data_4940 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignment of the honeybee pheromone carrier protein ASP1 ; _BMRB_accession_number 4940 _BMRB_flat_file_name bmr4940.str _Entry_type original _Submission_date 2001-01-17 _Accession_date 2001-01-17 _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 Birlirakis Nicolas . . 2 Briand Loic . . 3 Pernollet Jean-Claude . . 4 Guittet Eric . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 562 "13C chemical shifts" 386 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-06-29 original BMRB . stop_ _Original_release_date 2001-01-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N chemical shift assignment of the honeybee pheromone carrier protein ASP1 ; _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 Birlirakis Nicolas . . 2 Briand Loic . . 3 Pernollet Jean-Claude . . 4 Guittet Eric . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 20 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183 _Page_last 184 _Year 2001 _Details . loop_ _Keyword 'Apis mellifera L.' Insect Olfaction 'Pheromone-binding protein.' stop_ save_ ################################## # Molecular system description # ################################## save_system_ASP1 _Saveframe_category molecular_system _Mol_system_name 'Antennal Specific Protein 1' _Abbreviation_common ASP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ASP1 $ASP1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Honeybee pheromone carrier protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ASP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Antennal Specific Protein 1' _Abbreviation_common ASP1 _Molecular_mass 13180 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; APDWVPPEVFDLVAEDKARC MSEHGTTQAQIDDVDKGNLV NEPSITCYMYCLLEAFSLVD DEANVDEDIMLGLLPDQLQE RAQSVMGKCLPTSGSDNCNK IYNLAKCVQESAPDVWFVI ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PRO 3 ASP 4 TRP 5 VAL 6 PRO 7 PRO 8 GLU 9 VAL 10 PHE 11 ASP 12 LEU 13 VAL 14 ALA 15 GLU 16 ASP 17 LYS 18 ALA 19 ARG 20 CYS 21 MET 22 SER 23 GLU 24 HIS 25 GLY 26 THR 27 THR 28 GLN 29 ALA 30 GLN 31 ILE 32 ASP 33 ASP 34 VAL 35 ASP 36 LYS 37 GLY 38 ASN 39 LEU 40 VAL 41 ASN 42 GLU 43 PRO 44 SER 45 ILE 46 THR 47 CYS 48 TYR 49 MET 50 TYR 51 CYS 52 LEU 53 LEU 54 GLU 55 ALA 56 PHE 57 SER 58 LEU 59 VAL 60 ASP 61 ASP 62 GLU 63 ALA 64 ASN 65 VAL 66 ASP 67 GLU 68 ASP 69 ILE 70 MET 71 LEU 72 GLY 73 LEU 74 LEU 75 PRO 76 ASP 77 GLN 78 LEU 79 GLN 80 GLU 81 ARG 82 ALA 83 GLN 84 SER 85 VAL 86 MET 87 GLY 88 LYS 89 CYS 90 LEU 91 PRO 92 THR 93 SER 94 GLY 95 SER 96 ASP 97 ASN 98 CYS 99 ASN 100 LYS 101 ILE 102 TYR 103 ASN 104 LEU 105 ALA 106 LYS 107 CYS 108 VAL 109 GLN 110 GLU 111 SER 112 ALA 113 PRO 114 ASP 115 VAL 116 TRP 117 PHE 118 VAL 119 ILE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 2H8V 'Structure Of Empty Pheromone Binding Protein Asp1 From The Honeybee Apis Mellifera L' 100.00 119 100.00 100.00 4.97e-64 PDB 3BFA 'Crystal Structure Of A Pheromone Binding Protein From Apis Mellifera In Complex With The Queen Mandibular Pheromone' 100.00 119 100.00 100.00 4.97e-64 PDB 3BFB 'Crystal Structure Of A Pheromone Binding Protein From Apis Mellifera In Complex With The 9-Keto-2(E)-Decenoic Acid' 100.00 119 100.00 100.00 4.97e-64 PDB 3BFH 'Crystal Structure Of A Pheromone Binding Protein From Apis Mellifera In Complex With Hexadecanoic Acid' 100.00 119 100.00 100.00 4.97e-64 PDB 3BJH 'Soft-Sad Crystal Structure Of A Pheromone Binding Protein From The Honeybee Apis Mellifera L.' 100.00 119 100.00 100.00 4.97e-64 PDB 3CAB 'Crystal Structure Of A Pheromone Binding Protein From Apis Mellifera Soaked At Ph 7.0' 100.00 119 100.00 100.00 4.97e-64 PDB 3CDN 'Crystal Structure Of A Pheromone Binding Protein From Apis Mellifera Soaked At Ph 4.0' 100.00 119 100.00 100.00 4.97e-64 GenBank AAD51944 'pheromone-binding protein ASP1 [Apis mellifera]' 100.00 144 100.00 100.00 1.22e-64 GenBank AAL60419 'odorant binding protein ASP1 [Apis mellifera]' 100.00 144 100.00 100.00 1.17e-64 REF NP_001011590 'odorant binding protein ASP1 [Apis mellifera]' 100.00 144 100.00 100.00 1.17e-64 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $ASP1 Honeybee 7460 Eukaryota Metazoa Apis 'mellifera lingustica' Antenne 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 $ASP1 'recombinant technology' 'Pichia pastoris' . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ASP1 . mM 1.0 1.5 . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ASP1 . mM 1.0 1.5 '[U-95% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ASP1 . mM 1.0 1.5 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR_(Bruker) _Saveframe_category software _Name 'XWINNMR (Bruker)' _Version 2.6 _Details . save_ save_FELIX_(MSI) _Saveframe_category software _Name 'FELIX (MSI)' _Version 98 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_For_DRX800:_TXI_x/y/z_gradient_probe_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'For DRX800: TXI x/y/z gradient probe' _Sample_label . save_ save_For_DRX500:_TXI_z_gradient_cryoprobe_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'For DRX500: TXI z gradient cryoprobe' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.1 n/a temperature 295 0.1 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 _Indirect_shift_ratio TSP C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0.0 external direct . . . . TSP N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 'For DRX800: TXI x/y/z gradient probe' 'For DRX500: TXI z gradient cryoprobe' stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ASP1 _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 3.99 . 1 2 . 1 ALA HB H 1.04 . 1 3 . 1 ALA C C 171.37 . 1 4 . 1 ALA CA C 50.38 . 1 5 . 1 ALA CB C 16.77 . 1 6 . 2 PRO HA H 4.32 . 1 7 . 2 PRO HB2 H 2.10 . 1 8 . 2 PRO HB3 H 2.10 . 1 9 . 2 PRO HG2 H 2.48 . 1 10 . 2 PRO HG3 H 2.48 . 1 11 . 2 PRO HD2 H 4.33 . 2 12 . 2 PRO HD3 H 3.47 . 2 13 . 2 PRO C C 176.99 . 1 14 . 2 PRO CA C 62.35 . 1 15 . 2 PRO CB C 31.90 . 1 16 . 2 PRO CD C 51.16 . 1 17 . 3 ASP H H 8.7 . 1 18 . 3 ASP HA H 4.17 . 1 19 . 3 ASP HB2 H 2.77 . 2 20 . 3 ASP HB3 H 2.71 . 2 21 . 3 ASP C C 176.21 . 1 22 . 3 ASP CA C 56.13 . 1 23 . 3 ASP CB C 40.01 . 1 24 . 3 ASP N N 120.1 . 1 25 . 4 TRP H H 6.79 . 1 26 . 4 TRP HA H 4.51 . 1 27 . 4 TRP HB2 H 3.61 . 2 28 . 4 TRP HB3 H 3.12 . 2 29 . 4 TRP C C 176.20 . 1 30 . 4 TRP CA C 54.63 . 1 31 . 4 TRP CB C 28.33 . 1 32 . 4 TRP N N 113.02 . 1 33 . 5 VAL H H 6.90 . 1 34 . 5 VAL HA H 3.81 . 1 35 . 5 VAL HB H 1.52 . 1 36 . 5 VAL HG1 H -0.61 . 2 37 . 5 VAL HG2 H 0.30 . 2 38 . 5 VAL C C 173.36 . 1 39 . 5 VAL CA C 60.74 . 1 40 . 5 VAL CB C 31.18 . 1 41 . 5 VAL CG1 C 21.34 . 2 42 . 5 VAL CG2 C 20.82 . 2 43 . 5 VAL N N 123.95 . 1 44 . 6 PRO HA H 4.74 . 1 45 . 6 PRO HB2 H 2.47 . 2 46 . 6 PRO HB3 H 2.09 . 2 47 . 6 PRO C C 175.68 . 1 48 . 6 PRO CA C 61.57 . 1 49 . 6 PRO CB C 31.52 . 1 50 . 7 PRO HA H 4.28 . 1 51 . 7 PRO HB2 H 2.40 . 2 52 . 7 PRO HB3 H 1.98 . 2 53 . 7 PRO HG2 H 2.15 . 2 54 . 7 PRO HG3 H 2.07 . 2 55 . 7 PRO HD2 H 3.90 . 1 56 . 7 PRO HD3 H 3.90 . 1 57 . 7 PRO C C 179.16 . 1 58 . 7 PRO CA C 64.99 . 1 59 . 7 PRO CB C 31.88 . 1 60 . 7 PRO CG C 27.52 . 1 61 . 7 PRO CD C 50.68 . 1 62 . 8 GLU H H 9.18 . 1 63 . 8 GLU HA H 4.24 . 1 64 . 8 GLU HB2 H 2.10 . 1 65 . 8 GLU HB3 H 2.10 . 1 66 . 8 GLU HG2 H 2.42 . 2 67 . 8 GLU HG3 H 2.38 . 2 68 . 8 GLU C C 178.88 . 1 69 . 8 GLU CA C 59.31 . 1 70 . 8 GLU CB C 28.50 . 1 71 . 8 GLU CG C 35.50 . 1 72 . 8 GLU N N 116.31 . 1 73 . 10 PHE HA H 4.36 . 1 74 . 10 PHE HB2 H 3.08 . 2 75 . 10 PHE HB3 H 2.95 . 2 76 . 10 PHE C C 176.4 . 1 77 . 10 PHE CA C 58.25 . 1 78 . 10 PHE CB C 39.28 . 1 79 . 11 ASP H H 7.28 . 1 80 . 11 ASP HA H 4.61 . 1 81 . 11 ASP HB2 H 2.75 . 1 82 . 11 ASP HB3 H 2.75 . 1 83 . 11 ASP C C 178.56 . 1 84 . 11 ASP CA C 56.61 . 1 85 . 11 ASP CB C 40.14 . 1 86 . 11 ASP N N 113.46 . 1 87 . 12 LEU H H 7.95 . 1 88 . 12 LEU HA H 4.24 . 1 89 . 12 LEU HB2 H 1.74 . 1 90 . 12 LEU HB3 H 1.74 . 1 91 . 12 LEU HG H 1.72 . 1 92 . 12 LEU HD1 H 0.92 . 2 93 . 12 LEU HD2 H 0.86 . 2 94 . 12 LEU C C 179.86 . 1 95 . 12 LEU CA C 58.02 . 1 96 . 12 LEU CB C 42.55 . 1 97 . 12 LEU N N 121.16 . 1 98 . 13 VAL H H 7.77 . 1 99 . 13 VAL HA H 4.58 . 1 100 . 13 VAL HB H 2.39 . 1 101 . 13 VAL HG1 H 0.90 . 2 102 . 13 VAL HG2 H 0.70 . 2 103 . 13 VAL C C 176.11 . 1 104 . 13 VAL CA C 61.61 . 1 105 . 13 VAL CB C 32.90 . 1 106 . 13 VAL CG1 C 19.80 . 2 107 . 13 VAL CG2 C 20.93 . 2 108 . 13 VAL N N 108.99 . 1 109 . 14 ALA H H 7.19 . 1 110 . 14 ALA HA H 4.02 . 1 111 . 14 ALA HB H 1.63 . 1 112 . 14 ALA C C 180.22 . 1 113 . 14 ALA CA C 56.75 . 1 114 . 14 ALA CB C 18.92 . 1 115 . 14 ALA N N 122.44 . 1 116 . 15 GLU H H 8.80 . 1 117 . 15 GLU HA H 4.18 . 1 118 . 15 GLU HB2 H 2.18 . 1 119 . 15 GLU HB3 H 2.18 . 1 120 . 15 GLU HG2 H 2.44 . 2 121 . 15 GLU HG3 H 2.35 . 2 122 . 15 GLU C C 179.65 . 1 123 . 15 GLU CA C 60.11 . 1 124 . 15 GLU CB C 28.90 . 1 125 . 15 GLU CG C 35.24 . 1 126 . 15 GLU N N 119.03 . 1 127 . 16 ASP H H 9.01 . 1 128 . 16 ASP HA H 4.50 . 1 129 . 16 ASP HB2 H 2.59 . 2 130 . 16 ASP HB3 H 2.28 . 2 131 . 16 ASP C C 177.57 . 1 132 . 16 ASP CA C 57.92 . 1 133 . 16 ASP CB C 41.13 . 1 134 . 16 ASP N N 121.41 . 1 135 . 17 LYS H H 9.40 . 1 136 . 17 LYS HA H 4.05 . 1 137 . 17 LYS HB2 H 2.11 . 2 138 . 17 LYS HB3 H 1.68 . 2 139 . 17 LYS C C 177.93 . 1 140 . 17 LYS CA C 60.04 . 1 141 . 17 LYS CB C 32.98 . 1 142 . 17 LYS N N 121.77 . 1 143 . 18 ALA H H 8.02 . 1 144 . 18 ALA HA H 4.18 . 1 145 . 18 ALA HB H 1.57 . 1 146 . 18 ALA C C 181.08 . 1 147 . 18 ALA CA C 55.34 . 1 148 . 18 ALA CB C 17.71 . 1 149 . 18 ALA N N 120.74 . 1 150 . 19 ARG H H 8.10 . 1 151 . 19 ARG HA H 4.15 . 1 152 . 19 ARG HB2 H 2.06 . 2 153 . 19 ARG HB3 H 1.92 . 2 154 . 19 ARG HG2 H 1.62 . 1 155 . 19 ARG HG3 H 1.62 . 1 156 . 19 ARG HD2 H 3.34 . 2 157 . 19 ARG HD3 H 3.16 . 2 158 . 19 ARG C C 179.00 . 1 159 . 19 ARG CA C 59.80 . 1 160 . 19 ARG CB C 29.92 . 1 161 . 19 ARG N N 120.07 . 1 162 . 20 CYS H H 9.15 . 1 163 . 20 CYS HA H 4.61 . 1 164 . 20 CYS HB2 H 3.23 . 2 165 . 20 CYS HB3 H 3.03 . 2 166 . 20 CYS C C 177.92 . 1 167 . 20 CYS CA C 58.09 . 1 168 . 20 CYS CB C 38.67 . 1 169 . 20 CYS N N 117.96 . 1 170 . 21 MET H H 9.04 . 1 171 . 21 MET HA H 4.31 . 1 172 . 21 MET HB2 H 2.23 . 2 173 . 21 MET HB3 H 2.12 . 2 174 . 21 MET C C 178.92 . 1 175 . 21 MET CA C 59.84 . 1 176 . 21 MET CB C 34.10 . 1 177 . 21 MET N N 119.03 . 1 178 . 22 SER H H 8.12 . 1 179 . 22 SER HA H 4.27 . 1 180 . 22 SER HB2 H 4.13 . 1 181 . 22 SER HB3 H 4.13 . 1 182 . 22 SER C C 177.83 . 1 183 . 22 SER CA C 61.29 . 1 184 . 22 SER CB C 62.77 . 1 185 . 22 SER N N 114.48 . 1 186 . 23 GLU H H 8.49 . 1 187 . 23 GLU HA H 4.00 . 1 188 . 23 GLU HB2 H 2.00 . 2 189 . 23 GLU HB3 H 1.56 . 2 190 . 23 GLU HG2 H 2.38 . 1 191 . 23 GLU HG3 H 2.38 . 1 192 . 23 GLU C C 177.61 . 1 193 . 23 GLU CA C 58.66 . 1 194 . 23 GLU CB C 29.83 . 1 195 . 23 GLU N N 118.69 . 1 196 . 24 HIS H H 7.24 . 1 197 . 24 HIS HA H 4.80 . 1 198 . 24 HIS HB2 H 3.48 . 2 199 . 24 HIS HB3 H 3.17 . 2 200 . 24 HIS C C 174.36 . 1 201 . 24 HIS CA C 56.03 . 1 202 . 24 HIS CB C 29.83 . 1 203 . 24 HIS N N 111.14 . 1 204 . 25 GLY H H 7.86 . 1 205 . 25 GLY HA2 H 4.01 . 2 206 . 25 GLY HA3 H 3.96 . 2 207 . 25 GLY C C 173.63 . 1 208 . 25 GLY CA C 46.58 . 1 209 . 25 GLY N N 110.49 . 1 210 . 26 THR H H 8.33 . 1 211 . 26 THR HA H 4.21 . 1 212 . 26 THR HB H 3.34 . 1 213 . 26 THR HG2 H 1.01 . 1 214 . 26 THR C C 175.01 . 1 215 . 26 THR CA C 63.23 . 1 216 . 26 THR CB C 70.34 . 1 217 . 26 THR CG2 C 22.37 . 1 218 . 26 THR N N 119.11 . 1 219 . 27 THR H H 8.77 . 1 220 . 27 THR HA H 4.69 . 1 221 . 27 THR HB H 4.56 . 1 222 . 27 THR HG2 H 1.23 . 1 223 . 27 THR C C 175.49 . 1 224 . 27 THR CA C 59.01 . 1 225 . 27 THR CB C 70.86 . 1 226 . 27 THR CG2 C 21.32 . 1 227 . 27 THR N N 115.83 . 1 228 . 28 GLN H H 9.15 . 1 229 . 28 GLN HA H 3.68 . 1 230 . 28 GLN HB2 H 2.07 . 2 231 . 28 GLN HB3 H 1.85 . 2 232 . 28 GLN HG2 H 2.40 . 1 233 . 28 GLN HG3 H 2.40 . 1 234 . 28 GLN C C 177.25 . 1 235 . 28 GLN CA C 57.64 . 1 236 . 28 GLN CB C 27.07 . 1 237 . 28 GLN CG C 33.15 . 1 238 . 28 GLN N N 122.27 . 1 239 . 29 ALA H H 8.28 . 1 240 . 29 ALA HA H 4.15 . 1 241 . 29 ALA HB H 1.37 . 1 242 . 29 ALA C C 180.87 . 1 243 . 29 ALA CA C 55.14 . 1 244 . 29 ALA CB C 17.69 . 1 245 . 29 ALA N N 120.66 . 1 246 . 30 GLN H H 7.61 . 1 247 . 30 GLN HA H 4.14 . 1 248 . 30 GLN HB2 H 2.43 . 2 249 . 30 GLN HB3 H 1.84 . 2 250 . 30 GLN HG2 H 2.28 . 1 251 . 30 GLN HG3 H 2.28 . 1 252 . 30 GLN C C 179.23 . 1 253 . 30 GLN CA C 59.20 . 1 254 . 30 GLN CB C 30.83 . 1 255 . 30 GLN N N 116.61 . 1 256 . 31 ILE H H 7.23 . 1 257 . 31 ILE HA H 3.43 . 1 258 . 31 ILE HB H 1.82 . 1 259 . 31 ILE HG12 H 1.43 . 1 260 . 31 ILE HG13 H 1.43 . 1 261 . 31 ILE HG2 H 0.76 . 1 262 . 31 ILE HD1 H 0.27 . 1 263 . 31 ILE C C 177.40 . 1 264 . 31 ILE CA C 65.51 . 1 265 . 31 ILE CB C 37.87 . 1 266 . 31 ILE CG1 C 29.10 . 1 267 . 31 ILE CG2 C 17.30 . 1 268 . 31 ILE CD1 C 14.77 . 1 269 . 31 ILE N N 121.57 . 1 270 . 32 ASP H H 8.96 . 1 271 . 32 ASP HA H 4.34 . 1 272 . 32 ASP HB2 H 2.76 . 2 273 . 32 ASP HB3 H 2.64 . 2 274 . 32 ASP C C 179.03 . 1 275 . 32 ASP CA C 57.28 . 1 276 . 32 ASP CB C 40.10 . 1 277 . 32 ASP N N 120.22 . 1 278 . 33 ASP H H 7.70 . 1 279 . 33 ASP HA H 4.20 . 1 280 . 33 ASP HB2 H 2.37 . 2 281 . 33 ASP HB3 H 2.07 . 2 282 . 33 ASP C C 178.89 . 1 283 . 33 ASP CA C 58.84 . 1 284 . 33 ASP N N 118.94 . 1 285 . 34 VAL H H 7.99 . 1 286 . 34 VAL HA H 3.57 . 1 287 . 34 VAL HB H 1.80 . 1 288 . 34 VAL HG1 H 0.40 . 2 289 . 34 VAL HG2 H 0.88 . 2 290 . 34 VAL C C 176.42 . 1 291 . 34 VAL CA C 65.89 . 1 292 . 34 VAL CB C 30.83 . 1 293 . 34 VAL CG1 C 20.79 . 2 294 . 34 VAL CG2 C 23.50 . 2 295 . 34 VAL N N 120.16 . 1 296 . 35 ASP H H 7.14 . 1 297 . 35 ASP HA H 3.93 . 1 298 . 35 ASP HB2 H 3.15 . 2 299 . 35 ASP HB3 H 3.02 . 2 300 . 35 ASP C C 178.02 . 1 301 . 35 ASP CA C 61.80 . 1 302 . 35 ASP CB C 37.90 . 1 303 . 35 ASP N N 116.69 . 1 304 . 36 LYS H H 7.40 . 1 305 . 36 LYS HA H 4.39 . 1 306 . 36 LYS HB2 H 2.12 . 2 307 . 36 LYS HB3 H 2.01 . 2 308 . 36 LYS HG2 H 1.76 . 2 309 . 36 LYS HG3 H 1.70 . 2 310 . 36 LYS C C 177.06 . 1 311 . 36 LYS CA C 56.54 . 1 312 . 36 LYS CB C 32.18 . 1 313 . 36 LYS N N 117.09 . 1 314 . 37 GLY H H 8.17 . 1 315 . 37 GLY HA2 H 4.34 . 2 316 . 37 GLY HA3 H 3.23 . 2 317 . 37 GLY C C 173.28 . 1 318 . 37 GLY CA C 44.68 . 1 319 . 37 GLY N N 105.27 . 1 320 . 38 ASN H H 7.74 . 1 321 . 38 ASN HA H 4.89 . 1 322 . 38 ASN HB2 H 2.62 . 1 323 . 38 ASN HB3 H 2.62 . 1 324 . 38 ASN C C 173.39 . 1 325 . 38 ASN CA C 52.22 . 1 326 . 38 ASN N N 119.89 . 1 327 . 39 LEU H H 8.12 . 1 328 . 39 LEU HA H 4.41 . 1 329 . 39 LEU HG H 1.47 . 1 330 . 39 LEU HD1 H 0.64 . 1 331 . 39 LEU HD2 H 0.64 . 1 332 . 39 LEU C C 175.97 . 1 333 . 39 LEU CA C 55.56 . 1 334 . 39 LEU CG C 28.00 . 1 335 . 39 LEU CD1 C 24.80 . 1 336 . 39 LEU CD2 C 24.80 . 1 337 . 39 LEU N N 124.66 . 1 338 . 40 VAL HA H 4.52 . 1 339 . 40 VAL HB H 2.01 . 1 340 . 40 VAL HG1 H 0.89 . 1 341 . 40 VAL HG2 H 0.89 . 1 342 . 40 VAL C C 174.54 . 1 343 . 40 VAL CA C 59.85 . 1 344 . 40 VAL CB C 35.14 . 1 345 . 40 VAL CG1 C 19.26 . 1 346 . 40 VAL CG2 C 19.26 . 1 347 . 41 ASN H H 8.63 . 1 348 . 41 ASN HA H 4.06 . 1 349 . 41 ASN HB2 H 2.46 . 1 350 . 41 ASN HB3 H 2.46 . 1 351 . 41 ASN C C 174.28 . 1 352 . 41 ASN CA C 51.69 . 1 353 . 41 ASN CB C 35.35 . 1 354 . 41 ASN N N 123.75 . 1 355 . 42 GLU H H 7.25 . 1 356 . 42 GLU HA H 4.92 . 1 357 . 42 GLU HB2 H 2.00 . 2 358 . 42 GLU HB3 H 1.82 . 2 359 . 42 GLU HG2 H 2.23 . 1 360 . 42 GLU HG3 H 2.23 . 1 361 . 42 GLU C C 174.66 . 1 362 . 42 GLU CA C 52.08 . 1 363 . 42 GLU CB C 31.93 . 1 364 . 42 GLU N N 122.96 . 1 365 . 43 PRO HA H 4.93 . 1 366 . 43 PRO HB2 H 2.49 . 2 367 . 43 PRO HB3 H 2.04 . 2 368 . 43 PRO HG2 H 2.15 . 2 369 . 43 PRO HG3 H 1.94 . 2 370 . 43 PRO HD2 H 3.89 . 2 371 . 43 PRO HD3 H 3.82 . 2 372 . 43 PRO C C 177.40 . 1 373 . 43 PRO CA C 64.87 . 1 374 . 43 PRO CB C 32.75 . 1 375 . 43 PRO CG C 27.32 . 1 376 . 43 PRO CD C 51.71 . 1 377 . 44 SER H H 8.49 . 1 378 . 44 SER HA H 4.41 . 1 379 . 44 SER HB2 H 3.95 . 2 380 . 44 SER HB3 H 4.07 . 2 381 . 44 SER C C 174.94 . 1 382 . 44 SER CA C 61.39 . 1 383 . 44 SER CB C 62.28 . 1 384 . 44 SER N N 110.77 . 1 385 . 45 ILE H H 8.01 . 1 386 . 45 ILE HA H 5.19 . 1 387 . 45 ILE HB H 1.85 . 1 388 . 45 ILE HG12 H 1.57 . 1 389 . 45 ILE HG13 H 1.43 . 1 390 . 45 ILE HG2 H 1.34 . 1 391 . 45 ILE HD1 H 0.99 . 1 392 . 45 ILE C C 176.96 . 1 393 . 45 ILE CA C 58.70 . 1 394 . 45 ILE CB C 40.72 . 1 395 . 45 ILE CG1 C 29.77 . 1 396 . 45 ILE CG2 C 19.60 . 1 397 . 45 ILE CD1 C 14.64 . 1 398 . 45 ILE N N 115.92 . 1 399 . 46 THR H H 9.26 . 1 400 . 46 THR HA H 4.17 . 1 401 . 46 THR HB H 4.47 . 1 402 . 46 THR HG2 H 1.53 . 1 403 . 46 THR C C 178.38 . 1 404 . 46 THR CA C 65.86 . 1 405 . 46 THR CB C 65.79 . 1 406 . 46 THR CG2 C 25.76 . 1 407 . 46 THR N N 120.43 . 1 408 . 47 CYS H H 9.24 . 1 409 . 47 CYS HA H 4.82 . 1 410 . 47 CYS HB2 H 2.58 . 2 411 . 47 CYS HB3 H 2.07 . 2 412 . 47 CYS C C 178.70 . 1 413 . 47 CYS CA C 54.02 . 1 414 . 47 CYS CB C 36.31 . 1 415 . 47 CYS N N 117.82 . 1 416 . 48 TYR H H 6.62 . 1 417 . 48 TYR HA H 3.90 . 1 418 . 48 TYR HB2 H 3.76 . 2 419 . 48 TYR HB3 H 3.29 . 2 420 . 48 TYR C C 175.58 . 1 421 . 48 TYR CA C 62.48 . 1 422 . 48 TYR CB C 37.38 . 1 423 . 48 TYR N N 120.88 . 1 424 . 49 MET H H 7.73 . 1 425 . 49 MET HA H 3.58 . 1 426 . 49 MET HB2 H 2.10 . 1 427 . 49 MET HB3 H 2.10 . 1 428 . 49 MET HG2 H 2.55 . 2 429 . 49 MET HG3 H 2.48 . 2 430 . 49 MET C C 177.42 . 1 431 . 49 MET CA C 60.42 . 1 432 . 49 MET CB C 34.17 . 1 433 . 49 MET N N 116.92 . 1 434 . 50 TYR H H 7.9 . 1 435 . 50 TYR HA H 3.91 . 1 436 . 50 TYR HB2 H 3.08 . 2 437 . 50 TYR HB3 H 2.96 . 2 438 . 50 TYR HD1 H 6.85 . 1 439 . 50 TYR HD2 H 6.85 . 1 440 . 50 TYR HE1 H 6.44 . 1 441 . 50 TYR HE2 H 6.44 . 1 442 . 50 TYR C C 174.00 . 1 443 . 50 TYR CA C 62.48 . 1 444 . 50 TYR CB C 37.88 . 1 445 . 50 TYR N N 115.74 . 1 446 . 51 CYS H H 8.06 . 1 447 . 51 CYS HA H 3.88 . 1 448 . 51 CYS HB2 H 3.40 . 2 449 . 51 CYS HB3 H 3.33 . 2 450 . 51 CYS C C 176.99 . 1 451 . 51 CYS CA C 59.65 . 1 452 . 51 CYS CB C 36.92 . 1 453 . 51 CYS N N 118.21 . 1 454 . 52 LEU H H 8.19 . 1 455 . 52 LEU HA H 3.87 . 1 456 . 52 LEU HB2 H 1.40 . 1 457 . 52 LEU HB3 H 1.40 . 1 458 . 52 LEU HD1 H 0.96 . 2 459 . 52 LEU HD2 H 0.76 . 2 460 . 52 LEU C C 178.22 . 1 461 . 52 LEU CA C 57.60 . 1 462 . 52 LEU CB C 42.34 . 1 463 . 52 LEU N N 122.28 . 1 464 . 53 LEU H H 7.59 . 1 465 . 53 LEU HA H 3.95 . 1 466 . 53 LEU HB2 H 1.87 . 1 467 . 53 LEU HB3 H 1.87 . 1 468 . 53 LEU HG H 1.20 . 1 469 . 53 LEU HD1 H 0.78 . 1 470 . 53 LEU HD2 H 0.78 . 1 471 . 53 LEU C C 180.10 . 1 472 . 53 LEU CA C 57.95 . 1 473 . 53 LEU CB C 42.47 . 1 474 . 53 LEU N N 115.24 . 1 475 . 54 GLU H H 8.64 . 1 476 . 54 GLU HA H 3.76 . 1 477 . 54 GLU HB2 H 1.78 . 1 478 . 54 GLU HB3 H 1.78 . 1 479 . 54 GLU HG2 H 2.33 . 2 480 . 54 GLU HG3 H 2.22 . 2 481 . 54 GLU C C 179.87 . 1 482 . 54 GLU CA C 59.29 . 1 483 . 54 GLU CB C 27.58 . 1 484 . 54 GLU N N 121.08 . 1 485 . 55 ALA H H 7.82 . 1 486 . 55 ALA HA H 3.86 . 1 487 . 55 ALA HB H 1.20 . 1 488 . 55 ALA C C 178.28 . 1 489 . 55 ALA CA C 54.28 . 1 490 . 55 ALA CB C 17.09 . 1 491 . 55 ALA N N 121.92 . 1 492 . 56 PHE H H 6.96 . 1 493 . 56 PHE HA H 4.55 . 1 494 . 56 PHE HB2 H 3.51 . 2 495 . 56 PHE HB3 H 2.42 . 2 496 . 56 PHE C C 173.82 . 1 497 . 56 PHE CA C 58.30 . 1 498 . 56 PHE CB C 39.42 . 1 499 . 56 PHE N N 113.49 . 1 500 . 57 SER H H 7.92 . 1 501 . 57 SER HA H 4.15 . 1 502 . 57 SER HB2 H 4.02 . 2 503 . 57 SER HB3 H 3.77 . 2 504 . 57 SER C C 173.60 . 1 505 . 57 SER CA C 59.69 . 1 506 . 57 SER CB C 60.73 . 1 507 . 57 SER N N 108.49 . 1 508 . 58 LEU H H 8.10 . 1 509 . 58 LEU HA H 4.15 . 1 510 . 58 LEU HB2 H 1.80 . 2 511 . 58 LEU HB3 H 1.72 . 2 512 . 58 LEU HG H 1.46 . 1 513 . 58 LEU HD1 H 0.93 . 2 514 . 58 LEU HD2 H 0.88 . 2 515 . 58 LEU C C 177.19 . 1 516 . 58 LEU CA C 56.87 . 1 517 . 58 LEU CB C 43.21 . 1 518 . 58 LEU N N 117.09 . 1 519 . 59 VAL H H 6.94 . 1 520 . 59 VAL HA H 5.24 . 1 521 . 59 VAL HB H 1.96 . 1 522 . 59 VAL HG1 H 0.57 . 2 523 . 59 VAL HG2 H 0.72 . 2 524 . 59 VAL C C 174.70 . 1 525 . 59 VAL CA C 56.96 . 1 526 . 59 VAL CB C 36.07 . 1 527 . 59 VAL CG1 C 19.10 . 2 528 . 59 VAL CG2 C 22.57 . 2 529 . 59 VAL N N 104.59 . 1 530 . 60 ASP H H 7.64 . 1 531 . 60 ASP HA H 4.91 . 1 532 . 60 ASP HB2 H 3.42 . 2 533 . 60 ASP HB3 H 2.86 . 2 534 . 60 ASP C C 178.75 . 1 535 . 60 ASP CA C 51.99 . 1 536 . 60 ASP CB C 41.74 . 1 537 . 60 ASP N N 119.38 . 1 538 . 61 ASP H H 8.42 . 1 539 . 61 ASP HA H 4.63 . 1 540 . 61 ASP HB2 H 2.89 . 2 541 . 61 ASP HB3 H 2.79 . 2 542 . 61 ASP C C 176.53 . 1 543 . 61 ASP CA C 55.64 . 1 544 . 61 ASP CB C 39.32 . 1 545 . 61 ASP N N 116.77 . 1 546 . 62 GLU H H 8.24 . 1 547 . 62 GLU HA H 4.76 . 1 548 . 62 GLU HB2 H 2.25 . 2 549 . 62 GLU HB3 H 1.69 . 2 550 . 62 GLU HG2 H 2.17 . 1 551 . 62 GLU HG3 H 2.17 . 1 552 . 62 GLU C C 174.44 . 1 553 . 62 GLU CA C 55.27 . 1 554 . 62 GLU CB C 29.52 . 1 555 . 62 GLU N N 120.24 . 1 556 . 63 ALA H H 8.06 . 1 557 . 63 ALA HA H 3.65 . 1 558 . 63 ALA HB H 1.38 . 1 559 . 63 ALA C C 175.31 . 1 560 . 63 ALA CA C 53.53 . 1 561 . 63 ALA CB C 17.16 . 1 562 . 63 ALA N N 113.66 . 1 563 . 64 ASN H H 8.72 . 1 564 . 64 ASN HA H 4.94 . 1 565 . 64 ASN HB2 H 2.92 . 2 566 . 64 ASN HB3 H 2.54 . 2 567 . 64 ASN C C 176.65 . 1 568 . 64 ASN CA C 53.10 . 1 569 . 64 ASN CB C 38.42 . 1 570 . 64 ASN N N 114.74 . 1 571 . 65 VAL H H 8.13 . 1 572 . 65 VAL HA H 4.41 . 1 573 . 65 VAL HB H 1.98 . 1 574 . 65 VAL HG1 H 0.88 . 2 575 . 65 VAL HG2 H 0.81 . 2 576 . 65 VAL C C 175.38 . 1 577 . 65 VAL CA C 61.93 . 1 578 . 65 VAL CB C 33.62 . 1 579 . 65 VAL CG1 C 20.44 . 2 580 . 65 VAL CG2 C 20.79 . 2 581 . 65 VAL N N 124.53 . 1 582 . 66 ASP H H 8.31 . 1 583 . 66 ASP HA H 4.74 . 1 584 . 66 ASP HB2 H 3.03 . 2 585 . 66 ASP HB3 H 2.48 . 2 586 . 66 ASP C C 175.23 . 1 587 . 66 ASP CA C 52.28 . 1 588 . 66 ASP CB C 38.72 . 1 589 . 66 ASP N N 127.38 . 1 590 . 67 GLU H H 8.63 . 1 591 . 67 GLU HA H 3.61 . 1 592 . 67 GLU HB2 H 2.04 . 2 593 . 67 GLU HB3 H 1.91 . 2 594 . 67 GLU HG2 H 2.36 . 1 595 . 67 GLU HG3 H 2.36 . 1 596 . 67 GLU C C 176.97 . 1 597 . 67 GLU CA C 59.86 . 1 598 . 67 GLU CB C 28.74 . 1 599 . 67 GLU N N 125.49 . 1 600 . 68 ASP H H 8.23 . 1 601 . 68 ASP HA H 4.35 . 1 602 . 68 ASP HB2 H 2.76 . 2 603 . 68 ASP HB3 H 2.66 . 2 604 . 68 ASP C C 179.65 . 1 605 . 68 ASP CA C 57.35 . 1 606 . 68 ASP CB C 39.46 . 1 607 . 68 ASP N N 116.85 . 1 608 . 69 ILE H H 7.52 . 1 609 . 69 ILE HA H 3.81 . 1 610 . 69 ILE HB H 1.80 . 1 611 . 69 ILE HG12 H 1.57 . 1 612 . 69 ILE HG13 H 1.57 . 1 613 . 69 ILE HG2 H 1.20 . 1 614 . 69 ILE HD1 H 0.82 . 1 615 . 69 ILE C C 178.81 . 1 616 . 69 ILE CA C 63.24 . 1 617 . 69 ILE CB C 37.02 . 1 618 . 69 ILE CG2 C 17.23 . 1 619 . 69 ILE CD1 C 11.50 . 1 620 . 69 ILE N N 120.60 . 1 621 . 70 MET H H 7.78 . 1 622 . 70 MET HA H 3.88 . 1 623 . 70 MET HB2 H 1.94 . 1 624 . 70 MET HB3 H 1.94 . 1 625 . 70 MET C C 177.65 . 1 626 . 70 MET CA C 59.59 . 1 627 . 70 MET CB C 32.82 . 1 628 . 70 MET N N 118.21 . 1 629 . 71 LEU H H 8.55 . 1 630 . 71 LEU HA H 3.89 . 1 631 . 71 LEU HB2 H 1.80 . 2 632 . 71 LEU HB3 H 1.63 . 2 633 . 71 LEU HG H 1.63 . 1 634 . 71 LEU HD1 H 0.90 . 2 635 . 71 LEU HD2 H 0.78 . 2 636 . 71 LEU C C 179.76 . 1 637 . 71 LEU CA C 58.04 . 1 638 . 71 LEU CB C 40.57 . 1 639 . 71 LEU CD2 C 23.44 . 2 640 . 71 LEU N N 115.40 . 1 641 . 72 GLY H H 7.52 . 1 642 . 72 GLY HA2 H 3.99 . 2 643 . 72 GLY HA3 H 3.81 . 2 644 . 72 GLY C C 175.20 . 1 645 . 72 GLY CA C 46.10 . 1 646 . 72 GLY N N 103.14 . 1 647 . 73 LEU H H 7.36 . 1 648 . 73 LEU HA H 4.35 . 1 649 . 73 LEU HB2 H 1.95 . 2 650 . 73 LEU HB3 H 1.55 . 2 651 . 73 LEU HG H 1.63 . 1 652 . 73 LEU HD1 H 0.90 . 2 653 . 73 LEU HD2 H 0.85 . 2 654 . 73 LEU C C 177.04 . 1 655 . 73 LEU CA C 55.15 . 1 656 . 73 LEU CB C 43.01 . 1 657 . 73 LEU N N 118.43 . 1 658 . 74 LEU H H 7.23 . 1 659 . 74 LEU HA H 4.43 . 1 660 . 74 LEU HB2 H 2.01 . 2 661 . 74 LEU HB3 H 1.43 . 2 662 . 74 LEU HG H 1.65 . 1 663 . 74 LEU HD1 H 0.99 . 2 664 . 74 LEU HD2 H 0.75 . 2 665 . 74 LEU C C 174.42 . 1 666 . 74 LEU CA C 52.11 . 1 667 . 74 LEU CB C 41.82 . 1 668 . 74 LEU N N 117.72 . 1 669 . 75 PRO HA H 4.45 . 1 670 . 75 PRO HB2 H 2.36 . 2 671 . 75 PRO HB3 H 1.75 . 2 672 . 75 PRO C C 178.11 . 1 673 . 75 PRO CA C 62.32 . 1 674 . 75 PRO CB C 32.50 . 1 675 . 76 ASP H H 8.89 . 1 676 . 76 ASP HA H 4.21 . 1 677 . 76 ASP HB2 H 2.65 . 1 678 . 76 ASP HB3 H 2.65 . 1 679 . 76 ASP C C 179.06 . 1 680 . 76 ASP CA C 57.86 . 1 681 . 76 ASP CB C 40.42 . 1 682 . 76 ASP N N 122.88 . 1 683 . 77 GLN H H 9.09 . 1 684 . 77 GLN HA H 4.20 . 1 685 . 77 GLN HB2 H 2.07 . 1 686 . 77 GLN HB3 H 2.07 . 1 687 . 77 GLN HG2 H 2.45 . 2 688 . 77 GLN HG3 H 2.27 . 2 689 . 77 GLN C C 176.39 . 1 690 . 77 GLN CA C 58.10 . 1 691 . 77 GLN CB C 27.54 . 1 692 . 77 GLN CG C 33.10 . 1 693 . 77 GLN N N 115.55 . 1 694 . 78 LEU H H 7.62 . 1 695 . 78 LEU HA H 4.51 . 1 696 . 78 LEU HB2 H 1.54 . 2 697 . 78 LEU HB3 H 1.21 . 2 698 . 78 LEU HG H 1.30 . 1 699 . 78 LEU HD1 H 0.60 . 2 700 . 78 LEU HD2 H 0.44 . 2 701 . 78 LEU C C 176.76 . 1 702 . 78 LEU CA C 53.78 . 1 703 . 78 LEU CB C 43.83 . 1 704 . 78 LEU N N 119.10 . 1 705 . 79 GLN H H 7.30 . 1 706 . 79 GLN HA H 3.58 . 1 707 . 79 GLN HB2 H 2.08 . 1 708 . 79 GLN HB3 H 2.08 . 1 709 . 79 GLN HG2 H 2.46 . 1 710 . 79 GLN HG3 H 2.46 . 1 711 . 79 GLN C C 177.48 . 1 712 . 79 GLN CA C 60.43 . 1 713 . 79 GLN CB C 27.84 . 1 714 . 79 GLN N N 119.25 . 1 715 . 80 GLU H H 8.63 . 1 716 . 80 GLU HA H 4.01 . 1 717 . 80 GLU HB2 H 2.02 . 1 718 . 80 GLU HB3 H 2.02 . 1 719 . 80 GLU HG2 H 2.30 . 2 720 . 80 GLU HG3 H 2.16 . 2 721 . 80 GLU C C 179.79 . 1 722 . 80 GLU CA C 60.14 . 1 723 . 80 GLU CB C 28.60 . 1 724 . 80 GLU N N 119.25 . 1 725 . 81 ARG H H 8.55 . 1 726 . 81 ARG HA H 4.10 . 1 727 . 81 ARG HB2 H 2.05 . 2 728 . 81 ARG HB3 H 1.80 . 2 729 . 81 ARG C C 178.61 . 1 730 . 81 ARG CA C 59.10 . 1 731 . 81 ARG N N 121.00 . 1 732 . 82 ALA HA H 3.88 . 1 733 . 82 ALA HB H 1.27 . 1 734 . 82 ALA C C 179.32 . 1 735 . 82 ALA CA C 55.42 . 1 736 . 82 ALA CB C 18.99 . 1 737 . 83 GLN H H 8.41 . 1 738 . 83 GLN HA H 3.95 . 1 739 . 83 GLN HB2 H 2.21 . 2 740 . 83 GLN HB3 H 2.16 . 2 741 . 83 GLN HG2 H 2.55 . 2 742 . 83 GLN HG3 H 2.34 . 2 743 . 83 GLN C C 179.56 . 1 744 . 83 GLN CA C 59.72 . 1 745 . 83 GLN CB C 28.32 . 1 746 . 83 GLN N N 116.78 . 1 747 . 84 SER H H 7.83 . 1 748 . 84 SER HA H 4.27 . 1 749 . 84 SER HB2 H 4.05 . 1 750 . 84 SER HB3 H 4.05 . 1 751 . 84 SER C C 177.69 . 1 752 . 84 SER CA C 61.29 . 1 753 . 84 SER CB C 62.48 . 1 754 . 84 SER N N 115.42 . 1 755 . 85 VAL H H 8.38 . 1 756 . 85 VAL HA H 3.72 . 1 757 . 85 VAL HB H 2.11 . 1 758 . 85 VAL HG1 H 1.09 . 2 759 . 85 VAL HG2 H 0.97 . 2 760 . 85 VAL C C 178.49 . 1 761 . 85 VAL CA C 66.32 . 1 762 . 85 VAL CB C 31.50 . 1 763 . 85 VAL CG1 C 23.66 . 2 764 . 85 VAL CG2 C 23.04 . 2 765 . 85 VAL N N 122.11 . 1 766 . 86 MET H H 8.78 . 1 767 . 86 MET HA H 3.97 . 1 768 . 86 MET HB2 H 2.16 . 2 769 . 86 MET HB3 H 1.91 . 2 770 . 86 MET HG2 H 2.73 . 2 771 . 86 MET HG3 H 2.48 . 2 772 . 86 MET C C 178.07 . 1 773 . 86 MET CA C 58.77 . 1 774 . 86 MET CB C 31.14 . 1 775 . 86 MET N N 117.63 . 1 776 . 87 GLY H H 7.87 . 1 777 . 87 GLY HA2 H 3.96 . 2 778 . 87 GLY HA3 H 3.89 . 2 779 . 87 GLY C C 175.13 . 1 780 . 87 GLY CA C 46.56 . 1 781 . 87 GLY N N 104.54 . 1 782 . 88 LYS H H 7.22 . 1 783 . 88 LYS HA H 4.39 . 1 784 . 88 LYS HB2 H 1.95 . 1 785 . 88 LYS HB3 H 1.95 . 1 786 . 88 LYS HG2 H 1.50 . 2 787 . 88 LYS HG3 H 1.34 . 2 788 . 88 LYS HD2 H 1.67 . 1 789 . 88 LYS HD3 H 1.67 . 1 790 . 88 LYS HE2 H 2.97 . 1 791 . 88 LYS HE3 H 2.97 . 1 792 . 88 LYS C C 178.68 . 1 793 . 88 LYS CA C 57.40 . 1 794 . 88 LYS CB C 33.63 . 1 795 . 88 LYS N N 117.52 . 1 796 . 89 CYS H H 7.89 . 1 797 . 89 CYS HA H 4.87 . 1 798 . 89 CYS HB2 H 3.29 . 2 799 . 89 CYS HB3 H 2.37 . 2 800 . 89 CYS C C 172.93 . 1 801 . 89 CYS CA C 53.61 . 1 802 . 89 CYS CB C 40.52 . 1 803 . 89 CYS N N 114.13 . 1 804 . 90 LEU H H 7.63 . 1 805 . 90 LEU HA H 4.60 . 1 806 . 90 LEU HB2 H 1.91 . 2 807 . 90 LEU HB3 H 1.73 . 2 808 . 90 LEU HG H 1.37 . 1 809 . 90 LEU HD1 H 0.99 . 2 810 . 90 LEU HD2 H 0.88 . 2 811 . 90 LEU C C 175.69 . 1 812 . 90 LEU CA C 52.04 . 1 813 . 90 LEU N N 118.45 . 1 814 . 91 PRO HA H 4.67 . 1 815 . 91 PRO HB2 H 2.53 . 2 816 . 91 PRO HB3 H 2.28 . 2 817 . 91 PRO HG2 H 1.95 . 2 818 . 91 PRO HG3 H 1.85 . 2 819 . 91 PRO HD2 H 3.62 . 2 820 . 91 PRO HD3 H 3.49 . 2 821 . 91 PRO C C 176.63 . 1 822 . 91 PRO CA C 62.02 . 1 823 . 91 PRO CB C 34.08 . 1 824 . 91 PRO CG C 24.79 . 1 825 . 91 PRO CD C 50.47 . 1 826 . 92 THR H H 8.62 . 1 827 . 92 THR HA H 4.70 . 1 828 . 92 THR HB H 4.24 . 1 829 . 92 THR HG2 H 1.46 . 1 830 . 92 THR C C 174.90 . 1 831 . 92 THR CA C 60.76 . 1 832 . 92 THR CB C 71.17 . 1 833 . 92 THR CG2 C 23.16 . 1 834 . 92 THR N N 111.42 . 1 835 . 93 SER H H 9.22 . 1 836 . 93 SER HA H 4.73 . 1 837 . 93 SER HB2 H 3.80 . 1 838 . 93 SER HB3 H 3.80 . 1 839 . 93 SER C C 172.76 . 1 840 . 93 SER CA C 57.27 . 1 841 . 93 SER CB C 65.46 . 1 842 . 93 SER N N 114.29 . 1 843 . 94 GLY H H 8.47 . 1 844 . 94 GLY HA2 H 4.21 . 2 845 . 94 GLY HA3 H 3.95 . 2 846 . 94 GLY C C 173.07 . 1 847 . 94 GLY CA C 44.94 . 1 848 . 94 GLY N N 109.56 . 1 849 . 95 SER H H 9.00 . 1 850 . 95 SER HA H 4.20 . 1 851 . 95 SER HB2 H 3.99 . 2 852 . 95 SER HB3 H 3.74 . 2 853 . 95 SER C C 173.91 . 1 854 . 95 SER CA C 60.14 . 1 855 . 95 SER CB C 63.73 . 1 856 . 95 SER N N 113.15 . 1 857 . 96 ASP H H 7.72 . 1 858 . 96 ASP HA H 4.61 . 1 859 . 96 ASP HB2 H 3.01 . 2 860 . 96 ASP HB3 H 2.88 . 2 861 . 96 ASP C C 175.67 . 1 862 . 96 ASP CA C 52.95 . 1 863 . 96 ASP CB C 41.61 . 1 864 . 96 ASP N N 115.53 . 1 865 . 97 ASN H H 8.92 . 1 866 . 97 ASN HA H 3.96 . 1 867 . 97 ASN HB2 H 2.13 . 2 868 . 97 ASN HB3 H 1.29 . 2 869 . 97 ASN C C 177.14 . 1 870 . 97 ASN CA C 56.17 . 1 871 . 97 ASN CB C 36.29 . 1 872 . 97 ASN N N 117.75 . 1 873 . 98 CYS H H 7.80 . 1 874 . 98 CYS HA H 4.10 . 1 875 . 98 CYS HB2 H 3.51 . 2 876 . 98 CYS HB3 H 3.29 . 2 877 . 98 CYS C C 176.11 . 1 878 . 98 CYS CA C 59.79 . 1 879 . 98 CYS CB C 41.41 . 1 880 . 98 CYS N N 115.48 . 1 881 . 99 ASN H H 8.78 . 1 882 . 99 ASN HA H 4.48 . 1 883 . 99 ASN HB2 H 2.98 . 2 884 . 99 ASN HB3 H 2.35 . 2 885 . 99 ASN C C 177.33 . 1 886 . 99 ASN CA C 57.06 . 1 887 . 99 ASN CB C 41.53 . 1 888 . 99 ASN N N 120.71 . 1 889 . 100 LYS H H 8.49 . 1 890 . 100 LYS HA H 4.30 . 1 891 . 100 LYS HB2 H 1.93 . 2 892 . 100 LYS HB3 H 1.57 . 2 893 . 100 LYS C C 179.69 . 1 894 . 100 LYS CA C 59.95 . 1 895 . 100 LYS CB C 33.44 . 1 896 . 100 LYS N N 117.86 . 1 897 . 101 ILE H H 7.29 . 1 898 . 101 ILE HA H 4.07 . 1 899 . 101 ILE HB H 2.54 . 1 900 . 101 ILE HG12 H 1.34 . 1 901 . 101 ILE HG13 H 1.34 . 1 902 . 101 ILE HG2 H 1.06 . 1 903 . 101 ILE HD1 H 0.78 . 1 904 . 101 ILE C C 177.51 . 1 905 . 101 ILE CA C 61.07 . 1 906 . 101 ILE CB C 33.99 . 1 907 . 101 ILE CG2 C 19.30 . 1 908 . 101 ILE CD1 C 8.88 . 1 909 . 101 ILE N N 118.21 . 1 910 . 102 TYR H H 8.60 . 1 911 . 102 TYR HA H 3.95 . 1 912 . 102 TYR HB2 H 3.34 . 2 913 . 102 TYR HB3 H 3.27 . 2 914 . 102 TYR HD1 H 6.96 . 1 915 . 102 TYR HD2 H 6.96 . 1 916 . 102 TYR HE1 H 6.70 . 1 917 . 102 TYR HE2 H 6.70 . 1 918 . 102 TYR C C 175.89 . 1 919 . 102 TYR CA C 62.39 . 1 920 . 102 TYR CB C 37.43 . 1 921 . 102 TYR N N 122.77 . 1 922 . 103 ASN H H 8.48 . 1 923 . 103 ASN HA H 4.03 . 1 924 . 103 ASN HB2 H 3.14 . 2 925 . 103 ASN HB3 H 2.75 . 2 926 . 103 ASN C C 178.51 . 1 927 . 103 ASN CA C 55.89 . 1 928 . 103 ASN CB C 37.82 . 1 929 . 103 ASN N N 115.52 . 1 930 . 104 LEU H H 8.01 . 1 931 . 104 LEU HA H 4.58 . 1 932 . 104 LEU HB2 H 2.11 . 2 933 . 104 LEU HB3 H 1.64 . 2 934 . 104 LEU HG H 1.50 . 1 935 . 104 LEU HD1 H 0.88 . 2 936 . 104 LEU HD2 H 0.82 . 2 937 . 104 LEU C C 177.30 . 1 938 . 104 LEU CA C 57.61 . 1 939 . 104 LEU CB C 42.11 . 1 940 . 104 LEU N N 123.14 . 1 941 . 105 ALA H H 9.13 . 1 942 . 105 ALA HA H 3.76 . 1 943 . 105 ALA HB H 1.46 . 1 944 . 105 ALA C C 178.02 . 1 945 . 105 ALA CA C 55.18 . 1 946 . 105 ALA CB C 18.52 . 1 947 . 105 ALA N N 125.97 . 1 948 . 106 LYS H H 8.20 . 1 949 . 106 LYS HA H 3.51 . 1 950 . 106 LYS HB2 H 1.44 . 2 951 . 106 LYS HB3 H 1.24 . 2 952 . 106 LYS HG2 H 1.00 . 1 953 . 106 LYS HG3 H 1.00 . 1 954 . 106 LYS HD2 H 1.42 . 1 955 . 106 LYS HD3 H 1.42 . 1 956 . 106 LYS HE2 H 2.92 . 2 957 . 106 LYS HE3 H 2.85 . 2 958 . 106 LYS C C 178.10 . 1 959 . 106 LYS CA C 58.51 . 1 960 . 106 LYS CB C 31.53 . 1 961 . 106 LYS CE C 41.46 . 1 962 . 106 LYS N N 116.05 . 1 963 . 107 CYS H H 7.46 . 1 964 . 107 CYS HA H 4.14 . 1 965 . 107 CYS HB2 H 3.34 . 2 966 . 107 CYS HB3 H 3.28 . 2 967 . 107 CYS C C 177.86 . 1 968 . 107 CYS CA C 60.04 . 1 969 . 107 CYS CB C 40.10 . 1 970 . 107 CYS N N 118.45 . 1 971 . 108 VAL H H 9.03 . 1 972 . 108 VAL HA H 3.39 . 1 973 . 108 VAL HB H 2.17 . 1 974 . 108 VAL HG1 H 1.01 . 2 975 . 108 VAL HG2 H 1.14 . 2 976 . 108 VAL C C 176.99 . 1 977 . 108 VAL CA C 66.96 . 1 978 . 108 VAL CB C 32.01 . 1 979 . 108 VAL CG1 C 23.46 . 2 980 . 108 VAL CG2 C 22.20 . 2 981 . 108 VAL N N 122.93 . 1 982 . 110 GLU HA H 3.85 . 1 983 . 110 GLU HB2 H 2.06 . 2 984 . 110 GLU HB3 H 1.95 . 2 985 . 110 GLU HG2 H 2.39 . 2 986 . 110 GLU HG3 H 2.27 . 2 987 . 110 GLU C C 179.12 . 1 988 . 110 GLU CA C 58.22 . 1 989 . 110 GLU CB C 28.82 . 1 990 . 110 GLU CG C 36.00 . 1 991 . 111 SER H H 7.55 . 1 992 . 111 SER HA H 4.43 . 1 993 . 111 SER HB2 H 3.92 . 1 994 . 111 SER HB3 H 3.92 . 1 995 . 111 SER C C 174.40 . 1 996 . 111 SER CA C 60.56 . 1 997 . 111 SER CB C 64.61 . 1 998 . 111 SER N N 112.83 . 1 999 . 112 ALA H H 8.46 . 1 1000 . 112 ALA HA H 4.81 . 1 1001 . 112 ALA HB H 1.27 . 1 1002 . 112 ALA C C 173.36 . 1 1003 . 112 ALA CA C 50.56 . 1 1004 . 112 ALA CB C 19.13 . 1 1005 . 112 ALA N N 124.30 . 1 1006 . 113 PRO HA H 4.55 . 1 1007 . 113 PRO HB2 H 2.53 . 2 1008 . 113 PRO HB3 H 2.16 . 2 1009 . 113 PRO HG2 H 2.04 . 1 1010 . 113 PRO HG3 H 2.04 . 1 1011 . 113 PRO C C 178.51 . 1 1012 . 113 PRO CA C 65.80 . 1 1013 . 114 ASP H H 9.60 . 1 1014 . 114 ASP HA H 4.55 . 1 1015 . 114 ASP HB2 H 2.77 . 1 1016 . 114 ASP HB3 H 2.77 . 1 1017 . 114 ASP C C 176.65 . 1 1018 . 114 ASP CA C 54.78 . 1 1019 . 114 ASP CB C 39.40 . 1 1020 . 114 ASP N N 114.08 . 1 1021 . 117 PHE HA H 4.65 . 1 1022 . 117 PHE HB2 H 2.86 . 1 1023 . 117 PHE HB3 H 2.86 . 1 1024 . 117 PHE C C 179.22 . 1 1025 . 117 PHE CA C 57.50 . 1 1026 . 117 PHE CB C 41.78 . 1 1027 . 118 VAL H H 7.98 . 1 1028 . 118 VAL HA H 4.10 . 1 1029 . 118 VAL HB H 2.44 . 1 1030 . 118 VAL HG1 H 1.41 . 2 1031 . 118 VAL HG2 H 1.36 . 2 1032 . 118 VAL C C 181.04 . 1 1033 . 118 VAL CA C 65.65 . 1 1034 . 118 VAL CB C 31.78 . 1 1035 . 118 VAL CG1 C 23.80 . 2 1036 . 118 VAL CG2 C 23.33 . 2 1037 . 118 VAL N N 118.36 . 1 1038 . 119 ILE HA H 4.05 . 1 1039 . 119 ILE HB H 1.53 . 1 1040 . 119 ILE HG12 H 1.44 . 1 1041 . 119 ILE HG13 H 0.90 . 1 1042 . 119 ILE HG2 H 0.86 . 1 1043 . 119 ILE HD1 H 0.42 . 1 1044 . 119 ILE C C 178.70 . 1 1045 . 119 ILE CA C 62.40 . 1 1046 . 119 ILE CB C 40.82 . 1 1047 . 119 ILE CG1 C 27.28 . 1 1048 . 119 ILE CG2 C 18.40 . 1 1049 . 119 ILE CD1 C 14.22 . 1 stop_ save_