data_1673 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Resonance Assignments of Oxidized Flavodoxin from Anacystis nidulans with 3D NMR ; _BMRB_accession_number 1673 _BMRB_flat_file_name bmr1673.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Clubb Robert T. . 2 Thanabal V. . . 3 Osborne C. . . 4 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 552 "15N chemical shifts" 174 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Clubb, Robert T., Thanabal, V., Osborne, C., Wagner, Gerhard, "1H and 15N Resonance Assignments of Oxidized Flavodoxin from Anacystis nidulans with 3D NMR," Biochemistry 30 (31), 7718-7730 (1991). ; _Citation_title ; 1H and 15N Resonance Assignments of Oxidized Flavodoxin from Anacystis nidulans with 3D NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Clubb Robert T. . 2 Thanabal V. . . 3 Osborne C. . . 4 Wagner Gerhard . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue 31 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7718 _Page_last 7730 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_flavodoxin _Saveframe_category molecular_system _Mol_system_name flavodoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label flavodoxin $flavodoxin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_flavodoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common flavodoxin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 169 _Mol_residue_sequence ; AKIGLFYGTQTGVTQTIAQS IQQEFGGESIVDLNDIANAD ASDLNAYDYLIIGCPTWNVG ELQSDWEGIYDDLDSVNFQG KKVAYFGAGDQVGYSDNFQD AMGILEEKISSLGSQTVGYW PIEGYDFNESKAVRNNQFVG LAIDEDNQPDLTKNRIKTWV SQLKSEFGL ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LYS 3 ILE 4 GLY 5 LEU 6 PHE 7 TYR 8 GLY 9 THR 10 GLN 11 THR 12 GLY 13 VAL 14 THR 15 GLN 16 THR 17 ILE 18 ALA 19 GLN 20 SER 21 ILE 22 GLN 23 GLN 24 GLU 25 PHE 26 GLY 27 GLY 28 GLU 29 SER 30 ILE 31 VAL 32 ASP 33 LEU 34 ASN 35 ASP 36 ILE 37 ALA 38 ASN 39 ALA 40 ASP 41 ALA 42 SER 43 ASP 44 LEU 45 ASN 46 ALA 47 TYR 48 ASP 49 TYR 50 LEU 51 ILE 52 ILE 53 GLY 54 CYS 55 PRO 56 THR 57 TRP 58 ASN 59 VAL 60 GLY 61 GLU 62 LEU 63 GLN 64 SER 65 ASP 66 TRP 67 GLU 68 GLY 69 ILE 70 TYR 71 ASP 72 ASP 73 LEU 74 ASP 75 SER 76 VAL 77 ASN 78 PHE 79 GLN 80 GLY 81 LYS 82 LYS 83 VAL 84 ALA 85 TYR 86 PHE 87 GLY 88 ALA 89 GLY 90 ASP 91 GLN 92 VAL 93 GLY 94 TYR 95 SER 96 ASP 97 ASN 98 PHE 99 GLN 100 ASP 101 ALA 102 MET 103 GLY 104 ILE 105 LEU 106 GLU 107 GLU 108 LYS 109 ILE 110 SER 111 SER 112 LEU 113 GLY 114 SER 115 GLN 116 THR 117 VAL 118 GLY 119 TYR 120 TRP 121 PRO 122 ILE 123 GLU 124 GLY 125 TYR 126 ASP 127 PHE 128 ASN 129 GLU 130 SER 131 LYS 132 ALA 133 VAL 134 ARG 135 ASN 136 ASN 137 GLN 138 PHE 139 VAL 140 GLY 141 LEU 142 ALA 143 ILE 144 ASP 145 GLU 146 ASP 147 ASN 148 GLN 149 PRO 150 ASP 151 LEU 152 THR 153 LYS 154 ASN 155 ARG 156 ILE 157 LYS 158 THR 159 TRP 160 VAL 161 SER 162 GLN 163 LEU 164 LYS 165 SER 166 GLU 167 PHE 168 GLY 169 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-26 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 1CZH "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials." 100.00 169 98.82 99.41 1.94e-115 PDB 1CZK "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials" 100.00 169 98.82 100.00 7.76e-116 PDB 1CZL "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials." 100.00 169 99.41 100.00 1.90e-116 PDB 1CZN "Refined Structures Of Oxidized Flavodoxin From Anacystis Nidulans" 100.00 169 99.41 100.00 1.90e-116 PDB 1CZO "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials." 100.00 169 98.82 99.41 1.94e-115 PDB 1CZR "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials" 100.00 169 98.82 100.00 7.76e-116 PDB 1CZU "Refined Structures Of Oxidized Flavodoxin From Anacystis Nidulans" 100.00 169 99.41 100.00 1.90e-116 PDB 1D03 "Refined Structures Of Oxidized Flavodoxin From Anacystis Nidulans" 100.00 169 98.82 99.41 1.94e-115 PDB 1D04 "Comparisons Of Wild Type And Mutant Flavodoxins From Anacystis Nidulans. Structural Determinants Of The Redox Potentials." 100.00 169 99.41 100.00 1.90e-116 PDB 1OFV "Flavodoxin From Anacystis Nidulans: Refinement Of Two Forms Of The Oxidized Protein" 100.00 169 99.41 100.00 1.90e-116 DBJ BAD80716 "flavodoxin [Synechococcus elongatus PCC 6301]" 100.00 170 99.41 100.00 1.58e-116 GB AAA22050 "flavodoxin protein [Synechococcus elongatus PCC 6301]" 100.00 170 99.41 100.00 1.58e-116 GB ABB57571 "Flavodoxin, long chain [Synechococcus elongatus PCC 7942]" 100.00 170 99.41 100.00 1.58e-116 GB AJD57916 "flavodoxin FldA [Synechococcus sp. UTEX 2973]" 100.00 170 99.41 100.00 1.58e-116 PIR A28670 "flavodoxin [validated] - Synechococcus sp" 100.00 170 99.41 100.00 1.58e-116 REF WP_011242314 "MULTISPECIES: flavodoxin [Synechococcus]" 100.00 170 99.41 100.00 1.58e-116 SP P10340 "RecName: Full=Flavodoxin" 100.00 170 99.41 100.00 1.58e-116 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 $flavodoxin . 1140 Bacteria . Anacystis nidulans R2 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 $flavodoxin 'not available' . Escherichia coli W1485 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_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 TSP H . . . 0 . . . . . 'liquid ammonia' N . . . 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name flavodoxin _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 ALA HA H 4.1 . 1 2 . 1 ALA HB H 1.44 . 1 3 . 1 ALA N N 41.8 . 1 4 . 2 LYS H H 8.61 . 1 5 . 2 LYS HA H 4.31 . 1 6 . 2 LYS N N 120.7 . 1 7 . 3 ILE H H 7.61 . 1 8 . 3 ILE HA H 4.56 . 1 9 . 3 ILE N N 119.1 . 1 10 . 4 GLY H H 8.26 . 1 11 . 4 GLY HA2 H 1.61 . 2 12 . 4 GLY HA3 H 3.36 . 2 13 . 4 GLY N N 118.6 . 1 14 . 5 LEU H H 8.65 . 1 15 . 5 LEU N N 131.6 . 1 16 . 6 PHE H H 9.62 . 1 17 . 6 PHE HA H 5.68 . 1 18 . 6 PHE HB2 H 2.83 . 2 19 . 6 PHE HB3 H 3.16 . 2 20 . 6 PHE N N 128.7 . 1 21 . 7 TYR H H 8.52 . 1 22 . 7 TYR HA H 6.45 . 1 23 . 7 TYR HB2 H 2.93 . 2 24 . 7 TYR HB3 H 2.65 . 2 25 . 7 TYR N N 121.9 . 1 26 . 8 GLY H H 7.53 . 1 27 . 8 GLY HA2 H 3.56 . 2 28 . 8 GLY HA3 H 4.89 . 2 29 . 8 GLY N N 118.6 . 1 30 . 9 THR H H 8.92 . 1 31 . 9 THR HA H 5.01 . 1 32 . 9 THR HB H 4.04 . 1 33 . 9 THR HG2 H 1.3 . 1 34 . 9 THR N N 116.3 . 1 35 . 10 GLN H H 10.98 . 1 36 . 10 GLN HA H 4.61 . 1 37 . 10 GLN N N 132.9 . 1 38 . 11 THR H H 9.67 . 1 39 . 11 THR HA H 4.8 . 1 40 . 11 THR HG2 H 1.47 . 1 41 . 11 THR N N 112.4 . 1 42 . 11 THR HG1 H 6.94 . 1 43 . 12 GLY H H 8.29 . 1 44 . 12 GLY HA2 H 3.67 . 2 45 . 12 GLY HA3 H 4.5 . 2 46 . 12 GLY N N 113.5 . 1 47 . 13 VAL H H 10.79 . 1 48 . 13 VAL HA H 3.65 . 1 49 . 13 VAL HB H 2.64 . 1 50 . 13 VAL HG1 H 1.14 . 2 51 . 13 VAL HG2 H .9 . 2 52 . 13 VAL N N 132 . 1 53 . 14 THR H H 11.1 . 1 54 . 14 THR HA H 3.71 . 1 55 . 14 THR HB H 4.31 . 1 56 . 14 THR HG2 H 1.31 . 1 57 . 14 THR N N 121.9 . 1 58 . 15 GLN H H 6.62 . 1 59 . 15 GLN HA H 2.94 . 1 60 . 15 GLN N N 119.9 . 1 61 . 16 THR H H 7.81 . 1 62 . 16 THR HA H 4.41 . 1 63 . 16 THR HB H 4.01 . 1 64 . 16 THR HG2 H 1.31 . 1 65 . 16 THR N N 118.2 . 1 66 . 17 ILE H H 8.32 . 1 67 . 17 ILE HA H 3.49 . 1 68 . 17 ILE N N 124 . 1 69 . 18 ALA H H 8.31 . 1 70 . 18 ALA HA H 3.56 . 1 71 . 18 ALA HB H 1.31 . 1 72 . 18 ALA N N 123.8 . 1 73 . 19 GLN H H 8.24 . 1 74 . 19 GLN HA H 3.76 . 1 75 . 19 GLN N N 118.6 . 1 76 . 20 SER H H 7.9 . 1 77 . 20 SER HA H 4.31 . 1 78 . 20 SER HB2 H 3.89 . 2 79 . 20 SER HB3 H 4.11 . 2 80 . 20 SER N N 119 . 1 81 . 21 ILE H H 8.67 . 1 82 . 21 ILE HA H 3.38 . 1 83 . 21 ILE N N 125.5 . 1 84 . 22 GLN H H 8.41 . 1 85 . 22 GLN HA H 3.71 . 1 86 . 22 GLN N N 120.3 . 1 87 . 23 GLN H H 8.1 . 1 88 . 23 GLN HA H 3.94 . 1 89 . 23 GLN NE2 N 111.1 . 1 90 . 23 GLN HE21 H 7.36 . 2 91 . 23 GLN HE22 H 7.66 . 2 92 . 23 GLN N N 119.6 . 1 93 . 24 GLU H H 8.51 . 1 94 . 24 GLU HA H 4.01 . 1 95 . 24 GLU N N 123.6 . 1 96 . 25 PHE H H 8.06 . 1 97 . 25 PHE HA H 3.91 . 1 98 . 25 PHE HB2 H 1.9 . 2 99 . 25 PHE HB3 H 3.03 . 2 100 . 25 PHE N N 118 . 1 101 . 26 GLY H H 7.59 . 1 102 . 26 GLY HA2 H 3.74 . 2 103 . 26 GLY HA3 H 4.64 . 2 104 . 26 GLY N N 103.9 . 1 105 . 27 GLY H H 8.44 . 1 106 . 27 GLY HA2 H 3.63 . 2 107 . 27 GLY HA3 H 4.66 . 2 108 . 27 GLY N N 110.1 . 1 109 . 28 GLU H H 9.16 . 1 110 . 28 GLU HA H 4.49 . 1 111 . 28 GLU N N 121.1 . 1 112 . 29 SER H H 8.74 . 1 113 . 29 SER HA H 4.36 . 1 114 . 29 SER HB2 H 3.96 . 1 115 . 29 SER HB3 H 3.96 . 1 116 . 29 SER N N 115.3 . 1 117 . 30 ILE H H 7.76 . 1 118 . 30 ILE HA H 4.3 . 1 119 . 30 ILE N N 122.4 . 1 120 . 31 VAL H H 7.51 . 1 121 . 31 VAL HA H 4.61 . 1 122 . 31 VAL N N 119.8 . 1 123 . 32 ASP H H 8.41 . 1 124 . 32 ASP HA H 4.91 . 1 125 . 32 ASP HB2 H 2.41 . 2 126 . 32 ASP HB3 H 2.61 . 2 127 . 32 ASP N N 127.8 . 1 128 . 33 LEU H H 8.66 . 1 129 . 33 LEU HA H 4.6 . 1 130 . 33 LEU N N 125.6 . 1 131 . 34 ASN H H 8.69 . 1 132 . 34 ASN HA H 4.74 . 1 133 . 34 ASN HB2 H 1.95 . 2 134 . 34 ASN HB3 H 3.94 . 2 135 . 34 ASN N N 124.2 . 1 136 . 35 ASP H H 8.42 . 1 137 . 35 ASP HA H 3.55 . 1 138 . 35 ASP HB2 H 2.34 . 2 139 . 35 ASP HB3 H 2.64 . 2 140 . 35 ASP N N 126.1 . 1 141 . 36 ILE H H 9.49 . 1 142 . 36 ILE HA H 3.79 . 1 143 . 36 ILE N N 133.6 . 1 144 . 37 ALA H H 8.57 . 1 145 . 37 ALA HA H 3.83 . 1 146 . 37 ALA HB H 1.14 . 1 147 . 37 ALA N N 125.1 . 1 148 . 38 ASN H H 7.59 . 1 149 . 38 ASN HA H 4.9 . 1 150 . 38 ASN HB2 H 2.58 . 2 151 . 38 ASN HB3 H 3.03 . 2 152 . 38 ASN N N 113.6 . 1 153 . 39 ALA H H 7.17 . 1 154 . 39 ALA HA H 4.57 . 1 155 . 39 ALA HB H 1.53 . 1 156 . 39 ALA N N 124.1 . 1 157 . 40 ASP H H 6.96 . 1 158 . 40 ASP HA H 4.16 . 1 159 . 40 ASP HB2 H 2.26 . 2 160 . 40 ASP HB3 H 2.56 . 2 161 . 40 ASP N N 120.4 . 1 162 . 41 ALA H H 9.06 . 1 163 . 41 ALA HA H 3.65 . 1 164 . 41 ALA HB H 1.14 . 1 165 . 41 ALA N N 127.3 . 1 166 . 42 SER H H 8.16 . 1 167 . 42 SER HA H 3.86 . 1 168 . 42 SER N N 109.3 . 1 169 . 43 ASP H H 8.25 . 1 170 . 43 ASP HA H 4.51 . 1 171 . 43 ASP HB2 H 3.01 . 1 172 . 43 ASP HB3 H 3.01 . 1 173 . 43 ASP N N 126.4 . 1 174 . 44 LEU H H 7.52 . 1 175 . 44 LEU HA H 3.86 . 1 176 . 44 LEU N N 119.8 . 1 177 . 45 ASN H H 7.36 . 1 178 . 45 ASN HA H 4.16 . 1 179 . 45 ASN HB2 H 2.76 . 1 180 . 45 ASN HB3 H 2.76 . 1 181 . 45 ASN N N 113.2 . 1 182 . 46 ALA H H 7.1 . 1 183 . 46 ALA HA H 3.95 . 1 184 . 46 ALA HB H 1.28 . 1 185 . 46 ALA N N 119.8 . 1 186 . 47 TYR H H 6.81 . 1 187 . 47 TYR HA H 4.61 . 1 188 . 47 TYR HB2 H 3.35 . 2 189 . 47 TYR HB3 H 2.58 . 2 190 . 47 TYR N N 115.7 . 1 191 . 48 ASP H H 9.23 . 1 192 . 48 ASP HA H 4.51 . 1 193 . 48 ASP HB2 H 2.04 . 2 194 . 48 ASP HB3 H 2.25 . 2 195 . 48 ASP N N 123.6 . 1 196 . 49 TYR H H 7.09 . 1 197 . 49 TYR HA H 5.34 . 1 198 . 49 TYR HB2 H 2.45 . 2 199 . 49 TYR HB3 H 1.69 . 2 200 . 49 TYR N N 118.3 . 1 201 . 50 LEU H H 8.61 . 1 202 . 50 LEU HA H 5.66 . 1 203 . 50 LEU N N 124.3 . 1 204 . 51 ILE H H 8.87 . 1 205 . 51 ILE HA H 5.04 . 1 206 . 51 ILE N N 119.9 . 1 207 . 52 ILE H H 9.56 . 1 208 . 52 ILE HA H 5.03 . 1 209 . 52 ILE N N 132.3 . 1 210 . 53 GLY H H 9.33 . 1 211 . 53 GLY HA2 H 4.14 . 1 212 . 53 GLY HA3 H 4.14 . 1 213 . 53 GLY N N 114.7 . 1 214 . 54 CYS H H 8.08 . 1 215 . 54 CYS HA H 5.27 . 1 216 . 54 CYS HB2 H 1.53 . 2 217 . 54 CYS HB3 H 2.43 . 2 218 . 54 CYS HG H 2.95 . 1 219 . 54 CYS N N 126.4 . 1 220 . 56 THR H H 7.11 . 1 221 . 56 THR HA H 4.56 . 1 222 . 56 THR HB H 3.56 . 1 223 . 56 THR HG2 H 1.28 . 1 224 . 56 THR N N 113.8 . 1 225 . 57 TRP H H 8.41 . 1 226 . 57 TRP HA H 2.86 . 1 227 . 57 TRP HB2 H 2.06 . 1 228 . 57 TRP HB3 H 2.06 . 1 229 . 57 TRP NE1 N 133.2 . 1 230 . 57 TRP HD1 H 6.38 . 1 231 . 57 TRP HE1 H 11.47 . 1 232 . 57 TRP HE3 H 7 . 1 233 . 57 TRP HZ2 H 8 . 1 234 . 57 TRP HZ3 H 7.08 . 1 235 . 57 TRP HH2 H 7.33 . 1 236 . 57 TRP N N 129.2 . 1 237 . 58 ASN H H 6.41 . 1 238 . 58 ASN HA H 4.87 . 1 239 . 58 ASN HB2 H 2.77 . 2 240 . 58 ASN HB3 H 3.13 . 2 241 . 58 ASN N N 115.5 . 1 242 . 59 VAL H H 8.21 . 1 243 . 59 VAL HA H 3.8 . 1 244 . 59 VAL HB H 2.95 . 1 245 . 59 VAL HG1 H 1.19 . 2 246 . 59 VAL HG2 H 1.02 . 2 247 . 59 VAL N N 113.9 . 1 248 . 60 GLY H H 7.96 . 1 249 . 60 GLY HA2 H 3.67 . 2 250 . 60 GLY HA3 H 4.5 . 2 251 . 60 GLY N N 107.4 . 1 252 . 61 GLU H H 8.54 . 1 253 . 61 GLU HA H 4.61 . 1 254 . 61 GLU N N 119.2 . 1 255 . 62 LEU H H 8.42 . 1 256 . 62 LEU HA H 3.85 . 1 257 . 62 LEU N N 118.9 . 1 258 . 63 GLN H H 5.64 . 1 259 . 63 GLN HA H 4.01 . 1 260 . 63 GLN N N 121.1 . 1 261 . 64 SER H H 8.45 . 1 262 . 64 SER HA H 3.98 . 1 263 . 64 SER HB2 H 3.76 . 1 264 . 64 SER HB3 H 3.76 . 1 265 . 65 ASP H H 7.49 . 1 266 . 65 ASP HA H 4.51 . 1 267 . 65 ASP HB2 H 2.81 . 2 268 . 65 ASP HB3 H 2.14 . 2 269 . 65 ASP N N 120.1 . 1 270 . 66 TRP H H 7.35 . 1 271 . 66 TRP HA H 4.51 . 1 272 . 66 TRP HB2 H 3.27 . 2 273 . 66 TRP HB3 H 3.37 . 2 274 . 66 TRP NE1 N 126.5 . 1 275 . 66 TRP HD1 H 7.45 . 1 276 . 66 TRP HE1 H 9.35 . 1 277 . 66 TRP N N 122.4 . 1 278 . 67 GLU H H 8.41 . 1 279 . 67 GLU HA H 3.96 . 1 280 . 67 GLU N N 121.4 . 1 281 . 68 GLY H H 7.81 . 1 282 . 68 GLY HA2 H 3.86 . 2 283 . 68 GLY HA3 H 4.06 . 2 284 . 68 GLY N N 104.4 . 1 285 . 69 ILE H H 7.15 . 1 286 . 69 ILE HA H 4.63 . 1 287 . 69 ILE N N 118.9 . 1 288 . 70 TYR H H 7.73 . 1 289 . 70 TYR HA H 4.01 . 1 290 . 70 TYR HB2 H 3.41 . 2 291 . 70 TYR HB3 H 3.11 . 2 292 . 70 TYR HD1 H 7.04 . 1 293 . 70 TYR HD2 H 7.04 . 1 294 . 70 TYR N N 125.7 . 1 295 . 71 ASP H H 8.79 . 1 296 . 71 ASP HA H 4.43 . 1 297 . 71 ASP HB2 H 2.79 . 2 298 . 71 ASP HB3 H 2.69 . 2 299 . 71 ASP N N 118.3 . 1 300 . 72 ASP H H 8.02 . 1 301 . 72 ASP HA H 4.78 . 1 302 . 72 ASP HB2 H 2.76 . 2 303 . 72 ASP HB3 H 2.72 . 2 304 . 72 ASP N N 119.9 . 1 305 . 73 LEU H H 7.66 . 1 306 . 73 LEU HA H 3.99 . 1 307 . 73 LEU N N 122.4 . 1 308 . 74 ASP H H 7.78 . 1 309 . 74 ASP HA H 4.49 . 1 310 . 74 ASP HB2 H 2.64 . 1 311 . 74 ASP HB3 H 2.64 . 1 312 . 74 ASP N N 114.7 . 1 313 . 75 SER H H 7.76 . 1 314 . 75 SER HA H 4.41 . 1 315 . 75 SER N N 114.7 . 1 316 . 76 VAL H H 7.81 . 1 317 . 76 VAL HA H 3.61 . 1 318 . 76 VAL HB H 1.94 . 1 319 . 76 VAL HG1 H .68 . 2 320 . 76 VAL HG2 H .33 . 2 321 . 76 VAL N N 128 . 1 322 . 77 ASN H H 8.28 . 1 323 . 77 ASN HA H 4.88 . 1 324 . 77 ASN HB2 H 2.72 . 2 325 . 77 ASN HB3 H 2.97 . 2 326 . 77 ASN N N 124.9 . 1 327 . 78 PHE H H 8.41 . 1 328 . 78 PHE HA H 4.22 . 1 329 . 78 PHE HB2 H 2.54 . 2 330 . 78 PHE HB3 H 3.19 . 2 331 . 78 PHE N N 125.4 . 1 332 . 79 GLN H H 8.02 . 1 333 . 79 GLN HA H 3.96 . 1 334 . 79 GLN N N 121.6 . 1 335 . 80 GLY H H 8.46 . 1 336 . 80 GLY HA2 H 3.84 . 2 337 . 80 GLY HA3 H 4.27 . 2 338 . 80 GLY N N 115.2 . 1 339 . 81 LYS H H 7.98 . 1 340 . 81 LYS HA H 4.61 . 1 341 . 81 LYS N N 121.3 . 1 342 . 82 LYS H H 7.98 . 1 343 . 82 LYS HA H 5.46 . 1 344 . 82 LYS N N 124.8 . 1 345 . 83 VAL H H 8.61 . 1 346 . 83 VAL HA H 5.09 . 1 347 . 83 VAL HB H 2.03 . 1 348 . 83 VAL HG1 H .87 . 1 349 . 83 VAL HG2 H .87 . 1 350 . 83 VAL N N 125.3 . 1 351 . 84 ALA H H 8.8 . 1 352 . 84 ALA HA H 5.64 . 1 353 . 84 ALA HB H 1.53 . 1 354 . 84 ALA N N 130.5 . 1 355 . 85 TYR H H 11.08 . 1 356 . 85 TYR HA H 5.6 . 1 357 . 85 TYR HB2 H 2.6 . 2 358 . 85 TYR HB3 H 2.47 . 2 359 . 85 TYR N N 121 . 1 360 . 86 PHE H H 8.84 . 1 361 . 86 PHE HA H 5.11 . 1 362 . 86 PHE HB2 H 2.39 . 2 363 . 86 PHE HB3 H 2.55 . 2 364 . 86 PHE N N 113.5 . 1 365 . 87 GLY H H 8.08 . 1 366 . 87 GLY HA2 H 3.59 . 2 367 . 87 GLY HA3 H 4 . 2 368 . 87 GLY N N 107 . 1 369 . 88 ALA H H 6.05 . 1 370 . 88 ALA HA H 5.42 . 1 371 . 88 ALA HB H 1.47 . 1 372 . 88 ALA N N 125 . 1 373 . 89 GLY H H 7.8 . 1 374 . 89 GLY HA2 H 3.98 . 2 375 . 89 GLY HA3 H 5.41 . 2 376 . 89 GLY N N 107.1 . 1 377 . 90 ASP H H 8.41 . 1 378 . 90 ASP HA H 4.91 . 1 379 . 90 ASP HB2 H 2.61 . 2 380 . 90 ASP HB3 H 2.41 . 2 381 . 90 ASP N N 121.5 . 1 382 . 91 GLN H H 8.79 . 1 383 . 91 GLN HA H 3.42 . 1 384 . 91 GLN NE2 N 111.5 . 1 385 . 91 GLN HE21 H 6.29 . 2 386 . 91 GLN HE22 H 9.4 . 2 387 . 91 GLN N N 123.8 . 1 388 . 92 VAL H H 7.4 . 1 389 . 92 VAL HA H 3.79 . 1 390 . 92 VAL HG1 H .84 . 2 391 . 92 VAL HG2 H 1.86 . 2 392 . 92 VAL N N 121.4 . 1 393 . 93 GLY H H 9.23 . 1 394 . 93 GLY HA2 H 3.09 . 2 395 . 93 GLY HA3 H 3.48 . 2 396 . 93 GLY N N 110.1 . 1 397 . 94 TYR H H 6.83 . 1 398 . 94 TYR HA H 4.61 . 1 399 . 94 TYR HB2 H 2.71 . 2 400 . 94 TYR HB3 H 2.57 . 2 401 . 94 TYR N N 118.9 . 1 402 . 95 SER H H 7.36 . 1 403 . 95 SER HA H 4.26 . 1 404 . 95 SER HB2 H 3.96 . 1 405 . 95 SER HB3 H 3.96 . 1 406 . 95 SER N N 114.8 . 1 407 . 96 ASP H H 8.39 . 1 408 . 96 ASP HA H 5.06 . 1 409 . 96 ASP HB2 H 2.9 . 2 410 . 96 ASP HB3 H 2.58 . 2 411 . 96 ASP N N 119 . 1 412 . 97 ASN H H 7.96 . 1 413 . 97 ASN HA H 5.45 . 1 414 . 97 ASN HB2 H 2.11 . 2 415 . 97 ASN HB3 H 3.27 . 2 416 . 97 ASN ND2 N 111.6 . 1 417 . 97 ASN HD21 H 6.66 . 2 418 . 97 ASN HD22 H 8.34 . 2 419 . 97 ASN N N 121.6 . 1 420 . 98 PHE H H 7.85 . 1 421 . 98 PHE HA H 5.31 . 1 422 . 98 PHE HB2 H 2.69 . 2 423 . 98 PHE HB3 H 3.4 . 2 424 . 98 PHE N N 127.1 . 1 425 . 99 GLN H H 7.94 . 1 426 . 99 GLN HA H 3.54 . 1 427 . 99 GLN HB2 H 1.34 . 1 428 . 99 GLN HB3 H 1.34 . 1 429 . 99 GLN N N 118.2 . 1 430 . 100 ASP H H 6.96 . 1 431 . 100 ASP HA H 4.16 . 1 432 . 100 ASP HB2 H 2.56 . 2 433 . 100 ASP HB3 H 2.29 . 2 434 . 100 ASP N N 118.4 . 1 435 . 101 ALA H H 8.95 . 1 436 . 101 ALA HA H 3.69 . 1 437 . 101 ALA HB H 1.31 . 1 438 . 101 ALA N N 119.9 . 1 439 . 102 MET H H 6.92 . 1 440 . 102 MET HA H 3.8 . 1 441 . 102 MET N N 115.9 . 1 442 . 103 GLY H H 6.98 . 1 443 . 103 GLY HA2 H 3.38 . 2 444 . 103 GLY HA3 H 3.59 . 2 445 . 103 GLY N N 104.6 . 1 446 . 104 ILE H H 8.2 . 1 447 . 104 ILE HA H 3.69 . 1 448 . 104 ILE N N 126 . 1 449 . 105 LEU H H 7.86 . 1 450 . 105 LEU HA H 3.96 . 1 451 . 105 LEU HB2 H .96 . 2 452 . 105 LEU HB3 H 1.46 . 2 453 . 105 LEU HG H 1.61 . 1 454 . 105 LEU HD1 H .24 . 2 455 . 105 LEU HD2 H .61 . 2 456 . 105 LEU N N 121 . 1 457 . 106 GLU H H 7.68 . 1 458 . 106 GLU HA H 3.82 . 1 459 . 106 GLU N N 121.4 . 1 460 . 107 GLU H H 8.05 . 1 461 . 107 GLU HA H 3.73 . 1 462 . 107 GLU N N 121.8 . 1 463 . 108 LYS H H 7.21 . 1 464 . 108 LYS HA H 4.14 . 1 465 . 108 LYS N N 119.2 . 1 466 . 109 ILE H H 8.74 . 1 467 . 109 ILE HA H 3.01 . 1 468 . 109 ILE N N 123.3 . 1 469 . 110 SER H H 9.02 . 1 470 . 110 SER HA H 4.3 . 1 471 . 110 SER HB2 H 3.92 . 1 472 . 110 SER HB3 H 3.92 . 1 473 . 110 SER N N 120.8 . 1 474 . 111 SER H H 7.41 . 1 475 . 111 SER HA H 4.47 . 1 476 . 111 SER HB2 H 4.12 . 2 477 . 111 SER HB3 H 4.2 . 2 478 . 111 SER N N 121.5 . 1 479 . 112 LEU H H 7.21 . 1 480 . 112 LEU HA H 4.63 . 1 481 . 112 LEU N N 123.4 . 1 482 . 113 GLY H H 7.81 . 1 483 . 113 GLY HA2 H 3.9 . 2 484 . 113 GLY HA3 H 4.46 . 2 485 . 113 GLY N N 106.7 . 1 486 . 114 SER H H 7 . 1 487 . 114 SER HA H 4.84 . 1 488 . 114 SER HB2 H 3.76 . 2 489 . 114 SER HB3 H 3.92 . 2 490 . 114 SER N N 115.7 . 1 491 . 115 GLN H H 8.66 . 1 492 . 115 GLN HA H 4.76 . 1 493 . 115 GLN N N 122.5 . 1 494 . 116 THR H H 8.82 . 1 495 . 116 THR HA H 5.29 . 1 496 . 116 THR HB H 4.24 . 1 497 . 116 THR N N 128.1 . 1 498 . 117 VAL H H 8.22 . 1 499 . 117 VAL HA H 4.67 . 1 500 . 117 VAL HB H 2.11 . 1 501 . 117 VAL HG1 H .56 . 2 502 . 117 VAL HG2 H .96 . 2 503 . 117 VAL N N 123.6 . 1 504 . 118 GLY H H 9.13 . 1 505 . 118 GLY HA2 H 3.82 . 2 506 . 118 GLY HA3 H 4.69 . 2 507 . 118 GLY N N 109.1 . 1 508 . 119 TYR H H 7.31 . 1 509 . 119 TYR HA H 4.42 . 1 510 . 119 TYR HB2 H 2.95 . 2 511 . 119 TYR HB3 H 2.82 . 2 512 . 119 TYR N N 117.7 . 1 513 . 120 TRP H H 8.78 . 1 514 . 120 TRP HA H 5.93 . 1 515 . 120 TRP HB2 H 3.06 . 2 516 . 120 TRP HB3 H 3.37 . 2 517 . 120 TRP NE1 N 129.6 . 1 518 . 120 TRP HD1 H 7.26 . 1 519 . 120 TRP HE1 H 10.32 . 1 520 . 120 TRP HE3 H 8.25 . 1 521 . 120 TRP HZ2 H 7.58 . 1 522 . 120 TRP HZ3 H 7.27 . 1 523 . 120 TRP HH2 H 7.4 . 1 524 . 120 TRP N N 126.5 . 1 525 . 122 ILE H H 7.63 . 1 526 . 122 ILE HA H 4.59 . 1 527 . 122 ILE N N 114.5 . 1 528 . 123 GLU H H 7.36 . 1 529 . 123 GLU HA H 4.26 . 1 530 . 123 GLU N N 124.7 . 1 531 . 124 GLY H H 9.11 . 1 532 . 124 GLY HA2 H 3.63 . 2 533 . 124 GLY HA3 H 4.13 . 2 534 . 124 GLY N N 113.4 . 1 535 . 125 TYR H H 7.63 . 1 536 . 125 TYR HA H 5.09 . 1 537 . 125 TYR HB2 H 3.3 . 2 538 . 125 TYR HB3 H 2.99 . 2 539 . 125 TYR N N 118.1 . 1 540 . 126 ASP H H 9.27 . 1 541 . 126 ASP HA H 4.97 . 1 542 . 126 ASP HB2 H 2.67 . 2 543 . 126 ASP HB3 H 2.43 . 2 544 . 126 ASP N N 125.1 . 1 545 . 127 PHE H H 7.54 . 1 546 . 127 PHE HA H 4.89 . 1 547 . 127 PHE HB2 H 2.94 . 2 548 . 127 PHE HB3 H 3.31 . 2 549 . 127 PHE N N 118.7 . 1 550 . 128 ASN H H 9.04 . 1 551 . 128 ASN HA H 4.79 . 1 552 . 128 ASN N N 120.8 . 1 553 . 129 GLU H H 8.9 . 1 554 . 129 GLU HA H 4.83 . 1 555 . 129 GLU N N 119.9 . 1 556 . 130 SER H H 8.37 . 1 557 . 130 SER HA H 4.86 . 1 558 . 130 SER HB2 H 3.42 . 2 559 . 130 SER HB3 H 3.96 . 2 560 . 130 SER N N 113.7 . 1 561 . 130 SER HG H 5.94 . 1 562 . 131 LYS H H 9.24 . 1 563 . 131 LYS HA H 4.43 . 1 564 . 131 LYS N N 129.4 . 1 565 . 132 ALA H H 8.81 . 1 566 . 132 ALA HA H 4.19 . 1 567 . 132 ALA HB H 1.41 . 1 568 . 132 ALA N N 121.2 . 1 569 . 133 VAL H H 6.83 . 1 570 . 133 VAL HA H 4.65 . 1 571 . 133 VAL HB H 1.92 . 1 572 . 133 VAL HG1 H .5 . 2 573 . 133 VAL HG2 H .76 . 2 574 . 133 VAL N N 119.4 . 1 575 . 134 ARG H H 9.19 . 1 576 . 134 ARG HA H 4.57 . 1 577 . 134 ARG N N 129.4 . 1 578 . 135 ASN H H 9.36 . 1 579 . 135 ASN HA H 4.22 . 1 580 . 135 ASN HB2 H 2.74 . 2 581 . 135 ASN HB3 H 2.93 . 2 582 . 135 ASN N N 126.5 . 1 583 . 136 ASN H H 8.54 . 1 584 . 136 ASN HA H 4.21 . 1 585 . 136 ASN HB2 H 2.84 . 2 586 . 136 ASN HB3 H 3.04 . 2 587 . 136 ASN N N 114.1 . 1 588 . 137 GLN H H 7.65 . 1 589 . 137 GLN HA H 4.77 . 1 590 . 137 GLN NE2 N 111.3 . 1 591 . 137 GLN HE21 H 6.49 . 2 592 . 137 GLN HE22 H 7.14 . 2 593 . 137 GLN N N 116.9 . 1 594 . 138 PHE H H 9.82 . 1 595 . 138 PHE HA H 5.22 . 1 596 . 138 PHE HB2 H 3.33 . 2 597 . 138 PHE HB3 H 3.58 . 2 598 . 138 PHE N N 121.1 . 1 599 . 139 VAL H H 8.46 . 1 600 . 139 VAL HA H 3.96 . 1 601 . 139 VAL N N 113.4 . 1 602 . 140 GLY H H 6.64 . 1 603 . 140 GLY HA2 H 4.51 . 2 604 . 140 GLY HA3 H 4.61 . 2 605 . 140 GLY N N 104.4 . 1 606 . 141 LEU H H 7.08 . 1 607 . 141 LEU HA H 2.53 . 1 608 . 141 LEU N N 119 . 1 609 . 142 ALA H H 5.24 . 1 610 . 142 ALA HA H 3.99 . 1 611 . 142 ALA HB H 0 . 1 612 . 142 ALA N N 129 . 1 613 . 143 ILE H H 8.78 . 1 614 . 143 ILE HA H 4.33 . 1 615 . 143 ILE N N 128.4 . 1 616 . 144 ASP H H 8.16 . 1 617 . 144 ASP HA H 5.66 . 1 618 . 144 ASP HB2 H 3.06 . 2 619 . 144 ASP HB3 H 2.57 . 2 620 . 144 ASP N N 126.1 . 1 621 . 145 GLU H H 9.69 . 1 622 . 145 GLU HA H 4.24 . 1 623 . 145 GLU N N 129 . 1 624 . 146 ASP H H 8.21 . 1 625 . 146 ASP HA H 4.61 . 1 626 . 146 ASP HB2 H 2.89 . 2 627 . 146 ASP HB3 H 2.59 . 2 628 . 146 ASP N N 121.9 . 1 629 . 147 ASN H H 9.26 . 1 630 . 147 ASN HA H 5.01 . 1 631 . 147 ASN HB2 H 2.41 . 2 632 . 147 ASN HB3 H 2.86 . 2 633 . 147 ASN ND2 N 126.6 . 1 634 . 147 ASN HD21 H 8.32 . 2 635 . 147 ASN HD22 H 9.95 . 2 636 . 147 ASN N N 114.5 . 1 637 . 148 GLN H H 7.84 . 1 638 . 148 GLN HA H 5.17 . 1 639 . 148 GLN N N 117.8 . 1 640 . 150 ASP H H 9.26 . 1 641 . 150 ASP HA H 4.48 . 1 642 . 150 ASP HB2 H 2.77 . 2 643 . 150 ASP HB3 H 2.69 . 2 644 . 150 ASP N N 118.7 . 1 645 . 151 LEU H H 8.39 . 1 646 . 151 LEU HA H 4.89 . 1 647 . 151 LEU N N 118.6 . 1 648 . 152 THR H H 7.38 . 1 649 . 152 THR HA H 4.32 . 1 650 . 152 THR HB H 3.56 . 1 651 . 152 THR HG2 H 1.15 . 1 652 . 152 THR N N 119.8 . 1 653 . 153 LYS H H 8.96 . 1 654 . 153 LYS HA H 3.89 . 1 655 . 153 LYS N N 122.4 . 1 656 . 154 ASN H H 8.77 . 1 657 . 154 ASN HA H 4.57 . 1 658 . 154 ASN HB2 H 2.69 . 2 659 . 154 ASN HB3 H 2.79 . 2 660 . 154 ASN N N 118.8 . 1 661 . 155 ARG H H 8.24 . 1 662 . 155 ARG HA H 4.24 . 1 663 . 155 ARG N N 123.6 . 1 664 . 156 ILE H H 8.28 . 1 665 . 156 ILE HA H 3.36 . 1 666 . 156 ILE N N 118.5 . 1 667 . 157 LYS H H 8.05 . 1 668 . 157 LYS HA H 3.65 . 1 669 . 157 LYS N N 119.5 . 1 670 . 158 THR H H 8.34 . 1 671 . 158 THR HA H 4.03 . 1 672 . 158 THR HB H 4.66 . 1 673 . 158 THR HG2 H 1.63 . 1 674 . 158 THR N N 117.8 . 1 675 . 159 TRP H H 8.83 . 1 676 . 159 TRP HA H 4.46 . 1 677 . 159 TRP HB2 H 2.71 . 2 678 . 159 TRP HB3 H 2.96 . 2 679 . 159 TRP NE1 N 134.6 . 1 680 . 159 TRP HD1 H 7.53 . 1 681 . 159 TRP HE1 H 11.41 . 1 682 . 159 TRP HE3 H 6.95 . 1 683 . 159 TRP HZ2 H 8.33 . 1 684 . 159 TRP HZ3 H 6.56 . 1 685 . 159 TRP HH2 H 6.78 . 1 686 . 159 TRP N N 126.9 . 1 687 . 160 VAL H H 8.9 . 1 688 . 160 VAL HA H 3.52 . 1 689 . 160 VAL HB H 1.86 . 1 690 . 160 VAL HG1 H .26 . 2 691 . 160 VAL HG2 H .95 . 2 692 . 160 VAL N N 118.4 . 1 693 . 161 SER H H 7.46 . 1 694 . 161 SER HA H 4.03 . 1 695 . 161 SER HB2 H 3.98 . 1 696 . 161 SER HB3 H 3.98 . 1 697 . 161 SER N N 114.6 . 1 698 . 162 GLN H H 7.56 . 1 699 . 162 GLN HA H 4.18 . 1 700 . 162 GLN N N 123.1 . 1 701 . 163 LEU H H 8.36 . 1 702 . 163 LEU HA H 3.51 . 1 703 . 163 LEU N N 122.3 . 1 704 . 164 LYS H H 8.31 . 1 705 . 164 LYS HA H 3.83 . 1 706 . 164 LYS N N 119.4 . 1 707 . 165 SER H H 7.28 . 1 708 . 165 SER HA H 3.83 . 1 709 . 165 SER HB2 H 1.29 . 2 710 . 165 SER HB3 H 1.84 . 2 711 . 165 SER N N 113 . 1 712 . 166 GLU H H 7.96 . 1 713 . 166 GLU HA H 4.25 . 1 714 . 166 GLU N N 123.1 . 1 715 . 167 PHE H H 8.49 . 1 716 . 167 PHE HA H 4.49 . 1 717 . 167 PHE HB2 H 2.83 . 2 718 . 167 PHE HB3 H 2.86 . 2 719 . 167 PHE N N 117.7 . 1 720 . 168 GLY H H 7.56 . 1 721 . 168 GLY HA2 H 3.96 . 2 722 . 168 GLY HA3 H 4.06 . 2 723 . 168 GLY N N 108.4 . 1 724 . 169 LEU H H 7.9 . 1 725 . 169 LEU HA H 4.29 . 1 726 . 169 LEU N N 127.6 . 1 stop_ save_