 2.69 0.01 1 30 . 5 PHE HB3 H 2.69 0.01 1 31 . 5 PHE HD1 H 6.88 0.01 1 32 . 5 PHE HD2 H 6.88 0.01 1 33 . 5 PHE HE1 H 6.47 0.01 1 34 . 5 PHE HE2 H 6.47 0.01 1 35 . 5 PHE HZ H 7.06 0.01 1 36 . 6 GLY H H 7.27 0.01 1 37 . 6 GLY HA2 H 3.94 0.01 2 38 . 6 GLY HA3 H 3.90 0.01 2 39 . 7 ILE H H 7.49 0.01 1 40 . 7 ILE HA H 4.13 0.01 1 41 . 7 ILE HB H 1.48 0.01 1 42 . 7 ILE HG12 H 1.43 0.01 2 43 . 7 ILE HG13 H 0.94 0.01 2 44 . 7 ILE HG2 H 0.86 0.01 1 45 . 7 ILE HD1 H 0.63 0.01 1 46 . 8 PRO HA H 4.44 0.01 1 47 . 8 PRO HB2 H 2.54 0.01 1 48 . 8 PRO HB3 H 1.89 0.01 1 49 . 8 PRO HG2 H 2.11 0.01 2 50 . 8 PRO HG3 H 1.98 0.01 2 51 . 8 PRO HD2 H 4.27 0.01 2 52 . 8 PRO HD3 H 3.37 0.01 2 53 . 9 ALA H H 8.94 0.01 1 54 . 9 ALA HA H 4.13 0.01 1 55 . 9 ALA HB H 1.44 0.01 1 56 . 10 ALA H H 9.26 0.01 1 57 . 10 ALA HA H 4.16 0.01 1 58 . 10 ALA HB H 1.45 0.01 1 59 . 11 VAL H H 7.02 0.01 1 60 . 11 VAL HA H 3.65 0.01 1 61 . 11 VAL HB H 2.02 0.01 1 62 . 11 VAL HG1 H 1.02 0.01 1 63 . 11 VAL HG2 H 0.74 0.01 1 64 . 12 ALA H H 8.65 0.01 1 65 . 12 ALA HA H 3.73 0.01 1 66 . 12 ALA HB H 1.60 0.01 1 67 . 13 GLY H H 8.64 0.01 1 68 . 13 GLY HA2 H 3.99 0.01 2 69 . 13 GLY HA3 H 3.62 0.01 2 70 . 14 THR H H 7.38 0.01 1 71 . 14 THR HA H 3.99 0.01 1 72 . 14 THR HB H 4.38 0.01 1 73 . 14 THR HG2 H 1.20 0.01 1 74 . 15 VAL H H 8.36 0.01 1 75 . 15 VAL HA H 3.35 0.01 1 76 . 15 VAL HB H 2.27 0.01 1 77 . 15 VAL HG1 H 0.97 0.01 1 78 . 15 VAL HG2 H 0.81 0.01 1 79 . 16 LEU H H 8.36 0.01 1 80 . 16 LEU HA H 3.96 0.01 1 81 . 16 LEU HB2 H 1.93 0.01 1 82 . 16 LEU HB3 H 1.42 0.01 1 83 . 16 LEU HG H 2.10 0.01 1 84 . 16 LEU HD1 H 0.93 0.01 1 85 . 16 LEU HD2 H 0.89 0.01 1 86 . 17 ASN H H 8.15 0.01 1 87 . 17 ASN HA H 4.51 0.01 1 88 . 17 ASN HB2 H 3.10 0.01 1 89 . 17 ASN HB3 H 2.86 0.01 1 90 . 17 ASN HD21 H 7.63 0.01 1 91 . 17 ASN HD22 H 6.77 0.01 1 92 . 18 VAL H H 8.01 0.01 1 93 . 18 VAL HA H 3.76 0.01 1 94 . 18 VAL HB H 2.17 0.01 1 95 . 18 VAL HG1 H 1.00 0.01 1 96 . 18 VAL HG2 H 0.87 0.01 1 97 . 19 VAL H H 8.06 0.01 1 98 . 19 VAL HA H 3.36 0.01 1 99 . 19 VAL HB H 2.45 0.01 1 100 . 19 VAL HG1 H 1.13 0.01 1 101 . 19 VAL HG2 H 0.90 0.01 1 102 . 20 GLU H H 8.52 0.01 1 103 . 20 GLU HA H 4.08 0.01 1 104 . 20 GLU HB2 H 2.42 0.01 1 105 . 20 GLU HB3 H 2.16 0.01 1 106 . 20 GLU HG2 H 2.58 0.01 2 107 . 20 GLU HG3 H 2.41 0.01 2 108 . 21 ALA H H 7.91 0.01 1 109 . 21 ALA HA H 4.40 0.01 1 110 . 21 ALA HB H 1.45 0.01 1 111 . 22 GLY H H 7.83 0.01 1 112 . 22 GLY HA2 H 4.08 0.01 2 113 . 22 GLY HA3 H 3.77 0.01 2 114 . 23 GLY H H 8.32 0.01 1 115 . 23 GLY HA2 H 3.95 0.01 2 116 . 23 GLY HA3 H 3.66 0.01 2 117 . 24 TRP H H 8.28 0.01 1 118 . 24 TRP HB2 H 3.36 0.01 1 119 . 24 TRP HB3 H 3.52 0.01 1 120 . 24 TRP HD1 H 7.35 0.01 1 121 . 24 TRP HE1 H 10.24 0.01 1 122 . 24 TRP HE3 H 7.64 0.01 1 123 . 24 TRP HZ2 H 7.54 0.01 1 124 . 24 TRP HZ3 H 7.18 0.01 1 125 . 24 TRP HH2 H 7.23 0.01 1 126 . 25 VAL H H 9.04 0.01 1 127 . 25 VAL HA H 3.61 0.01 1 128 . 25 VAL HB H 2.20 0.01 1 129 . 25 VAL HG1 H 1.19 0.01 1 130 . 25 VAL HG2 H 1.05 0.01 1 131 . 26 THR H H 7.87 0.01 1 132 . 26 THR HA H 3.90 0.01 1 133 . 26 THR HB H 3.98 0.01 1 134 . 26 THR HG2 H 1.27 0.01 1 135 . 27 THR H H 7.26 0.01 1 136 . 27 THR HA H 3.98 0.01 1 137 . 27 THR HB H 4.40 0.01 1 138 . 27 THR HG2 H 1.24 0.01 1 139 . 28 ILE H H 7.39 0.01 1 140 . 28 ILE HA H 3.40 0.01 1 141 . 28 ILE HB H 2.00 0.01 1 142 . 28 ILE HG12 H 1.81 0.01 1 143 . 28 ILE HG13 H 1.81 0.01 1 144 . 28 ILE HG2 H 0.79 0.01 1 145 . 28 ILE HD1 H 0.75 0.01 1 146 . 29 VAL H H 8.63 0.01 1 147 . 29 VAL HA H 3.49 0.01 1 148 . 29 VAL HB H 2.09 0.01 1 149 . 29 VAL HG1 H 1.06 0.01 1 150 . 29 VAL HG2 H 0.88 0.01 1 151 . 30 SER H H 8.37 0.01 1 152 . 30 SER HA H 4.18 0.01 1 153 . 30 SER HB2 H 4.05 0.01 2 154 . 30 SER HB3 H 4.03 0.01 2 155 . 31 ILE H H 7.92 0.01 1 156 . 31 ILE HA H 3.65 0.01 1 157 . 31 ILE HB H 1.69 0.01 1 158 . 31 ILE HG12 H 1.96 0.01 1 159 . 31 ILE HG13 H 1.89 0.01 1 160 . 31 ILE HG2 H 0.72 0.01 1 161 . 31 ILE HD1 H 1.01 0.01 1 162 . 32 LEU H H 8.04 0.01 1 163 . 32 LEU HA H 3.99 0.01 1 164 . 32 LEU HB2 H 1.85 0.01 1 165 . 32 LEU HB3 H 1.22 0.01 1 166 . 32 LEU HG H 1.83 0.01 1 167 . 32 LEU HD1 H 0.76 0.01 1 168 . 32 LEU HD2 H 0.75 0.01 1 169 . 33 THR H H 8.56 0.01 1 170 . 33 THR HA H 3.77 0.01 1 171 . 33 THR HB H 4.21 0.01 1 172 . 33 THR HG2 H 1.19 0.01 1 173 . 34 ALA H H 7.43 0.01 1 174 . 34 ALA HA H 4.19 0.01 1 175 . 34 ALA HB H 1.57 0.01 1 176 . 35 VAL H H 7.45 0.01 1 177 . 35 VAL HA H 4.06 0.01 1 178 . 35 VAL HB H 2.32 0.01 1 179 . 35 VAL HG1 H 1.21 0.01 1 180 . 35 VAL HG2 H 1.08 0.01 1 181 . 36 GLY H H 7.39 0.01 1 182 . 36 GLY HA2 H 4.66 0.01 2 183 . 36 GLY HA3 H 3.73 0.01 2 184 . 37 SER H H 9.07 0.01 1 185 . 37 SER HA H 4.06 0.01 1 186 . 37 SER HB2 H 3.98 0.01 1 187 . 37 SER HB3 H 3.98 0.01 1 188 . 38 GLY H H 9.39 0.01 1 189 . 38 GLY HA2 H 4.24 0.01 2 190 . 38 GLY HA3 H 4.12 0.01 2 191 . 39 GLY H H 7.24 0.01 1 192 . 39 GLY HA2 H 4.47 0.01 1 193 . 39 GLY HA3 H 3.53 0.01 1 194 . 40 LEU H H 7.88 0.01 1 195 . 40 LEU HA H 4.01 0.01 1 196 . 40 LEU HB2 H 1.92 0.01 1 197 . 40 LEU HB3 H 1.51 0.01 1 198 . 40 LEU HG H 1.76 0.01 1 199 . 40 LEU HD1 H 0.92 0.01 1 200 . 40 LEU HD2 H 0.89 0.01 1 201 . 41 SER H H 8.44 0.01 1 202 . 41 SER HA H 4.30 0.01 1 203 . 41 SER HB2 H 4.19 0.01 1 204 . 41 SER HB3 H 4.19 0.01 1 205 . 42 LEU H H 7.43 0.01 1 206 . 42 LEU HA H 3.34 0.01 1 207 . 42 LEU HB2 H 1.57 0.01 1 208 . 42 LEU HB3 H 0.29 0.01 1 209 . 42 LEU HG H 1.18 0.01 1 210 . 42 LEU HD1 H 0.67 0.01 2 211 . 42 LEU HD2 H 0.54 0.01 2 212 . 43 LEU H H 7.76 0.01 1 213 . 43 LEU HA H 3.77 0.01 1 214 . 43 LEU HB2 H 1.90 0.01 1 215 . 43 LEU HB3 H 1.39 0.01 1 216 . 43 LEU HG H 1.74 0.01 1 217 . 43 LEU HD1 H 0.89 0.01 2 218 . 43 LEU HD2 H 0.85 0.01 2 219 . 44 ALA H H 7.91 0.01 1 220 . 44 ALA HA H 4.11 0.01 1 221 . 44 ALA HB H 1.49 0.01 1 222 . 45 ALA H H 7.79 0.01 1 223 . 45 ALA HA H 4.05 0.01 1 224 . 45 ALA HB H 1.62 0.01 1 225 . 46 ALA H H 7.05 0.01 1 226 . 46 ALA HA H 3.10 0.01 1 227 . 46 ALA HB H 0.99 0.01 1 228 . 47 GLY H H 7.49 0.01 1 229 . 47 GLY HA2 H 3.92 0.01 1 230 . 47 GLY HA3 H 3.64 0.01 1 231 . 48 ARG H H 8.84 0.01 1 232 . 48 ARG HA H 4.14 0.01 1 233 . 48 ARG HB2 H 1.72 0.01 1 234 . 48 ARG HB3 H 1.98 0.01 1 235 . 48 ARG HG2 H 1.84 0.01 2 236 . 48 ARG HG3 H 1.72 0.01 2 237 . 48 ARG HD2 H 3.21 0.01 1 238 . 48 ARG HD3 H 3.21 0.01 1 239 . 48 ARG HE H 7.22 0.01 1 240 . 49 GLU H H 7.98 0.01 1 241 . 49 GLU HA H 4.35 0.01 1 242 . 49 GLU HB2 H 2.23 0.01 1 243 . 49 GLU HB3 H 2.13 0.01 1 244 . 49 GLU HG2 H 2.62 0.01 2 245 . 49 GLU HG3 H 2.54 0.01 2 246 . 50 SER H H 8.36 0.01 1 247 . 50 SER HA H 4.51 0.01 1 248 . 50 SER HB2 H 4.24 0.01 2 249 . 50 SER HB3 H 3.99 0.01 2 250 . 51 ILE H H 8.79 0.01 1 251 . 51 ILE HA H 4.19 0.01 1 252 . 51 ILE HB H 2.00 0.01 1 253 . 51 ILE HG12 H 1.86 0.01 2 254 . 51 ILE HG13 H 1.21 0.01 2 255 . 51 ILE HG2 H 0.93 0.01 1 256 . 51 ILE HD1 H 0.89 0.01 1 257 . 52 LYS H H 7.24 0.01 1 258 . 52 LYS HA H 3.93 0.01 1 259 . 52 LYS HB2 H 1.87 0.01 1 260 . 52 LYS HB3 H 1.63 0.01 1 261 . 52 LYS HG2 H 1.42 0.01 1 262 . 52 LYS HG3 H 1.42 0.01 1 263 . 52 LYS HD2 H 1.62 0.01 2 264 . 52 LYS HD3 H 1.55 0.01 2 265 . 52 LYS HE2 H 2.93 0.01 1 266 . 52 LYS HE3 H 2.93 0.01 1 267 . 53 ALA H H 7.37 0.01 1 268 . 53 ALA HA H 4.04 0.01 1 269 . 53 ALA HB H 1.55 0.01 1 270 . 54 TYR H H 8.78 0.01 1 271 . 54 TYR HA H 4.16 0.01 1 272 . 54 TYR HB2 H 2.97 0.01 1 273 . 54 TYR HB3 H 3.16 0.01 1 274 . 54 TYR HD1 H 7.01 0.01 1 275 . 54 TYR HD2 H 7.01 0.01 1 276 . 54 TYR HE1 H 6.79 0.01 1 277 . 54 TYR HE2 H 6.79 0.01 1 278 . 55 LEU H H 8.25 0.01 1 279 . 55 LEU HA H 3.95 0.01 1 280 . 55 LEU HB2 H 2.11 0.01 2 281 . 55 LEU HB3 H 1.22 0.01 2 282 . 55 LEU HG H 2.19 0.01 1 283 . 55 LEU HD1 H 1.01 0.01 2 284 . 55 LEU HD2 H 0.79 0.01 2 285 . 56 LYS H H 8.49 0.01 1 286 . 56 LYS HA H 3.79 0.01 1 287 . 56 LYS HB2 H 1.86 0.01 1 288 . 56 LYS HB3 H 1.86 0.01 1 289 . 56 LYS HG2 H 1.33 0.01 1 290 . 56 LYS HG3 H 1.33 0.01 1 291 . 56 LYS HD2 H 1.67 0.01 2 292 . 56 LYS HD3 H 1.55 0.01 2 293 . 56 LYS HE2 H 2.93 0.01 1 294 . 56 LYS HE3 H 2.93 0.01 1 295 . 57 LYS H H 7.80 0.01 1 296 . 57 LYS HA H 3.93 0.01 1 297 . 57 LYS HB2 H 1.88 0.01 1 298 . 57 LYS HB3 H 1.88 0.01 1 299 . 57 LYS HG2 H 1.34 0.01 1 300 . 57 LYS HG3 H 1.34 0.01 1 301 . 57 LYS HD2 H 1.51 0.01 1 302 . 57 LYS HD3 H 1.51 0.01 1 303 . 57 LYS HE2 H 2.97 0.01 1 304 . 57 LYS HE3 H 2.97 0.01 1 305 . 58 GLU H H 7.58 0.01 1 306 . 58 GLU HA H 3.69 0.01 1 307 . 58 GLU HB2 H 1.78 0.01 2 308 . 58 GLU HB3 H 1.71 0.01 2 309 . 58 GLU HG2 H 1.88 0.01 2 310 . 58 GLU HG3 H 1.62 0.01 2 311 . 59 ILE H H 8.45 0.01 1 312 . 59 ILE HA H 3.22 0.01 1 313 . 59 ILE HB H 1.84 0.01 1 314 . 59 ILE HG12 H 1.99 0.01 2 315 . 59 ILE HG13 H 0.66 0.01 2 316 . 59 ILE HG2 H 0.84 0.01 1 317 . 59 ILE HD1 H 0.86 0.01 1 318 . 60 LYS H H 7.91 0.01 1 319 . 60 LYS HA H 3.93 0.01 1 320 . 60 LYS HB2 H 1.90 0.01 2 321 . 60 LYS HB3 H 1.87 0.01 2 322 . 60 LYS HG2 H 1.41 0.01 1 323 . 60 LYS HG3 H 1.41 0.01 1 324 . 60 LYS HD2 H 1.80 0.01 5 325 . 60 LYS HD3 H 1.80 0.01 5 326 . 60 LYS HE2 H 3.03 0.01 5 327 . 60 LYS HE3 H 3.03 0.01 5 328 . 61 LYS H H 7.59 0.01 1 329 . 61 LYS HA H 4.08 0.01 1 330 . 61 LYS HB2 H 1.71 0.01 1 331 . 61 LYS HB3 H 1.71 0.01 1 332 . 61 LYS HG2 H 1.41 0.01 1 333 . 61 LYS HG3 H 1.41 0.01 1 334 . 61 LYS HD2 H 1.53 0.01 5 335 . 61 LYS HD3 H 1.53 0.01 5 336 . 61 LYS HE2 H 2.82 0.01 5 337 . 61 LYS HE3 H 2.82 0.01 5 338 . 62 LYS H H 8.20 0.01 1 339 . 62 LYS HA H 4.41 0.01 1 340 . 62 LYS HB2 H 1.73 0.01 1 341 . 62 LYS HB3 H 1.67 0.01 1 342 . 62 LYS HG2 H 0.88 0.01 1 343 . 62 LYS HG3 H 0.88 0.01 1 344 . 62 LYS HD2 H 1.22 0.01 1 345 . 62 LYS HD3 H 1.22 0.01 1 346 . 62 LYS HE2 H 2.52 0.01 2 347 . 62 LYS HE3 H 2.38 0.01 2 348 . 63 GLY H H 8.27 0.01 1 349 . 63 GLY HA2 H 4.50 0.01 2 350 . 63 GLY HA3 H 3.88 0.01 2 351 . 64 LYS H H 8.67 0.01 1 352 . 64 LYS HA H 3.65 0.01 1 353 . 64 LYS HB2 H 1.84 0.01 1 354 . 64 LYS HB3 H 1.82 0.01 1 355 . 64 LYS HG2 H 1.31 0.01 1 356 . 64 LYS HG3 H 1.45 0.01 1 357 . 64 LYS HD2 H 1.56 0.01 1 358 . 64 LYS HD3 H 1.56 0.01 1 359 . 64 LYS HE2 H 2.92 0.01 1 360 . 64 LYS HE3 H 2.86 0.01 1 361 . 65 ARG H H 8.55 0.01 1 362 . 65 ARG HA H 3.91 0.01 1 363 . 65 ARG HB2 H 1.87 0.01 1 364 . 65 ARG HB3 H 1.81 0.01 1 365 . 65 ARG HG2 H 1.79 0.01 2 366 . 65 ARG HG3 H 1.63 0.01 2 367 . 65 ARG HD2 H 3.23 0.01 1 368 . 65 ARG HD3 H 3.23 0.01 1 369 . 65 ARG HE H 7.25 0.01 1 370 . 66 ALA H H 8.40 0.01 1 371 . 66 ALA HA H 4.28 0.01 1 372 . 66 ALA HB H 1.45 0.01 1 373 . 67 VAL H H 8.06 0.01 1 374 . 67 VAL HA H 3.88 0.01 1 375 . 67 VAL HB H 2.21 0.01 1 376 . 67 VAL HG1 H 0.88 0.01 1 377 . 67 VAL HG2 H 1.18 0.01 1 378 . 68 ILE H H 8.33 0.01 1 379 . 68 ILE HA H 3.63 0.01 1 380 . 68 ILE HB H 2.04 0.01 1 381 . 68 ILE HG12 H 1.93 0.01 1 382 . 68 ILE HG13 H 1.93 0.01 1 383 . 68 ILE HG2 H 0.97 0.01 1 384 . 68 ILE HD1 H 0.88 0.01 1 385 . 69 ALA H H 7.71 0.01 1 386 . 69 ALA HA H 4.24 0.01 1 387 . 69 ALA HB H 1.57 0.01 1 388 . 70 TRP H H 8.38 0.01 1 389 . 70 TRP HA H 4.53 0.01 1 390 . 70 TRP HB2 H 3.69 0.01 1 391 . 70 TRP HB3 H 3.42 0.01 1 392 . 70 TRP HD1 H 7.36 0.01 1 393 . 70 TRP HE1 H 10.31 0.01 1 394 . 70 TRP HE3 H 7.89 0.01 1 395 . 70 TRP HZ2 H 7.68 0.01 1 396 . 70 TRP HZ3 H 6.79 0.01 1 397 . 70 TRP HH2 H 7.37 0.01 1 stop_ save_