data_6588 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone resonance assignments of apolipoprotein A-I(1-186) in ipid-mimetic solution ; _BMRB_accession_number 6588 _BMRB_flat_file_name bmr6588.str _Entry_type original _Submission_date 2005-04-12 _Accession_date 2005-04-12 _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 Okon Mark S. . 2 Frank Philippe G. . 3 Marcel Yves L. . 4 Cushley Robert J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 334 "13C chemical shifts" 360 "15N chemical shifts" 173 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-26 original author . stop_ _Original_release_date 2005-05-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full 'Okon M, Frank PG, Marcel YL, Cushley RJ. Secondary structure of human lipoprotein A-I(1-186) in lipid-mimetic solution. FEBS Lett. 487 (2001) 390-396' _Citation_title 'Secondary structure of human lipoprotein A-I(1-186) in lipid-mimetic solution' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11163364 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Okon Mark . . 2 Frank Philippe G. . 3 Marcel Yves L. . 4 Cushley Robert J. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 487 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 390 _Page_last 396 _Year 2001 _Details . loop_ _Keyword apolipoprotein 'chemical shift index' 'nuclear magnetic resonance' 'protein structure' 'sodium dodecyl sulfate' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'apolipoprotein A-I(1-186)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'apolipoprotein A-I(1-186)' $apolipoprotein_A-I(1-186) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_apolipoprotein_A-I(1-186) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'apolipoprotein A-I(1-186)' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 186 _Mol_residue_sequence ; DEPPQSPWDRVKDLATVYVD VLKDSGRDYVSQFEGSALGK QLNLKLLDNWDSVTSTFSKL REQLGPVTQEFWDNLEKETE GLRQEMSKDLEEVKAKVQPY LDDFQKKWQEEMELYRQKVE PLRAELQEGARQKLHELQEK LSPLGEEMRDRARAHVDALR THLAPYSDELRQRLAARLEA LKENGG ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 GLU 3 PRO 4 PRO 5 GLN 6 SER 7 PRO 8 TRP 9 ASP 10 ARG 11 VAL 12 LYS 13 ASP 14 LEU 15 ALA 16 THR 17 VAL 18 TYR 19 VAL 20 ASP 21 VAL 22 LEU 23 LYS 24 ASP 25 SER 26 GLY 27 ARG 28 ASP 29 TYR 30 VAL 31 SER 32 GLN 33 PHE 34 GLU 35 GLY 36 SER 37 ALA 38 LEU 39 GLY 40 LYS 41 GLN 42 LEU 43 ASN 44 LEU 45 LYS 46 LEU 47 LEU 48 ASP 49 ASN 50 TRP 51 ASP 52 SER 53 VAL 54 THR 55 SER 56 THR 57 PHE 58 SER 59 LYS 60 LEU 61 ARG 62 GLU 63 GLN 64 LEU 65 GLY 66 PRO 67 VAL 68 THR 69 GLN 70 GLU 71 PHE 72 TRP 73 ASP 74 ASN 75 LEU 76 GLU 77 LYS 78 GLU 79 THR 80 GLU 81 GLY 82 LEU 83 ARG 84 GLN 85 GLU 86 MET 87 SER 88 LYS 89 ASP 90 LEU 91 GLU 92 GLU 93 VAL 94 LYS 95 ALA 96 LYS 97 VAL 98 GLN 99 PRO 100 TYR 101 LEU 102 ASP 103 ASP 104 PHE 105 GLN 106 LYS 107 LYS 108 TRP 109 GLN 110 GLU 111 GLU 112 MET 113 GLU 114 LEU 115 TYR 116 ARG 117 GLN 118 LYS 119 VAL 120 GLU 121 PRO 122 LEU 123 ARG 124 ALA 125 GLU 126 LEU 127 GLN 128 GLU 129 GLY 130 ALA 131 ARG 132 GLN 133 LYS 134 LEU 135 HIS 136 GLU 137 LEU 138 GLN 139 GLU 140 LYS 141 LEU 142 SER 143 PRO 144 LEU 145 GLY 146 GLU 147 GLU 148 MET 149 ARG 150 ASP 151 ARG 152 ALA 153 ARG 154 ALA 155 HIS 156 VAL 157 ASP 158 ALA 159 LEU 160 ARG 161 THR 162 HIS 163 LEU 164 ALA 165 PRO 166 TYR 167 SER 168 ASP 169 GLU 170 LEU 171 ARG 172 GLN 173 ARG 174 LEU 175 ALA 176 ALA 177 ARG 178 LEU 179 GLU 180 ALA 181 LEU 182 LYS 183 GLU 184 ASN 185 GLY 186 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 15093 preB_ApoAI 100.00 243 100.00 100.00 1.23e-129 BMRB 6587 apolipoprotein_A-I 100.00 243 100.00 100.00 1.23e-129 PDB 1AV1 "Crystal Structure Of Human Apolipoprotein A-I" 76.88 201 100.00 100.00 3.11e-95 PDB 2A01 "Crystal Structure Of Lipid-Free Human Apolipoprotein A-I" 100.00 243 100.00 100.00 1.23e-129 PDB 3J00 "Structure Of The Ribosome-secye Complex In The Membrane Environment" 76.88 200 100.00 100.00 3.18e-95 PDB 3K2S "Solution Structure Of Double Super Helix Model" 100.00 243 100.00 100.00 1.23e-129 PDB 3R2P "2.2 Angstrom Crystal Structure Of C Terminal Truncated Human Apolipoprotein A-I Reveals The Assembly Of Hdl By Dimerization" 98.92 185 100.00 100.00 1.88e-127 DBJ BAF84920 "unnamed protein product [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 DBJ BAI46675 "apolipoprotein A-I [synthetic construct]" 100.00 267 100.00 100.00 1.68e-129 EMBL CAA25232 "unnamed protein product [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 EMBL CAA25519 "apolipoprotein AI precursor [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 EMBL CAA26097 "preproapolipoprotein AI [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 EMBL CAA30377 "ApoA-I [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 GB AAA35545 "proapo-A-I protein [Homo sapiens]" 100.00 267 99.46 100.00 1.02e-128 GB AAA51747 "proapolipoprotein, partial [Homo sapiens]" 100.00 249 100.00 100.00 2.86e-129 GB AAA62829 "proapolipoprotein [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 GB AAB59514 "preproapolipoprotein A-I [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 GB AAH05380 "Apolipoprotein A-I [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 REF NP_000030 "apolipoprotein A-I preproprotein [Homo sapiens]" 100.00 267 100.00 100.00 1.68e-129 REF XP_001153383 "PREDICTED: apolipoprotein A-I [Pan troglodytes]" 100.00 267 100.00 100.00 1.68e-129 REF XP_001153517 "PREDICTED: apolipoprotein A-I [Pan troglodytes]" 100.00 267 100.00 100.00 1.68e-129 REF XP_003253233 "PREDICTED: apolipoprotein A-I isoform 1 [Nomascus leucogenys]" 100.00 267 97.85 98.39 6.59e-127 REF XP_003253235 "PREDICTED: apolipoprotein A-I isoform 3 [Nomascus leucogenys]" 100.00 267 97.85 98.39 6.59e-127 SP G3QY98 "RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapoli" 100.00 267 100.00 100.00 1.68e-129 SP P02647 "RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapoli" 100.00 267 100.00 100.00 1.68e-129 SP P0DJG0 "RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapoli" 100.00 267 100.00 100.00 1.68e-129 SP P0DJG1 "RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapoli" 100.00 267 97.85 99.46 1.32e-127 SP P0DM91 "RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapoli" 100.00 267 99.46 99.46 7.66e-129 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $apolipoprotein_A-I(1-186) human 9606 Eukaryota Metazoa Homo sapiens 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 $apolipoprotein_A-I(1-186) 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'SDS was used to mimic lipid environment' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $assembly 2 mM . $assembly 280 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.1 pH temperature 312 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'apolipoprotein A-I(1-186)' _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 1 ASP H H 8.33 0.02 1 2 1 1 ASP HA H 4.56 0.02 1 3 1 1 ASP C C 175.9 0.2 1 4 1 1 ASP CA C 55.2 0.3 1 5 1 1 ASP N N 121.2 0.1 1 6 2 2 GLU H H 7.98 0.02 1 7 2 2 GLU HA H 4.62 0.02 1 8 2 2 GLU C C 173.6 0.2 1 9 2 2 GLU CA C 54.1 0.3 1 10 2 2 GLU N N 120.2 0.1 1 11 4 4 PRO HA H 4.44 0.02 1 12 4 4 PRO C C 176.7 0.2 1 13 4 4 PRO CA C 63.1 0.3 1 14 5 5 GLN H H 8.21 0.02 1 15 5 5 GLN HA H 4.37 0.02 1 16 5 5 GLN C C 175.7 0.2 1 17 5 5 GLN CA C 55.9 0.3 1 18 5 5 GLN N N 119.6 0.1 1 19 6 6 SER H H 8.63 0.02 1 20 6 6 SER C C 175.7 0.2 1 21 6 6 SER CA C 56.5 0.3 1 22 6 6 SER N N 117.9 0.1 1 23 7 7 PRO HA H 4.3 0.02 1 24 7 7 PRO C C 177.6 0.2 1 25 7 7 PRO CA C 65.1 0.3 1 26 8 8 TRP H H 7.71 0.02 1 27 8 8 TRP HA H 4.62 0.02 1 28 8 8 TRP C C 177.4 0.2 1 29 8 8 TRP CA C 58.6 0.3 1 30 8 8 TRP N N 116.2 0.1 1 31 9 9 ASP H H 7.74 0.02 1 32 9 9 ASP HA H 4.22 0.02 1 33 9 9 ASP C C 178.6 0.2 1 34 9 9 ASP CA C 57.5 0.3 1 35 9 9 ASP N N 118.5 0.1 1 36 10 10 ARG H H 7.76 0.02 1 37 10 10 ARG HA H 4.13 0.02 1 38 10 10 ARG C C 178.7 0.2 1 39 10 10 ARG CA C 58.7 0.3 1 40 10 10 ARG N N 118.1 0.1 1 41 11 11 VAL H H 7.89 0.02 1 42 11 11 VAL HA H 3.66 0.02 1 43 11 11 VAL C C 177.3 0.2 1 44 11 11 VAL CA C 66.2 0.3 1 45 11 11 VAL N N 118.3 0.1 1 46 12 12 LYS H H 8.03 0.02 1 47 12 12 LYS HA H 3.69 0.02 1 48 12 12 LYS C C 178.9 0.2 1 49 12 12 LYS CA C 60.5 0.3 1 50 12 12 LYS N N 119.2 0.1 1 51 13 13 ASP H H 7.88 0.02 1 52 13 13 ASP HA H 4.42 0.02 1 53 13 13 ASP C C 178.8 0.2 1 54 13 13 ASP CA C 57.2 0.3 1 55 13 13 ASP N N 119 0.1 1 56 14 14 LEU H H 7.87 0.02 1 57 14 14 LEU HA H 4.19 0.02 1 58 14 14 LEU C C 178.8 0.2 1 59 14 14 LEU CA C 57.6 0.3 1 60 14 14 LEU N N 120.2 0.1 1 61 15 15 ALA H H 8.48 0.02 1 62 15 15 ALA HA H 4.08 0.02 1 63 15 15 ALA C C 179.1 0.2 1 64 15 15 ALA CA C 55.2 0.3 1 65 15 15 ALA N N 119.7 0.1 1 66 16 16 THR H H 7.87 0.02 1 67 16 16 THR HA H 3.95 0.02 1 68 16 16 THR C C 176.2 0.2 1 69 16 16 THR CA C 66.4 0.3 1 70 16 16 THR N N 110 0.1 1 71 17 17 VAL H H 7.45 0.02 1 72 17 17 VAL HA H 3.8 0.02 1 73 17 17 VAL C C 178.2 0.2 1 74 17 17 VAL CA C 65.5 0.3 1 75 17 17 VAL N N 120.3 0.1 1 76 18 18 TYR H H 7.78 0.02 1 77 18 18 TYR HA H 4.4 0.02 1 78 18 18 TYR C C 177.6 0.2 1 79 18 18 TYR CA C 61.3 0.3 1 80 18 18 TYR N N 117.8 0.1 1 81 19 19 VAL H H 8.2 0.02 1 82 19 19 VAL HA H 3.68 0.02 1 83 19 19 VAL C C 177.2 0.2 1 84 19 19 VAL CA C 67.4 0.3 1 85 19 19 VAL N N 119.7 0.1 1 86 20 20 ASP H H 7.9 0.02 1 87 20 20 ASP HA H 4.45 0.02 1 88 20 20 ASP C C 178.7 0.2 1 89 20 20 ASP CA C 57.4 0.3 1 90 20 20 ASP N N 119.1 0.1 1 91 21 21 VAL H H 7.58 0.02 1 92 21 21 VAL HA H 3.92 0.02 1 93 21 21 VAL C C 178.7 0.2 1 94 21 21 VAL CA C 65.7 0.3 1 95 21 21 VAL N N 118.8 0.1 1 96 22 22 LEU H H 8.01 0.02 1 97 22 22 LEU HA H 4.08 0.02 1 98 22 22 LEU C C 179.2 0.2 1 99 22 22 LEU CA C 57.9 0.3 1 100 22 22 LEU N N 120.7 0.1 1 101 23 23 LYS H H 8.34 0.02 1 102 23 23 LYS HA H 4 0.02 1 103 23 23 LYS C C 178 0.2 1 104 23 23 LYS CA C 59.7 0.3 1 105 23 23 LYS N N 118.5 0.1 1 106 24 24 ASP H H 7.99 0.02 1 107 24 24 ASP HA H 4.62 0.02 1 108 24 24 ASP C C 178.1 0.2 1 109 24 24 ASP CA C 56.4 0.3 1 110 24 24 ASP N N 118.5 0.1 1 111 25 25 SER H H 8.18 0.02 1 112 25 25 SER HA H 4.5 0.02 1 113 25 25 SER C C 176.2 0.2 1 114 25 25 SER CA C 60.7 0.3 1 115 25 25 SER N N 114.9 0.1 1 116 26 26 GLY H H 8.52 0.02 1 117 26 26 GLY HA2 H 3.9 0.02 1 118 26 26 GLY HA3 H 3.9 0.02 1 119 26 26 GLY C C 174.7 0.2 1 120 26 26 GLY CA C 47.1 0.3 1 121 26 26 GLY N N 110.3 0.1 1 122 27 27 ARG H H 8.15 0.02 1 123 27 27 ARG HA H 4.06 0.02 1 124 27 27 ARG C C 177.7 0.2 1 125 27 27 ARG CA C 58.6 0.3 1 126 27 27 ARG N N 120.2 0.1 1 127 28 28 ASP H H 8.08 0.02 1 128 28 28 ASP HA H 4.5 0.02 1 129 28 28 ASP C C 177.9 0.2 1 130 28 28 ASP CA C 56.2 0.3 1 131 28 28 ASP N N 120 0.1 1 132 29 29 TYR H H 8.01 0.02 1 133 29 29 TYR HA H 4.29 0.02 1 134 29 29 TYR C C 177.9 0.2 1 135 29 29 TYR CA C 61.3 0.3 1 136 29 29 TYR N N 120 0.1 1 137 30 30 VAL H H 7.97 0.02 1 138 30 30 VAL HA H 3.85 0.02 1 139 30 30 VAL C C 177.8 0.2 1 140 30 30 VAL CA C 65.6 0.3 1 141 30 30 VAL N N 116.4 0.1 1 142 31 31 SER H H 7.93 0.02 1 143 31 31 SER HA H 4.32 0.02 1 144 31 31 SER C C 176.1 0.2 1 145 31 31 SER CA C 61 0.3 1 146 31 31 SER N N 115.1 0.1 1 147 32 32 GLN H H 7.65 0.02 1 148 32 32 GLN HA H 4.2 0.02 1 149 32 32 GLN C C 176.5 0.2 1 150 32 32 GLN CA C 57 0.3 1 151 32 32 GLN N N 119.3 0.1 1 152 33 33 PHE H H 7.77 0.02 1 153 33 33 PHE HA H 4.52 0.02 1 154 33 33 PHE C C 176.4 0.2 1 155 33 33 PHE CA C 58.8 0.3 1 156 33 33 PHE N N 119.3 0.1 1 157 34 34 GLU H H 8.09 0.02 1 158 34 34 GLU HA H 4.18 0.02 1 159 34 34 GLU C C 177.1 0.2 1 160 34 34 GLU CA C 57.5 0.3 1 161 34 34 GLU N N 122.3 0.1 1 162 35 35 GLY H H 7.98 0.02 1 163 35 35 GLY HA2 H 4 0.02 1 164 35 35 GLY HA3 H 3.95 0.02 1 165 35 35 GLY C C 174.6 0.2 1 166 35 35 GLY CA C 46 0.3 1 167 35 35 GLY N N 109.3 0.1 1 168 36 36 SER H H 7.91 0.02 1 169 36 36 SER HA H 4.45 0.02 1 170 36 36 SER C C 174.6 0.2 1 171 36 36 SER CA C 59.1 0.3 1 172 36 36 SER N N 115.4 0.1 1 173 37 37 ALA H H 8.29 0.02 1 174 37 37 ALA HA H 4.29 0.02 1 175 37 37 ALA C C 178.3 0.2 1 176 37 37 ALA CA C 53.5 0.3 1 177 37 37 ALA N N 124.9 0.1 1 178 38 38 LEU H H 7.89 0.02 1 179 38 38 LEU HA H 4.18 0.02 1 180 38 38 LEU C C 178.2 0.2 1 181 38 38 LEU CA C 56.6 0.3 1 182 38 38 LEU N N 118.6 0.1 1 183 39 39 GLY H H 8.17 0.02 1 184 39 39 GLY HA2 H 3.86 0.02 1 185 39 39 GLY HA3 H 3.75 0.02 1 186 39 39 GLY C C 175.1 0.2 1 187 39 39 GLY CA C 46.5 0.3 1 188 39 39 GLY N N 107.2 0.1 1 189 40 40 LYS H H 7.72 0.02 1 190 40 40 LYS HA H 4.26 0.02 1 191 40 40 LYS C C 177.1 0.2 1 192 40 40 LYS CA C 57.1 0.3 1 193 40 40 LYS N N 119.1 0.1 1 194 41 41 GLN H H 8.04 0.02 1 195 41 41 GLN HA H 4.3 0.02 1 196 41 41 GLN C C 176.5 0.2 1 197 41 41 GLN CA C 56.6 0.3 1 198 41 41 GLN N N 118.1 0.1 1 199 42 42 LEU H H 7.92 0.03 1 200 42 42 LEU HA H 4.25 0.02 1 201 42 42 LEU C C 176.9 0.2 1 202 42 42 LEU CA C 56 0.3 1 203 42 42 LEU N N 120.7 0.1 1 204 43 43 ASN H H 8.22 0.02 1 205 43 43 ASN HA H 4.61 0.02 1 206 43 43 ASN C C 175.3 0.2 1 207 43 43 ASN CA C 54.2 0.3 1 208 43 43 ASN N N 118.7 0.1 1 209 44 44 LEU H H 7.85 0.02 1 210 44 44 LEU HA H 4.23 0.02 1 211 44 44 LEU C C 177.7 0.2 1 212 44 44 LEU CA C 56.2 0.3 1 213 44 44 LEU N N 120 0.1 1 214 45 45 LYS H H 8.15 0.02 1 215 45 45 LYS HA H 4.21 0.02 1 216 45 45 LYS C C 178.1 0.2 1 217 45 45 LYS CA C 57.7 0.3 1 218 45 45 LYS N N 120.7 0.1 1 219 46 46 LEU H H 7.96 0.02 1 220 46 46 LEU HA H 4.15 0.02 1 221 46 46 LEU C C 178 0.2 1 222 46 46 LEU CA C 57.6 0.3 1 223 46 46 LEU N N 119.8 0.1 1 224 47 47 LEU H H 7.66 0.02 1 225 47 47 LEU HA H 4.2 0.02 1 226 47 47 LEU C C 179.1 0.2 1 227 47 47 LEU CA C 57 0.3 1 228 47 47 LEU N N 116.6 0.1 1 229 48 48 ASP H H 8.04 0.02 1 230 48 48 ASP HA H 4.57 0.02 1 231 48 48 ASP C C 177.2 0.2 1 232 48 48 ASP CA C 56.5 0.3 1 233 48 48 ASP N N 119.2 0.1 1 234 49 49 ASN H H 7.86 0.02 1 235 49 49 ASN HA H 5.03 0.02 1 236 49 49 ASN C C 175.7 0.2 1 237 49 49 ASN CA C 53.4 0.3 1 238 49 49 ASN N N 116 0.1 1 239 50 50 TRP H H 7.95 0.02 1 240 50 50 TRP HA H 4.52 0.02 1 241 50 50 TRP C C 177.2 0.2 1 242 50 50 TRP CA C 59.9 0.3 1 243 50 50 TRP N N 123 0.1 1 244 51 51 ASP H H 8.54 0.02 1 245 51 51 ASP HA H 4.39 0.02 1 246 51 51 ASP C C 178.5 0.2 1 247 51 51 ASP CA C 56.9 0.3 1 248 51 51 ASP N N 118.4 0.1 1 249 52 52 SER H H 7.88 0.02 1 250 52 52 SER HA H 4.38 0.02 1 251 52 52 SER C C 176.6 0.2 1 252 52 52 SER CA C 61.2 0.3 1 253 52 52 SER N N 115.5 0.1 1 254 53 53 VAL H H 7.97 0.02 1 255 53 53 VAL HA H 3.6 0.02 1 256 53 53 VAL C C 177.9 0.2 1 257 53 53 VAL CA C 66.6 0.3 1 258 53 53 VAL N N 123.6 0.1 1 259 54 54 THR H H 8.11 0.02 1 260 54 54 THR HA H 3.8 0.02 1 261 54 54 THR C C 178 0.2 1 262 54 54 THR CA C 66 0.3 1 263 54 54 THR N N 111.3 0.1 1 264 55 55 SER H H 7.93 0.02 1 265 55 55 SER HA H 4.29 0.02 1 266 55 55 SER C C 177.2 0.2 1 267 55 55 SER CA C 61.7 0.3 1 268 55 55 SER N N 118.6 0.1 1 269 56 56 THR H H 7.88 0.02 1 270 56 56 THR HA H 4.35 0.02 1 271 56 56 THR C C 175.9 0.2 1 272 56 56 THR CA C 67.3 0.3 1 273 56 56 THR N N 119.5 0.1 1 274 57 57 PHE H H 8.38 0.02 1 275 57 57 PHE HA H 4.15 0.02 1 276 57 57 PHE C C 177.1 0.2 1 277 57 57 PHE CA C 61.8 0.3 1 278 57 57 PHE N N 120.9 0.1 1 279 58 58 SER H H 8.24 0.02 1 280 58 58 SER HA H 4.07 0.02 1 281 58 58 SER C C 176.9 0.2 1 282 58 58 SER CA C 62.1 0.3 1 283 58 58 SER N N 113.7 0.1 1 284 59 59 LYS H H 7.67 0.02 1 285 59 59 LYS HA H 4.15 0.02 1 286 59 59 LYS C C 179.2 0.2 1 287 59 59 LYS CA C 59.2 0.3 1 288 59 59 LYS N N 121.9 0.1 1 289 60 60 LEU H H 8.02 0.02 1 290 60 60 LEU HA H 4.08 0.02 1 291 60 60 LEU C C 178.9 0.2 1 292 60 60 LEU CA C 57.8 0.3 1 293 60 60 LEU N N 120 0.1 1 294 61 61 ARG H H 8.26 0.02 1 295 61 61 ARG HA H 3.76 0.02 1 296 61 61 ARG C C 178.9 0.2 1 297 61 61 ARG CA C 59.9 0.3 1 298 61 61 ARG N N 118.3 0.1 1 299 62 62 GLU H H 7.75 0.02 1 300 62 62 GLU HA H 4.08 0.02 1 301 62 62 GLU C C 178.4 0.2 1 302 62 62 GLU CA C 58.9 0.3 1 303 62 62 GLU N N 118 0.1 1 304 63 63 GLN H H 7.83 0.02 1 305 63 63 GLN HA H 4.27 0.02 1 306 63 63 GLN C C 177.4 0.2 1 307 63 63 GLN CA C 57.4 0.3 1 308 63 63 GLN N N 116.6 0.1 1 309 64 64 LEU H H 8.1 0.02 1 310 64 64 LEU HA H 4.3 0.02 1 311 64 64 LEU C C 178.4 0.2 1 312 64 64 LEU CA C 56.1 0.3 1 313 64 64 LEU N N 117.5 0.1 1 314 65 65 GLY H H 8.07 0.02 1 315 65 65 GLY HA2 H 3.95 0.02 1 316 65 65 GLY HA3 H 4.2 0.02 1 317 65 65 GLY C C 173.6 0.2 1 318 65 65 GLY CA C 48 0.3 1 319 65 65 GLY N N 108.5 0.1 1 320 66 66 PRO HA H 4.4 0.02 1 321 66 66 PRO C C 178.9 0.2 1 322 66 66 PRO CA C 65.1 0.3 1 323 67 67 VAL H H 7.52 0.02 1 324 67 67 VAL HA H 4.02 0.02 1 325 67 67 VAL C C 177.8 0.2 1 326 67 67 VAL CA C 64.7 0.3 1 327 67 67 VAL N N 116.7 0.1 1 328 68 68 THR H H 8.05 0.02 1 329 68 68 THR HA H 4.16 0.02 1 330 68 68 THR C C 176.2 0.2 1 331 68 68 THR CA C 65.1 0.3 1 332 68 68 THR N N 113.9 0.1 1 333 69 69 GLN H H 8.15 0.02 1 334 69 69 GLN HA H 4.15 0.02 1 335 69 69 GLN C C 177.8 0.2 1 336 69 69 GLN CA C 59 0.3 1 337 69 69 GLN N N 120.5 0.1 1 338 70 70 GLU H H 7.93 0.02 1 339 70 70 GLU HA H 4.14 0.02 1 340 70 70 GLU C C 178.2 0.2 1 341 70 70 GLU CA C 59 0.3 1 342 70 70 GLU N N 118.6 0.1 1 343 71 71 PHE H H 7.89 0.02 1 344 71 71 PHE HA H 4.29 0.02 1 345 71 71 PHE C C 177.5 0.2 1 346 71 71 PHE CA C 61.1 0.3 1 347 71 71 PHE N N 119.9 0.1 1 348 72 72 TRP H H 8.12 0.02 1 349 72 72 TRP HA H 4.3 0.02 1 350 72 72 TRP C C 178.5 0.2 1 351 72 72 TRP CA C 59.4 0.3 1 352 72 72 TRP N N 119.5 0.1 1 353 73 73 ASP H H 8.38 0.02 1 354 73 73 ASP HA H 4.42 0.02 1 355 73 73 ASP C C 178.1 0.2 1 356 73 73 ASP CA C 56.8 0.3 1 357 73 73 ASP N N 118.9 0.1 1 358 74 74 ASN H H 7.82 0.02 1 359 74 74 ASN HA H 4.56 0.02 1 360 74 74 ASN C C 176.1 0.2 1 361 74 74 ASN CA C 54.8 0.3 1 362 74 74 ASN N N 116.9 0.1 1 363 75 75 LEU H H 7.67 0.02 1 364 75 75 LEU HA H 3.99 0.02 1 365 75 75 LEU C C 178.1 0.2 1 366 75 75 LEU CA C 56.6 0.3 1 367 75 75 LEU N N 121.9 0.1 1 368 76 76 GLU C C 177.78 0.2 1 369 76 76 GLU CA C 57.83 0.3 1 370 77 77 LYS H H 7.87 0.02 1 371 77 77 LYS N N 119.6 0.1 1 372 78 78 GLU H H 8.23 0.02 1 373 78 78 GLU HA H 4.35 0.02 1 374 78 78 GLU C C 178.9 0.2 1 375 78 78 GLU CA C 53.6 0.3 1 376 78 78 GLU N N 119.5 0.1 1 377 79 79 THR H H 8.01 0.02 1 378 79 79 THR HA H 4.35 0.02 1 379 79 79 THR C C 176.2 0.2 1 380 79 79 THR CA C 62.5 0.3 1 381 79 79 THR N N 111.7 0.1 1 382 80 80 GLU H H 8.14 0.02 1 383 80 80 GLU HA H 4.18 0.02 1 384 80 80 GLU C C 177.3 0.2 1 385 80 80 GLU CA C 57.9 0.3 1 386 80 80 GLU N N 122.7 0.1 1 387 81 81 GLY H H 8.3 0.02 1 388 81 81 GLY HA2 H 4.02 0.02 1 389 81 81 GLY HA3 H 3.92 0.02 1 390 81 81 GLY C C 175 0.2 1 391 81 81 GLY CA C 45.8 0.3 1 392 81 81 GLY N N 108.8 0.1 1 393 82 82 LEU H H 8.01 0.02 1 394 82 82 LEU HA H 4.2 0.02 1 395 82 82 LEU C C 178.3 0.2 1 396 82 82 LEU CA C 57.3 0.3 1 397 82 82 LEU N N 122.3 0.1 1 398 83 83 ARG H H 8.2 0.02 1 399 83 83 ARG HA H 4.02 0.02 1 400 83 83 ARG C C 177.5 0.2 1 401 83 83 ARG CA C 59.4 0.3 1 402 83 83 ARG N N 118 0.1 1 403 84 84 GLN H H 7.94 0.02 1 404 84 84 GLN C C 177.5 0.2 1 405 84 84 GLN CA C 58.2 0.3 1 406 84 84 GLN N N 118 0.1 1 407 85 85 GLU H H 8.1 0.02 1 408 85 85 GLU C C 178.1 0.2 1 409 85 85 GLU CA C 57.7 0.3 1 410 85 85 GLU N N 119.2 0.1 1 411 86 86 MET H H 8.13 0.02 1 412 86 86 MET HA H 4.38 0.02 1 413 86 86 MET C C 176.8 0.2 1 414 86 86 MET CA C 57 0.3 1 415 86 86 MET N N 118.5 0.1 1 416 87 87 SER H H 8.12 0.02 1 417 87 87 SER HA H 4.3 0.02 1 418 87 87 SER C C 175.5 0.2 1 419 87 87 SER CA C 60.1 0.3 1 420 87 87 SER N N 115.1 0.1 1 421 88 88 LYS H H 7.84 0.02 1 422 88 88 LYS HA H 4.28 0.02 1 423 88 88 LYS C C 176.9 0.2 1 424 88 88 LYS CA C 57.2 0.3 1 425 88 88 LYS N N 121.8 0.1 1 426 89 89 ASP H H 8.18 0.02 1 427 89 89 ASP HA H 4.65 0.02 1 428 89 89 ASP C C 177.4 0.2 1 429 89 89 ASP CA C 54.9 0.3 1 430 89 89 ASP N N 120.1 0.1 1 431 90 90 LEU H H 8.43 0.02 1 432 90 90 LEU HA H 4.15 0.02 1 433 90 90 LEU C C 178.4 0.2 1 434 90 90 LEU CA C 57.5 0.3 1 435 90 90 LEU N N 122.2 0.1 1 436 91 91 GLU H H 8.14 0.02 1 437 91 91 GLU HA H 3.98 0.02 1 438 91 91 GLU C C 179.5 0.2 1 439 91 91 GLU CA C 59.8 0.3 1 440 91 91 GLU N N 118.7 0.1 1 441 92 92 GLU H H 7.95 0.02 1 442 92 92 GLU HA H 4.2 0.02 1 443 92 92 GLU C C 179.1 0.2 1 444 92 92 GLU CA C 59 0.3 1 445 92 92 GLU N N 119.2 0.1 1 446 93 93 VAL H H 7.87 0.02 1 447 93 93 VAL C C 178.7 0.2 1 448 93 93 VAL CA C 66.7 0.3 1 449 93 93 VAL N N 119.7 0.1 1 450 94 94 LYS H H 8.35 0.02 1 451 94 94 LYS C C 178.1 0.2 1 452 94 94 LYS CA C 60.4 0.3 1 453 94 94 LYS N N 118.9 0.1 1 454 95 95 ALA H H 7.63 0.02 1 455 95 95 ALA HA H 4.18 0.02 1 456 95 95 ALA C C 180.1 0.2 1 457 95 95 ALA CA C 54.7 0.3 1 458 95 95 ALA N N 118.2 0.1 1 459 96 96 LYS H H 7.72 0.02 1 460 96 96 LYS HA H 4.25 0.02 1 461 96 96 LYS C C 178.2 0.2 1 462 96 96 LYS CA C 57.9 0.3 1 463 96 96 LYS N N 116.6 0.1 1 464 97 97 VAL H H 7.8 0.02 1 465 97 97 VAL HA H 4.4 0.02 1 466 97 97 VAL C C 177 0.2 1 467 97 97 VAL CA C 63.2 0.3 1 468 97 97 VAL N N 111.9 0.1 1 469 98 98 GLN H H 8.03 0.02 1 470 98 98 GLN HA H 4.02 0.02 1 471 98 98 GLN C C 174.1 0.2 1 472 98 98 GLN CA C 61 0.3 1 473 98 98 GLN N N 121.5 0.1 1 474 99 99 PRO HA H 4.3 0.02 1 475 99 99 PRO C C 178.7 0.2 1 476 99 99 PRO CA C 66.2 0.3 1 477 100 100 TYR H H 7.39 0.02 1 478 100 100 TYR HA H 4.35 0.02 1 479 100 100 TYR C C 177.9 0.2 1 480 100 100 TYR CA C 60.4 0.3 1 481 100 100 TYR N N 114.9 0.1 1 482 101 101 LEU H H 7.78 0.02 1 483 101 101 LEU HA H 4.2 0.02 1 484 101 101 LEU C C 178.8 0.2 1 485 101 101 LEU CA C 58.1 0.3 1 486 101 101 LEU N N 119.4 0.1 1 487 102 102 ASP H H 8.36 0.02 1 488 102 102 ASP HA H 4.43 0.02 1 489 102 102 ASP C C 178.7 0.2 1 490 102 102 ASP CA C 57.4 0.3 1 491 102 102 ASP N N 119.4 0.1 1 492 103 103 ASP H H 7.85 0.02 1 493 103 103 ASP HA H 4.58 0.02 1 494 103 103 ASP C C 178.6 0.2 1 495 103 103 ASP CA C 57.4 0.3 1 496 103 103 ASP N N 119.2 0.1 1 497 104 104 PHE H H 8.37 0.02 1 498 104 104 PHE HA H 4.33 0.02 1 499 104 104 PHE C C 177.1 0.2 1 500 104 104 PHE CA C 61.5 0.3 1 501 104 104 PHE N N 120.9 0.1 1 502 105 105 GLN H H 8.59 0.02 1 503 105 105 GLN HA H 3.92 0.02 1 504 105 105 GLN C C 178.1 0.2 1 505 105 105 GLN CA C 59.6 0.3 1 506 105 105 GLN N N 118.2 0.1 1 507 106 106 LYS H H 7.81 0.02 1 508 106 106 LYS HA H 4.1 0.02 1 509 106 106 LYS C C 178.7 0.2 1 510 106 106 LYS CA C 59.3 0.3 1 511 106 106 LYS N N 118.1 0.1 1 512 107 107 LYS H H 7.87 0.02 1 513 107 107 LYS HA H 4.21 0.02 1 514 107 107 LYS C C 178.5 0.2 1 515 107 107 LYS CA C 58.8 0.3 1 516 107 107 LYS N N 119.7 0.1 1 517 108 108 TRP H H 8.38 0.02 1 518 108 108 TRP HA H 4.35 0.02 1 519 108 108 TRP C C 177.5 0.2 1 520 108 108 TRP CA C 59.9 0.3 1 521 108 108 TRP N N 119.3 0.1 1 522 109 109 GLN H H 8.07 0.02 1 523 109 109 GLN HA H 3.92 0.02 1 524 109 109 GLN CA C 59.3 0.3 1 525 109 109 GLN N N 117.3 0.1 1 526 111 111 GLU HA H 4.23 0.02 1 527 111 111 GLU C C 178.2 0.2 1 528 111 111 GLU CA C 58.8 0.3 1 529 112 112 MET H H 8.33 0.02 1 530 112 112 MET HA H 4.31 0.02 1 531 112 112 MET C C 178.4 0.2 1 532 112 112 MET CA C 58 0.3 1 533 112 112 MET N N 118 0.1 1 534 113 113 GLU H H 7.84 0.02 1 535 113 113 GLU C C 178.7 0.2 1 536 113 113 GLU CA C 59.2 0.3 1 537 113 113 GLU N N 118.5 0.1 1 538 114 114 LEU H H 7.59 0.02 1 539 114 114 LEU C C 179.7 0.2 1 540 114 114 LEU CA C 57.7 0.3 1 541 114 114 LEU N N 120 0.1 1 542 115 115 TYR H H 8.12 0.02 1 543 115 115 TYR C C 177.4 0.2 1 544 115 115 TYR CA C 61.4 0.3 1 545 115 115 TYR N N 118.6 0.1 1 546 116 116 ARG H H 8.21 0.02 1 547 116 116 ARG C C 178.5 0.2 1 548 116 116 ARG CA C 59.7 0.3 1 549 116 116 ARG N N 119 0.1 1 550 117 117 GLN H H 7.63 0.02 1 551 117 117 GLN C C 177.6 0.2 1 552 117 117 GLN CA C 58.2 0.3 1 553 117 117 GLN N N 116.8 0.1 1 554 118 118 LYS H H 7.8 0.02 1 555 118 118 LYS C C 177.4 0.2 1 556 118 118 LYS CA C 57.7 0.3 1 557 118 118 LYS N N 117.4 0.1 1 558 119 119 VAL H H 7.72 0.02 1 559 119 119 VAL HA H 3.7 0.02 1 560 119 119 VAL C C 176.4 0.2 1 561 119 119 VAL CA C 64.1 0.3 1 562 119 119 VAL N N 114.9 0.1 1 563 120 120 GLU H H 7.94 0.02 1 564 120 120 GLU C C 178.4 0.2 1 565 120 120 GLU CA C 60.9 0.3 1 566 120 120 GLU N N 121.8 0.1 1 567 122 122 LEU C C 178.4 0.2 1 568 122 122 LEU CA C 59.4 0.3 1 569 123 123 ARG H H 8.12 0.02 1 570 123 123 ARG C C 177.8 0.2 1 571 123 123 ARG CA C 57.5 0.3 1 572 123 123 ARG N N 118.9 0.1 1 573 124 124 ALA H H 8.01 0.02 1 574 124 124 ALA HA H 4.21 0.02 1 575 124 124 ALA C C 180.2 0.2 1 576 124 124 ALA CA C 54.9 0.3 1 577 124 124 ALA N N 120 0.1 1 578 125 125 GLU H H 7.88 0.02 1 579 125 125 GLU C C 179.1 0.2 1 580 125 125 GLU CA C 58.4 0.3 1 581 125 125 GLU N N 117.6 0.1 1 582 126 126 LEU H H 8.12 0.02 1 583 126 126 LEU C C 178.4 0.2 1 584 126 126 LEU CA C 57.2 0.3 1 585 126 126 LEU N N 120.5 0.1 1 586 127 127 GLN H H 8.24 0.1 1 587 127 127 GLN HA H 3.89 0.02 1 588 127 127 GLN C C 177.6 0.2 1 589 127 127 GLN CA C 59.4 0.3 1 590 127 127 GLN N N 118.2 0.1 1 591 128 128 GLU H H 8.02 0.02 1 592 128 128 GLU HA H 4.17 0.02 1 593 128 128 GLU C C 178.9 0.2 1 594 128 128 GLU CA C 59 0.3 1 595 128 128 GLU N N 118.1 0.1 1 596 129 129 GLY H H 8.33 0.02 1 597 129 129 GLY HA2 H 3.9 0.02 1 598 129 129 GLY HA3 H 4 0.02 1 599 129 129 GLY C C 176.1 0.2 1 600 129 129 GLY CA C 47 0.3 1 601 129 129 GLY N N 108.2 0.1 1 602 130 130 ALA H H 8.49 0.02 1 603 130 130 ALA HA H 4.04 0.02 1 604 130 130 ALA C C 179 0.2 1 605 130 130 ALA CA C 55.4 0.3 1 606 130 130 ALA N N 124.1 0.1 1 607 131 131 ARG H H 8.13 0.02 1 608 131 131 ARG HA H 3.99 0.02 1 609 131 131 ARG C C 178.6 0.2 1 610 131 131 ARG CA C 60.1 0.3 1 611 131 131 ARG N N 116.3 0.1 1 612 132 132 GLN H H 8.03 0.02 1 613 132 132 GLN C C 177.1 0.2 1 614 132 132 GLN CA C 57.1 0.3 1 615 132 132 GLN N N 118.1 0.1 1 616 133 133 LYS H H 8.11 0.02 1 617 133 133 LYS C C 178.9 0.2 1 618 133 133 LYS CA C 59.1 0.3 1 619 133 133 LYS N N 119.7 0.1 1 620 134 134 LEU H H 8.25 0.05 1 621 134 134 LEU C C 178.7 0.2 1 622 134 134 LEU CA C 58.1 0.3 1 623 134 134 LEU N N 118.9 0.1 1 624 135 135 HIS H H 8.11 0.02 1 625 135 135 HIS HA H 4.53 0.02 1 626 135 135 HIS C C 177.6 0.2 1 627 135 135 HIS CA C 59.1 0.3 1 628 135 135 HIS N N 116.8 0.1 1 629 136 136 GLU H H 8.13 0.02 1 630 136 136 GLU C C 178.9 0.2 1 631 136 136 GLU CA C 59.3 0.3 1 632 136 136 GLU N N 119.9 0.1 1 633 137 137 LEU H H 8.08 0.02 1 634 137 137 LEU C C 178.5 0.2 1 635 137 137 LEU CA C 58.1 0.3 1 636 137 137 LEU N N 119.4 0.1 1 637 138 138 GLN H H 8.33 0.02 1 638 138 138 GLN HA H 4.3 0.02 1 639 138 138 GLN C C 178.4 0.2 1 640 138 138 GLN CA C 59.9 0.3 1 641 138 138 GLN N N 118.1 0.1 1 642 139 139 GLU H H 7.82 0.02 1 643 139 139 GLU C C 178.7 0.2 1 644 139 139 GLU CA C 59.1 0.3 1 645 139 139 GLU N N 117.5 0.1 1 646 140 140 LYS H H 7.79 0.02 1 647 140 140 LYS C C 177.9 0.2 1 648 140 140 LYS CA C 58.2 0.3 1 649 140 140 LYS N N 118.1 0.1 1 650 141 141 LEU H H 7.92 0.02 1 651 141 141 LEU HA H 4.39 0.02 1 652 141 141 LEU C C 177.8 0.2 1 653 141 141 LEU CA C 55.8 0.3 1 654 141 141 LEU N N 115.9 0.1 1 655 142 142 SER H H 7.96 0.02 1 656 142 142 SER C C 177.8 0.2 1 657 142 142 SER CA C 62.2 0.3 1 658 142 142 SER N N 115.7 0.1 1 659 143 143 PRO C C 178.2 0.2 1 660 143 143 PRO CA C 65.4 0.3 1 661 144 144 LEU H H 7.69 0.02 1 662 144 144 LEU HA H 4.35 0.02 1 663 144 144 LEU C C 178.6 0.2 1 664 144 144 LEU CA C 56.2 0.3 1 665 144 144 LEU N N 118.1 0.1 1 666 145 145 GLY H H 8.22 0.02 1 667 145 145 GLY HA2 H 3.81 0.02 1 668 145 145 GLY HA3 H 4.1 0.02 1 669 145 145 GLY C C 175.2 0.2 1 670 145 145 GLY CA C 47.3 0.3 1 671 145 145 GLY N N 107.5 0.1 1 672 146 146 GLU H H 8.23 0.02 1 673 146 146 GLU HA H 4 0.02 1 674 146 146 GLU CA C 59.6 0.3 1 675 146 146 GLU N N 120.3 0.1 1 676 147 147 GLU C C 179 0.2 1 677 147 147 GLU CA C 59.1 0.3 1 678 148 148 MET H H 8.28 0.02 1 679 148 148 MET C C 178.2 0.2 1 680 148 148 MET CA C 58.5 0.3 1 681 148 148 MET N N 118.2 0.1 1 682 149 149 ARG H H 8.22 0.02 1 683 149 149 ARG C C 178.2 0.2 1 684 149 149 ARG CA C 60.4 0.3 1 685 149 149 ARG N N 118.9 0.1 1 686 150 150 ASP H H 8.07 0.02 1 687 150 150 ASP HA H 4.44 0.02 1 688 150 150 ASP C C 179.5 0.2 1 689 150 150 ASP CA C 57.6 0.3 1 690 150 150 ASP N N 118.7 0.1 1 691 151 151 ARG H H 8.18 0.02 1 692 151 151 ARG HA H 4.13 0.02 1 693 151 151 ARG C C 179.1 0.2 1 694 151 151 ARG CA C 59.1 0.3 1 695 151 151 ARG N N 119.9 0.1 1 696 152 152 ALA H H 8.5 0.02 1 697 152 152 ALA HA H 4.14 0.02 1 698 152 152 ALA C C 179.4 0.2 1 699 152 152 ALA CA C 55.7 0.3 1 700 152 152 ALA N N 122.2 0.1 1 701 153 153 ARG H H 8.39 0.02 1 702 153 153 ARG HA H 3.95 0.02 1 703 153 153 ARG C C 178.3 0.2 1 704 153 153 ARG CA C 59.5 0.3 1 705 153 153 ARG N N 117.4 0.1 1 706 154 154 ALA H H 7.89 0.02 1 707 154 154 ALA C C 180.7 0.2 1 708 154 154 ALA CA C 54.9 0.3 1 709 154 154 ALA N N 120.1 0.1 1 710 155 155 HIS H H 7.94 0.02 1 711 155 155 HIS HA H 4.63 0.02 1 712 155 155 HIS C C 176.9 0.2 1 713 155 155 HIS CA C 58.2 0.3 1 714 155 155 HIS N N 115.9 0.1 1 715 156 156 VAL H H 8.22 0.02 1 716 156 156 VAL HA H 3.72 0.02 1 717 156 156 VAL C C 177.4 0.2 1 718 156 156 VAL CA C 67.4 0.3 1 719 156 156 VAL N N 120.6 0.1 1 720 157 157 ASP H H 8.43 0.02 1 721 157 157 ASP HA H 4.44 0.02 1 722 157 157 ASP C C 178.9 0.2 1 723 157 157 ASP CA C 57.7 0.3 1 724 157 157 ASP N N 119.9 0.1 1 725 158 158 ALA H H 7.82 0.02 1 726 158 158 ALA HA H 4.22 0.02 1 727 158 158 ALA C C 180.5 0.2 1 728 158 158 ALA CA C 55.1 0.3 1 729 158 158 ALA N N 122.2 0.1 1 730 159 159 LEU H H 8.1 0.02 1 731 159 159 LEU HA H 4.15 0.02 1 732 159 159 LEU C C 179 0.2 1 733 159 159 LEU CA C 58.8 0.3 1 734 159 159 LEU N N 120.2 0.1 1 735 160 160 ARG H H 8.58 0.02 1 736 160 160 ARG HA H 3.88 0.02 1 737 160 160 ARG C C 178.7 0.2 1 738 160 160 ARG CA C 60.7 0.3 1 739 160 160 ARG N N 118.2 0.1 1 740 161 161 THR H H 8.05 0.02 1 741 161 161 THR HA H 4.23 0.02 1 742 161 161 THR C C 176.6 0.2 1 743 161 161 THR CA C 66.1 0.3 1 744 161 161 THR N N 112.5 0.1 1 745 162 162 HIS H H 7.96 0.02 1 746 162 162 HIS HA H 4.56 0.02 1 747 162 162 HIS CA C 58.3 0.3 1 748 162 162 HIS N N 118.4 0.1 1 749 163 163 LEU H H 8.08 0.02 1 750 163 163 LEU HA H 4.55 0.02 1 751 163 163 LEU C C 177.8 0.2 1 752 163 163 LEU CA C 56 0.3 1 753 163 163 LEU N N 116.2 0.1 1 754 164 164 ALA H H 7.85 0.02 1 755 164 164 ALA HA H 4.31 0.02 1 756 164 164 ALA C C 176.6 0.2 1 757 164 164 ALA CA C 56.6 0.3 1 758 164 164 ALA N N 122.7 0.1 1 759 165 165 PRO HA H 4.37 0.02 1 760 165 165 PRO C C 177.9 0.2 1 761 165 165 PRO CA C 65.6 0.3 1 762 166 166 TYR H H 7.72 0.02 1 763 166 166 TYR HA H 4.65 0.02 1 764 166 166 TYR C C 177.1 0.2 1 765 166 166 TYR CA C 58.6 0.3 1 766 166 166 TYR N N 115.4 0.1 1 767 167 167 SER H H 8.05 0.02 1 768 167 167 SER HA H 4.44 0.02 1 769 167 167 SER C C 175.9 0.2 1 770 167 167 SER CA C 62.3 0.3 1 771 167 167 SER N N 115.7 0.1 1 772 168 168 ASP H H 8.32 0.02 1 773 168 168 ASP HA H 4.55 0.02 1 774 168 168 ASP C C 178.6 0.2 1 775 168 168 ASP CA C 57.7 0.3 1 776 168 168 ASP N N 121.1 0.1 1 777 169 169 GLU H H 7.98 0.02 1 778 169 169 GLU HA H 4.15 0.02 1 779 169 169 GLU C C 179.1 0.2 1 780 169 169 GLU CA C 59.1 0.3 1 781 169 169 GLU N N 120 0.1 1 782 170 170 LEU H H 8.3 0.02 1 783 170 170 LEU HA H 4.02 0.02 1 784 170 170 LEU C C 178.7 0.2 1 785 170 170 LEU CA C 58.5 0.3 1 786 170 170 LEU N N 119.5 0.1 1 787 171 171 ARG H H 8.35 0.02 1 788 171 171 ARG HA H 3.84 0.02 1 789 171 171 ARG C C 178.5 0.2 1 790 171 171 ARG CA C 60.6 0.3 1 791 171 171 ARG N N 117.8 0.1 1 792 172 172 GLN H H 7.95 0.02 1 793 172 172 GLN HA H 4.09 0.02 1 794 172 172 GLN C C 179.5 0.2 1 795 172 172 GLN CA C 59.2 0.3 1 796 172 172 GLN N N 117.2 0.1 1 797 173 173 ARG H H 8.22 0.02 1 798 173 173 ARG HA H 4.14 0.02 1 799 173 173 ARG C C 179.6 0.2 1 800 173 173 ARG CA C 59.3 0.3 1 801 173 173 ARG N N 120.4 0.1 1 802 174 174 LEU H H 8.39 0.02 1 803 174 174 LEU HA H 4.06 0.02 1 804 174 174 LEU C C 178.5 0.2 1 805 174 174 LEU CA C 58.2 0.3 1 806 174 174 LEU N N 119.9 0.1 1 807 175 175 ALA H H 8.44 0.02 1 808 175 175 ALA HA H 4.01 0.02 1 809 175 175 ALA C C 180.4 0.2 1 810 175 175 ALA CA C 55.5 0.3 1 811 175 175 ALA N N 120.8 0.1 1 812 176 176 ALA H H 7.8 0.02 1 813 176 176 ALA HA H 4.21 0.02 1 814 176 176 ALA C C 181 0.2 1 815 176 176 ALA CA C 55 0.3 1 816 176 176 ALA N N 118.9 0.1 1 817 177 177 ARG H H 7.81 0.02 1 818 177 177 ARG HA H 4.2 0.02 1 819 177 177 ARG C C 178.7 0.2 1 820 177 177 ARG CA C 57.9 0.3 1 821 177 177 ARG N N 118.7 0.1 1 822 178 178 LEU H H 8.2 0.02 1 823 178 178 LEU HA H 4.09 0.02 1 824 178 178 LEU C C 179 0.2 1 825 178 178 LEU CA C 57.8 0.3 1 826 178 178 LEU N N 119 0.1 1 827 179 179 GLU H H 8.04 0.02 1 828 179 179 GLU HA H 3.97 0.02 1 829 179 179 GLU C C 178.6 0.2 1 830 179 179 GLU CA C 59.2 0.3 1 831 179 179 GLU N N 118.5 0.1 1 832 180 180 ALA H H 7.53 0.02 1 833 180 180 ALA HA H 4.21 0.02 1 834 180 180 ALA C C 179.5 0.2 1 835 180 180 ALA CA C 54.2 0.3 1 836 180 180 ALA N N 119.9 0.1 1 837 181 181 LEU H H 7.66 0.02 1 838 181 181 LEU HA H 4.23 0.02 1 839 181 181 LEU C C 178.2 0.2 1 840 181 181 LEU CA C 56.6 0.3 1 841 181 181 LEU N N 117.8 0.1 1 842 182 182 LYS H H 7.57 0.02 1 843 182 182 LYS HA H 4.25 0.02 1 844 182 182 LYS C C 176.9 0.2 1 845 182 182 LYS CA C 56.8 0.3 1 846 182 182 LYS N N 117.5 0.1 1 847 183 183 GLU H H 7.84 0.02 1 848 183 183 GLU HA H 4.28 0.02 1 849 183 183 GLU C C 175.7 0.2 1 850 183 183 GLU CA C 56.9 0.3 1 851 183 183 GLU N N 120.5 0.1 1 852 184 184 ASN H H 8.28 0.02 1 853 184 184 ASN HA H 4.28 0.02 1 854 184 184 ASN C C 175.9 0.2 1 855 184 184 ASN CA C 54.6 0.3 1 856 184 184 ASN N N 121.3 0.1 1 857 185 185 GLY H H 8.29 0.02 1 858 185 185 GLY HA2 H 3.99 0.02 1 859 185 185 GLY HA3 H 3.89 0.02 1 860 185 185 GLY CA C 46.71 0.3 1 861 185 185 GLY N N 109.8 0.1 1 862 186 186 GLY H H 7.99 0.02 1 863 186 186 GLY HA2 H 3.9 0.02 1 864 186 186 GLY HA3 H 4.1 0.02 1 865 186 186 GLY C C 179.4 0.2 1 866 186 186 GLY CA C 46.1 0.3 1 867 186 186 GLY N N 115.4 0.1 1 stop_ save_