data_5898 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N resonance assignments for the 24.4 kDa human gankyrin protein ; _BMRB_accession_number 5898 _BMRB_flat_file_name bmr5898.str _Entry_type original _Submission_date 2003-08-05 _Accession_date 2003-08-05 _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 Yuan Chunhua . . 2 Li Junan . . 3 Poi Mingjye . . 4 Byeon In-Ja L. . 5 Tsai Ming-Daw . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 428 "13C chemical shifts" 642 "15N chemical shifts" 217 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-10-25 original author . stop_ _Original_release_date 2004-10-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure--function relationship. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15379554 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuan Chunhua . . 2 Li Junan . . 3 Mahajan A. . . 4 Poi Mingjye . . 5 Byeon In-Ja L. . 6 Tsai Ming-Daw . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 38 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12152 _Page_last 12161 _Year 2004 _Details . loop_ _Keyword gankyrin oncoprotein 'resonance assignment' TROSY stop_ save_ ################################## # Molecular system description # ################################## save_system_gankyrin _Saveframe_category molecular_system _Mol_system_name '26S proteasome non-ATPase regulatory subunit 10' _Abbreviation_common gankyrin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gankyrin $gankyrin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_gankyrin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common gankyrin _Abbreviation_common gankyrin _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 226 _Mol_residue_sequence ; MEGCVSNLMVCNLAYSGKLE ELKESILADKSLATRTDQDS RTALHWACSAGHTEIVEFLL QLGVPVNDKDDAGWSPLHIA ASAGRDEIVKALLGKGAQVN AVNQNGCTPLHYAASKNRHE IAVMLLEGGANPDAKDHYEA TAMHRAAAKGNLKMIHILLY YKASTNIQDTEGNTPLHLAC DEERVEEAKLLVSQGASIYI ENKEEKTPLQVAKGGLGLIL KRMVEG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLY 4 CYS 5 VAL 6 SER 7 ASN 8 LEU 9 MET 10 VAL 11 CYS 12 ASN 13 LEU 14 ALA 15 TYR 16 SER 17 GLY 18 LYS 19 LEU 20 GLU 21 GLU 22 LEU 23 LYS 24 GLU 25 SER 26 ILE 27 LEU 28 ALA 29 ASP 30 LYS 31 SER 32 LEU 33 ALA 34 THR 35 ARG 36 THR 37 ASP 38 GLN 39 ASP 40 SER 41 ARG 42 THR 43 ALA 44 LEU 45 HIS 46 TRP 47 ALA 48 CYS 49 SER 50 ALA 51 GLY 52 HIS 53 THR 54 GLU 55 ILE 56 VAL 57 GLU 58 PHE 59 LEU 60 LEU 61 GLN 62 LEU 63 GLY 64 VAL 65 PRO 66 VAL 67 ASN 68 ASP 69 LYS 70 ASP 71 ASP 72 ALA 73 GLY 74 TRP 75 SER 76 PRO 77 LEU 78 HIS 79 ILE 80 ALA 81 ALA 82 SER 83 ALA 84 GLY 85 ARG 86 ASP 87 GLU 88 ILE 89 VAL 90 LYS 91 ALA 92 LEU 93 LEU 94 GLY 95 LYS 96 GLY 97 ALA 98 GLN 99 VAL 100 ASN 101 ALA 102 VAL 103 ASN 104 GLN 105 ASN 106 GLY 107 CYS 108 THR 109 PRO 110 LEU 111 HIS 112 TYR 113 ALA 114 ALA 115 SER 116 LYS 117 ASN 118 ARG 119 HIS 120 GLU 121 ILE 122 ALA 123 VAL 124 MET 125 LEU 126 LEU 127 GLU 128 GLY 129 GLY 130 ALA 131 ASN 132 PRO 133 ASP 134 ALA 135 LYS 136 ASP 137 HIS 138 TYR 139 GLU 140 ALA 141 THR 142 ALA 143 MET 144 HIS 145 ARG 146 ALA 147 ALA 148 ALA 149 LYS 150 GLY 151 ASN 152 LEU 153 LYS 154 MET 155 ILE 156 HIS 157 ILE 158 LEU 159 LEU 160 TYR 161 TYR 162 LYS 163 ALA 164 SER 165 THR 166 ASN 167 ILE 168 GLN 169 ASP 170 THR 171 GLU 172 GLY 173 ASN 174 THR 175 PRO 176 LEU 177 HIS 178 LEU 179 ALA 180 CYS 181 ASP 182 GLU 183 GLU 184 ARG 185 VAL 186 GLU 187 GLU 188 ALA 189 LYS 190 LEU 191 LEU 192 VAL 193 SER 194 GLN 195 GLY 196 ALA 197 SER 198 ILE 199 TYR 200 ILE 201 GLU 202 ASN 203 LYS 204 GLU 205 GLU 206 LYS 207 THR 208 PRO 209 LEU 210 GLN 211 VAL 212 ALA 213 LYS 214 GLY 215 GLY 216 LEU 217 GLY 218 LEU 219 ILE 220 LEU 221 LYS 222 ARG 223 MET 224 VAL 225 GLU 226 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 PDB 1QYM "X-Ray Structure Of Human Gankyrin" 99.56 227 100.00 100.00 8.27e-163 PDB 1TR4 "Solution Structure Of Human Oncogenic Protein Gankyrin" 100.00 226 100.00 100.00 9.77e-164 PDB 1UOH "Human Gankyrin" 100.00 226 100.00 100.00 9.77e-164 PDB 4NIK "Structure Of Human Gankyrin In Complex To The Single Chain Antibody F5" 100.00 230 100.00 100.00 1.77e-163 DBJ BAA33215 "26S proteasome subunit p28 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164 DBJ BAA34594 "gankyrin [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164 DBJ BAE87161 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163 DBJ BAE87972 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163 DBJ BAE88401 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163 GB AAH11960 "Proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164 GB AAV38495 "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]" 100.00 226 99.56 99.56 4.05e-163 GB AAX41449 "proteasome 26S subunit 10 [synthetic construct]" 100.00 226 99.56 99.56 4.05e-163 GB AAY18907 "proteasome 26S subunit non-ATPase 10-like [synthetic construct]" 99.56 250 100.00 100.00 5.00e-162 GB ACT64478 "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 protein [synthetic construct]" 100.00 226 100.00 100.00 9.77e-164 REF NP_001248034 "26S proteasome non-ATPase regulatory subunit 10 [Macaca mulatta]" 100.00 226 99.56 99.56 9.51e-163 REF NP_002805 "26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164 REF XP_001926942 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Sus scrofa]" 99.56 226 99.56 99.56 4.03e-162 REF XP_002763200 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Callithrix jacchus]" 100.00 226 98.23 98.67 2.55e-160 REF XP_002832022 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Pongo abelii]" 100.00 226 100.00 100.00 9.77e-164 SP O75832 "RecName: Full=26S proteasome non-ATPase regulatory subunit 10; AltName: Full=26S proteasome regulatory subunit p28; AltName: Fu" 100.00 226 100.00 100.00 9.77e-164 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $gankyrin 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 $gankyrin 'recombinant technology' . . . . . 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 $gankyrin . mM 0.4 0.5 '[U-13C; U-15N; U-70% 2H]' HEPES 5 mM . . . EDTA 1 uM . . . DTT 1 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_TROSY-HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label . save_ save_TROSY-HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label . save_ save_TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label . save_ save_TROSY-HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label . save_ save_15N-edited_NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Calibation followed the reference Journal of Biolmolecular NMR 6 (1995) 135-140. 1H, 13C and 15N chemical shift referencing in biomolecular NMR by Wishart et al. ; 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 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.0 DSS C 13 'methyl carbons' ppm 0.0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 external 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name gankyrin _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET H H 8.37 0.03 1 2 . 1 MET C C 176.1 0.1 1 3 . 1 MET CA C 56.0 0.1 1 4 . 1 MET CB C 33.1 0.1 1 5 . 1 MET N N 122.2 0.1 1 6 . 2 GLU H H 8.29 0.03 1 7 . 2 GLU HA H 4.22 0.03 1 8 . 2 GLU C C 176.9 0.1 1 9 . 2 GLU CA C 57.5 0.1 1 10 . 2 GLU CB C 30.3 0.1 1 11 . 2 GLU N N 121.7 0.1 1 12 . 3 GLY H H 8.39 0.03 1 13 . 3 GLY C C 173.5 0.1 1 14 . 3 GLY CA C 45.9 0.1 1 15 . 3 GLY N N 110.2 0.1 1 16 . 4 CYS H H 7.86 0.03 1 17 . 4 CYS C C 174.4 0.1 1 18 . 4 CYS CA C 58.9 0.1 1 19 . 4 CYS CB C 28.7 0.1 1 20 . 4 CYS N N 119.1 0.1 1 21 . 5 VAL H H 7.42 0.03 1 22 . 5 VAL HA H 3.96 0.03 1 23 . 5 VAL C C 174.8 0.1 1 24 . 5 VAL CA C 61.7 0.1 1 25 . 5 VAL CB C 32.6 0.1 1 26 . 5 VAL N N 117.5 0.1 1 27 . 6 SER H H 7.83 0.03 1 28 . 6 SER HA H 4.64 0.03 1 29 . 6 SER C C 174.6 0.1 1 30 . 6 SER CA C 57.5 0.1 1 31 . 6 SER CB C 63.8 0.1 1 32 . 6 SER N N 115.1 0.1 1 33 . 7 ASN H H 8.78 0.03 1 34 . 7 ASN HA H 4.55 0.03 1 35 . 7 ASN C C 175.0 0.1 1 36 . 7 ASN CA C 54.3 0.1 1 37 . 7 ASN CB C 37.4 0.1 1 38 . 7 ASN N N 123.3 0.1 1 39 . 8 LEU H H 8.18 0.03 1 40 . 8 LEU CA C 53.4 0.1 1 41 . 8 LEU CB C 43.9 0.1 1 42 . 8 LEU N N 121.1 0.1 1 43 . 9 MET C C 179.2 0.1 1 44 . 9 MET CA C 59.4 0.1 1 45 . 10 VAL H H 8.88 0.03 1 46 . 10 VAL HA H 3.89 0.03 1 47 . 10 VAL C C 177.0 0.1 1 48 . 10 VAL CA C 66.3 0.1 1 49 . 10 VAL CB C 31.6 0.1 1 50 . 10 VAL N N 115.0 0.1 1 51 . 11 CYS H H 6.80 0.03 1 52 . 11 CYS HA H 4.02 0.03 1 53 . 11 CYS C C 175.8 0.1 1 54 . 11 CYS CA C 63.1 0.1 1 55 . 11 CYS CB C 27.8 0.1 1 56 . 11 CYS N N 118.6 0.1 1 57 . 12 ASN H H 7.31 0.03 1 58 . 12 ASN HA H 4.37 0.03 1 59 . 12 ASN C C 178.9 0.1 1 60 . 12 ASN CA C 57.2 0.1 1 61 . 12 ASN CB C 38.4 0.1 1 62 . 12 ASN N N 118.6 0.1 1 63 . 13 LEU H H 8.68 0.03 1 64 . 13 LEU HA H 4.00 0.03 1 65 . 13 LEU C C 178.5 0.1 1 66 . 13 LEU CA C 58.5 0.1 1 67 . 13 LEU CB C 42.5 0.1 1 68 . 13 LEU N N 121.2 0.1 1 69 . 14 ALA H H 7.71 0.03 1 70 . 14 ALA HA H 4.05 0.03 1 71 . 14 ALA C C 178.5 0.1 1 72 . 14 ALA CA C 55.6 0.1 1 73 . 14 ALA CB C 20.1 0.1 1 74 . 14 ALA N N 120.2 0.1 1 75 . 15 TYR H H 8.26 0.03 1 76 . 15 TYR HA H 4.26 0.03 1 77 . 15 TYR C C 177.3 0.1 1 78 . 15 TYR CA C 61.2 0.1 1 79 . 15 TYR CB C 39.9 0.1 1 80 . 15 TYR N N 116.3 0.1 1 81 . 16 SER H H 8.10 0.03 1 82 . 16 SER HA H 4.34 0.03 1 83 . 16 SER C C 174.7 0.1 1 84 . 16 SER CA C 59.9 0.1 1 85 . 16 SER CB C 64.6 0.1 1 86 . 16 SER N N 110.4 0.1 1 87 . 17 GLY H H 7.27 0.03 1 88 . 17 GLY HA2 H 3.15 0.03 2 89 . 17 GLY HA3 H 2.65 0.03 2 90 . 17 GLY C C 174.9 0.1 1 91 . 17 GLY CA C 44.7 0.1 1 92 . 17 GLY N N 109.6 0.1 1 93 . 18 LYS H H 7.69 0.03 1 94 . 18 LYS HA H 4.36 0.03 1 95 . 18 LYS C C 174.6 0.1 1 96 . 18 LYS CA C 55.1 0.1 1 97 . 18 LYS CB C 30.6 0.1 1 98 . 18 LYS N N 123.2 0.1 1 99 . 19 LEU H H 7.43 0.03 1 100 . 19 LEU HA H 3.62 0.03 1 101 . 19 LEU C C 177.2 0.1 1 102 . 19 LEU CA C 59.1 0.1 1 103 . 19 LEU CB C 41.6 0.1 1 104 . 19 LEU N N 124.2 0.1 1 105 . 20 GLU H H 8.70 0.03 1 106 . 20 GLU HA H 3.76 0.03 1 107 . 20 GLU C C 179.3 0.1 1 108 . 20 GLU CA C 60.8 0.1 1 109 . 20 GLU CB C 28.4 0.1 1 110 . 20 GLU N N 117.8 0.1 1 111 . 21 GLU H H 8.82 0.03 1 112 . 21 GLU HA H 3.99 0.03 1 113 . 21 GLU C C 179.6 0.1 1 114 . 21 GLU CA C 60.3 0.1 1 115 . 21 GLU CB C 29.9 0.1 1 116 . 21 GLU N N 120.4 0.1 1 117 . 22 LEU H H 8.30 0.03 1 118 . 22 LEU HA H 3.88 0.03 1 119 . 22 LEU C C 178.1 0.1 1 120 . 22 LEU CA C 59.3 0.1 1 121 . 22 LEU CB C 41.6 0.1 1 122 . 22 LEU N N 123.1 0.1 1 123 . 23 LYS H H 8.67 0.03 1 124 . 23 LYS HA H 3.56 0.03 1 125 . 23 LYS C C 178.5 0.1 1 126 . 23 LYS CA C 60.8 0.1 1 127 . 23 LYS CB C 32.3 0.1 1 128 . 23 LYS N N 119.8 0.1 1 129 . 24 GLU H H 7.83 0.03 1 130 . 24 GLU HA H 3.93 0.03 1 131 . 24 GLU C C 179.7 0.1 1 132 . 24 GLU CA C 59.9 0.1 1 133 . 24 GLU CB C 29.8 0.1 1 134 . 24 GLU N N 117.4 0.1 1 135 . 25 SER H H 7.85 0.03 1 136 . 25 SER HA H 4.22 0.03 1 137 . 25 SER C C 176.7 0.1 1 138 . 25 SER CA C 62.7 0.1 1 139 . 25 SER CB C 63.8 0.1 1 140 . 25 SER N N 114.9 0.1 1 141 . 26 ILE H H 8.09 0.03 1 142 . 26 ILE HA H 3.97 0.03 1 143 . 26 ILE C C 177.1 0.1 1 144 . 26 ILE CA C 63.7 0.1 1 145 . 26 ILE CB C 38.4 0.1 1 146 . 26 ILE N N 122.0 0.1 1 147 . 27 LEU H H 8.52 0.03 1 148 . 27 LEU HA H 4.13 0.03 1 149 . 27 LEU C C 179.6 0.1 1 150 . 27 LEU CA C 58.2 0.1 1 151 . 27 LEU CB C 41.1 0.1 1 152 . 27 LEU N N 119.3 0.1 1 153 . 28 ALA H H 7.10 0.03 1 154 . 28 ALA HA H 4.28 0.03 1 155 . 28 ALA C C 178.0 0.1 1 156 . 28 ALA CA C 54.1 0.1 1 157 . 28 ALA CB C 19.4 0.1 1 158 . 28 ALA N N 118.8 0.1 1 159 . 29 ASP H H 7.45 0.03 1 160 . 29 ASP HA H 4.66 0.03 1 161 . 29 ASP C C 175.3 0.1 1 162 . 29 ASP CA C 54.0 0.1 1 163 . 29 ASP CB C 40.6 0.1 1 164 . 29 ASP N N 117.4 0.1 1 165 . 30 LYS H H 8.73 0.03 1 166 . 30 LYS HA H 4.40 0.03 1 167 . 30 LYS C C 180.0 0.1 1 168 . 30 LYS CA C 59.6 0.1 1 169 . 30 LYS CB C 32.4 0.1 1 170 . 30 LYS N N 125.6 0.1 1 171 . 31 SER H H 8.31 0.03 1 172 . 31 SER HA H 4.26 0.03 1 173 . 31 SER C C 176.3 0.1 1 174 . 31 SER CA C 61.7 0.1 1 175 . 31 SER CB C 63.4 0.1 1 176 . 31 SER N N 116.9 0.1 1 177 . 32 LEU H H 8.08 0.03 1 178 . 32 LEU HA H 4.07 0.03 1 179 . 32 LEU C C 178.2 0.1 1 180 . 32 LEU CA C 57.5 0.1 1 181 . 32 LEU CB C 42.7 0.1 1 182 . 32 LEU N N 122.3 0.1 1 183 . 33 ALA H H 7.63 0.03 1 184 . 33 ALA HA H 3.96 0.03 1 185 . 33 ALA C C 176.0 0.1 1 186 . 33 ALA CA C 55.3 0.1 1 187 . 33 ALA CB C 19.5 0.1 1 188 . 33 ALA N N 117.2 0.1 1 189 . 34 THR H H 7.14 0.03 1 190 . 34 THR HA H 4.49 0.03 1 191 . 34 THR C C 173.8 0.1 1 192 . 34 THR CA C 60.4 0.1 1 193 . 34 THR CB C 69.5 0.1 1 194 . 34 THR N N 99.6 0.1 1 195 . 35 ARG H H 7.00 0.03 1 196 . 35 ARG HA H 4.29 0.03 1 197 . 35 ARG C C 175.2 0.1 1 198 . 35 ARG CA C 57.0 0.1 1 199 . 35 ARG CB C 30.7 0.1 1 200 . 35 ARG N N 125.1 0.1 1 201 . 36 THR H H 7.88 0.03 1 202 . 36 THR HA H 4.73 0.03 1 203 . 36 THR C C 175.7 0.1 1 204 . 36 THR CA C 59.5 0.1 1 205 . 36 THR CB C 71.7 0.1 1 206 . 36 THR N N 112.4 0.1 1 207 . 37 ASP H H 9.10 0.03 1 208 . 37 ASP C C 179.1 0.1 1 209 . 37 ASP CA C 52.1 0.1 1 210 . 37 ASP CB C 42.2 0.1 1 211 . 37 ASP N N 123.6 0.1 1 212 . 38 GLN H H 8.78 0.03 1 213 . 38 GLN HA H 4.29 0.03 1 214 . 38 GLN C C 176.0 0.1 1 215 . 38 GLN CA C 58.6 0.1 1 216 . 38 GLN CB C 27.2 0.1 1 217 . 38 GLN N N 118.2 0.1 1 218 . 39 ASP H H 8.39 0.03 1 219 . 39 ASP HA H 5.11 0.03 1 220 . 39 ASP C C 175.4 0.1 1 221 . 39 ASP CA C 55.0 0.1 1 222 . 39 ASP CB C 42.2 0.1 1 223 . 39 ASP N N 122.6 0.1 1 224 . 40 SER H H 8.46 0.03 1 225 . 40 SER HA H 3.81 0.03 1 226 . 40 SER C C 172.5 0.1 1 227 . 40 SER CA C 60.5 0.1 1 228 . 40 SER CB C 62.2 0.1 1 229 . 40 SER N N 111.6 0.1 1 230 . 41 ARG H H 8.25 0.03 1 231 . 41 ARG HA H 3.92 0.03 1 232 . 41 ARG C C 176.2 0.1 1 233 . 41 ARG CA C 55.8 0.1 1 234 . 41 ARG CB C 33.4 0.1 1 235 . 41 ARG N N 116.9 0.1 1 236 . 42 THR H H 9.73 0.03 1 237 . 42 THR HA H 5.04 0.03 1 238 . 42 THR C C 177.0 0.1 1 239 . 42 THR CA C 59.8 0.1 1 240 . 42 THR CB C 72.7 0.1 1 241 . 42 THR N N 112.3 0.1 1 242 . 43 ALA H H 9.62 0.03 1 243 . 43 ALA HA H 4.13 0.03 1 244 . 43 ALA C C 178.5 0.1 1 245 . 43 ALA CA C 56.3 0.1 1 246 . 43 ALA CB C 18.5 0.1 1 247 . 43 ALA N N 121.7 0.1 1 248 . 44 LEU H H 8.25 0.03 1 249 . 44 LEU HA H 4.00 0.03 1 250 . 44 LEU C C 178.9 0.1 1 251 . 44 LEU CA C 58.8 0.1 1 252 . 44 LEU CB C 41.9 0.1 1 253 . 44 LEU N N 115.4 0.1 1 254 . 45 HIS H H 7.65 0.03 1 255 . 45 HIS HA H 3.64 0.03 1 256 . 45 HIS C C 178.1 0.1 1 257 . 45 HIS CA C 64.3 0.1 1 258 . 45 HIS CB C 31.5 0.1 1 259 . 45 HIS N N 117.6 0.1 1 260 . 46 TRP H H 7.39 0.03 1 261 . 46 TRP HA H 4.60 0.03 1 262 . 46 TRP C C 178.6 0.1 1 263 . 46 TRP CA C 60.7 0.1 1 264 . 46 TRP CB C 31.4 0.1 1 265 . 46 TRP N N 116.3 0.1 1 266 . 47 ALA H H 8.85 0.03 1 267 . 47 ALA HA H 4.35 0.03 1 268 . 47 ALA C C 180.2 0.1 1 269 . 47 ALA CA C 56.0 0.1 1 270 . 47 ALA CB C 19.6 0.1 1 271 . 47 ALA N N 122.1 0.1 1 272 . 48 CYS H H 8.04 0.03 1 273 . 48 CYS HA H 4.10 0.03 1 274 . 48 CYS C C 175.3 0.1 1 275 . 48 CYS CA C 65.1 0.1 1 276 . 48 CYS CB C 27.7 0.1 1 277 . 48 CYS N N 114.2 0.1 1 278 . 49 SER H H 7.54 0.03 1 279 . 49 SER HA H 3.77 0.03 1 280 . 49 SER C C 177.1 0.1 1 281 . 49 SER CA C 61.6 0.1 1 282 . 49 SER CB C 64.0 0.1 1 283 . 49 SER N N 113.0 0.1 1 284 . 50 ALA H H 7.69 0.03 1 285 . 50 ALA HA H 4.15 0.03 1 286 . 50 ALA C C 177.1 0.1 1 287 . 50 ALA CA C 53.4 0.1 1 288 . 50 ALA CB C 22.2 0.1 1 289 . 50 ALA N N 119.0 0.1 1 290 . 51 GLY H H 7.40 0.03 1 291 . 51 GLY HA2 H 3.83 0.03 2 292 . 51 GLY HA3 H 3.28 0.03 2 293 . 51 GLY C C 173.7 0.1 1 294 . 51 GLY CA C 46.6 0.1 1 295 . 51 GLY N N 103.7 0.1 1 296 . 52 HIS H H 7.20 0.03 1 297 . 52 HIS HA H 5.26 0.03 1 298 . 52 HIS C C 175.6 0.1 1 299 . 52 HIS CA C 55.0 0.1 1 300 . 52 HIS CB C 30.6 0.1 1 301 . 52 HIS N N 118.7 0.1 1 302 . 53 THR H H 8.51 0.03 1 303 . 53 THR HA H 3.44 0.03 1 304 . 53 THR C C 175.5 0.1 1 305 . 53 THR CA C 67.2 0.1 1 306 . 53 THR CB C 69.1 0.1 1 307 . 53 THR N N 125.8 0.1 1 308 . 54 GLU H H 9.60 0.03 1 309 . 54 GLU HA H 4.20 0.03 1 310 . 54 GLU C C 180.1 0.1 1 311 . 54 GLU CA C 60.4 0.1 1 312 . 54 GLU CB C 29.2 0.1 1 313 . 54 GLU N N 119.8 0.1 1 314 . 55 ILE H H 7.38 0.03 1 315 . 55 ILE HA H 3.81 0.03 1 316 . 55 ILE C C 177.0 0.1 1 317 . 55 ILE CA C 65.8 0.1 1 318 . 55 ILE CB C 37.4 0.1 1 319 . 55 ILE N N 119.5 0.1 1 320 . 56 VAL H H 7.78 0.03 1 321 . 56 VAL HA H 3.38 0.03 1 322 . 56 VAL C C 177.0 0.1 1 323 . 56 VAL CA C 68.8 0.1 1 324 . 56 VAL CB C 31.6 0.1 1 325 . 56 VAL N N 120.1 0.1 1 326 . 57 GLU H H 8.74 0.03 1 327 . 57 GLU HA H 3.87 0.03 1 328 . 57 GLU C C 178.7 0.1 1 329 . 57 GLU CA C 60.6 0.1 1 330 . 57 GLU CB C 29.8 0.1 1 331 . 57 GLU N N 117.7 0.1 1 332 . 58 PHE H H 7.60 0.03 1 333 . 58 PHE HA H 4.35 0.03 1 334 . 58 PHE C C 176.8 0.1 1 335 . 58 PHE CA C 61.2 0.1 1 336 . 58 PHE CB C 39.3 0.1 1 337 . 58 PHE N N 119.7 0.1 1 338 . 59 LEU H H 8.13 0.03 1 339 . 59 LEU HA H 3.67 0.03 1 340 . 59 LEU C C 179.3 0.1 1 341 . 59 LEU CA C 58.0 0.1 1 342 . 59 LEU CB C 41.4 0.1 1 343 . 59 LEU N N 118.9 0.1 1 344 . 60 LEU H H 8.88 0.03 1 345 . 60 LEU HA H 4.00 0.03 1 346 . 60 LEU C C 181.9 0.1 1 347 . 60 LEU CA C 58.4 0.1 1 348 . 60 LEU CB C 40.2 0.1 1 349 . 60 LEU N N 118.4 0.1 1 350 . 61 GLN H H 8.07 0.03 1 351 . 61 GLN HA H 4.09 0.03 1 352 . 61 GLN C C 177.7 0.1 1 353 . 61 GLN CA C 58.6 0.1 1 354 . 61 GLN CB C 28.0 0.1 1 355 . 61 GLN N N 120.4 0.1 1 356 . 62 LEU H H 7.36 0.03 1 357 . 62 LEU HA H 4.10 0.03 1 358 . 62 LEU C C 178.0 0.1 1 359 . 62 LEU CA C 56.1 0.1 1 360 . 62 LEU CB C 42.5 0.1 1 361 . 62 LEU N N 119.5 0.1 1 362 . 63 GLY H H 7.70 0.03 1 363 . 63 GLY HA2 H 4.15 0.03 2 364 . 63 GLY HA3 H 3.75 0.03 2 365 . 63 GLY C C 175.0 0.1 1 366 . 63 GLY CA C 45.8 0.1 1 367 . 63 GLY N N 105.2 0.1 1 368 . 64 VAL H H 6.84 0.03 1 369 . 64 VAL HA H 4.26 0.03 1 370 . 64 VAL CA C 60.8 0.1 1 371 . 64 VAL CB C 30.1 0.1 1 372 . 64 VAL N N 113.9 0.1 1 373 . 65 PRO HA H 4.48 0.03 1 374 . 65 PRO C C 179.2 0.1 1 375 . 65 PRO CA C 63.4 0.1 1 376 . 65 PRO CB C 32.9 0.1 1 377 . 66 VAL H H 8.18 0.03 1 378 . 66 VAL HA H 4.16 0.03 1 379 . 66 VAL C C 174.8 0.1 1 380 . 66 VAL CA C 62.2 0.1 1 381 . 66 VAL CB C 33.4 0.1 1 382 . 66 VAL N N 114.7 0.1 1 383 . 67 ASN H H 7.89 0.03 1 384 . 67 ASN HA H 5.16 0.03 1 385 . 67 ASN C C 176.0 0.1 1 386 . 67 ASN CA C 53.8 0.1 1 387 . 67 ASN CB C 41.7 0.1 1 388 . 67 ASN N N 116.6 0.1 1 389 . 68 ASP H H 8.15 0.03 1 390 . 68 ASP HA H 4.56 0.03 1 391 . 68 ASP C C 176.2 0.1 1 392 . 68 ASP CA C 56.0 0.1 1 393 . 68 ASP CB C 40.6 0.1 1 394 . 68 ASP N N 123.0 0.1 1 395 . 69 LYS H H 8.78 0.03 1 396 . 69 LYS HA H 4.63 0.03 1 397 . 69 LYS C C 177.1 0.1 1 398 . 69 LYS CA C 55.8 0.1 1 399 . 69 LYS CB C 35.7 0.1 1 400 . 69 LYS N N 122.6 0.1 1 401 . 70 ASP H H 8.06 0.03 1 402 . 70 ASP HA H 4.50 0.03 1 403 . 70 ASP C C 178.1 0.1 1 404 . 70 ASP CA C 52.7 0.1 1 405 . 70 ASP CB C 42.2 0.1 1 406 . 70 ASP N N 122.2 0.1 1 407 . 71 ASP H H 7.91 0.03 1 408 . 71 ASP HA H 4.44 0.03 1 409 . 71 ASP C C 176.8 0.1 1 410 . 71 ASP CA C 57.6 0.1 1 411 . 71 ASP CB C 40.4 0.1 1 412 . 71 ASP N N 117.0 0.1 1 413 . 72 ALA H H 7.99 0.03 1 414 . 72 ALA HA H 4.68 0.03 1 415 . 72 ALA C C 177.7 0.1 1 416 . 72 ALA CA C 51.7 0.1 1 417 . 72 ALA CB C 19.6 0.1 1 418 . 72 ALA N N 122.0 0.1 1 419 . 73 GLY H H 8.68 0.03 1 420 . 73 GLY HA2 H 3.83 0.03 1 421 . 73 GLY HA3 H 4.07 0.03 1 422 . 73 GLY C C 172.8 0.1 1 423 . 73 GLY CA C 46.7 0.1 1 424 . 73 GLY N N 110.8 0.1 1 425 . 74 TRP H H 9.00 0.03 1 426 . 74 TRP HA H 3.84 0.03 1 427 . 74 TRP C C 176.1 0.1 1 428 . 74 TRP CA C 59.8 0.1 1 429 . 74 TRP CB C 27.7 0.1 1 430 . 74 TRP N N 121.1 0.1 1 431 . 75 SER H H 9.05 0.03 1 432 . 75 SER HA H 5.31 0.03 1 433 . 75 SER CA C 56.9 0.1 1 434 . 75 SER CB C 65.1 0.1 1 435 . 75 SER N N 123.2 0.1 1 436 . 76 PRO C C 176.9 0.1 1 437 . 76 PRO CA C 67.7 0.1 1 438 . 77 LEU H H 8.82 0.03 1 439 . 77 LEU C C 179.3 0.1 1 440 . 77 LEU CA C 58.5 0.1 1 441 . 77 LEU CB C 42.1 0.1 1 442 . 77 LEU N N 116.5 0.1 1 443 . 78 HIS H H 7.95 0.03 1 444 . 78 HIS C C 177.4 0.1 1 445 . 78 HIS CA C 64.6 0.1 1 446 . 78 HIS CB C 32.3 0.1 1 447 . 78 HIS N N 117.0 0.1 1 448 . 79 ILE H H 7.94 0.03 1 449 . 79 ILE C C 178.2 0.1 1 450 . 79 ILE CA C 65.4 0.1 1 451 . 79 ILE CB C 40.9 0.1 1 452 . 79 ILE N N 117.5 0.1 1 453 . 80 ALA H H 8.89 0.03 1 454 . 80 ALA HA H 3.94 0.03 1 455 . 80 ALA C C 178.4 0.1 1 456 . 80 ALA CA C 55.2 0.1 1 457 . 80 ALA CB C 20.6 0.1 1 458 . 80 ALA N N 120.0 0.1 1 459 . 81 ALA H H 8.35 0.03 1 460 . 81 ALA HA H 4.12 0.03 1 461 . 81 ALA C C 178.9 0.1 1 462 . 81 ALA CA C 55.7 0.1 1 463 . 81 ALA CB C 19.4 0.1 1 464 . 81 ALA N N 118.5 0.1 1 465 . 82 SER H H 8.03 0.03 1 466 . 82 SER HA H 3.97 0.03 1 467 . 82 SER C C 177.4 0.1 1 468 . 82 SER CA C 62.0 0.1 1 469 . 82 SER CB C 64.2 0.1 1 470 . 82 SER N N 109.5 0.1 1 471 . 83 ALA H H 8.06 0.03 1 472 . 83 ALA HA H 4.44 0.03 1 473 . 83 ALA C C 177.3 0.1 1 474 . 83 ALA CA C 52.9 0.1 1 475 . 83 ALA CB C 19.9 0.1 1 476 . 83 ALA N N 118.1 0.1 1 477 . 84 GLY H H 7.51 0.03 1 478 . 84 GLY HA2 H 3.84 0.03 2 479 . 84 GLY HA3 H 3.52 0.03 2 480 . 84 GLY C C 174.0 0.1 1 481 . 84 GLY CA C 47.7 0.1 1 482 . 84 GLY N N 107.1 0.1 1 483 . 85 ARG H H 8.17 0.03 1 484 . 85 ARG C C 175.3 0.03 1 485 . 85 ARG CA C 51.6 0.1 1 486 . 85 ARG CB C 27.7 0.1 1 487 . 85 ARG N N 117.0 0.1 1 488 . 86 ASP H H 8.55 0.03 1 489 . 86 ASP HA H 3.72 0.03 1 490 . 86 ASP C C 177.1 0.1 1 491 . 86 ASP CA C 59.5 0.1 1 492 . 86 ASP CB C 40.5 0.1 1 493 . 86 ASP N N 125.1 0.1 1 494 . 87 GLU H H 8.92 0.03 1 495 . 87 GLU HA H 3.95 0.03 1 496 . 87 GLU C C 179.9 0.1 1 497 . 87 GLU CA C 59.9 0.1 1 498 . 87 GLU CB C 29.6 0.1 1 499 . 87 GLU N N 116.3 0.1 1 500 . 88 ILE H H 7.44 0.03 1 501 . 88 ILE HA H 3.67 0.03 1 502 . 88 ILE C C 177.1 0.1 1 503 . 88 ILE CA C 65.4 0.1 1 504 . 88 ILE CB C 38.0 0.1 1 505 . 88 ILE N N 120.6 0.1 1 506 . 89 VAL H H 8.10 0.03 1 507 . 89 VAL HA H 3.26 0.03 1 508 . 89 VAL C C 176.7 0.1 1 509 . 89 VAL CA C 68.7 0.1 1 510 . 89 VAL CB C 30.9 0.1 1 511 . 89 VAL N N 121.0 0.1 1 512 . 90 LYS H H 7.69 0.03 1 513 . 90 LYS HA H 3.81 0.03 1 514 . 90 LYS C C 179.3 0.1 1 515 . 90 LYS CA C 60.4 0.1 1 516 . 90 LYS CB C 33.1 0.1 1 517 . 90 LYS N N 118.6 0.1 1 518 . 91 ALA H H 7.66 0.03 1 519 . 91 ALA HA H 4.12 0.03 1 520 . 91 ALA C C 180.9 0.1 1 521 . 91 ALA CA C 55.2 0.1 1 522 . 91 ALA CB C 18.2 0.1 1 523 . 91 ALA N N 122.1 0.1 1 524 . 92 LEU H H 8.60 0.03 1 525 . 92 LEU HA H 3.80 0.03 1 526 . 92 LEU C C 180.2 0.1 1 527 . 92 LEU CA C 58.1 0.1 1 528 . 92 LEU CB C 41.7 0.1 1 529 . 92 LEU N N 117.6 0.1 1 530 . 93 LEU H H 8.62 0.03 1 531 . 93 LEU HA H 3.98 0.03 1 532 . 93 LEU C C 181.3 0.1 1 533 . 93 LEU CA C 58.8 0.1 1 534 . 93 LEU CB C 40.7 0.1 1 535 . 93 LEU N N 120.1 0.1 1 536 . 94 GLY H H 7.84 0.03 1 537 . 94 GLY HA2 H 4.09 0.03 2 538 . 94 GLY HA3 H 3.90 0.03 2 539 . 94 GLY C C 174.3 0.1 1 540 . 94 GLY CA C 46.7 0.1 1 541 . 94 GLY N N 106.7 0.1 1 542 . 95 LYS H H 7.24 0.03 1 543 . 95 LYS HA H 4.62 0.03 1 544 . 95 LYS C C 176.2 0.1 1 545 . 95 LYS CA C 53.8 0.1 1 546 . 95 LYS CB C 32.7 0.1 1 547 . 95 LYS N N 119.1 0.1 1 548 . 96 GLY H H 7.66 0.03 1 549 . 96 GLY HA2 H 4.14 0.03 2 550 . 96 GLY HA3 H 3.80 0.03 2 551 . 96 GLY C C 175.8 0.1 1 552 . 96 GLY CA C 46.4 0.1 1 553 . 96 GLY N N 105.2 0.1 1 554 . 97 ALA H H 7.76 0.03 1 555 . 97 ALA HA H 4.40 0.03 1 556 . 97 ALA C C 177.4 0.1 1 557 . 97 ALA CA C 52.9 0.1 1 558 . 97 ALA CB C 20.6 0.1 1 559 . 97 ALA N N 122.8 0.1 1 560 . 98 GLN H H 8.84 0.03 1 561 . 98 GLN HA H 4.25 0.03 1 562 . 98 GLN C C 177.5 0.1 1 563 . 98 GLN CA C 56.1 0.1 1 564 . 98 GLN CB C 28.8 0.1 1 565 . 98 GLN N N 121.2 0.1 1 566 . 99 VAL H H 8.16 0.03 1 567 . 99 VAL HA H 3.62 0.03 1 568 . 99 VAL C C 174.7 0.1 1 569 . 99 VAL CA C 64.6 0.1 1 570 . 99 VAL CB C 32.7 0.1 1 571 . 99 VAL N N 124.5 0.1 1 572 . 100 ASN H H 8.59 0.03 1 573 . 100 ASN HA H 5.07 0.03 1 574 . 100 ASN C C 173.9 0.1 1 575 . 100 ASN CA C 52.8 0.1 1 576 . 100 ASN CB C 39.2 0.1 1 577 . 100 ASN N N 116.8 0.1 1 578 . 101 ALA H H 6.46 0.03 1 579 . 101 ALA HA H 4.25 0.03 1 580 . 101 ALA C C 170.5 0.1 1 581 . 101 ALA CA C 53.1 0.1 1 582 . 101 ALA CB C 21.0 0.1 1 583 . 101 ALA N N 121.5 0.1 1 584 . 102 VAL H H 8.21 0.03 1 585 . 102 VAL HA H 5.00 0.03 1 586 . 102 VAL C C 176.0 0.1 1 587 . 102 VAL CA C 59.3 0.1 1 588 . 102 VAL CB C 35.7 0.1 1 589 . 102 VAL N N 111.6 0.1 1 590 . 103 ASN H H 7.34 0.03 1 591 . 103 ASN HA H 5.23 0.03 1 592 . 103 ASN C C 178.3 0.1 1 593 . 103 ASN CA C 50.8 0.1 1 594 . 103 ASN CB C 40.1 0.1 1 595 . 103 ASN N N 119.9 0.1 1 596 . 104 GLN H H 7.88 0.03 1 597 . 104 GLN HA H 4.20 0.03 1 598 . 104 GLN C C 175.5 0.1 1 599 . 104 GLN CA C 59.0 0.1 1 600 . 104 GLN CB C 28.1 0.1 1 601 . 104 GLN N N 117.1 0.1 1 602 . 105 ASN H H 7.23 0.03 1 603 . 105 ASN HA H 4.89 0.03 1 604 . 105 ASN C C 174.7 0.1 1 605 . 105 ASN CA C 53.5 0.1 1 606 . 105 ASN CB C 40.3 0.1 1 607 . 105 ASN N N 114.8 0.1 1 608 . 106 GLY H H 7.90 0.03 1 609 . 106 GLY HA2 H 3.35 0.03 1 610 . 106 GLY HA3 H 3.54 0.03 1 611 . 106 GLY C C 172.9 0.1 1 612 . 106 GLY CA C 46.1 0.1 1 613 . 106 GLY N N 108.0 0.1 1 614 . 107 CYS H H 7.33 0.03 1 615 . 107 CYS HA H 4.35 0.03 1 616 . 107 CYS C C 176.5 0.1 1 617 . 107 CYS CA C 58.7 0.1 1 618 . 107 CYS CB C 30.2 0.1 1 619 . 107 CYS N N 116.0 0.1 1 620 . 108 THR H H 10.76 0.03 1 621 . 108 THR HA H 5.67 0.03 1 622 . 108 THR CA C 59.8 0.1 1 623 . 108 THR CB C 69.3 0.1 1 624 . 108 THR N N 121.4 0.1 1 625 . 109 PRO C C 177.0 0.1 1 626 . 109 PRO CA C 66.7 0.1 1 627 . 109 PRO CB C 29.7 0.1 9 628 . 110 LEU H H 8.36 0.03 1 629 . 110 LEU HA H 3.94 0.03 1 630 . 110 LEU C C 177.9 0.1 1 631 . 110 LEU CA C 57.9 0.1 1 632 . 110 LEU CB C 40.8 0.1 1 633 . 110 LEU N N 117.0 0.1 1 634 . 111 HIS H H 7.60 0.03 1 635 . 111 HIS HA H 3.71 0.03 1 636 . 111 HIS C C 178.3 0.1 1 637 . 111 HIS CA C 64.5 0.1 1 638 . 111 HIS CB C 31.0 0.1 1 639 . 111 HIS N N 117.9 0.1 1 640 . 112 TYR H H 6.74 0.03 1 641 . 112 TYR HA H 4.40 0.03 1 642 . 112 TYR C C 177.8 0.1 1 643 . 112 TYR CA C 61.6 0.1 1 644 . 112 TYR CB C 38.4 0.1 1 645 . 112 TYR N N 114.9 0.1 1 646 . 113 ALA H H 8.27 0.03 1 647 . 113 ALA HA H 3.90 0.03 1 648 . 113 ALA C C 179.0 0.1 1 649 . 113 ALA CA C 55.6 0.1 1 650 . 113 ALA CB C 18.7 0.1 1 651 . 113 ALA N N 121.5 0.1 1 652 . 114 ALA H H 8.64 0.03 1 653 . 114 ALA HA H 4.24 0.03 1 654 . 114 ALA C C 179.8 0.1 1 655 . 114 ALA CA C 55.1 0.1 1 656 . 114 ALA CB C 20.0 0.1 1 657 . 114 ALA N N 117.1 0.1 1 658 . 115 SER H H 7.90 0.03 1 659 . 115 SER C C 175.7 0.1 1 660 . 115 SER CA C 62.3 0.1 1 661 . 115 SER N N 112.4 0.1 1 662 . 116 LYS H H 7.61 0.03 1 663 . 116 LYS HA H 4.54 0.03 1 664 . 116 LYS C C 175.1 0.1 1 665 . 116 LYS CA C 55.4 0.1 1 666 . 116 LYS CB C 32.5 0.1 1 667 . 116 LYS N N 116.4 0.1 1 668 . 117 ASN H H 7.44 0.03 1 669 . 117 ASN HA H 4.04 0.03 1 670 . 117 ASN C C 174.3 0.1 1 671 . 117 ASN CA C 54.7 0.1 1 672 . 117 ASN CB C 37.8 0.1 1 673 . 117 ASN N N 115.5 0.1 1 674 . 118 ARG H H 8.53 0.03 1 675 . 118 ARG HA H 4.62 0.03 1 676 . 118 ARG C C 175.8 0.1 1 677 . 118 ARG CA C 52.2 0.1 1 678 . 118 ARG CB C 27.1 0.1 1 679 . 118 ARG N N 115.6 0.1 1 680 . 119 HIS H H 7.39 0.03 1 681 . 119 HIS HA H 3.85 0.03 1 682 . 119 HIS C C 176.3 0.1 1 683 . 119 HIS CA C 62.1 0.1 1 684 . 119 HIS CB C 31.2 0.1 1 685 . 119 HIS N N 121.9 0.1 1 686 . 120 GLU H H 8.87 0.03 1 687 . 120 GLU HA H 4.01 0.03 1 688 . 120 GLU C C 180.6 0.1 1 689 . 120 GLU CA C 60.7 0.1 1 690 . 120 GLU CB C 28.2 0.1 1 691 . 120 GLU N N 118.8 0.1 1 692 . 121 ILE H H 8.12 0.03 1 693 . 121 ILE HA H 3.70 0.03 1 694 . 121 ILE C C 176.7 0.1 1 695 . 121 ILE CA C 65.6 0.1 1 696 . 121 ILE CB C 38.5 0.1 1 697 . 121 ILE N N 121.0 0.1 1 698 . 122 ALA H H 8.44 0.03 1 699 . 122 ALA HA H 3.67 0.03 1 700 . 122 ALA C C 178.4 0.1 1 701 . 122 ALA CA C 56.7 0.1 1 702 . 122 ALA CB C 18.2 0.1 1 703 . 122 ALA N N 121.9 0.1 1 704 . 123 VAL H H 7.82 0.03 1 705 . 123 VAL HA H 3.31 0.03 1 706 . 123 VAL C C 177.3 0.1 1 707 . 123 VAL CA C 68.2 0.1 1 708 . 123 VAL CB C 32.2 0.1 1 709 . 123 VAL N N 116.4 0.1 1 710 . 124 MET H H 7.77 0.03 1 711 . 124 MET HA H 3.86 0.03 1 712 . 124 MET C C 180.0 0.1 1 713 . 124 MET CA C 60.4 0.1 1 714 . 124 MET CB C 34.0 0.1 1 715 . 124 MET N N 117.5 0.1 1 716 . 125 LEU H H 8.36 0.03 1 717 . 125 LEU HA H 3.75 0.03 1 718 . 125 LEU C C 178.5 0.1 1 719 . 125 LEU CA C 58.0 0.1 1 720 . 125 LEU CB C 40.8 0.1 1 721 . 125 LEU N N 117.4 0.1 1 722 . 126 LEU H H 8.39 0.03 1 723 . 126 LEU HA H 3.73 0.03 1 724 . 126 LEU C C 181.7 0.1 1 725 . 126 LEU CA C 59.0 0.1 1 726 . 126 LEU CB C 38.9 0.1 1 727 . 126 LEU N N 122.3 0.1 1 728 . 127 GLU H H 9.20 0.03 1 729 . 127 GLU HA H 4.04 0.03 1 730 . 127 GLU C C 177.9 0.1 1 731 . 127 GLU CA C 59.5 0.1 1 732 . 127 GLU CB C 29.8 0.1 1 733 . 127 GLU N N 122.8 0.1 1 734 . 128 GLY H H 7.47 0.03 1 735 . 128 GLY HA2 H 4.34 0.03 2 736 . 128 GLY HA3 H 3.44 0.03 2 737 . 128 GLY C C 173.6 0.1 1 738 . 128 GLY CA C 45.4 0.1 1 739 . 128 GLY N N 105.2 0.1 1 740 . 129 GLY H H 7.33 0.03 1 741 . 129 GLY HA2 H 3.76 0.03 1 742 . 129 GLY HA3 H 4.35 0.03 1 743 . 129 GLY C C 175.2 0.1 1 744 . 129 GLY CA C 45.3 0.1 1 745 . 129 GLY N N 104.9 0.1 1 746 . 130 ALA H H 8.51 0.03 1 747 . 130 ALA HA H 3.98 0.03 1 748 . 130 ALA C C 176.1 0.1 1 749 . 130 ALA CA C 52.9 0.1 1 750 . 130 ALA CB C 19.3 0.1 1 751 . 130 ALA N N 123.9 0.1 1 752 . 131 ASN H H 9.04 0.03 1 753 . 131 ASN HA H 4.93 0.03 1 754 . 131 ASN CA C 50.1 0.1 1 755 . 131 ASN CB C 38.4 0.1 1 756 . 131 ASN N N 121.2 0.1 1 757 . 132 PRO C C 177.3 0.1 1 758 . 132 PRO CA C 64.5 0.1 1 759 . 133 ASP H H 7.63 0.03 1 760 . 133 ASP HA H 4.79 0.03 9 761 . 133 ASP C C 174.3 0.1 1 762 . 133 ASP CA C 53.6 0.1 1 763 . 133 ASP CB C 40.8 0.1 1 764 . 133 ASP N N 118.6 0.1 1 765 . 134 ALA H H 6.62 0.03 1 766 . 134 ALA HA H 4.03 0.03 1 767 . 134 ALA C C 177.9 0.1 1 768 . 134 ALA CA C 54.3 0.1 1 769 . 134 ALA CB C 19.1 0.1 1 770 . 134 ALA N N 122.6 0.1 1 771 . 135 LYS H H 8.85 0.03 1 772 . 135 LYS C C 176.9 0.1 1 773 . 135 LYS CA C 55.4 0.1 1 774 . 135 LYS CB C 36.8 0.1 1 775 . 135 LYS N N 123.7 0.1 1 776 . 136 ASP H H 8.55 0.03 1 777 . 136 ASP HA H 4.82 0.03 1 778 . 136 ASP C C 178.8 0.1 1 779 . 136 ASP CA C 52.9 0.1 1 780 . 136 ASP CB C 42.2 0.1 1 781 . 136 ASP N N 124.0 0.1 1 782 . 137 HIS H H 7.67 0.03 1 783 . 137 HIS HA H 4.57 0.03 1 784 . 137 HIS C C 176.1 0.1 1 785 . 137 HIS CA C 57.6 0.1 1 786 . 137 HIS CB C 30.2 0.1 1 787 . 137 HIS N N 115.6 0.1 1 788 . 138 TYR H H 8.52 0.03 1 789 . 138 TYR HA H 4.59 0.03 1 790 . 138 TYR C C 174.0 0.1 1 791 . 138 TYR CA C 57.9 0.1 1 792 . 138 TYR CB C 38.0 0.1 1 793 . 138 TYR N N 122.1 0.1 1 794 . 139 GLU H H 8.23 0.03 1 795 . 139 GLU HA H 3.62 0.03 1 796 . 139 GLU C C 171.3 0.1 1 797 . 139 GLU CA C 58.2 0.1 1 798 . 139 GLU CB C 27.0 0.1 1 799 . 139 GLU N N 113.2 0.1 1 800 . 140 ALA H H 8.11 0.03 1 801 . 140 ALA HA H 4.15 0.03 1 802 . 140 ALA C C 179.2 0.1 1 803 . 140 ALA CA C 51.1 0.1 1 804 . 140 ALA CB C 21.6 0.1 1 805 . 140 ALA N N 116.1 0.1 1 806 . 141 THR H H 9.14 0.03 1 807 . 141 THR HA H 5.23 0.03 1 808 . 141 THR C C 176.9 0.1 1 809 . 141 THR CA C 60.8 0.1 1 810 . 141 THR CB C 74.5 0.1 1 811 . 141 THR N N 114.6 0.1 1 812 . 142 ALA H H 10.24 0.03 1 813 . 142 ALA HA H 3.90 0.03 1 814 . 142 ALA C C 178.4 0.1 1 815 . 142 ALA CA C 56.1 0.1 1 816 . 142 ALA CB C 18.3 0.1 1 817 . 142 ALA N N 125.3 0.1 1 818 . 143 MET H H 9.15 0.03 1 819 . 143 MET HA H 3.90 0.03 1 820 . 143 MET C C 178.8 0.1 1 821 . 143 MET CA C 58.5 0.1 1 822 . 143 MET CB C 31.6 0.1 1 823 . 143 MET N N 119.0 0.1 1 824 . 144 HIS H H 8.04 0.03 1 825 . 144 HIS HA H 3.73 0.03 1 826 . 144 HIS C C 177.5 0.1 1 827 . 144 HIS CA C 64.6 0.1 1 828 . 144 HIS CB C 30.9 0.1 1 829 . 144 HIS N N 118.8 0.1 1 830 . 145 ARG H H 7.26 0.03 1 831 . 145 ARG HA H 4.10 0.03 1 832 . 145 ARG C C 178.5 0.1 1 833 . 145 ARG CA C 58.2 0.1 1 834 . 145 ARG CB C 30.2 0.1 1 835 . 145 ARG N N 115.2 0.1 1 836 . 146 ALA H H 8.37 0.03 1 837 . 146 ALA HA H 4.11 0.03 1 838 . 146 ALA C C 179.0 0.1 1 839 . 146 ALA CA C 55.2 0.1 1 840 . 146 ALA CB C 19.3 0.1 1 841 . 146 ALA N N 119.5 0.1 1 842 . 147 ALA H H 8.43 0.03 1 843 . 147 ALA HA H 3.85 0.03 1 844 . 147 ALA C C 178.0 0.1 1 845 . 147 ALA CA C 56.0 0.1 1 846 . 147 ALA CB C 20.2 0.1 1 847 . 147 ALA N N 119.5 0.1 1 848 . 148 ALA H H 7.59 0.03 1 849 . 148 ALA HA H 3.83 0.03 1 850 . 148 ALA C C 179.5 0.1 1 851 . 148 ALA CA C 55.3 0.1 1 852 . 148 ALA CB C 20.2 0.1 1 853 . 148 ALA N N 116.2 0.1 1 854 . 149 LYS H H 7.36 0.03 1 855 . 149 LYS HA H 4.28 0.03 1 856 . 149 LYS CA C 55.7 0.1 1 857 . 149 LYS CB C 33.4 0.1 1 858 . 149 LYS N N 111.4 0.1 1 859 . 150 GLY C C 173.3 0.1 1 860 . 150 GLY CA C 47.1 0.1 1 861 . 151 ASN H H 8.25 0.03 1 862 . 151 ASN HA H 5.11 0.03 1 863 . 151 ASN C C 175.2 0.1 1 864 . 151 ASN CA C 51.7 0.1 1 865 . 151 ASN CB C 38.5 0.1 1 866 . 151 ASN N N 119.4 0.1 1 867 . 152 LEU H H 7.60 0.03 1 868 . 152 LEU C C 178.0 0.1 1 869 . 152 LEU CA C 59.9 0.1 1 870 . 152 LEU N N 124.3 0.1 1 871 . 153 LYS H H 8.53 0.03 1 872 . 153 LYS C C 178.7 0.1 1 873 . 153 LYS CA C 60.1 0.1 1 874 . 153 LYS CB C 31.9 0.1 1 875 . 153 LYS N N 117.8 0.1 1 876 . 154 MET H H 7.90 0.03 1 877 . 154 MET C C 177.7 0.1 1 878 . 154 MET CA C 56.2 0.1 1 879 . 154 MET N N 116.7 0.1 1 880 . 155 ILE H H 7.88 0.03 1 881 . 155 ILE HA H 3.51 0.03 1 882 . 155 ILE C C 177.4 0.1 1 883 . 155 ILE CA C 67.1 0.1 1 884 . 155 ILE CB C 37.6 0.1 1 885 . 155 ILE N N 119.6 0.1 1 886 . 156 HIS H H 7.98 0.03 1 887 . 156 HIS HA H 4.09 0.03 1 888 . 156 HIS C C 179.3 0.1 1 889 . 156 HIS CA C 61.8 0.1 1 890 . 156 HIS N N 117.7 0.1 1 891 . 157 ILE H H 8.05 0.03 1 892 . 157 ILE HA H 3.82 0.03 1 893 . 157 ILE C C 177.5 0.1 1 894 . 157 ILE CA C 66.0 0.1 1 895 . 157 ILE CB C 39.1 0.1 1 896 . 157 ILE N N 120.9 0.1 1 897 . 158 LEU H H 8.30 0.03 1 898 . 158 LEU C C 179.4 0.1 1 899 . 158 LEU CA C 59.3 0.1 1 900 . 158 LEU CB C 41.2 0.1 1 901 . 158 LEU N N 119.0 0.1 1 902 . 159 LEU H H 8.64 0.03 1 903 . 159 LEU HA H 4.08 0.03 1 904 . 159 LEU C C 181.4 0.1 1 905 . 159 LEU CA C 58.2 0.1 1 906 . 159 LEU CB C 41.4 0.1 1 907 . 159 LEU N N 117.8 0.1 1 908 . 160 TYR H H 8.32 0.03 1 909 . 160 TYR HA H 4.03 0.03 1 910 . 160 TYR C C 177.3 0.1 1 911 . 160 TYR CA C 61.9 0.1 1 912 . 160 TYR CB C 37.9 0.1 1 913 . 160 TYR N N 124.5 0.1 1 914 . 161 TYR H H 7.49 0.03 1 915 . 161 TYR HA H 4.29 0.03 1 916 . 161 TYR C C 173.2 0.1 1 917 . 161 TYR CA C 59.8 0.1 1 918 . 161 TYR CB C 38.1 0.1 1 919 . 161 TYR N N 115.8 0.1 1 920 . 162 LYS H H 7.67 0.03 1 921 . 162 LYS HA H 3.85 0.03 1 922 . 162 LYS C C 176.3 0.1 1 923 . 162 LYS CA C 57.2 0.1 1 924 . 162 LYS CB C 27.9 0.1 1 925 . 162 LYS N N 109.5 0.1 1 926 . 163 ALA H H 8.14 0.03 1 927 . 163 ALA HA H 4.10 0.03 1 928 . 163 ALA C C 177.2 0.1 1 929 . 163 ALA CA C 53.2 0.1 1 930 . 163 ALA CB C 21.5 0.1 1 931 . 163 ALA N N 121.7 0.1 1 932 . 164 SER H H 10.09 0.03 1 933 . 164 SER HA H 4.51 0.03 1 934 . 164 SER C C 176.3 0.1 1 935 . 164 SER CA C 59.7 0.1 1 936 . 164 SER CB C 63.6 0.1 1 937 . 164 SER N N 118.9 0.1 1 938 . 165 THR H H 8.43 0.03 1 939 . 165 THR HA H 4.18 0.03 1 940 . 165 THR C C 175.2 0.1 1 941 . 165 THR CA C 63.1 0.1 1 942 . 165 THR CB C 70.3 0.1 1 943 . 165 THR N N 112.0 0.1 1 944 . 166 ASN H H 8.08 0.03 1 945 . 166 ASN HA H 5.11 0.03 1 946 . 166 ASN C C 174.0 0.1 1 947 . 166 ASN CA C 53.7 0.1 1 948 . 166 ASN CB C 39.7 0.1 1 949 . 166 ASN N N 119.0 0.1 1 950 . 167 ILE H H 6.96 0.03 1 951 . 167 ILE HA H 4.10 0.03 1 952 . 167 ILE C C 174.9 0.1 1 953 . 167 ILE CA C 62.4 0.1 1 954 . 167 ILE CB C 38.6 0.1 1 955 . 167 ILE N N 120.1 0.1 1 956 . 168 GLN H H 8.52 0.03 1 957 . 168 GLN HA H 4.57 0.03 1 958 . 168 GLN C C 174.9 0.1 1 959 . 168 GLN CA C 55.3 0.1 1 960 . 168 GLN CB C 33.9 0.1 1 961 . 168 GLN N N 124.7 0.1 1 962 . 169 ASP H H 8.20 0.03 1 963 . 169 ASP HA H 4.95 0.03 1 964 . 169 ASP C C 179.8 0.1 1 965 . 169 ASP CA C 53.4 0.1 1 966 . 169 ASP CB C 41.7 0.1 1 967 . 169 ASP N N 122.0 0.1 1 968 . 170 THR H H 7.92 0.03 1 969 . 170 THR HA H 4.01 0.03 1 970 . 170 THR C C 176.1 0.1 1 971 . 170 THR CA C 65.5 0.1 1 972 . 170 THR CB C 69.4 0.1 1 973 . 170 THR N N 111.3 0.1 1 974 . 171 GLU H H 8.18 0.03 1 975 . 171 GLU HA H 4.49 0.03 1 976 . 171 GLU C C 177.0 0.1 1 977 . 171 GLU CA C 56.7 0.1 1 978 . 171 GLU CB C 30.0 0.1 1 979 . 171 GLU N N 120.2 0.1 1 980 . 172 GLY H H 8.73 0.03 1 981 . 172 GLY C C 172.9 0.1 1 982 . 172 GLY CA C 46.2 0.1 1 983 . 172 GLY N N 110.6 0.1 1 984 . 173 ASN H H 8.69 0.03 1 985 . 173 ASN HA H 4.53 0.03 1 986 . 173 ASN C C 178.0 0.1 1 987 . 173 ASN CA C 54.3 0.1 1 988 . 173 ASN CB C 39.4 0.1 1 989 . 173 ASN N N 119.8 0.1 1 990 . 174 THR H H 10.78 0.03 1 991 . 174 THR HA H 5.63 0.03 1 992 . 174 THR CA C 60.1 0.1 1 993 . 174 THR CB C 69.1 0.1 1 994 . 174 THR N N 122.1 0.1 1 995 . 175 PRO C C 176.8 0.1 1 996 . 175 PRO CA C 66.2 0.1 1 997 . 175 PRO CB C 31.5 0.1 1 998 . 176 LEU H H 8.60 0.03 1 999 . 176 LEU HA H 4.01 0.03 1 1000 . 176 LEU C C 179.3 0.1 1 1001 . 176 LEU CA C 58.0 0.1 1 1002 . 176 LEU CB C 41.5 0.1 1 1003 . 176 LEU N N 115.3 0.1 1 1004 . 177 HIS H H 7.82 0.03 1 1005 . 177 HIS HA H 3.65 0.03 1 1006 . 177 HIS C C 177.5 0.1 1 1007 . 177 HIS CA C 64.7 0.1 1 1008 . 177 HIS CB C 31.9 0.1 1 1009 . 177 HIS N N 118.3 0.1 1 1010 . 178 LEU H H 7.18 0.03 1 1011 . 178 LEU HA H 4.16 0.03 1 1012 . 178 LEU C C 179.2 0.1 1 1013 . 178 LEU CA C 58.1 0.1 1 1014 . 178 LEU CB C 40.4 0.1 1 1015 . 178 LEU N N 114.7 0.1 1 1016 . 179 ALA H H 8.22 0.03 1 1017 . 179 ALA C C 179.7 0.1 1 1018 . 179 ALA CA C 55.1 0.1 1 1019 . 179 ALA CB C 18.2 0.1 1 1020 . 179 ALA N N 119.7 0.1 1 1021 . 180 CYS H H 8.22 0.03 1 1022 . 180 CYS HA H 4.00 0.03 1 1023 . 180 CYS C C 177.8 0.1 1 1024 . 180 CYS CA C 65.0 0.1 1 1025 . 180 CYS CB C 27.6 0.1 1 1026 . 180 CYS N N 114.8 0.1 1 1027 . 181 ASP H H 8.56 0.03 1 1028 . 181 ASP HA H 4.55 0.03 1 1029 . 181 ASP C C 177.2 0.1 1 1030 . 181 ASP CA C 57.8 0.1 1 1031 . 181 ASP CB C 42.6 0.1 1 1032 . 181 ASP N N 122.5 0.1 1 1033 . 182 GLU H H 7.40 0.03 1 1034 . 182 GLU HA H 4.49 0.03 1 1035 . 182 GLU C C 174.8 0.1 1 1036 . 182 GLU CA C 56.6 0.1 1 1037 . 182 GLU CB C 30.3 0.1 1 1038 . 182 GLU N N 113.0 0.1 1 1039 . 183 GLU H H 7.78 0.03 1 1040 . 183 GLU HA H 3.46 0.03 1 1041 . 183 GLU C C 174.9 0.1 1 1042 . 183 GLU CA C 58.0 0.1 1 1043 . 183 GLU CB C 28.9 0.1 1 1044 . 183 GLU N N 118.2 0.1 1 1045 . 184 ARG H H 8.83 0.03 1 1046 . 184 ARG HA H 4.52 0.03 1 1047 . 184 ARG C C 175.5 0.1 1 1048 . 184 ARG CA C 53.1 0.1 1 1049 . 184 ARG CB C 28.8 0.1 1 1050 . 184 ARG N N 119.5 0.1 1 1051 . 185 VAL H H 7.47 0.03 1 1052 . 185 VAL HA H 3.46 0.03 1 1053 . 185 VAL C C 177.6 0.1 1 1054 . 185 VAL CA C 67.8 0.1 1 1055 . 185 VAL CB C 32.8 0.1 1 1056 . 185 VAL N N 122.1 0.1 1 1057 . 186 GLU H H 8.79 0.03 1 1058 . 186 GLU HA H 3.90 0.03 1 1059 . 186 GLU C C 179.7 0.1 1 1060 . 186 GLU CA C 59.5 0.1 1 1061 . 186 GLU CB C 28.8 0.1 1 1062 . 186 GLU N N 117.8 0.1 1 1063 . 187 GLU H H 10.24 0.03 1 1064 . 187 GLU HA H 3.58 0.03 1 1065 . 187 GLU C C 177.4 0.1 1 1066 . 187 GLU CA C 62.1 0.1 1 1067 . 187 GLU CB C 28.2 0.1 1 1068 . 187 GLU N N 123.7 0.1 1 1069 . 188 ALA H H 8.45 0.03 1 1070 . 188 ALA HA H 3.76 0.03 1 1071 . 188 ALA C C 178.8 0.1 1 1072 . 188 ALA CA C 55.7 0.1 1 1073 . 188 ALA CB C 19.7 0.1 1 1074 . 188 ALA N N 120.7 0.1 1 1075 . 189 LYS H H 8.06 0.03 1 1076 . 189 LYS HA H 3.57 0.03 1 1077 . 189 LYS C C 178.6 0.1 1 1078 . 189 LYS CA C 60.5 0.1 1 1079 . 189 LYS CB C 32.9 0.1 1 1080 . 189 LYS N N 115.6 0.1 1 1081 . 190 LEU H H 7.92 0.03 1 1082 . 190 LEU HA H 4.07 0.03 1 1083 . 190 LEU C C 179.7 0.1 1 1084 . 190 LEU CA C 58.0 0.1 1 1085 . 190 LEU CB C 41.2 0.1 1 1086 . 190 LEU N N 120.5 0.1 1 1087 . 191 LEU H H 8.13 0.03 1 1088 . 191 LEU HA H 3.70 0.03 1 1089 . 191 LEU C C 179.2 0.1 1 1090 . 191 LEU CA C 59.2 0.1 1 1091 . 191 LEU CB C 41.1 0.1 1 1092 . 191 LEU N N 118.6 0.1 1 1093 . 192 VAL H H 8.20 0.03 1 1094 . 192 VAL HA H 3.88 0.03 1 1095 . 192 VAL C C 179.9 0.1 1 1096 . 192 VAL CA C 67.4 0.1 1 1097 . 192 VAL CB C 31.8 0.1 1 1098 . 192 VAL N N 119.5 0.1 1 1099 . 193 SER H H 8.56 0.03 1 1100 . 193 SER HA H 4.30 0.03 1 1101 . 193 SER C C 174.9 0.1 1 1102 . 193 SER CA C 61.9 0.1 1 1103 . 193 SER CB C 63.6 0.1 1 1104 . 193 SER N N 118.2 0.1 1 1105 . 194 GLN H H 7.35 0.03 1 1106 . 194 GLN HA H 4.53 0.03 1 1107 . 194 GLN C C 175.7 0.1 1 1108 . 194 GLN CA C 55.2 0.1 1 1109 . 194 GLN CB C 28.4 0.1 1 1110 . 194 GLN N N 118.3 0.1 1 1111 . 195 GLY H H 7.53 0.03 1 1112 . 195 GLY HA2 H 4.37 0.03 2 1113 . 195 GLY HA3 H 3.72 0.03 2 1114 . 195 GLY C C 174.9 0.1 1 1115 . 195 GLY CA C 46.1 0.1 1 1116 . 195 GLY N N 105.9 0.1 1 1117 . 196 ALA H H 8.39 0.03 1 1118 . 196 ALA HA H 4.38 0.03 1 1119 . 196 ALA C C 177.2 0.1 1 1120 . 196 ALA CA C 53.1 0.1 1 1121 . 196 ALA CB C 20.8 0.1 1 1122 . 196 ALA N N 125.8 0.1 1 1123 . 197 SER H H 9.04 0.03 1 1124 . 197 SER HA H 4.07 0.03 1 1125 . 197 SER C C 177.7 0.1 1 1126 . 197 SER CA C 57.4 0.1 1 1127 . 197 SER CB C 64.5 0.1 1 1128 . 197 SER N N 116.6 0.1 1 1129 . 198 ILE H H 7.97 0.03 1 1130 . 198 ILE HA H 3.87 0.03 1 1131 . 198 ILE C C 175.0 0.1 1 1132 . 198 ILE CA C 62.7 0.1 1 1133 . 198 ILE CB C 37.7 0.1 1 1134 . 198 ILE N N 118.4 0.1 1 1135 . 199 TYR H H 8.12 0.03 1 1136 . 199 TYR HA H 4.67 0.03 1 1137 . 199 TYR C C 175.5 0.1 1 1138 . 199 TYR CA C 58.4 0.1 1 1139 . 199 TYR CB C 40.5 0.1 1 1140 . 199 TYR N N 117.8 0.1 1 1141 . 200 ILE H H 6.36 0.03 1 1142 . 200 ILE HA H 3.98 0.03 1 1143 . 200 ILE C C 174.6 0.1 1 1144 . 200 ILE CA C 62.1 0.1 1 1145 . 200 ILE CB C 39.8 0.1 1 1146 . 200 ILE N N 120.1 0.1 1 1147 . 201 GLU H H 8.57 0.03 1 1148 . 201 GLU HA H 4.37 0.03 1 1149 . 201 GLU C C 176.9 0.1 1 1150 . 201 GLU CA C 55.8 0.1 1 1151 . 201 GLU CB C 32.4 0.1 1 1152 . 201 GLU N N 126.4 0.1 1 1153 . 202 ASN H H 8.13 0.03 1 1154 . 202 ASN C C 178.0 0.1 1 1155 . 202 ASN CA C 51.4 0.1 1 1156 . 202 ASN CB C 38.7 0.1 1 1157 . 202 ASN N N 119.6 0.1 1 1158 . 203 LYS H H 7.86 0.03 1 1159 . 203 LYS HA H 4.08 0.03 1 1160 . 203 LYS C C 177.6 0.1 1 1161 . 203 LYS CA C 59.8 0.1 1 1162 . 203 LYS CB C 32.3 0.1 1 1163 . 203 LYS N N 117.4 0.1 1 1164 . 204 GLU H H 7.44 0.03 1 1165 . 204 GLU HA H 4.38 0.03 1 1166 . 204 GLU C C 174.6 0.1 1 1167 . 204 GLU CA C 56.5 0.1 1 1168 . 204 GLU CB C 29.6 0.1 1 1169 . 204 GLU N N 119.0 0.1 1 1170 . 205 GLU H H 8.17 0.03 1 1171 . 205 GLU HA H 3.76 0.03 1 1172 . 205 GLU C C 174.8 0.1 1 1173 . 205 GLU CA C 58.2 0.1 1 1174 . 205 GLU CB C 26.7 0.1 1 1175 . 205 GLU N N 112.7 0.1 1 1176 . 206 LYS H H 7.67 0.03 1 1177 . 206 LYS HA H 5.27 0.03 1 1178 . 206 LYS C C 178.9 0.1 1 1179 . 206 LYS CA C 54.3 0.1 1 1180 . 206 LYS CB C 35.3 0.1 1 1181 . 206 LYS N N 114.7 0.1 1 1182 . 207 THR H H 9.29 0.03 1 1183 . 207 THR HA H 5.33 0.03 1 1184 . 207 THR CA C 60.8 0.1 1 1185 . 207 THR CB C 69.0 0.1 1 1186 . 207 THR N N 118.0 0.1 1 1187 . 208 PRO HA H 3.90 0.03 1 1188 . 208 PRO C C 176.8 0.1 1 1189 . 208 PRO CA C 65.5 0.1 1 1190 . 209 LEU H H 6.59 0.03 1 1191 . 209 LEU HA H 3.80 0.03 1 1192 . 209 LEU C C 179.2 0.1 1 1193 . 209 LEU CA C 57.5 0.1 1 1194 . 209 LEU CB C 40.6 0.1 1 1195 . 209 LEU N N 107.2 0.1 1 1196 . 210 GLN H H 7.35 0.03 1 1197 . 210 GLN HA H 4.21 0.03 1 1198 . 210 GLN C C 177.6 0.1 1 1199 . 210 GLN CA C 58.1 0.1 1 1200 . 210 GLN CB C 30.7 0.1 1 1201 . 210 GLN N N 116.1 0.1 1 1202 . 211 VAL H H 7.17 0.03 1 1203 . 211 VAL HA H 4.40 0.03 1 1204 . 211 VAL C C 175.2 0.1 1 1205 . 211 VAL CA C 61.9 0.1 1 1206 . 211 VAL CB C 32.3 0.1 1 1207 . 211 VAL N N 112.2 0.1 1 1208 . 212 ALA H H 6.94 0.03 1 1209 . 212 ALA HA H 4.10 0.03 1 1210 . 212 ALA C C 176.9 0.1 1 1211 . 212 ALA CA C 52.9 0.1 1 1212 . 212 ALA CB C 19.2 0.1 1 1213 . 212 ALA N N 121.5 0.1 1 1214 . 213 LYS H H 8.26 0.03 1 1215 . 213 LYS HA H 4.57 0.03 1 1216 . 213 LYS C C 177.9 0.1 1 1217 . 213 LYS CA C 55.5 0.1 1 1218 . 213 LYS CB C 35.3 0.1 1 1219 . 213 LYS N N 123.2 0.1 1 1220 . 214 GLY H H 8.76 0.03 1 1221 . 214 GLY CA C 47.4 0.1 1 1222 . 214 GLY N N 108.1 0.1 1 1223 . 215 GLY C C 175.9 0.1 1 1224 . 215 GLY CA C 45.7 0.1 1 1225 . 216 LEU H H 7.73 0.03 1 1226 . 216 LEU HA H 4.14 0.03 1 1227 . 216 LEU C C 177.5 0.1 1 1228 . 216 LEU CA C 58.0 0.1 1 1229 . 216 LEU CB C 42.2 0.1 1 1230 . 216 LEU N N 121.8 0.1 1 1231 . 217 GLY H H 8.60 0.03 1 1232 . 217 GLY HA2 H 3.95 0.03 2 1233 . 217 GLY HA3 H 3.47 0.03 2 1234 . 217 GLY C C 175.0 0.1 1 1235 . 217 GLY CA C 47.8 0.1 1 1236 . 217 GLY N N 106.2 0.1 1 1237 . 218 LEU H H 7.38 0.03 1 1238 . 218 LEU HA H 4.09 0.03 1 1239 . 218 LEU C C 179.3 0.1 1 1240 . 218 LEU CA C 58.0 0.1 1 1241 . 218 LEU CB C 41.9 0.1 1 1242 . 218 LEU N N 120.2 0.1 1 1243 . 219 ILE H H 7.12 0.03 1 1244 . 219 ILE HA H 3.60 0.03 1 1245 . 219 ILE C C 179.0 0.1 1 1246 . 219 ILE CA C 65.0 0.1 1 1247 . 219 ILE CB C 38.6 0.1 1 1248 . 219 ILE N N 119.1 0.1 1 1249 . 220 LEU H H 7.96 0.03 1 1250 . 220 LEU C C 178.4 0.1 1 1251 . 220 LEU CA C 57.8 0.1 1 1252 . 220 LEU CB C 39.0 0.1 1 1253 . 220 LEU N N 117.4 0.1 1 1254 . 221 LYS H H 8.07 0.03 1 1255 . 221 LYS C C 178.8 0.1 1 1256 . 221 LYS CA C 60.6 0.1 1 1257 . 221 LYS CB C 33.4 0.1 1 1258 . 221 LYS N N 118.3 0.1 1 1259 . 222 ARG H H 7.82 0.03 1 1260 . 222 ARG HA H 4.14 0.03 1 1261 . 222 ARG C C 179.3 0.1 1 1262 . 222 ARG CA C 58.9 0.1 1 1263 . 222 ARG CB C 29.8 0.1 1 1264 . 222 ARG N N 116.9 0.1 1 1265 . 223 MET H H 7.68 0.03 1 1266 . 223 MET HA H 4.00 0.03 1 1267 . 223 MET C C 177.3 0.1 1 1268 . 223 MET CA C 59.7 0.1 1 1269 . 223 MET CB C 33.7 0.1 1 1270 . 223 MET N N 118.1 0.1 1 1271 . 224 VAL H H 7.26 0.03 1 1272 . 224 VAL HA H 3.97 0.03 1 1273 . 224 VAL C C 177.3 0.1 1 1274 . 224 VAL CA C 65.2 0.1 1 1275 . 224 VAL CB C 34.1 0.1 1 1276 . 224 VAL N N 116.8 0.1 1 1277 . 225 GLU H H 8.62 0.03 1 1278 . 225 GLU HA H 4.33 0.03 1 1279 . 225 GLU C C 176.9 0.1 1 1280 . 225 GLU CA C 57.7 0.1 1 1281 . 225 GLU CB C 30.8 0.1 1 1282 . 225 GLU N N 117.9 0.1 1 1283 . 226 GLY H H 7.74 0.03 1 1284 . 226 GLY HA2 H 3.98 0.03 2 1285 . 226 GLY HA3 H 3.68 0.03 2 1286 . 226 GLY CA C 46.6 0.1 1 1287 . 226 GLY N N 115.1 0.1 1 stop_ save_