data_4046 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Evidence for Similarities between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and the Helix-Turn-Helix and HNF-3/forkhead Families of Transcription Factors ; _BMRB_accession_number 4046 _BMRB_flat_file_name bmr4046.str _Entry_type update _Submission_date 1997-07-20 _Accession_date 1997-07-20 _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 Vuister Geerten W. . 2 Kim Soon-Jong . . 3 Wu Carl . . 4 Bax Ad . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 432 "13C chemical shifts" 370 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-24 reformat BMRB 'format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Vuister, G. W., Kim, S-J., Wu, C., and Bax, A., "NMR Evidence for Similarities between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and the Helix-Turn-Helix and HNF-3/forkhead Families of Transcription Factors," Biochemistry 33, 10-16 (1994). ; _Citation_title ; NMR Evidence for Similarities between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and the Helix-Turn-Helix and HNF-3/forkhead Families of Transcription Factors ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 94114471 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vuister Geerten W. . 2 Kim Soon-Jong . . 3 Wu Carl . . 4 Bax Ad . . stop_ _Journal_abbreviation . _Journal_name_full Biochemistry _Journal_volume 33 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10 _Page_last 16 _Year 1994 _Details . loop_ _Keyword 'Heat shcok factor (HSF)' NMR 'Transcription factor' stop_ save_ ################################## # Molecular system description # ################################## save_system_Drosophila_HSF _Saveframe_category molecular_system _Mol_system_name 'Drosophila Heat Shock Factor' _Abbreviation_common dHSF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label dHSF $dHSF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; mediate protein-protein interactions and the translocation of proteins across cellular membranes ; stop_ _Database_query_date . _Details ; Heat shock factor (HSF) is produced in response to heat or chemical stress ; save_ ######################## # Monomeric polymers # ######################## save_dHSF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Drosophila Heat Shock Factor' _Abbreviation_common dHSF _Molecular_mass 15259 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 136 _Mol_residue_sequence ; AAEHSYGDAAAIGSGVPAFL AKLWRIVDDADTNRLICWTK DGQSFVIQNQAQFAKELLPL NYKHNNMASFIRQLNMYGFH KITSIDNGGLRFDRDEIEFS HPFFKRNSPFLLDQIKRKIS NNKNGDDKGVLKPAAE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . ALA 2 . ALA 3 . GLU 4 34 HIS 5 35 SER 6 36 TYR 7 37 GLY 8 38 ASP 9 39 ALA 10 40 ALA 11 41 ALA 12 42 ILE 13 43 GLY 14 44 SER 15 45 GLY 16 46 VAL 17 47 PRO 18 48 ALA 19 49 PHE 20 50 LEU 21 51 ALA 22 52 LYS 23 53 LEU 24 54 TRP 25 55 ARG 26 56 ILE 27 57 VAL 28 58 ASP 29 59 ASP 30 60 ALA 31 61 ASP 32 62 THR 33 63 ASN 34 64 ARG 35 65 LEU 36 66 ILE 37 67 CYS 38 68 TRP 39 69 THR 40 70 LYS 41 71 ASP 42 72 GLY 43 73 GLN 44 74 SER 45 75 PHE 46 76 VAL 47 77 ILE 48 78 GLN 49 79 ASN 50 80 GLN 51 81 ALA 52 82 GLN 53 83 PHE 54 84 ALA 55 85 LYS 56 86 GLU 57 87 LEU 58 88 LEU 59 89 PRO 60 90 LEU 61 91 ASN 62 92 TYR 63 93 LYS 64 94 HIS 65 95 ASN 66 96 ASN 67 97 MET 68 98 ALA 69 99 SER 70 100 PHE 71 101 ILE 72 102 ARG 73 103 GLN 74 104 LEU 75 105 ASN 76 106 MET 77 107 TYR 78 108 GLY 79 109 PHE 80 110 HIS 81 111 LYS 82 112 ILE 83 113 THR 84 114 SER 85 115 ILE 86 116 ASP 87 117 ASN 88 118 GLY 89 119 GLY 90 120 LEU 91 121 ARG 92 122 PHE 93 123 ASP 94 124 ARG 95 125 ASP 96 126 GLU 97 127 ILE 98 128 GLU 99 129 PHE 100 130 SER 101 131 HIS 102 132 PRO 103 133 PHE 104 134 PHE 105 135 LYS 106 136 ARG 107 137 ASN 108 138 SER 109 139 PRO 110 140 PHE 111 141 LEU 112 142 LEU 113 143 ASP 114 144 GLN 115 145 ILE 116 145 LYS 117 147 ARG 118 148 LYS 119 149 ILE 120 150 SER 121 151 ASN 122 152 ASN 123 153 LYS 124 154 ASN 125 155 GLY 126 156 ASP 127 157 ASP 128 158 LYS 129 159 GLY 130 160 VAL 131 161 LEU 132 162 LYS 133 163 PRO 134 164 ALA 135 165 ALA 136 166 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1HKS "Solution Structure Of The Dna-Binding Domain Of Drosophila Heat Shock Transcription Factor" 77.21 106 99.05 100.00 7.53e-71 PDB 1HKT "Solution Structure Of The Dna-Binding Domain Of Drosophila Heat Shock Transcription Factor" 77.21 106 99.05 100.00 7.53e-71 DBJ BAE16321 "heat shock transcription factor b [Drosophila melanogaster]" 97.06 715 98.48 99.24 2.62e-88 DBJ BAE16322 "heat shock transcription factor c [Drosophila melanogaster]" 97.06 709 98.48 99.24 2.37e-88 DBJ BAE16323 "heat shock transcription factor d [Drosophila melanogaster]" 97.06 733 98.48 99.24 3.38e-88 GB AAA28642 "heat shock transcription factor [Drosophila melanogaster]" 97.06 691 98.48 99.24 1.43e-88 GB AAF57749 "heat shock factor, isoform A [Drosophila melanogaster]" 97.06 691 98.48 99.24 1.43e-88 GB AAL13990 "SD02833p [Drosophila melanogaster]" 97.06 662 98.48 99.24 7.96e-89 GB ABI31102 "heat shock factor, isoform D [Drosophila melanogaster]" 97.06 733 98.48 99.24 3.38e-88 GB ABI31103 "heat shock factor, isoform C [Drosophila melanogaster]" 97.06 709 98.48 99.24 2.37e-88 REF NP_001036555 "heat shock factor, isoform D [Drosophila melanogaster]" 97.06 733 98.48 99.24 3.38e-88 REF NP_001036556 "heat shock factor, isoform C [Drosophila melanogaster]" 97.06 709 98.48 99.24 2.37e-88 REF NP_001036557 "heat shock factor, isoform B [Drosophila melanogaster]" 97.06 715 98.48 99.24 2.62e-88 REF NP_476575 "heat shock factor, isoform A [Drosophila melanogaster]" 97.06 691 98.48 99.24 1.43e-88 REF XP_002034392 "GM19926 [Drosophila sechellia]" 97.06 709 96.97 97.73 7.29e-87 SP P22813 "RecName: Full=Heat shock factor protein; Short=HSF; AltName: Full=Heat shock transcription factor; Short=HSTF" 97.06 691 98.48 99.24 1.43e-88 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dHSF 'Fruit Fly' 7227 Eukaryota Metazoa Drosophila melanogaster stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $dHSF 'recombinant technology' 'E. coli' Escherichia coli (BL21/DE3) plasmid pHSF33-163 ; The recombinant protein includes three additional C-terminal amino acids, ALA-ALA-GLU ; 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $dHSF . mM 0.7 1.1 [U-15N] D2O 5 % . . . 'potassium phosphate' 10 mM . . . KCl 50 mM . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $dHSF . mM 0.7 1.1 '[U-13C; U-15N]' D2O 5 % . . . 'potassium phosphate' 10 mM . . . KCl 50 mM . . . stop_ 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_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 . na temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_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 C 13 'methyl carbons' ppm 0 . . . . . TSP H 1 'methyl protons' ppm 0 . . . . . TSP N 15 . ppm 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_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name dHSF _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 . 4 HIS HA H 4.67 . 1 2 . 4 HIS HB2 H 3.06 . 1 3 . 4 HIS HB3 H 3.06 . 1 4 . 4 HIS CA C 56.14 . 1 5 . 4 HIS CB C 30.49 . 1 6 . 5 SER H H 8.38 . 1 7 . 5 SER HA H 4.44 . 1 8 . 5 SER HB2 H 3.77 . 1 9 . 5 SER HB3 H 3.77 . 1 10 . 5 SER C C 174.10 . 1 11 . 5 SER CA C 58.03 . 1 12 . 5 SER CB C 63.96 . 1 13 . 5 SER N N 117.48 . 1 14 . 6 TYR H H 8.37 . 1 15 . 6 TYR HA H 4.58 . 1 16 . 6 TYR HB2 H 3.10 . 2 17 . 6 TYR HB3 H 2.95 . 2 18 . 6 TYR C C 176.41 . 1 19 . 6 TYR CA C 58.25 . 1 20 . 6 TYR CB C 38.78 . 1 21 . 6 TYR N N 121.90 . 1 22 . 7 GLY H H 8.35 . 1 23 . 7 GLY HA2 H 3.91 . 1 24 . 7 GLY HA3 H 3.91 . 1 25 . 7 GLY C C 173.96 . 1 26 . 7 GLY CA C 45.49 . 1 27 . 7 GLY N N 109.98 . 1 28 . 8 ASP H H 8.16 . 1 29 . 8 ASP HA H 4.59 . 1 30 . 8 ASP HB2 H 2.69 . 1 31 . 8 ASP HB3 H 2.69 . 1 32 . 8 ASP C C 176.48 . 1 33 . 8 ASP CA C 54.41 . 1 34 . 8 ASP CB C 41.40 . 1 35 . 8 ASP N N 120.52 . 1 36 . 9 ALA H H 8.29 . 1 37 . 9 ALA HA H 4.23 . 1 38 . 9 ALA HB H 1.42 . 1 39 . 9 ALA C C 177.77 . 1 40 . 9 ALA CA C 53.12 . 1 41 . 9 ALA CB C 19.09 . 1 42 . 9 ALA N N 123.96 . 1 43 . 10 ALA H H 8.19 . 1 44 . 10 ALA HA H 4.26 . 1 45 . 10 ALA HB H 1.37 . 1 46 . 10 ALA C C 177.36 . 1 47 . 10 ALA CA C 52.52 . 1 48 . 10 ALA CB C 19.19 . 1 49 . 10 ALA N N 121.57 . 1 50 . 11 ALA H H 7.93 . 1 51 . 11 ALA HA H 4.25 . 1 52 . 11 ALA HB H 1.33 . 1 53 . 11 ALA C C 177.16 . 1 54 . 11 ALA CA C 52.45 . 1 55 . 11 ALA CB C 19.26 . 1 56 . 11 ALA N N 122.38 . 1 57 . 12 ILE H H 7.78 . 1 58 . 12 ILE HA H 3.89 . 1 59 . 12 ILE HB H 1.70 . 1 60 . 12 ILE C C 176.75 . 1 61 . 12 ILE CA C 61.22 . 1 62 . 12 ILE CB C 38.51 . 1 63 . 12 ILE N N 119.37 . 1 64 . 13 GLY H H 8.61 . 1 65 . 13 GLY HA2 H 3.99 . 1 66 . 13 GLY HA3 H 3.99 . 1 67 . 13 GLY C C 174.89 . 1 68 . 13 GLY CA C 45.61 . 1 69 . 13 GLY N N 113.74 . 1 70 . 14 SER H H 8.48 . 1 71 . 14 SER HA H 4.31 . 1 72 . 14 SER HB2 H 3.94 . 1 73 . 14 SER HB3 H 3.94 . 1 74 . 14 SER C C 175.50 . 1 75 . 14 SER CA C 59.82 . 1 76 . 14 SER CB C 63.54 . 1 77 . 14 SER N N 116.26 . 1 78 . 15 GLY H H 8.72 . 1 79 . 15 GLY HA2 H 4.10 . 2 80 . 15 GLY HA3 H 3.85 . 2 81 . 15 GLY C C 174.31 . 1 82 . 15 GLY CA C 45.09 . 1 83 . 15 GLY N N 110.05 . 1 84 . 16 VAL H H 7.43 . 1 85 . 16 VAL HA H 4.19 . 1 86 . 16 VAL HB H 1.97 . 1 87 . 16 VAL CA C 60.60 . 1 88 . 16 VAL CB C 32.98 . 1 89 . 16 VAL N N 122.43 . 1 90 . 17 PRO HA H 4.47 . 1 91 . 17 PRO C C 177.53 . 1 92 . 17 PRO CA C 63.36 . 1 93 . 17 PRO CB C 32.94 . 1 94 . 18 ALA H H 8.96 . 1 95 . 18 ALA HA H 4.17 . 1 96 . 18 ALA HB H 1.57 . 1 97 . 18 ALA C C 179.37 . 1 98 . 18 ALA CA C 55.77 . 1 99 . 18 ALA CB C 18.51 . 1 100 . 18 ALA N N 128.10 . 1 101 . 19 PHE H H 9.15 . 1 102 . 19 PHE HA H 4.34 . 1 103 . 19 PHE HB2 H 3.63 . 1 104 . 19 PHE HB3 H 3.63 . 1 105 . 19 PHE C C 178.10 . 1 106 . 19 PHE CA C 62.59 . 1 107 . 19 PHE CB C 40.83 . 1 108 . 19 PHE N N 115.40 . 1 109 . 20 LEU H H 6.96 . 1 110 . 20 LEU HA H 3.91 . 1 111 . 20 LEU HB2 H 1.88 . 2 112 . 20 LEU HB3 H 1.35 . 2 113 . 20 LEU C C 177.72 . 1 114 . 20 LEU CA C 56.08 . 1 115 . 20 LEU CB C 43.36 . 1 116 . 20 LEU N N 115.18 . 1 117 . 21 ALA H H 8.08 . 1 118 . 21 ALA HA H 4.02 . 1 119 . 21 ALA HB H 1.41 . 1 120 . 21 ALA C C 180.35 . 1 121 . 21 ALA CA C 55.60 . 1 122 . 21 ALA CB C 18.45 . 1 123 . 21 ALA N N 123.46 . 1 124 . 22 LYS H H 8.36 . 1 125 . 22 LYS HA H 3.89 . 1 126 . 22 LYS C C 178.96 . 1 127 . 22 LYS CA C 59.14 . 1 128 . 22 LYS CB C 32.86 . 1 129 . 22 LYS N N 115.50 . 1 130 . 23 LEU H H 7.39 . 1 131 . 23 LEU HA H 3.81 . 1 132 . 23 LEU C C 177.66 . 1 133 . 23 LEU CA C 57.90 . 1 134 . 23 LEU CB C 41.56 . 1 135 . 23 LEU N N 121.31 . 1 136 . 24 TRP H H 8.67 . 1 137 . 24 TRP C C 177.30 . 1 138 . 24 TRP CA C 62.41 . 1 139 . 24 TRP N N 118.61 . 1 140 . 25 ARG H H 7.53 . 1 141 . 25 ARG HA H 3.86 . 1 142 . 25 ARG HB2 H 1.91 . 1 143 . 25 ARG HB3 H 1.91 . 1 144 . 25 ARG C C 178.20 . 1 145 . 25 ARG CA C 59.61 . 1 146 . 25 ARG CB C 29.92 . 1 147 . 25 ARG N N 114.62 . 1 148 . 26 ILE H H 7.98 . 1 149 . 26 ILE HA H 4.05 . 1 150 . 26 ILE C C 178.65 . 1 151 . 26 ILE CA C 57.61 . 1 152 . 26 ILE CB C 43.00 . 1 153 . 26 ILE N N 119.55 . 1 154 . 27 VAL H H 8.09 . 1 155 . 27 VAL HA H 2.54 . 1 156 . 27 VAL CA C 67.03 . 1 157 . 27 VAL N N 117.83 . 1 158 . 28 ASP HA H 4.23 . 1 159 . 28 ASP C C 176.68 . 1 160 . 28 ASP CA C 57.17 . 1 161 . 28 ASP CB C 43.51 . 1 162 . 29 ASP H H 7.44 . 1 163 . 29 ASP HA H 4.34 . 1 164 . 29 ASP HB2 H 2.87 . 1 165 . 29 ASP HB3 H 2.87 . 1 166 . 29 ASP C C 177.77 . 1 167 . 29 ASP CA C 55.00 . 1 168 . 29 ASP CB C 41.18 . 1 169 . 29 ASP N N 115.85 . 1 170 . 30 ALA H H 8.87 . 1 171 . 30 ALA HA H 4.18 . 1 172 . 30 ALA HB H 1.50 . 1 173 . 30 ALA C C 180.92 . 1 174 . 30 ALA CA C 54.36 . 1 175 . 30 ALA CB C 18.60 . 1 176 . 30 ALA N N 129.34 . 1 177 . 31 ASP H H 8.59 . 1 178 . 31 ASP HA H 4.50 . 1 179 . 31 ASP HB2 H 2.82 . 2 180 . 31 ASP HB3 H 2.70 . 2 181 . 31 ASP C C 178.30 . 1 182 . 31 ASP CA C 56.77 . 1 183 . 31 ASP CB C 40.64 . 1 184 . 31 ASP N N 115.42 . 1 185 . 32 THR H H 7.43 . 1 186 . 32 THR HA H 4.69 . 1 187 . 32 THR C C 175.92 . 1 188 . 32 THR CA C 60.75 . 1 189 . 32 THR CB C 69.19 . 1 190 . 32 THR N N 105.25 . 1 191 . 33 ASN H H 7.57 . 1 192 . 33 ASN HA H 4.87 . 1 193 . 33 ASN HB2 H 2.93 . 1 194 . 33 ASN HB3 H 2.93 . 1 195 . 33 ASN C C 175.63 . 1 196 . 33 ASN CA C 55.12 . 1 197 . 33 ASN CB C 38.01 . 1 198 . 33 ASN N N 122.05 . 1 199 . 34 ARG H H 8.52 . 1 200 . 34 ARG HA H 4.11 . 1 201 . 34 ARG HB2 H 1.82 . 1 202 . 34 ARG HB3 H 1.82 . 1 203 . 34 ARG C C 175.96 . 1 204 . 34 ARG CA C 58.36 . 1 205 . 34 ARG CB C 29.62 . 1 206 . 34 ARG N N 116.53 . 1 207 . 35 LEU H H 7.85 . 1 208 . 35 LEU HA H 4.79 . 1 209 . 35 LEU HB2 H 1.95 . 2 210 . 35 LEU HB3 H 1.55 . 2 211 . 35 LEU C C 175.85 . 1 212 . 35 LEU CA C 55.72 . 1 213 . 35 LEU CB C 46.34 . 1 214 . 35 LEU N N 116.00 . 1 215 . 36 ILE H H 8.29 . 1 216 . 36 ILE HA H 5.61 . 1 217 . 36 ILE HB H 1.79 . 1 218 . 36 ILE C C 172.87 . 1 219 . 36 ILE CA C 58.86 . 1 220 . 36 ILE CB C 38.82 . 1 221 . 36 ILE N N 118.08 . 1 222 . 37 CYS H H 8.84 . 1 223 . 37 CYS HA H 5.01 . 1 224 . 37 CYS HB2 H 3.00 . 2 225 . 37 CYS HB3 H 3.17 . 2 226 . 37 CYS C C 173.34 . 1 227 . 37 CYS CA C 55.37 . 1 228 . 37 CYS CB C 32.04 . 1 229 . 37 CYS N N 121.21 . 1 230 . 38 TRP H H 8.17 . 1 231 . 38 TRP HA H 5.19 . 1 232 . 38 TRP HB2 H 3.63 . 1 233 . 38 TRP HB3 H 3.16 . 1 234 . 38 TRP C C 179.18 . 1 235 . 38 TRP CA C 57.42 . 1 236 . 38 TRP CB C 32.24 . 1 237 . 38 TRP N N 120.77 . 1 238 . 39 THR H H 8.64 . 1 239 . 39 THR HA H 4.49 . 1 240 . 39 THR C C 177.37 . 1 241 . 39 THR CA C 61.95 . 1 242 . 39 THR CB C 70.08 . 1 243 . 39 THR N N 112.13 . 1 244 . 40 LYS H H 8.72 . 1 245 . 40 LYS HA H 4.05 . 1 246 . 40 LYS HB2 H 1.91 . 1 247 . 40 LYS HB3 H 1.91 . 1 248 . 40 LYS C C 178.32 . 1 249 . 40 LYS CA C 60.38 . 1 250 . 40 LYS CB C 32.28 . 1 251 . 40 LYS N N 120.50 . 1 252 . 41 ASP H H 8.34 . 1 253 . 41 ASP HA H 4.74 . 1 254 . 41 ASP HB2 H 2.82 . 1 255 . 41 ASP HB3 H 2.82 . 1 256 . 41 ASP C C 177.99 . 1 257 . 41 ASP CA C 54.07 . 1 258 . 41 ASP CB C 40.67 . 1 259 . 41 ASP N N 115.68 . 1 260 . 42 GLY H H 8.36 . 1 261 . 42 GLY HA2 H 3.74 . 2 262 . 42 GLY HA3 H 3.48 . 2 263 . 42 GLY C C 173.56 . 1 264 . 42 GLY CA C 46.76 . 1 265 . 42 GLY N N 108.17 . 1 266 . 43 GLN H H 8.47 . 1 267 . 43 GLN HA H 4.60 . 1 268 . 43 GLN HB2 H 2.39 . 2 269 . 43 GLN HB3 H 2.09 . 2 270 . 43 GLN C C 176.16 . 1 271 . 43 GLN CA C 55.33 . 1 272 . 43 GLN CB C 29.49 . 1 273 . 43 GLN N N 113.61 . 1 274 . 44 SER H H 8.35 . 1 275 . 44 SER HA H 5.56 . 1 276 . 44 SER C C 171.70 . 1 277 . 44 SER CA C 57.11 . 1 278 . 44 SER CB C 65.03 . 1 279 . 44 SER N N 114.06 . 1 280 . 45 PHE H H 9.08 . 1 281 . 45 PHE HA H 5.85 . 1 282 . 45 PHE HB2 H 2.77 . 1 283 . 45 PHE HB3 H 2.77 . 1 284 . 45 PHE C C 171.42 . 1 285 . 45 PHE CA C 55.99 . 1 286 . 45 PHE CB C 43.72 . 1 287 . 45 PHE N N 115.22 . 1 288 . 46 VAL H H 9.20 . 1 289 . 46 VAL HA H 5.13 . 1 290 . 46 VAL HB H 1.72 . 1 291 . 46 VAL C C 174.73 . 1 292 . 46 VAL CA C 58.54 . 1 293 . 46 VAL CB C 36.27 . 1 294 . 46 VAL N N 117.59 . 1 295 . 47 ILE H H 8.87 . 1 296 . 47 ILE HA H 4.65 . 1 297 . 47 ILE HB H 1.64 . 1 298 . 47 ILE C C 175.91 . 1 299 . 47 ILE CA C 60.17 . 1 300 . 47 ILE CB C 38.77 . 1 301 . 47 ILE N N 124.93 . 1 302 . 48 GLN H H 8.60 . 1 303 . 48 GLN HA H 4.27 . 1 304 . 48 GLN HB2 H 2.22 . 2 305 . 48 GLN HB3 H 1.99 . 2 306 . 48 GLN C C 175.04 . 1 307 . 48 GLN CA C 57.38 . 1 308 . 48 GLN CB C 30.23 . 1 309 . 48 GLN N N 124.28 . 1 310 . 49 ASN H H 7.05 . 1 311 . 49 ASN HA H 4.71 . 1 312 . 49 ASN HB2 H 2.97 . 2 313 . 49 ASN HB3 H 2.81 . 2 314 . 49 ASN C C 175.45 . 1 315 . 49 ASN CA C 53.22 . 1 316 . 49 ASN CB C 39.11 . 1 317 . 49 ASN N N 112.74 . 1 318 . 50 GLN H H 9.20 . 1 319 . 50 GLN HA H 3.85 . 1 320 . 50 GLN HB2 H 2.27 . 1 321 . 50 GLN HB3 H 2.27 . 1 322 . 50 GLN C C 177.12 . 1 323 . 50 GLN CA C 61.06 . 1 324 . 50 GLN CB C 30.00 . 1 325 . 50 GLN N N 124.60 . 1 326 . 51 ALA H H 8.63 . 1 327 . 51 ALA HA H 4.22 . 1 328 . 51 ALA HB H 1.55 . 1 329 . 51 ALA C C 181.08 . 1 330 . 51 ALA CA C 55.45 . 1 331 . 51 ALA CB C 18.30 . 1 332 . 51 ALA N N 121.82 . 1 333 . 52 GLN H H 8.17 . 1 334 . 52 GLN HA H 4.08 . 1 335 . 52 GLN HB2 H 2.00 . 1 336 . 52 GLN HB3 H 2.00 . 1 337 . 52 GLN C C 178.20 . 1 338 . 52 GLN CA C 58.38 . 1 339 . 52 GLN CB C 28.42 . 1 340 . 52 GLN N N 118.30 . 1 341 . 53 PHE H H 8.60 . 1 342 . 53 PHE HA H 3.93 . 1 343 . 53 PHE HB2 H 3.31 . 2 344 . 53 PHE HB3 H 3.09 . 2 345 . 53 PHE C C 177.06 . 1 346 . 53 PHE CA C 62.79 . 1 347 . 53 PHE CB C 40.18 . 1 348 . 53 PHE N N 120.22 . 1 349 . 54 ALA H H 8.59 . 1 350 . 54 ALA HA H 3.74 . 1 351 . 54 ALA HB H 1.57 . 1 352 . 54 ALA C C 176.71 . 1 353 . 54 ALA CA C 54.51 . 1 354 . 54 ALA CB C 18.83 . 1 355 . 54 ALA N N 121.04 . 1 356 . 55 LYS H H 7.34 . 1 357 . 55 LYS HA H 4.15 . 1 358 . 55 LYS HB2 H 1.94 . 2 359 . 55 LYS HB3 H 1.82 . 2 360 . 55 LYS C C 177.95 . 1 361 . 55 LYS CA C 58.16 . 1 362 . 55 LYS CB C 33.97 . 1 363 . 55 LYS N N 112.26 . 1 364 . 56 GLU H H 8.17 . 1 365 . 56 GLU HA H 4.34 . 1 366 . 56 GLU HB2 H 1.92 . 1 367 . 56 GLU HB3 H 1.92 . 1 368 . 56 GLU C C 177.66 . 1 369 . 56 GLU CA C 58.01 . 1 370 . 56 GLU CB C 32.14 . 1 371 . 56 GLU N N 113.71 . 1 372 . 57 LEU H H 7.60 . 1 373 . 57 LEU HA H 4.42 . 1 374 . 57 LEU HB2 H 1.29 . 2 375 . 57 LEU HB3 H 0.93 . 2 376 . 57 LEU C C 179.28 . 1 377 . 57 LEU CA C 55.87 . 1 378 . 57 LEU CB C 42.64 . 1 379 . 57 LEU N N 115.46 . 1 380 . 58 LEU H H 7.14 . 1 381 . 58 LEU HA H 3.90 . 1 382 . 58 LEU HB2 H 1.83 . 2 383 . 58 LEU HB3 H 1.35 . 2 384 . 58 LEU CA C 59.96 . 1 385 . 58 LEU CB C 38.60 . 1 386 . 58 LEU N N 120.70 . 1 387 . 59 PRO HA H 4.02 . 1 388 . 59 PRO C C 179.29 . 1 389 . 59 PRO CA C 66.54 . 1 390 . 59 PRO CB C 31.20 . 1 391 . 60 LEU H H 6.33 . 1 392 . 60 LEU HA H 4.01 . 1 393 . 60 LEU HB2 H 1.57 . 2 394 . 60 LEU HB3 H 1.50 . 2 395 . 60 LEU C C 177.31 . 1 396 . 60 LEU CA C 56.67 . 1 397 . 60 LEU CB C 43.03 . 1 398 . 60 LEU N N 114.30 . 1 399 . 61 ASN H H 7.20 . 1 400 . 61 ASN HA H 4.39 . 1 401 . 61 ASN C C 174.20 . 1 402 . 61 ASN CA C 55.62 . 1 403 . 61 ASN CB C 42.76 . 1 404 . 61 ASN N N 112.78 . 1 405 . 62 TYR H H 8.66 . 1 406 . 62 TYR HA H 4.85 . 1 407 . 62 TYR C C 174.71 . 1 408 . 62 TYR CA C 57.51 . 1 409 . 62 TYR CB C 40.22 . 1 410 . 62 TYR N N 115.39 . 1 411 . 63 LYS H H 7.75 . 1 412 . 63 LYS HA H 4.17 . 1 413 . 63 LYS C C 174.88 . 1 414 . 63 LYS CA C 57.73 . 1 415 . 63 LYS CB C 29.38 . 1 416 . 63 LYS N N 114.74 . 1 417 . 64 HIS H H 7.43 . 1 418 . 64 HIS HA H 4.66 . 1 419 . 64 HIS C C 172.08 . 1 420 . 64 HIS CA C 55.61 . 1 421 . 64 HIS CB C 32.26 . 1 422 . 64 HIS N N 114.19 . 1 423 . 65 ASN H H 7.95 . 1 424 . 65 ASN HA H 4.93 . 1 425 . 65 ASN CA C 51.72 . 1 426 . 65 ASN CB C 39.73 . 1 427 . 65 ASN N N 115.75 . 1 428 . 66 ASN HA H 4.85 . 1 429 . 66 ASN C C 175.12 . 1 430 . 66 ASN CA C 52.93 . 1 431 . 66 ASN CB C 40.03 . 1 432 . 67 MET H H 9.04 . 1 433 . 67 MET HA H 4.39 . 1 434 . 67 MET HB2 H 2.34 . 2 435 . 67 MET HB3 H 2.04 . 2 436 . 67 MET C C 177.78 . 1 437 . 67 MET CA C 57.73 . 1 438 . 67 MET CB C 32.54 . 1 439 . 67 MET N N 126.38 . 1 440 . 68 ALA H H 8.40 . 1 441 . 68 ALA HA H 4.13 . 1 442 . 68 ALA HB H 1.50 . 1 443 . 68 ALA C C 181.25 . 1 444 . 68 ALA CA C 55.64 . 1 445 . 68 ALA CB C 17.62 . 1 446 . 68 ALA N N 120.08 . 1 447 . 69 SER H H 8.03 . 1 448 . 69 SER HA H 4.12 . 1 449 . 69 SER HB2 H 3.76 . 1 450 . 69 SER HB3 H 3.76 . 1 451 . 69 SER C C 176.63 . 1 452 . 69 SER CA C 61.28 . 1 453 . 69 SER CB C 62.80 . 1 454 . 69 SER N N 114.36 . 1 455 . 70 PHE H H 7.78 . 1 456 . 70 PHE HA H 4.39 . 1 457 . 70 PHE HB2 H 3.63 . 2 458 . 70 PHE HB3 H 3.14 . 2 459 . 70 PHE C C 176.29 . 1 460 . 70 PHE CA C 61.24 . 1 461 . 70 PHE CB C 39.97 . 1 462 . 70 PHE N N 123.45 . 1 463 . 71 ILE H H 8.68 . 1 464 . 71 ILE HA H 3.20 . 1 465 . 71 ILE HB H 1.98 . 1 466 . 71 ILE C C 177.93 . 1 467 . 71 ILE CA C 65.22 . 1 468 . 71 ILE CB C 37.51 . 1 469 . 71 ILE N N 119.05 . 1 470 . 72 ARG H H 8.05 . 1 471 . 72 ARG HA H 4.02 . 1 472 . 72 ARG HB2 H 1.91 . 1 473 . 72 ARG HB3 H 1.91 . 1 474 . 72 ARG C C 179.26 . 1 475 . 72 ARG CA C 59.93 . 1 476 . 72 ARG CB C 29.92 . 1 477 . 72 ARG N N 119.67 . 1 478 . 73 GLN H H 7.50 . 1 479 . 73 GLN HA H 3.72 . 1 480 . 73 GLN HB2 H 1.67 . 2 481 . 73 GLN HB3 H 0.93 . 2 482 . 73 GLN C C 177.96 . 1 483 . 73 GLN CA C 59.05 . 1 484 . 73 GLN CB C 28.20 . 1 485 . 73 GLN N N 119.13 . 1 486 . 74 LEU H H 7.51 . 1 487 . 74 LEU HA H 3.69 . 1 488 . 74 LEU HB2 H 1.57 . 2 489 . 74 LEU HB3 H 0.53 . 2 490 . 74 LEU C C 180.35 . 1 491 . 74 LEU CA C 58.09 . 1 492 . 74 LEU CB C 40.18 . 1 493 . 74 LEU N N 117.82 . 1 494 . 75 ASN H H 8.44 . 1 495 . 75 ASN HA H 4.59 . 1 496 . 75 ASN HB2 H 2.93 . 1 497 . 75 ASN HB3 H 2.93 . 1 498 . 75 ASN C C 179.61 . 1 499 . 75 ASN CA C 56.74 . 1 500 . 75 ASN CB C 38.72 . 1 501 . 75 ASN N N 118.11 . 1 502 . 76 MET H H 8.23 . 1 503 . 76 MET HA H 4.34 . 1 504 . 76 MET HB2 H 1.92 . 1 505 . 76 MET HB3 H 1.92 . 1 506 . 76 MET C C 177.05 . 1 507 . 76 MET CA C 58.42 . 1 508 . 76 MET CB C 32.14 . 1 509 . 76 MET N N 121.55 . 1 510 . 77 TYR H H 7.60 . 1 511 . 77 TYR HA H 4.71 . 1 512 . 77 TYR HB2 H 3.69 . 2 513 . 77 TYR HB3 H 2.87 . 2 514 . 77 TYR C C 174.55 . 1 515 . 77 TYR CA C 59.93 . 1 516 . 77 TYR CB C 39.15 . 1 517 . 77 TYR N N 115.62 . 1 518 . 78 GLY H H 7.95 . 1 519 . 78 GLY HA2 H 4.30 . 2 520 . 78 GLY HA3 H 3.87 . 2 521 . 78 GLY C C 176.07 . 1 522 . 78 GLY CA C 46.34 . 1 523 . 78 GLY N N 103.85 . 1 524 . 79 PHE H H 8.28 . 1 525 . 79 PHE HA H 4.68 . 1 526 . 79 PHE HB2 H 2.69 . 2 527 . 79 PHE HB3 H 2.93 . 2 528 . 79 PHE C C 175.95 . 1 529 . 79 PHE CA C 59.12 . 1 530 . 79 PHE CB C 40.13 . 1 531 . 79 PHE N N 118.14 . 1 532 . 80 HIS H H 9.52 . 1 533 . 80 HIS HA H 5.04 . 1 534 . 80 HIS HB2 H 3.16 . 1 535 . 80 HIS HB3 H 3.16 . 1 536 . 80 HIS C C 173.73 . 1 537 . 80 HIS CA C 54.42 . 1 538 . 80 HIS CB C 31.71 . 1 539 . 80 HIS N N 119.71 . 1 540 . 81 LYS H H 8.65 . 1 541 . 81 LYS HA H 4.32 . 1 542 . 81 LYS HB2 H 1.53 . 1 543 . 81 LYS HB3 H 1.53 . 1 544 . 81 LYS C C 176.02 . 1 545 . 81 LYS CA C 55.61 . 1 546 . 81 LYS CB C 33.35 . 1 547 . 81 LYS N N 125.82 . 1 548 . 82 ILE H H 8.39 . 1 549 . 82 ILE HA H 4.16 . 1 550 . 82 ILE HB H 1.53 . 1 551 . 82 ILE C C 175.94 . 1 552 . 82 ILE CA C 60.17 . 1 553 . 82 ILE CB C 38.40 . 1 554 . 82 ILE N N 128.10 . 1 555 . 83 THR H H 8.30 . 1 556 . 83 THR HA H 4.43 . 1 557 . 83 THR HB H 4.13 . 1 558 . 83 THR C C 174.20 . 1 559 . 83 THR CA C 61.38 . 1 560 . 83 THR CB C 70.32 . 1 561 . 83 THR N N 119.97 . 1 562 . 84 SER H H 8.53 . 1 563 . 84 SER HA H 4.49 . 1 564 . 84 SER HB2 H 3.82 . 1 565 . 84 SER HB3 H 3.82 . 1 566 . 84 SER C C 174.72 . 1 567 . 84 SER CA C 58.31 . 1 568 . 84 SER CB C 63.96 . 1 569 . 84 SER N N 119.43 . 1 570 . 85 ILE H H 8.20 . 1 571 . 85 ILE HA H 4.17 . 1 572 . 85 ILE HB H 1.85 . 1 573 . 85 ILE C C 176.11 . 1 574 . 85 ILE CA C 61.51 . 1 575 . 85 ILE CB C 38.85 . 1 576 . 85 ILE N N 121.59 . 1 577 . 86 ASP H H 8.26 . 1 578 . 86 ASP HA H 4.61 . 1 579 . 86 ASP HB2 H 2.66 . 1 580 . 86 ASP HB3 H 2.66 . 1 581 . 86 ASP C C 176.24 . 1 582 . 86 ASP CA C 54.33 . 1 583 . 86 ASP CB C 41.51 . 1 584 . 86 ASP N N 122.93 . 1 585 . 87 ASN H H 8.36 . 1 586 . 87 ASN HA H 4.68 . 1 587 . 87 ASN HB2 H 2.82 . 1 588 . 87 ASN HB3 H 2.82 . 1 589 . 87 ASN C C 176.15 . 1 590 . 87 ASN CA C 53.50 . 1 591 . 87 ASN CB C 38.78 . 1 592 . 87 ASN N N 119.41 . 1 593 . 88 GLY H H 8.48 . 1 594 . 88 GLY HA2 H 3.95 . 1 595 . 88 GLY HA3 H 3.95 . 1 596 . 88 GLY C C 174.94 . 1 597 . 88 GLY CA C 45.87 . 1 598 . 88 GLY N N 108.66 . 1 599 . 89 GLY H H 8.20 . 1 600 . 89 GLY HA2 H 3.92 . 1 601 . 89 GLY HA3 H 3.92 . 1 602 . 89 GLY C C 174.15 . 1 603 . 89 GLY CA C 45.33 . 1 604 . 89 GLY N N 108.21 . 1 605 . 90 LEU H H 8.01 . 1 606 . 90 LEU HA H 4.29 . 1 607 . 90 LEU HB2 H 1.56 . 2 608 . 90 LEU HB3 H 1.47 . 2 609 . 90 LEU C C 177.24 . 1 610 . 90 LEU CA C 55.45 . 1 611 . 90 LEU CB C 42.35 . 1 612 . 90 LEU N N 121.07 . 1 613 . 91 ARG H H 8.25 . 1 614 . 91 ARG HA H 4.31 . 1 615 . 91 ARG HB2 H 1.71 . 1 616 . 91 ARG HB3 H 1.71 . 1 617 . 91 ARG C C 176.11 . 1 618 . 91 ARG CA C 55.76 . 1 619 . 91 ARG CB C 30.92 . 1 620 . 91 ARG N N 120.64 . 1 621 . 92 PHE H H 8.25 . 1 622 . 92 PHE HA H 4.64 . 1 623 . 92 PHE HB2 H 3.22 . 2 624 . 92 PHE HB3 H 3.00 . 2 625 . 92 PHE C C 175.54 . 1 626 . 92 PHE CA C 57.79 . 1 627 . 92 PHE CB C 39.54 . 1 628 . 92 PHE N N 120.70 . 1 629 . 93 ASP H H 8.49 . 1 630 . 93 ASP HA H 4.78 . 1 631 . 93 ASP HB2 H 2.66 . 1 632 . 93 ASP HB3 H 2.66 . 1 633 . 93 ASP C C 175.93 . 1 634 . 93 ASP CA C 54.37 . 1 635 . 93 ASP CB C 41.12 . 1 636 . 93 ASP N N 120.52 . 1 637 . 94 ARG H H 8.06 . 1 638 . 94 ARG HA H 4.44 . 1 639 . 94 ARG HB2 H 1.95 . 2 640 . 94 ARG HB3 H 1.82 . 2 641 . 94 ARG C C 175.79 . 1 642 . 94 ARG CA C 56.03 . 1 643 . 94 ARG CB C 31.43 . 1 644 . 94 ARG N N 119.99 . 1 645 . 95 ASP H H 8.64 . 1 646 . 95 ASP HA H 4.62 . 1 647 . 95 ASP HB2 H 2.66 . 1 648 . 95 ASP HB3 H 2.66 . 1 649 . 95 ASP C C 176.17 . 1 650 . 95 ASP CA C 54.45 . 1 651 . 95 ASP CB C 41.44 . 1 652 . 95 ASP N N 121.82 . 1 653 . 96 GLU H H 8.40 . 1 654 . 96 GLU HA H 4.96 . 1 655 . 96 GLU HB2 H 1.86 . 1 656 . 96 GLU HB3 H 1.86 . 1 657 . 96 GLU C C 176.17 . 1 658 . 96 GLU CA C 55.70 . 1 659 . 96 GLU CB C 31.67 . 1 660 . 96 GLU N N 120.24 . 1 661 . 97 ILE H H 8.35 . 1 662 . 97 ILE HA H 4.39 . 1 663 . 97 ILE HB H 1.55 . 1 664 . 97 ILE C C 171.12 . 1 665 . 97 ILE CA C 60.66 . 1 666 . 97 ILE CB C 41.73 . 1 667 . 97 ILE N N 119.56 . 1 668 . 98 GLU H H 8.13 . 1 669 . 98 GLU HA H 5.17 . 1 670 . 98 GLU HB2 H 1.79 . 1 671 . 98 GLU HB3 H 1.79 . 1 672 . 98 GLU C C 174.01 . 1 673 . 98 GLU CA C 53.84 . 1 674 . 98 GLU CB C 33.47 . 1 675 . 98 GLU N N 127.85 . 1 676 . 99 PHE H H 8.24 . 1 677 . 99 PHE HA H 5.52 . 1 678 . 99 PHE C C 174.82 . 1 679 . 99 PHE CA C 56.08 . 1 680 . 99 PHE CB C 45.54 . 1 681 . 99 PHE N N 120.84 . 1 682 . 100 SER H H 8.86 . 1 683 . 100 SER HA H 5.61 . 1 684 . 100 SER HB2 H 3.97 . 2 685 . 100 SER HB3 H 3.63 . 2 686 . 100 SER C C 173.21 . 1 687 . 100 SER CA C 56.28 . 1 688 . 100 SER CB C 67.65 . 1 689 . 100 SER N N 110.11 . 1 690 . 101 HIS H H 10.12 . 1 691 . 101 HIS HA H 4.65 . 1 692 . 101 HIS CA C 55.87 . 1 693 . 101 HIS CB C 35.31 . 1 694 . 101 HIS N N 126.69 . 1 695 . 102 PRO HA H 4.21 . 1 696 . 102 PRO C C 176.95 . 1 697 . 102 PRO CA C 65.07 . 1 698 . 102 PRO CB C 32.04 . 1 699 . 103 PHE H H 11.10 . 1 700 . 103 PHE HA H 5.06 . 1 701 . 103 PHE HB2 H 2.69 . 1 702 . 103 PHE HB3 H 2.69 . 1 703 . 103 PHE C C 173.73 . 1 704 . 103 PHE CA C 55.05 . 1 705 . 103 PHE CB C 38.48 . 1 706 . 103 PHE N N 117.85 . 1 707 . 104 PHE H H 8.16 . 1 708 . 104 PHE HA H 5.05 . 1 709 . 104 PHE C C 172.89 . 1 710 . 104 PHE CA C 57.19 . 1 711 . 104 PHE CB C 42.89 . 1 712 . 104 PHE N N 124.88 . 1 713 . 105 LYS H H 9.55 . 1 714 . 105 LYS HA H 4.90 . 1 715 . 105 LYS CA C 54.81 . 1 716 . 105 LYS CB C 37.86 . 1 717 . 105 LYS N N 122.72 . 1 718 . 109 PRO HA H 3.27 . 1 719 . 109 PRO C C 176.66 . 1 720 . 109 PRO CA C 64.61 . 1 721 . 109 PRO CB C 29.68 . 1 722 . 110 PHE H H 6.61 . 1 723 . 110 PHE HA H 4.43 . 1 724 . 110 PHE HB2 H 3.28 . 2 725 . 110 PHE HB3 H 3.09 . 2 726 . 110 PHE C C 176.65 . 1 727 . 110 PHE CA C 57.19 . 1 728 . 110 PHE CB C 37.43 . 1 729 . 110 PHE N N 114.34 . 1 730 . 111 LEU H H 6.83 . 1 731 . 111 LEU HA H 4.25 . 1 732 . 111 LEU HB2 H 1.61 . 1 733 . 111 LEU HB3 H 1.61 . 1 734 . 111 LEU C C 177.65 . 1 735 . 111 LEU CA C 55.66 . 1 736 . 111 LEU CB C 42.74 . 1 737 . 111 LEU N N 119.37 . 1 738 . 112 LEU H H 7.25 . 1 739 . 112 LEU HA H 4.01 . 1 740 . 112 LEU HB2 H 1.78 . 1 741 . 112 LEU HB3 H 1.78 . 1 742 . 112 LEU C C 178.55 . 1 743 . 112 LEU CA C 57.84 . 1 744 . 112 LEU CB C 43.26 . 1 745 . 112 LEU N N 116.23 . 1 746 . 113 ASP H H 7.69 . 1 747 . 113 ASP HA H 4.27 . 1 748 . 113 ASP HB2 H 2.75 . 2 749 . 113 ASP HB3 H 2.50 . 2 750 . 113 ASP C C 176.58 . 1 751 . 113 ASP CA C 55.63 . 1 752 . 113 ASP CB C 40.27 . 1 753 . 113 ASP N N 114.68 . 1 754 . 114 GLN H H 7.88 . 1 755 . 114 GLN HA H 4.10 . 1 756 . 114 GLN HB2 H 1.70 . 2 757 . 114 GLN HB3 H 1.45 . 2 758 . 114 GLN C C 176.24 . 1 759 . 114 GLN CA C 55.50 . 1 760 . 114 GLN CB C 29.17 . 1 761 . 114 GLN N N 115.38 . 1 762 . 115 ILE H H 7.42 . 1 763 . 115 ILE HA H 3.94 . 1 764 . 115 ILE HB H 1.93 . 1 765 . 115 ILE C C 174.78 . 1 766 . 115 ILE CA C 63.82 . 1 767 . 115 ILE CB C 36.57 . 1 768 . 115 ILE N N 120.49 . 1 769 . 116 LYS H H 8.29 . 1 770 . 116 LYS HA H 4.80 . 1 771 . 116 LYS HB2 H 1.94 . 2 772 . 116 LYS HB3 H 1.78 . 2 773 . 116 LYS C C 176.06 . 1 774 . 116 LYS CA C 54.37 . 1 775 . 116 LYS CB C 34.96 . 1 776 . 116 LYS N N 126.06 . 1 777 . 117 ARG H H 8.52 . 1 778 . 117 ARG HA H 4.18 . 1 779 . 117 ARG HB2 H 1.59 . 1 780 . 117 ARG HB3 H 1.59 . 1 781 . 117 ARG C C 176.53 . 1 782 . 117 ARG CA C 56.21 . 1 783 . 117 ARG CB C 31.10 . 1 784 . 117 ARG N N 121.03 . 1 785 . 118 LYS H H 8.46 . 1 786 . 118 LYS HA H 4.31 . 1 787 . 118 LYS HB2 H 1.79 . 1 788 . 118 LYS HB3 H 1.79 . 1 789 . 118 LYS C C 176.16 . 1 790 . 118 LYS CA C 56.51 . 1 791 . 118 LYS CB C 33.22 . 1 792 . 118 LYS N N 124.77 . 1 793 . 119 ILE H H 8.19 . 1 794 . 119 ILE HA H 4.21 . 1 795 . 119 ILE HB H 1.86 . 1 796 . 119 ILE C C 176.12 . 1 797 . 119 ILE CA C 60.90 . 1 798 . 119 ILE CB C 38.99 . 1 799 . 119 ILE N N 122.34 . 1 800 . 120 SER H H 8.39 . 1 801 . 120 SER HA H 4.49 . 1 802 . 120 SER HB2 H 3.84 . 1 803 . 120 SER HB3 H 3.84 . 1 804 . 120 SER C C 174.11 . 1 805 . 120 SER CA C 58.04 . 1 806 . 120 SER CB C 64.11 . 1 807 . 120 SER N N 119.72 . 1 808 . 121 ASN H H 8.53 . 1 809 . 121 ASN HA H 4.74 . 1 810 . 121 ASN HB2 H 2.81 . 1 811 . 121 ASN HB3 H 2.81 . 1 812 . 121 ASN C C 174.89 . 1 813 . 121 ASN CA C 53.25 . 1 814 . 121 ASN CB C 38.98 . 1 815 . 121 ASN N N 121.01 . 1 816 . 122 ASN H H 8.40 . 1 817 . 122 ASN HA H 4.69 . 1 818 . 122 ASN HB2 H 2.80 . 1 819 . 122 ASN HB3 H 2.80 . 1 820 . 122 ASN C C 175.36 . 1 821 . 122 ASN CA C 53.41 . 1 822 . 122 ASN CB C 38.92 . 1 823 . 122 ASN N N 118.88 . 1 824 . 123 LYS H H 8.38 . 1 825 . 123 LYS HA H 4.30 . 1 826 . 123 LYS HB2 H 1.84 . 2 827 . 123 LYS HB3 H 1.79 . 2 828 . 123 LYS C C 176.48 . 1 829 . 123 LYS CA C 56.71 . 1 830 . 123 LYS CB C 32.76 . 1 831 . 123 LYS N N 121.58 . 1 832 . 124 ASN H H 8.44 . 1 833 . 124 ASN HA H 4.71 . 1 834 . 124 ASN HB2 H 2.84 . 2 835 . 124 ASN HB3 H 2.80 . 2 836 . 124 ASN C C 175.73 . 1 837 . 124 ASN CA C 53.49 . 1 838 . 124 ASN CB C 39.08 . 1 839 . 124 ASN N N 118.91 . 1 840 . 125 GLY H H 8.30 . 1 841 . 125 GLY HA2 H 3.96 . 1 842 . 125 GLY HA3 H 3.96 . 1 843 . 125 GLY C C 173.97 . 1 844 . 125 GLY CA C 45.60 . 1 845 . 125 GLY N N 109.01 . 1 846 . 126 ASP H H 8.21 . 1 847 . 126 ASP HA H 4.62 . 1 848 . 126 ASP HB2 H 2.66 . 1 849 . 126 ASP HB3 H 2.66 . 1 850 . 126 ASP C C 176.15 . 1 851 . 126 ASP CA C 54.40 . 1 852 . 126 ASP CB C 41.34 . 1 853 . 126 ASP N N 120.01 . 1 854 . 127 ASP H H 8.32 . 1 855 . 127 ASP HA H 4.57 . 1 856 . 127 ASP HB2 H 2.69 . 1 857 . 127 ASP HB3 H 2.69 . 1 858 . 127 ASP C C 176.67 . 1 859 . 127 ASP CA C 54.53 . 1 860 . 127 ASP CB C 41.08 . 1 861 . 127 ASP N N 120.29 . 1 862 . 128 LYS H H 8.29 . 1 863 . 128 LYS HA H 4.28 . 1 864 . 128 LYS HB2 H 1.89 . 2 865 . 128 LYS HB3 H 1.82 . 2 866 . 128 LYS C C 177.38 . 1 867 . 128 LYS CA C 56.66 . 1 868 . 128 LYS CB C 32.55 . 1 869 . 128 LYS N N 120.80 . 1 870 . 129 GLY H H 8.41 . 1 871 . 129 GLY HA2 H 3.93 . 1 872 . 129 GLY HA3 H 3.93 . 1 873 . 129 GLY C C 174.17 . 1 874 . 129 GLY CA C 45.56 . 1 875 . 129 GLY N N 108.94 . 1 876 . 130 VAL H H 7.85 . 1 877 . 130 VAL HA H 4.09 . 1 878 . 130 VAL HB H 2.08 . 1 879 . 130 VAL C C 176.08 . 1 880 . 130 VAL CA C 62.32 . 1 881 . 130 VAL CB C 32.73 . 1 882 . 130 VAL N N 118.67 . 1 883 . 131 LEU H H 8.26 . 1 884 . 131 LEU HA H 4.35 . 1 885 . 131 LEU HB2 H 1.58 . 1 886 . 131 LEU HB3 H 1.58 . 1 887 . 131 LEU C C 176.82 . 1 888 . 131 LEU CA C 55.06 . 1 889 . 131 LEU CB C 42.33 . 1 890 . 131 LEU N N 125.59 . 1 891 . 132 LYS H H 8.25 . 1 892 . 132 LYS HA H 4.61 . 1 893 . 132 LYS HB2 H 1.81 . 2 894 . 132 LYS HB3 H 1.72 . 2 895 . 132 LYS CA C 54.02 . 1 896 . 132 LYS CB C 32.71 . 1 897 . 132 LYS N N 123.64 . 1 898 . 133 PRO HA H 4.39 . 1 899 . 133 PRO HB2 H 2.29 . 2 900 . 133 PRO HB3 H 1.91 . 2 901 . 133 PRO C C 176.58 . 1 902 . 133 PRO CA C 63.08 . 1 903 . 133 PRO CB C 32.18 . 1 904 . 134 ALA H H 8.35 . 1 905 . 134 ALA HA H 4.28 . 1 906 . 134 ALA HB H 1.40 . 1 907 . 134 ALA C C 177.33 . 1 908 . 134 ALA CA C 52.44 . 1 909 . 134 ALA CB C 19.42 . 1 910 . 134 ALA N N 124.24 . 1 911 . 135 ALA H H 8.23 . 1 912 . 135 ALA HA H 4.33 . 1 913 . 135 ALA HB H 1.38 . 1 914 . 135 ALA C C 176.62 . 1 915 . 135 ALA CA C 52.39 . 1 916 . 135 ALA CB C 19.53 . 1 917 . 135 ALA N N 123.39 . 1 918 . 136 GLU H H 7.88 . 1 919 . 136 GLU HA H 4.12 . 1 920 . 136 GLU HB2 H 1.87 . 1 921 . 136 GLU HB3 H 1.87 . 1 922 . 136 GLU CA C 57.97 . 1 923 . 136 GLU CB C 31.39 . 1 924 . 136 GLU N N 124.81 . 1 stop_ save_