data_4836 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete 1H, 13C and 15N Backbone Assignments for the Hepatitis A Virus 3C Protease ; _BMRB_accession_number 4836 _BMRB_flat_file_name bmr4836.str _Entry_type original _Submission_date 2000-09-19 _Accession_date 2000-09-19 _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 Bjorndahl Trent C. . 2 Watson Scott M. . 3 Slupsky Carolyn M. . 4 Spyracopoulos Leo . . 5 Sykes Brian D. . 6 Wishart David S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 414 "13C chemical shifts" 615 "15N chemical shifts" 206 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-13 update author 'update of chemical shifts' 2000-11-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Complete 1H, 13C and 15N backbone assignments for the hepatitis A virus 3C protease ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bjorndahl Trent C. . 2 Watson M. Scott . 3 Slupsky Carolyn M. . 4 Spyracopoulos Leo . . 5 Sykes Brian D. . 6 Wishart David S. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 187 _Page_last 188 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_HAV3C _Saveframe_category molecular_system _Mol_system_name 'Hepatitis A 3C Protease monomer' _Abbreviation_common HAV3C _Enzyme_commission_number 3.4.22.28 loop_ _Mol_system_component_name _Mol_label 'Hepatis A 3C Protease' $HAV3C stop_ _System_molecular_weight 23976.59 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function hydrolase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HAV3C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HAV3C _Abbreviation_common HAV3C _Molecular_mass 23976.59 _Mol_thiol_state 'all free' _Details ; Proteolytic processes the RNA translated polyprotein of Hepatitis A viruses ; ############################## # Polymer residue sequence # ############################## _Residue_count 217 _Mol_residue_sequence ; STLEIAGLVRKNLVQFGVGE KNGSVRWVMNALGVKDDWLL VPSHAYKFEKDYEMMEFYFN RGGTYYSISAGNVVIQSLDV GFQDVVLMKVPTIPKFRDIT QHFIKKGDVPRALNRLATLV TTVNGTPMLISEGPLKMEEK ATYVHKKNDGTTVDLTVDQA WRGKGEGLPGMCGGALVSSN QSIQNAILGIHVAGGNSILV AKLVTQEMFQNIDKKIE ; loop_ _Residue_seq_code _Residue_label 1 SER 2 THR 3 LEU 4 GLU 5 ILE 6 ALA 7 GLY 8 LEU 9 VAL 10 ARG 11 LYS 12 ASN 13 LEU 14 VAL 15 GLN 16 PHE 17 GLY 18 VAL 19 GLY 20 GLU 21 LYS 22 ASN 23 GLY 24 SER 25 VAL 26 ARG 27 TRP 28 VAL 29 MET 30 ASN 31 ALA 32 LEU 33 GLY 34 VAL 35 LYS 36 ASP 37 ASP 38 TRP 39 LEU 40 LEU 41 VAL 42 PRO 43 SER 44 HIS 45 ALA 46 TYR 47 LYS 48 PHE 49 GLU 50 LYS 51 ASP 52 TYR 53 GLU 54 MET 55 MET 56 GLU 57 PHE 58 TYR 59 PHE 60 ASN 61 ARG 62 GLY 63 GLY 64 THR 65 TYR 66 TYR 67 SER 68 ILE 69 SER 70 ALA 71 GLY 72 ASN 73 VAL 74 VAL 75 ILE 76 GLN 77 SER 78 LEU 79 ASP 80 VAL 81 GLY 82 PHE 83 GLN 84 ASP 85 VAL 86 VAL 87 LEU 88 MET 89 LYS 90 VAL 91 PRO 92 THR 93 ILE 94 PRO 95 LYS 96 PHE 97 ARG 98 ASP 99 ILE 100 THR 101 GLN 102 HIS 103 PHE 104 ILE 105 LYS 106 LYS 107 GLY 108 ASP 109 VAL 110 PRO 111 ARG 112 ALA 113 LEU 114 ASN 115 ARG 116 LEU 117 ALA 118 THR 119 LEU 120 VAL 121 THR 122 THR 123 VAL 124 ASN 125 GLY 126 THR 127 PRO 128 MET 129 LEU 130 ILE 131 SER 132 GLU 133 GLY 134 PRO 135 LEU 136 LYS 137 MET 138 GLU 139 GLU 140 LYS 141 ALA 142 THR 143 TYR 144 VAL 145 HIS 146 LYS 147 LYS 148 ASN 149 ASP 150 GLY 151 THR 152 THR 153 VAL 154 ASP 155 LEU 156 THR 157 VAL 158 ASP 159 GLN 160 ALA 161 TRP 162 ARG 163 GLY 164 LYS 165 GLY 166 GLU 167 GLY 168 LEU 169 PRO 170 GLY 171 MET 172 CYS 173 GLY 174 GLY 175 ALA 176 LEU 177 VAL 178 SER 179 SER 180 ASN 181 GLN 182 SER 183 ILE 184 GLN 185 ASN 186 ALA 187 ILE 188 LEU 189 GLY 190 ILE 191 HIS 192 VAL 193 ALA 194 GLY 195 GLY 196 ASN 197 SER 198 ILE 199 LEU 200 VAL 201 ALA 202 LYS 203 LEU 204 VAL 205 THR 206 GLN 207 GLU 208 MET 209 PHE 210 GLN 211 ASN 212 ILE 213 ASP 214 LYS 215 LYS 216 ILE 217 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 16837 HAV_3C_protease_C24S 100.00 217 100.00 100.00 1.72e-157 PDB 1HAV "Hepatitis A Virus 3c Proteinase" 100.00 217 100.00 100.00 1.72e-157 PDB 1QA7 "Crystal Complex Of The 3c Proteinase From Hepatitis A Virus With Its Inhibitor And Implications For The Polyprotein Processing " 100.00 217 99.54 99.54 2.59e-156 PDB 2A4O "Dual Modes Of Modification Of Hepatitis A Virus 3c Protease By A Serine Derived Beta-Lactone: Selective Crytstallization And Hi" 100.00 219 100.00 100.00 1.78e-157 PDB 2CXV "Dual Modes Of Modification Of Hepatitis A Virus 3c Protease By A Serine-Derived Betalactone: Selective Crystallization And High" 100.00 219 100.00 100.00 1.78e-157 PDB 2H6M "An Episulfide Cation (Thiiranium Ring) Trapped In The Active Site Of Hav 3c Proteinase Inactivated By Peptide-Based Ketone Inhi" 97.70 212 100.00 100.00 1.44e-153 PDB 2H9H "An Episulfide Cation (Thiiranium Ring) Trapped In The Active Site Of Hav 3c Proteinase Inactivated By Peptide-Based Ketone Inhi" 97.70 212 100.00 100.00 1.44e-153 PDB 2HAL "An Episulfide Cation (Thiiranium Ring) Trapped In The Active Site Of Hav 3c Proteinase Inactivated By Peptide-Based Ketone Inhi" 97.70 212 100.00 100.00 1.44e-153 DBJ BAA35102 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.41e-141 DBJ BAA35103 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.35e-141 DBJ BAA35104 "polyprotein [Hepatitis A virus]" 100.00 2216 99.08 99.08 5.15e-140 DBJ BAA35105 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.45e-141 DBJ BAA35106 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.38e-141 EMBL CAA33491 "unnamed protein product [Hepatitis A virus]" 100.00 891 99.08 99.54 8.46e-148 EMBL CAA50195 "viral polyprotein [Hepatitis A virus]" 100.00 746 98.62 99.08 3.06e-148 EMBL CAA53024 "unnamed protein product [Hepatitis A virus]" 100.00 2218 98.62 99.08 5.41e-140 EMBL CAA53025 "unnamed protein product [Hepatitis A virus]" 100.00 2227 99.08 99.08 1.51e-140 EMBL CAA53026 "unnamed protein product [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.00e-141 GB AAA45465 "polyprotein a (alt.) [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.56e-141 GB AAA45466 "polyprotein b (alt.) [Hepatitis A virus]" 100.00 2225 99.54 99.54 2.34e-141 GB AAA45467 "viral protein [Hepatitis A virus]" 100.00 2226 99.08 99.54 1.05e-140 GB AAA45468 "viral protein [Hepatitis A virus]" 100.00 2226 99.08 99.54 9.29e-141 GB AAA45469 "viral protein [Hepatitis A virus]" 100.00 2226 98.62 99.08 2.34e-140 PIR GNNYHB "genome polyprotein - human hepatitis A virus (strain MBB)" 100.00 2227 99.54 99.54 3.00e-141 REF NP_041007 "hypothetical protein HAVgp1 [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.56e-141 REF NP_041008 "hypothetical protein HAVgp2 [Hepatitis A virus]" 100.00 2225 99.54 99.54 2.34e-141 REF NP_740558 "3C mature peptide [Hepatitis A virus]" 100.00 219 99.54 99.54 9.73e-157 SP A3FMB2 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Protein VP0; AltName: Full=VP4-VP2; Contains: RecName: Full=Protein V" 100.00 2227 99.54 99.54 3.00e-141 SP A5LGW7 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Protein VP0; AltName: Full=VP4-VP2; Contains: RecName: Full=Protein V" 99.54 2228 97.22 99.07 7.55e-139 SP P06441 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Protein VP0; AltName: Full=VP4-VP2; Contains: RecName: Full=Protein V" 100.00 2227 99.54 99.54 2.58e-141 SP P08617 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Protein VP0; AltName: Full=VP4-VP2; Contains: RecName: Full=Protein V" 100.00 2227 99.54 99.54 2.56e-141 SP P13901 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Protein VP0; AltName: Full=VP4-VP2; Contains: RecName: Full=Protein V" 100.00 2227 99.54 99.54 2.38e-141 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _Organism_acronym _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Plasmid _Gene_mnemonic $HAV3C 'Hepatitis A' HAV 52.0.3.0.001 39112 Virus Flaviviridae Hepatitis . A pHAV-3CEX lac 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 $HAV3C 'recombinant technology' 'E. coli' Escherichia coli 'MM294 and CT16' plasmid pHAV-3CEX 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 _Isotopic_labeling $HAV3C 1 mM [U-15N] KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[U-15N; U-13C]' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[U-15N; U-13C; U-2H]' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Gly' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_5 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Leu' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_6 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Ile' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_7 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Val' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_8 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Lys' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_9 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Ala' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ save_sample_10 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HAV3C 1 mM '[98% 15N]-Phe' KH2PO4 20 mM . NaCl 100 mM . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_1 loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $HAV3C 95 % 'SDS gel electrophoresis' stop_ save_ ############################ # Computer software used # ############################ save_NMR-PIPE _Saveframe_category software _Name NMR-PIPE _Version . loop_ _Task 'specta processing' 'peak picking' 'spectral analysis' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task 'peak picking' 'spectral analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_experiment_label _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 0.1 pH temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 external direct external . . . DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.25144954 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.10132900 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_shifts _Saveframe_category assigned_chemical_shifts _Details ; There are deuterium isotope effects for the CA, CB and N chemical shifts. These effects can result in an average upfield shifts of 0.43, 0.82 and 0.25 respectively (Gardner, K. H. et al, Biochemistry, 36, 1389-1401). ; loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 $sample_7 $sample_8 $sample_9 $sample_10 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Hepatis A 3C Protease' _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 SER C C 172.47 0.2 1 2 . 1 SER CA C 56.89 0.2 1 3 . 1 SER CB C 63.73 0.2 1 4 . 2 THR H H 9.03 0.02 1 5 . 2 THR HA H 4.17 0.02 1 6 . 2 THR C C 175.52 0.2 1 7 . 2 THR CA C 66.50 0.2 1 8 . 2 THR CB C 68.01 0.2 1 9 . 2 THR N N 119.60 0.2 1 10 . 3 LEU H H 8.22 0.02 1 11 . 3 LEU HA H 3.97 0.02 1 12 . 3 LEU C C 179.89 0.2 1 13 . 3 LEU CA C 57.34 0.2 1 14 . 3 LEU CB C 40.43 0.2 1 15 . 3 LEU N N 119.47 0.2 1 16 . 4 GLU H H 7.75 0.02 1 17 . 4 GLU HA H 3.98 0.02 1 18 . 4 GLU C C 179.48 0.2 1 19 . 4 GLU CA C 58.67 0.2 1 20 . 4 GLU CB C 28.79 0.2 1 21 . 4 GLU N N 120.75 0.2 1 22 . 5 ILE H H 7.45 0.02 1 23 . 5 ILE HA H 4.11 0.02 1 24 . 5 ILE C C 178.50 0.2 1 25 . 5 ILE CA C 61.02 0.2 1 26 . 5 ILE CB C 34.25 0.2 1 27 . 5 ILE N N 119.72 0.2 1 28 . 6 ALA H H 9.15 0.02 1 29 . 6 ALA HA H 3.88 0.02 1 30 . 6 ALA C C 179.58 0.2 1 31 . 6 ALA CA C 55.05 0.2 1 32 . 6 ALA CB C 17.61 0.2 1 33 . 6 ALA N N 122.16 0.2 1 34 . 7 GLY H H 7.86 0.02 1 35 . 7 GLY HA2 H 3.93 0.02 1 36 . 7 GLY HA3 H 3.84 0.02 1 37 . 7 GLY C C 176.13 0.2 1 38 . 7 GLY CA C 46.69 0.2 1 39 . 7 GLY N N 104.03 0.2 1 40 . 8 LEU H H 7.31 0.02 1 41 . 8 LEU HA H 4.02 0.02 1 42 . 8 LEU C C 180.06 0.2 1 43 . 8 LEU CA C 57.13 0.2 1 44 . 8 LEU CB C 40.67 0.2 1 45 . 8 LEU N N 121.69 0.2 1 46 . 9 VAL H H 8.24 0.02 1 47 . 9 VAL HA H 4.36 0.02 1 48 . 9 VAL C C 178.09 0.2 1 49 . 9 VAL CA C 66.16 0.2 1 50 . 9 VAL CB C 30.93 0.2 1 51 . 9 VAL N N 118.24 0.2 1 52 . 10 ARG H H 8.61 0.02 1 53 . 10 ARG HA H 3.91 0.02 1 54 . 10 ARG C C 179.11 0.2 1 55 . 10 ARG CA C 59.52 0.2 1 56 . 10 ARG CB C 28.55 0.2 1 57 . 10 ARG N N 116.92 0.2 1 58 . 11 LYS H H 7.29 0.02 1 59 . 11 LYS HA H 4.26 0.02 1 60 . 11 LYS C C 176.59 0.2 1 61 . 11 LYS CA C 57.75 0.2 1 62 . 11 LYS CB C 31.40 0.2 1 63 . 11 LYS N N 115.62 0.2 1 64 . 12 ASN H H 7.61 0.02 1 65 . 12 ASN HA H 5.02 0.02 1 66 . 12 ASN C C 174.01 0.2 1 67 . 12 ASN CA C 51.97 0.2 1 68 . 12 ASN CB C 38.29 0.2 1 69 . 12 ASN N N 118.63 0.2 1 70 . 13 LEU H H 7.53 0.02 1 71 . 13 LEU HA H 4.96 0.02 1 72 . 13 LEU C C 177.19 0.2 1 73 . 13 LEU CA C 55.41 0.2 1 74 . 13 LEU CB C 42.57 0.2 1 75 . 13 LEU N N 125.20 0.2 1 76 . 14 VAL H H 9.17 0.02 1 77 . 14 VAL HA H 5.15 0.02 1 78 . 14 VAL C C 175.44 0.2 1 79 . 14 VAL CA C 58.35 0.2 1 80 . 14 VAL CB C 34.49 0.2 1 81 . 14 VAL N N 117.25 0.2 1 82 . 15 GLN H H 7.81 0.02 1 83 . 15 GLN HA H 5.10 0.02 1 84 . 15 GLN C C 174.72 0.2 1 85 . 15 GLN CA C 56.42 0.2 1 86 . 15 GLN CB C 30.90 0.2 1 87 . 15 GLN N N 118.25 0.2 1 88 . 16 PHE H H 8.84 0.02 1 89 . 16 PHE HA H 5.24 0.02 1 90 . 16 PHE C C 175.63 0.2 1 91 . 16 PHE CA C 54.06 0.2 1 92 . 16 PHE CB C 33.54 0.2 1 93 . 16 PHE N N 122.51 0.2 1 94 . 17 GLY H H 8.67 0.02 1 95 . 17 GLY C C 169.63 0.2 1 96 . 17 GLY CA C 43.76 0.2 1 97 . 17 GLY N N 109.99 0.2 1 98 . 18 VAL H H 8.08 0.02 1 99 . 18 VAL HA H 5.24 0.02 1 100 . 18 VAL C C 175.40 0.2 1 101 . 18 VAL CA C 58.57 0.2 1 102 . 18 VAL CB C 34.97 0.2 1 103 . 18 VAL N N 112.74 0.2 1 104 . 19 GLY H H 8.94 0.02 1 105 . 19 GLY C C 172.47 0.2 1 106 . 19 GLY CA C 45.35 0.2 1 107 . 19 GLY N N 110.22 0.2 1 108 . 20 GLU H H 8.46 0.02 1 109 . 20 GLU HA H 4.71 0.02 1 110 . 20 GLU C C 177.87 0.2 1 111 . 20 GLU CA C 54.60 0.2 1 112 . 20 GLU CB C 31.16 0.2 1 113 . 20 GLU N N 120.24 0.2 1 114 . 21 LYS H H 8.93 0.02 1 115 . 21 LYS HA H 3.93 0.02 1 116 . 21 LYS C C 177.12 0.2 1 117 . 21 LYS CA C 58.04 0.2 1 118 . 21 LYS CB C 31.40 0.2 1 119 . 21 LYS N N 123.48 0.2 1 120 . 22 ASN H H 8.55 0.02 1 121 . 22 ASN HA H 4.62 0.02 1 122 . 22 ASN C C 174.22 0.2 1 123 . 22 ASN CA C 53.55 0.2 1 124 . 22 ASN CB C 37.34 0.2 1 125 . 22 ASN N N 116.99 0.2 1 126 . 23 GLY H H 7.94 0.02 1 127 . 23 GLY HA2 H 4.16 0.02 5 128 . 23 GLY HA3 H 3.98 0.02 5 129 . 23 GLY C C 173.90 0.2 1 130 . 23 GLY CA C 44.30 0.2 1 131 . 23 GLY N N 107.32 0.2 1 132 . 24 SER H H 8.03 0.02 1 133 . 24 SER HA H 4.40 0.02 1 134 . 24 SER C C 173.11 0.2 1 135 . 24 SER CA C 57.43 0.2 1 136 . 24 SER CB C 63.97 0.2 1 137 . 24 SER N N 116.01 0.2 1 138 . 25 VAL H H 7.97 0.02 1 139 . 25 VAL HA H 3.43 0.02 1 140 . 25 VAL C C 174.48 0.2 1 141 . 25 VAL CA C 61.19 0.2 1 142 . 25 VAL CB C 32.11 0.2 1 143 . 25 VAL N N 122.06 0.2 1 144 . 26 ARG H H 8.20 0.02 1 145 . 26 ARG HA H 4.35 0.02 1 146 . 26 ARG C C 174.47 0.2 1 147 . 26 ARG CA C 53.74 0.2 1 148 . 26 ARG CB C 30.21 0.2 1 149 . 26 ARG N N 127.54 0.2 1 150 . 27 TRP H H 8.58 0.02 1 151 . 27 TRP HA H 4.57 0.02 1 152 . 27 TRP C C 177.10 0.2 1 153 . 27 TRP CA C 57.03 0.2 1 154 . 27 TRP CB C 28.07 0.2 1 155 . 27 TRP N N 128.14 0.2 1 156 . 28 VAL H H 9.08 0.02 1 157 . 28 VAL HA H 4.58 0.02 1 158 . 28 VAL C C 175.84 0.2 1 159 . 28 VAL CA C 63.55 0.2 1 160 . 28 VAL CB C 34.49 0.2 1 161 . 28 VAL N N 120.69 0.2 1 162 . 29 MET H H 8.09 0.02 1 163 . 29 MET HA H 4.45 0.02 1 164 . 29 MET C C 173.36 0.2 1 165 . 29 MET CA C 56.06 0.2 1 166 . 29 MET CB C 29.26 0.2 1 167 . 29 MET N N 113.54 0.2 1 168 . 30 ASN H H 8.51 0.02 1 169 . 30 ASN HA H 5.77 0.02 1 170 . 30 ASN C C 171.78 0.2 1 171 . 30 ASN CA C 52.61 0.2 1 172 . 30 ASN CB C 42.10 0.2 1 173 . 30 ASN N N 119.40 0.2 1 174 . 31 ALA H H 9.14 0.02 1 175 . 31 ALA HA H 4.91 0.02 1 176 . 31 ALA C C 176.79 0.2 1 177 . 31 ALA CA C 50.78 0.2 1 178 . 31 ALA CB C 22.84 0.2 1 179 . 31 ALA N N 117.25 0.2 1 180 . 32 LEU H H 9.63 0.02 1 181 . 32 LEU HA H 5.22 0.02 1 182 . 32 LEU C C 176.55 0.2 1 183 . 32 LEU CA C 54.44 0.2 1 184 . 32 LEU CB C 44.95 0.2 1 185 . 32 LEU N N 120.04 0.2 1 186 . 33 GLY H H 7.89 0.02 1 187 . 33 GLY C C 174.05 0.2 1 188 . 33 GLY CA C 44.71 0.2 1 189 . 33 GLY N N 111.69 0.2 1 190 . 34 VAL H H 8.29 0.02 1 191 . 34 VAL HA H 4.21 0.02 1 192 . 34 VAL C C 174.01 0.2 1 193 . 34 VAL CA C 60.73 0.2 1 194 . 34 VAL CB C 32.35 0.2 1 195 . 34 VAL N N 124.03 0.2 1 196 . 35 LYS H H 6.76 0.02 1 197 . 35 LYS HA H 3.99 0.02 1 198 . 35 LYS C C 173.96 0.2 1 199 . 35 LYS CA C 56.86 0.2 1 200 . 35 LYS CB C 32.59 0.2 1 201 . 35 LYS N N 113.71 0.2 1 202 . 36 ASP H H 9.12 0.02 1 203 . 36 ASP HA H 4.26 0.02 1 204 . 36 ASP C C 173.02 0.2 1 205 . 36 ASP CA C 56.57 0.2 1 206 . 36 ASP CB C 38.77 0.2 1 207 . 36 ASP N N 123.46 0.2 1 208 . 37 ASP H H 8.85 0.02 1 209 . 37 ASP HA H 4.73 0.02 1 210 . 37 ASP CA C 51.18 0.2 1 211 . 37 ASP CB C 37.58 0.2 1 212 . 37 ASP N N 121.69 0.2 1 213 . 38 TRP C C 173.21 0.2 1 214 . 38 TRP CA C 54.08 0.2 1 215 . 38 TRP CB C 32.83 0.2 1 216 . 39 LEU H H 8.87 0.02 1 217 . 39 LEU HA H 4.76 0.02 1 218 . 39 LEU C C 176.05 0.2 1 219 . 39 LEU CA C 53.78 0.2 1 220 . 39 LEU CB C 45.66 0.0 1 221 . 39 LEU N N 130.92 0.2 1 222 . 40 LEU H H 9.09 0.02 1 223 . 40 LEU HA H 5.48 0.02 1 224 . 40 LEU C C 174.43 0.2 1 225 . 40 LEU CA C 52.96 0.2 1 226 . 40 LEU CB C 43.54 0.2 1 227 . 40 LEU N N 119.40 0.2 1 228 . 41 VAL H H 9.23 0.02 1 229 . 41 VAL HA H 4.40 0.02 1 230 . 41 VAL CA C 60.84 0.2 1 231 . 41 VAL CB C 33.54 0.2 1 232 . 41 VAL N N 126.69 0.2 1 233 . 42 PRO C C 174.64 0.2 1 234 . 42 PRO CA C 61.87 0.2 1 235 . 42 PRO CB C 29.26 0.2 1 236 . 43 SER H H 8.58 0.02 1 237 . 43 SER HA H 4.31 0.02 1 238 . 43 SER C C 176.85 0.2 1 239 . 43 SER CA C 60.55 0.2 1 240 . 43 SER CB C 63.02 0.2 1 241 . 43 SER N N 125.56 0.2 1 242 . 44 HIS H H 9.26 0.02 1 243 . 44 HIS HA H 4.54 0.02 1 244 . 44 HIS C C 174.09 0.2 1 245 . 44 HIS CA C 57.73 0.2 1 246 . 44 HIS CB C 26.01 0.2 1 247 . 44 HIS N N 119.98 0.2 1 248 . 45 ALA H H 7.61 0.02 1 249 . 45 ALA HA H 4.02 0.02 1 250 . 45 ALA C C 176.33 0.2 1 251 . 45 ALA CA C 54.22 0.2 1 252 . 45 ALA CB C 19.26 0.2 1 253 . 45 ALA N N 122.11 0.2 1 254 . 46 TYR H H 6.76 0.02 1 255 . 46 TYR HA H 5.01 0.02 1 256 . 46 TYR C C 176.27 0.2 1 257 . 46 TYR CA C 56.63 0.2 1 258 . 46 TYR CB C 41.35 0.2 1 259 . 46 TYR N N 108.20 0.2 1 260 . 47 LYS H H 7.06 0.02 1 261 . 47 LYS HA H 3.93 0.02 1 262 . 47 LYS C C 175.70 0.2 1 263 . 47 LYS CA C 57.27 0.2 1 264 . 47 LYS CB C 31.16 0.2 1 265 . 47 LYS N N 120.22 0.2 1 266 . 48 PHE H H 8.61 0.02 1 267 . 48 PHE HA H 4.63 0.02 1 268 . 48 PHE C C 175.66 0.2 1 269 . 48 PHE CA C 56.97 0.2 1 270 . 48 PHE CB C 37.34 0.2 1 271 . 48 PHE N N 115.75 0.2 1 272 . 49 GLU H H 7.46 0.02 1 273 . 49 GLU HA H 4.54 0.02 1 274 . 49 GLU C C 176.89 0.2 1 275 . 49 GLU CA C 54.14 0.2 1 276 . 49 GLU CB C 28.86 0.2 1 277 . 49 GLU N N 119.23 0.2 1 278 . 50 LYS H H 8.79 0.02 1 279 . 50 LYS HA H 4.16 0.02 1 280 . 50 LYS C C 176.79 0.2 1 281 . 50 LYS CA C 57.03 0.2 1 282 . 50 LYS CB C 31.64 0.2 1 283 . 50 LYS N N 124.78 0.2 1 284 . 51 ASP H H 8.95 0.02 1 285 . 51 ASP HA H 4.44 0.02 1 286 . 51 ASP C C 177.85 0.2 1 287 . 51 ASP CA C 54.68 0.2 1 288 . 51 ASP CB C 38.77 0.2 1 289 . 51 ASP N N 119.64 0.2 1 290 . 52 TYR H H 7.53 0.02 1 291 . 52 TYR HA H 4.39 0.02 1 292 . 52 TYR C C 176.81 0.2 1 293 . 52 TYR CA C 60.04 0.2 1 294 . 52 TYR CB C 37.34 0.2 1 295 . 52 TYR N N 117.69 0.2 1 296 . 53 GLU H H 8.42 0.02 1 297 . 53 GLU HA H 4.73 0.02 1 298 . 53 GLU C C 176.99 0.2 1 299 . 53 GLU CA C 58.19 0.2 1 300 . 53 GLU CB C 27.36 0.2 1 301 . 53 GLU N N 118.42 0.2 1 302 . 54 MET H H 7.69 0.02 1 303 . 54 MET HA H 4.49 0.02 1 304 . 54 MET C C 173.52 0.2 1 305 . 54 MET CA C 54.34 0.2 1 306 . 54 MET CB C 31.88 0.2 1 307 . 54 MET N N 115.54 0.2 1 308 . 55 MET CA C 54.34 0.2 1 309 . 55 MET CB C 33.54 0.2 1 310 . 55 MET N N 114.76 0.2 1 311 . 55 MET H H 7.23 0.02 1 312 . 56 GLU C C 174.58 0.2 1 313 . 56 GLU CA C 55.81 0.2 1 314 . 57 PHE H H 9.33 0.02 1 315 . 57 PHE HA H 5.95 0.02 1 316 . 57 PHE C C 173.73 0.2 1 317 . 57 PHE CA C 55.15 0.2 1 318 . 57 PHE CB C 42.34 0.2 1 319 . 57 PHE N N 115.88 0.2 1 320 . 58 TYR H H 8.56 0.02 1 321 . 58 TYR HA H 5.34 0.02 1 322 . 58 TYR C C 175.03 0.2 1 323 . 58 TYR CA C 55.81 0.2 1 324 . 58 TYR N N 123.10 0.2 1 325 . 59 PHE H H 9.24 0.02 1 326 . 59 PHE HA H 5.42 0.02 1 327 . 59 PHE C C 175.68 0.2 1 328 . 59 PHE CA C 55.15 0.2 1 329 . 59 PHE CB C 42.10 0.2 1 330 . 59 PHE N N 123.87 0.2 1 331 . 60 ASN H H 9.03 0.02 1 332 . 60 ASN HA H 5.42 0.02 1 333 . 60 ASN C C 175.56 0.2 1 334 . 60 ASN CA C 51.45 0.2 1 335 . 60 ASN CB C 38.53 0.2 1 336 . 60 ASN N N 120.99 0.2 1 337 . 61 ARG H H 9.02 0.02 1 338 . 61 ARG HA H 5.05 0.02 1 339 . 61 ARG C C 176.41 0.2 1 340 . 61 ARG CA C 53.99 0.2 1 341 . 61 ARG CB C 31.40 0.2 1 342 . 61 ARG N N 127.30 0.2 1 343 . 62 GLY H H 9.14 0.02 1 344 . 62 GLY HA2 H 4.07 0.02 1 345 . 62 GLY HA3 H 4.07 0.2 1 346 . 62 GLY C C 174.96 0.2 1 347 . 62 GLY CA C 46.79 0.2 1 348 . 62 GLY N N 116.34 0.2 1 349 . 63 GLY H H 8.38 0.02 1 350 . 63 GLY HA2 H 3.65 0.02 1 351 . 63 GLY HA3 H 4.35 0.02 1 352 . 63 GLY C C 173.87 0.2 1 353 . 63 GLY CA C 44.71 0.2 1 354 . 63 GLY N N 107.79 0.2 1 355 . 64 THR H H 7.41 0.02 1 356 . 64 THR HA H 4.21 0.02 1 357 . 64 THR C C 171.93 0.2 1 358 . 64 THR CA C 61.40 0.2 1 359 . 64 THR CB C 69.91 0.2 1 360 . 64 THR N N 117.52 0.2 1 361 . 65 TYR H H 8.37 0.02 1 362 . 65 TYR HA H 5.18 0.02 1 363 . 65 TYR C C 175.35 0.2 1 364 . 65 TYR CA C 53.98 0.2 1 365 . 65 TYR CB C 37.58 0.2 1 366 . 65 TYR N N 124.07 0.2 1 367 . 66 TYR H H 9.44 0.02 1 368 . 66 TYR HA H 4.77 0.02 1 369 . 66 TYR C C 174.53 0.2 1 370 . 66 TYR CA C 57.17 0.2 1 371 . 66 TYR CB C 40.67 0.2 1 372 . 66 TYR N N 122.77 0.2 1 373 . 67 SER H H 8.79 0.02 1 374 . 67 SER HA H 5.71 0.02 1 375 . 67 SER C C 173.60 0.2 1 376 . 67 SER CA C 55.89 0.2 1 377 . 67 SER CB C 66.79 0.2 1 378 . 67 SER N N 116.00 0.2 1 379 . 68 ILE H H 8.86 0.02 1 380 . 68 ILE HA H 4.44 0.02 1 381 . 68 ILE C C 172.12 0.2 1 382 . 68 ILE CA C 59.52 0.2 1 383 . 68 ILE CB C 41.15 0.2 1 384 . 68 ILE N N 120.73 0.2 1 385 . 69 SER H H 8.33 0.02 1 386 . 69 SER HA H 4.58 0.02 1 387 . 69 SER C C 176.23 0.2 1 388 . 69 SER CA C 58.31 0.2 1 389 . 69 SER CB C 63.02 0.2 1 390 . 69 SER N N 121.04 0.2 1 391 . 70 ALA H H 8.26 0.02 1 392 . 70 ALA C C 178.98 0.2 1 393 . 70 ALA CA C 54.60 0.2 1 394 . 70 ALA CB C 18.33 0.2 1 395 . 70 ALA N N 128.67 0.2 1 396 . 71 GLY H H 7.94 0.02 1 397 . 71 GLY HA2 H 3.75 0.02 1 398 . 71 GLY HA3 H 4.15 0.02 1 399 . 71 GLY C C 174.49 0.2 1 400 . 71 GLY CA C 45.35 0.2 1 401 . 71 GLY N N 101.48 0.2 1 402 . 72 ASN H H 7.87 0.02 1 403 . 72 ASN HA H 5.02 0.02 1 404 . 72 ASN C C 174.60 0.2 1 405 . 72 ASN CA C 52.30 0.2 1 406 . 72 ASN CB C 39.25 0.2 1 407 . 72 ASN N N 116.55 0.2 1 408 . 73 VAL H H 6.97 0.02 1 409 . 73 VAL HA H 4.59 0.02 1 410 . 73 VAL C C 175.03 0.2 1 411 . 73 VAL CA C 60.36 0.2 1 412 . 73 VAL CB C 32.35 0.2 1 413 . 73 VAL N N 114.03 0.2 1 414 . 74 VAL H H 7.90 0.02 1 415 . 74 VAL HA H 4.26 0.02 1 416 . 74 VAL C C 174.32 0.2 1 417 . 74 VAL CA C 62.14 0.2 1 418 . 74 VAL CB C 32.35 0.2 1 419 . 74 VAL N N 124.58 0.2 1 420 . 75 ILE H H 8.47 0.02 1 421 . 75 ILE HA H 5.34 0.02 1 422 . 75 ILE C C 176.51 0.2 1 423 . 75 ILE CA C 58.80 0.2 1 424 . 75 ILE CB C 39.48 0.2 1 425 . 75 ILE N N 126.38 0.2 1 426 . 76 GLN H H 9.86 0.02 1 427 . 76 GLN HA H 4.96 0.02 1 428 . 76 GLN C C 174.38 0.2 1 429 . 76 GLN CA C 53.42 0.2 1 430 . 76 GLN CB C 31.64 0.2 1 431 . 76 GLN N N 127.72 0.2 1 432 . 77 SER H H 8.64 0.02 1 433 . 77 SER HA H 4.79 0.02 1 434 . 77 SER C C 175.15 0.2 1 435 . 77 SER CA C 57.77 0.2 1 436 . 77 SER CB C 64.21 0.2 1 437 . 77 SER N N 119.41 0.2 1 438 . 78 LEU H H 9.56 0.02 1 439 . 78 LEU HA H 4.02 0.02 1 440 . 78 LEU C C 176.06 0.2 1 441 . 78 LEU CA C 55.93 0.2 1 442 . 78 LEU CB C 41.86 0.2 1 443 . 78 LEU N N 121.98 0.2 1 444 . 79 ASP H H 7.60 0.02 1 445 . 79 ASP HA H 4.54 0.02 1 446 . 79 ASP C C 174.77 0.2 1 447 . 79 ASP CA C 51.52 0.2 1 448 . 79 ASP CB C 42.34 0.2 1 449 . 79 ASP N N 112.82 0.2 1 450 . 80 VAL H H 8.92 0.02 1 451 . 80 VAL HA H 4.07 0.02 1 452 . 80 VAL C C 176.87 0.2 1 453 . 80 VAL CA C 62.50 0.2 1 454 . 80 VAL CB C 31.88 0.2 1 455 . 80 VAL N N 118.48 0.2 1 456 . 81 GLY H H 8.37 0.02 1 457 . 81 GLY HA2 H 3.84 0.02 1 458 . 81 GLY HA3 H 4.11 0.2 1 459 . 81 GLY C C 173.43 0.2 1 460 . 81 GLY CA C 43.86 0.2 1 461 . 81 GLY N N 111.59 0.2 1 462 . 82 PHE H H 8.61 0.02 1 463 . 82 PHE HA H 4.68 0.02 1 464 . 82 PHE C C 175.00 0.2 1 465 . 82 PHE CA C 58.50 0.2 1 466 . 82 PHE CB C 39.01 0.2 1 467 . 82 PHE N N 121.47 0.2 1 468 . 83 GLN H H 7.86 0.02 1 469 . 83 GLN C C 176.48 0.2 1 470 . 83 GLN CA C 52.96 0.2 1 471 . 83 GLN CB C 27.84 0.2 1 472 . 83 GLN N N 122.38 0.2 1 473 . 84 ASP H H 8.86 0.02 1 474 . 84 ASP C C 178.20 0.2 1 475 . 84 ASP CA C 54.69 0.2 1 476 . 84 ASP CB C 41.62 0.2 1 477 . 84 ASP N N 119.57 0.2 1 478 . 85 VAL H H 8.42 0.02 1 479 . 85 VAL HA H 4.64 0.02 1 480 . 85 VAL CA C 58.25 0.2 1 481 . 85 VAL CB C 35.20 0.2 1 482 . 85 VAL N N 118.89 0.2 1 483 . 86 VAL H H 8.79 0.02 1 484 . 86 VAL HA H 5.30 0.02 1 485 . 86 VAL C C 177.20 0.2 1 486 . 86 VAL CA C 61.80 0.2 1 487 . 86 VAL CB C 37.82 0.2 1 488 . 86 VAL N N 119.80 0.2 1 489 . 87 LEU H H 8.33 0.02 1 490 . 87 LEU CA C 56.01 0.2 1 491 . 87 LEU CB C 43.05 0.2 1 492 . 87 LEU N N 121.51 0.2 1 493 . 88 MET H H 8.39 0.02 1 494 . 88 MET HA H 5.01 0.02 1 495 . 88 MET C C 174.18 0.2 1 496 . 88 MET CA C 55.86 0.2 1 497 . 88 MET CB C 32.35 0.2 1 498 . 88 MET N N 129.00 0.2 1 499 . 89 LYS H H 8.69 0.02 1 500 . 89 LYS HA H 4.24 0.02 1 501 . 89 LYS C C 176.34 0.2 1 502 . 89 LYS CA C 54.03 0.2 1 503 . 89 LYS CB C 30.69 0.2 1 504 . 89 LYS N N 120.35 0.2 1 505 . 90 VAL H H 8.54 0.02 1 506 . 90 VAL HA H 4.34 0.02 1 507 . 90 VAL CA C 58.60 0.2 1 508 . 90 VAL CB C 29.02 0.2 1 509 . 90 VAL N N 126.73 0.2 1 510 . 91 PRO C C 177.50 0.2 1 511 . 91 PRO CA C 64.04 0.2 1 512 . 91 PRO CB C 31.63 0.2 1 513 . 92 THR H H 6.88 0.02 1 514 . 92 THR HA H 4.16 0.02 1 515 . 92 THR C C 174.37 0.2 1 516 . 92 THR CA C 60.80 0.2 1 517 . 92 THR CB C 68.72 0.2 1 518 . 92 THR N N 104.56 0.2 1 519 . 93 ILE H H 7.45 0.02 1 520 . 93 ILE HA H 3.74 0.02 1 521 . 93 ILE C C 172.42 0.2 1 522 . 93 ILE CA C 57.74 0.2 1 523 . 93 ILE CB C 40.43 0.2 1 524 . 93 ILE N N 123.81 0.2 1 525 . 94 PRO C C 176.67 0.2 1 526 . 94 PRO CA C 62.41 0.2 1 527 . 94 PRO CB C 30.45 0.2 1 528 . 95 LYS H H 7.77 0.02 1 529 . 95 LYS HA H 4.45 0.02 1 530 . 95 LYS C C 178.20 0.2 1 531 . 95 LYS CA C 56.77 0.2 1 532 . 95 LYS CB C 33.06 0.2 1 533 . 95 LYS N N 120.17 0.2 1 534 . 96 PHE H H 9.58 0.02 1 535 . 96 PHE HA H 4.48 0.02 1 536 . 96 PHE C C 176.41 0.2 1 537 . 96 PHE CA C 57.33 0.2 1 538 . 96 PHE CB C 39.72 0.2 1 539 . 96 PHE N N 121.72 0.2 1 540 . 97 ARG H H 8.76 0.02 1 541 . 97 ARG HA H 4.15 0.02 1 542 . 97 ARG C C 175.74 0.2 1 543 . 97 ARG CA C 55.96 0.2 1 544 . 97 ARG CB C 29.74 0.2 1 545 . 97 ARG N N 123.50 0.2 1 546 . 98 ASP H H 8.56 0.02 1 547 . 98 ASP HA H 4.74 0.02 1 548 . 98 ASP C C 178.47 0.2 1 549 . 98 ASP CA C 53.22 0.2 1 550 . 98 ASP CB C 39.48 0.2 1 551 . 98 ASP N N 123.16 0.2 1 552 . 99 ILE H H 8.93 0.02 1 553 . 99 ILE HA H 4.61 0.02 1 554 . 99 ILE C C 178.12 0.2 1 555 . 99 ILE CA C 60.88 0.2 1 556 . 99 ILE CB C 38.77 0.2 1 557 . 99 ILE N N 121.81 0.2 1 558 . 100 THR H H 9.00 0.02 1 559 . 100 THR HA H 3.32 0.02 1 560 . 100 THR C C 176.95 0.2 1 561 . 100 THR CA C 65.22 0.2 1 562 . 100 THR CB C 68.96 0.2 1 563 . 100 THR N N 117.06 0.2 1 564 . 101 GLN H H 8.44 0.02 1 565 . 101 GLN HA H 4.20 0.02 1 566 . 101 GLN C C 176.50 0.2 1 567 . 101 GLN CA C 56.24 0.2 1 568 . 101 GLN CB C 26.65 0.2 1 569 . 101 GLN N N 116.21 0.2 1 570 . 102 HIS H H 8.19 0.02 1 571 . 102 HIS HA H 4.65 0.02 1 572 . 102 HIS C C 174.17 0.2 1 573 . 102 HIS CA C 55.35 0.2 1 574 . 102 HIS CB C 27.84 0.2 1 575 . 102 HIS N N 113.75 0.2 1 576 . 103 PHE H H 7.72 0.02 1 577 . 103 PHE HA H 4.70 0.02 1 578 . 103 PHE C C 176.17 0.2 1 579 . 103 PHE CA C 53.94 0.2 1 580 . 103 PHE CB C 39.01 0.2 1 581 . 103 PHE N N 119.89 0.2 1 582 . 104 ILE H H 9.00 0.02 1 583 . 104 ILE HA H 4.45 0.02 1 584 . 104 ILE CA C 58.55 0.2 1 585 . 104 ILE CB C 42.34 0.2 1 586 . 104 ILE N N 124.69 0.2 1 587 . 105 LYS H H 8.40 0.02 1 588 . 105 LYS HA H 4.40 0.02 1 589 . 105 LYS C C 179.38 0.2 1 590 . 105 LYS CA C 55.86 0.2 1 591 . 105 LYS CB C 32.11 0.2 1 592 . 105 LYS N N 124.95 0.2 1 593 . 106 LYS H H 10.30 0.02 1 594 . 106 LYS HA H 4.63 0.02 1 595 . 106 LYS C C 179.86 0.2 1 596 . 106 LYS CA C 60.07 0.2 1 597 . 106 LYS CB C 31.16 0.2 1 598 . 106 LYS N N 126.23 0.2 1 599 . 107 GLY H H 9.37 0.02 1 600 . 107 GLY HA2 H 3.86 0.02 1 601 . 107 GLY HA3 H 3.70 0.02 1 602 . 107 GLY C C 174.38 0.2 1 603 . 107 GLY CA C 45.48 0.2 1 604 . 107 GLY N N 104.66 0.2 1 605 . 108 ASP H H 8.04 0.02 1 606 . 108 ASP HA H 5.05 0.02 1 607 . 108 ASP C C 177.03 0.2 1 608 . 108 ASP CA C 54.00 0.2 1 609 . 108 ASP CB C 41.86 0.2 1 610 . 108 ASP N N 117.21 0.2 1 611 . 109 VAL H H 7.40 0.02 1 612 . 109 VAL HA H 3.93 0.02 1 613 . 109 VAL C C 174.65 0.2 1 614 . 109 VAL CA C 68.66 0.2 1 615 . 109 VAL CB C 29.97 0.2 1 616 . 109 VAL N N 122.93 0.2 1 617 . 110 PRO C C 178.47 0.2 1 618 . 110 PRO CA C 65.11 0.2 1 619 . 110 PRO CB C 30.69 0.2 1 620 . 111 ARG H H 8.06 0.02 1 621 . 111 ARG HA H 4.25 0.02 1 622 . 111 ARG C C 176.36 0.2 1 623 . 111 ARG CA C 57.03 0.2 1 624 . 111 ARG CB C 29.70 0.2 1 625 . 111 ARG N N 113.50 0.2 1 626 . 112 ALA H H 7.99 0.02 1 627 . 112 ALA HA H 4.44 0.02 1 628 . 112 ALA C C 177.87 0.2 1 629 . 112 ALA CA C 51.14 0.2 1 630 . 112 ALA CB C 20.94 0.2 1 631 . 112 ALA N N 119.59 0.2 1 632 . 113 LEU H H 7.04 0.02 1 633 . 113 LEU HA H 4.10 0.02 1 634 . 113 LEU C C 176.73 0.2 1 635 . 113 LEU CA C 55.30 0.2 1 636 . 113 LEU CB C 42.34 0.2 1 637 . 113 LEU N N 118.07 0.2 1 638 . 114 ASN H H 9.81 0.02 1 639 . 114 ASN HA H 4.34 0.02 1 640 . 114 ASN C C 173.31 0.2 1 641 . 114 ASN CA C 54.53 0.2 1 642 . 114 ASN CB C 37.11 0.2 1 643 . 114 ASN N N 115.47 0.2 1 644 . 115 ARG H H 7.34 0.02 1 645 . 115 ARG HA H 4.82 0.02 1 646 . 115 ARG C C 176.05 0.2 1 647 . 115 ARG CA C 52.54 0.2 1 648 . 115 ARG CB C 31.64 0.2 1 649 . 115 ARG N N 115.47 0.2 1 650 . 116 LEU H H 8.44 0.02 1 651 . 116 LEU HA H 4.68 0.02 1 652 . 116 LEU C C 177.39 0.2 1 653 . 116 LEU CA C 55.10 0.2 1 654 . 116 LEU CB C 40.43 0.2 1 655 . 116 LEU N N 120.24 0.2 1 656 . 117 ALA H H 7.36 0.02 1 657 . 117 ALA HA H 4.81 0.02 1 658 . 117 ALA C C 174.32 0.2 1 659 . 117 ALA CA C 51.32 0.2 1 660 . 117 ALA CB C 23.79 0.2 1 661 . 117 ALA N N 121.57 0.2 1 662 . 118 THR H H 8.72 0.02 1 663 . 118 THR HA H 4.82 0.02 1 664 . 118 THR C C 172.42 0.2 1 665 . 118 THR CA C 61.12 0.2 1 666 . 118 THR CB C 71.34 0.2 1 667 . 118 THR N N 116.06 0.2 1 668 . 119 LEU H H 9.79 0.02 1 669 . 119 LEU HA H 4.63 0.02 1 670 . 119 LEU C C 173.76 0.2 1 671 . 119 LEU CA C 53.79 0.2 1 672 . 119 LEU CB C 40.43 0.2 1 673 . 119 LEU N N 130.89 0.2 1 674 . 120 VAL H H 9.23 0.02 1 675 . 120 VAL HA H 4.35 0.02 1 676 . 120 VAL C C 174.15 0.2 1 677 . 120 VAL CA C 61.06 0.2 1 678 . 120 VAL CB C 30.69 0.2 1 679 . 120 VAL N N 129.52 0.2 1 680 . 121 THR H H 8.09 0.02 1 681 . 121 THR HA H 4.87 0.02 1 682 . 121 THR C C 173.16 0.2 1 683 . 121 THR CA C 58.31 0.2 1 684 . 121 THR CB C 69.96 0.2 1 685 . 121 THR N N 118.15 0.2 1 686 . 122 THR H H 8.64 0.02 1 687 . 122 THR HA H 5.28 0.02 1 688 . 122 THR C C 173.19 0.2 1 689 . 122 THR CA C 60.63 0.2 1 690 . 122 THR CB C 71.10 0.2 1 691 . 122 THR N N 115.56 0.2 1 692 . 123 VAL H H 7.95 0.02 1 693 . 123 VAL HA H 5.10 0.02 1 694 . 123 VAL C C 176.36 0.2 1 695 . 123 VAL CA C 61.74 0.2 1 696 . 123 VAL CB C 32.83 0.2 1 697 . 123 VAL N N 117.81 0.2 1 698 . 124 ASN H H 9.67 0.02 1 699 . 124 ASN HA H 4.26 0.02 1 700 . 124 ASN C C 175.16 0.2 1 701 . 124 ASN CA C 53.67 0.2 1 702 . 124 ASN CB C 36.88 0.2 1 703 . 124 ASN N N 127.05 0.2 1 704 . 125 GLY H H 8.15 0.02 1 705 . 125 GLY HA2 H 3.32 0.02 1 706 . 125 GLY HA3 H 4.26 0.02 1 707 . 125 GLY C C 174.40 0.2 1 708 . 125 GLY CA C 44.65 0.2 1 709 . 125 GLY N N 102.87 0.2 1 710 . 126 THR H H 8.00 0.02 1 711 . 126 THR HA H 4.58 0.02 1 712 . 126 THR C C 172.19 0.02 1 713 . 126 THR CA C 60.23 0.2 1 714 . 126 THR CB C 69.44 0.2 1 715 . 126 THR N N 120.71 0.2 1 716 . 127 PRO C C 176.00 0.2 1 717 . 127 PRO CA C 62.77 0.2 1 718 . 127 PRO CB C 31.40 0.2 1 719 . 128 MET H H 8.32 0.02 1 720 . 128 MET HA H 4.73 0.02 1 721 . 128 MET C C 176.52 0.2 1 722 . 128 MET CA C 54.64 0.2 1 723 . 128 MET CB C 36.63 0.2 1 724 . 128 MET N N 119.73 0.2 1 725 . 129 LEU H H 9.62 0.02 1 726 . 129 LEU C C 175.40 0.2 1 727 . 129 LEU CA C 55.00 0.2 1 728 . 129 LEU CB C 43.76 0.2 1 729 . 129 LEU N N 113.79 0.2 1 730 . 130 ILE H H 8.83 0.02 1 731 . 130 ILE HA H 5.05 0.02 1 732 . 130 ILE C C 175.22 0.2 1 733 . 130 ILE CA C 58.25 0.2 1 734 . 130 ILE CB C 39.24 0.2 1 735 . 130 ILE N N 123.25 0.2 1 736 . 131 SER H H 8.97 0.02 1 737 . 131 SER HA H 4.40 0.02 1 738 . 131 SER C C 174.14 0.2 1 739 . 131 SER CA C 58.91 0.2 1 740 . 131 SER CB C 63.02 0.2 1 741 . 131 SER N N 124.47 0.2 1 742 . 132 GLU H H 8.44 0.02 1 743 . 132 GLU HA H 4.91 0.02 1 744 . 132 GLU C C 177.06 0.2 1 745 . 132 GLU CA C 55.63 0.2 1 746 . 132 GLU CB C 28.31 0.2 1 747 . 132 GLU N N 123.44 0.2 1 748 . 133 GLY H H 8.32 0.02 1 749 . 133 GLY HA2 H 3.98 0.02 1 750 . 133 GLY HA3 H 4.26 0.2 1 751 . 133 GLY CA C 44.80 0.2 1 752 . 133 GLY N N 107.36 0.2 1 753 . 134 PRO C C 179.80 0.2 1 754 . 134 PRO CA C 61.56 0.2 1 755 . 134 PRO CB C 30.45 0.2 1 756 . 135 LEU H H 7.51 0.02 1 757 . 135 LEU HA H 4.58 0.02 1 758 . 135 LEU C C 173.42 0.2 1 759 . 135 LEU CA C 55.67 0.2 1 760 . 135 LEU CB C 44.00 0.2 1 761 . 135 LEU N N 123.49 0.2 1 762 . 136 LYS H H 8.47 0.02 1 763 . 136 LYS HA H 4.82 0.02 1 764 . 136 LYS C C 174.72 0.2 1 765 . 136 LYS CA C 53.93 0.2 1 766 . 136 LYS CB C 35.20 0.2 1 767 . 136 LYS N N 119.02 0.2 1 768 . 137 MET H H 8.57 0.02 1 769 . 137 MET HA H 5.01 0.02 1 770 . 137 MET C C 174.89 0.2 1 771 . 137 MET CA C 53.83 0.2 1 772 . 137 MET CB C 33.06 0.2 1 773 . 137 MET N N 121.06 0.2 1 774 . 138 GLU H H 9.16 0.02 1 775 . 138 GLU HA H 4.68 0.02 1 776 . 138 GLU C C 176.44 0.2 1 777 . 138 GLU CA C 53.52 0.2 1 778 . 138 GLU CB C 29.97 0.2 1 779 . 138 GLU N N 126.50 0.2 1 780 . 139 GLU H H 8.83 0.02 1 781 . 139 GLU HA H 3.90 0.02 1 782 . 139 GLU C C 178.36 0.2 1 783 . 139 GLU CA C 59.25 0.2 1 784 . 139 GLU CB C 28.79 0.2 1 785 . 139 GLU N N 124.60 0.2 1 786 . 140 LYS H H 7.90 0.02 1 787 . 140 LYS HA H 4.07 0.02 1 788 . 140 LYS C C 174.82 0.2 1 789 . 140 LYS CA C 54.64 0.2 1 790 . 140 LYS CB C 35.20 0.2 1 791 . 140 LYS N N 117.41 0.2 1 792 . 141 ALA H H 8.78 0.02 1 793 . 141 ALA HA H 4.74 0.02 1 794 . 141 ALA C C 175.18 0.2 1 795 . 141 ALA CA C 50.64 0.2 1 796 . 141 ALA CB C 21.89 0.2 1 797 . 141 ALA N N 124.36 0.2 1 798 . 142 THR H H 8.45 0.02 1 799 . 142 THR HA H 5.68 0.02 1 800 . 142 THR C C 173.73 0.2 1 801 . 142 THR CA C 60.02 0.2 1 802 . 142 THR CB C 70.62 0.2 1 803 . 142 THR N N 116.93 0.2 1 804 . 143 TYR H H 8.98 0.02 1 805 . 143 TYR HA H 4.83 0.02 1 806 . 143 TYR C C 172.83 0.2 1 807 . 143 TYR CA C 54.80 0.2 1 808 . 143 TYR CB C 38.55 0.2 1 809 . 143 TYR N N 124.79 0.2 1 810 . 144 VAL H H 8.22 0.02 1 811 . 144 VAL HA H 4.81 0.02 1 812 . 144 VAL C C 175.64 0.2 1 813 . 144 VAL CA C 60.64 0.2 1 814 . 144 VAL CB C 33.54 0.2 1 815 . 144 VAL N N 116.39 0.2 1 816 . 145 HIS H H 8.86 0.02 1 817 . 145 HIS HA H 5.06 0.02 1 818 . 145 HIS C C 172.67 0.2 1 819 . 145 HIS CA C 54.76 0.2 1 820 . 145 HIS CB C 32.35 0.2 1 821 . 145 HIS N N 124.28 0.2 1 822 . 146 LYS H H 7.89 0.02 1 823 . 146 LYS HA H 4.17 0.02 1 824 . 146 LYS C C 175.44 0.2 1 825 . 146 LYS CA C 54.87 0.2 1 826 . 146 LYS CB C 32.11 0.2 1 827 . 146 LYS N N 128.13 0.2 1 828 . 147 LYS H H 8.65 0.02 1 829 . 147 LYS HA H 4.22 0.02 1 830 . 147 LYS C C 178.28 0.2 1 831 . 147 LYS CA C 55.84 0.2 1 832 . 147 LYS CB C 32.35 0.2 1 833 . 147 LYS N N 123.99 0.2 1 834 . 148 ASN H H 9.73 0.02 1 835 . 148 ASN C C 176.11 0.2 1 836 . 148 ASN CA C 55.50 0.2 1 837 . 148 ASN CB C 37.11 0.2 1 838 . 148 ASN N N 121.00 0.2 1 839 . 149 ASP H H 7.93 0.02 1 840 . 149 ASP HA H 4.54 0.02 1 841 . 149 ASP C C 177.19 0.2 1 842 . 149 ASP CA C 52.83 0.2 1 843 . 149 ASP CB C 39.48 0.2 1 844 . 149 ASP N N 116.40 0.2 1 845 . 150 GLY H H 8.03 0.02 1 846 . 150 GLY HA2 H 4.17 0.02 1 847 . 150 GLY HA3 H 4.35 0.02 1 848 . 150 GLY C C 174.66 0.2 1 849 . 150 GLY CA C 44.90 0.2 1 850 . 150 GLY N N 107.77 0.2 1 851 . 151 THR H H 8.08 0.02 1 852 . 151 THR HA H 4.46 0.02 1 853 . 151 THR C C 173.52 0.2 1 854 . 151 THR CA C 61.66 0.2 1 855 . 151 THR CB C 70.15 0.2 1 856 . 151 THR N N 113.90 0.2 1 857 . 152 THR H H 8.19 0.02 1 858 . 152 THR HA H 5.19 0.02 1 859 . 152 THR C C 174.50 0.2 1 860 . 152 THR CA C 59.87 0.2 1 861 . 152 THR CB C 71.10 0.2 1 862 . 152 THR N N 110.00 0.2 1 863 . 153 VAL H H 8.67 0.02 1 864 . 153 VAL HA H 4.27 0.02 1 865 . 153 VAL C C 173.09 0.2 1 866 . 153 VAL CA C 59.47 0.2 1 867 . 153 VAL CB C 34.02 0.2 1 868 . 153 VAL N N 119.60 0.2 1 869 . 154 ASP H H 8.22 0.02 1 870 . 154 ASP HA H 4.81 0.02 1 871 . 154 ASP C C 174.91 0.2 1 872 . 154 ASP CA C 53.13 0.2 1 873 . 154 ASP CB C 40.43 0.2 1 874 . 154 ASP N N 124.61 0.2 1 875 . 155 LEU H H 8.94 0.02 1 876 . 155 LEU HA H 4.30 0.02 1 877 . 155 LEU C C 174.49 0.2 1 878 . 155 LEU CA C 53.22 0.2 1 879 . 155 LEU CB C 41.86 0.2 1 880 . 155 LEU N N 125.58 0.2 1 881 . 156 THR H H 7.84 0.02 1 882 . 156 THR HA H 5.48 0.02 1 883 . 156 THR C C 173.90 0.2 1 884 . 156 THR CA C 60.63 0.2 1 885 . 156 THR CB C 71.10 0.2 1 886 . 156 THR N N 116.06 0.2 1 887 . 157 VAL H H 8.68 0.02 1 888 . 157 VAL HA H 4.99 0.02 1 889 . 157 VAL C C 173.80 0.2 1 890 . 157 VAL CA C 57.94 0.2 1 891 . 157 VAL CB C 34.49 0.2 1 892 . 157 VAL N N 117.11 0.2 1 893 . 158 ASP H H 9.14 0.02 1 894 . 158 ASP HA H 4.49 0.02 1 895 . 158 ASP C C 175.63 0.2 1 896 . 158 ASP CA C 53.47 0.2 1 897 . 158 ASP CB C 42.34 0.2 1 898 . 158 ASP N N 120.95 0.2 1 899 . 159 GLN H H 8.20 0.02 1 900 . 159 GLN HA H 3.74 0.02 1 901 . 159 GLN C C 172.51 0.2 1 902 . 159 GLN CA C 57.40 0.2 1 903 . 159 GLN CB C 26.17 0.2 1 904 . 159 GLN N N 112.03 0.2 1 905 . 160 ALA H H 8.33 0.02 1 906 . 160 ALA HA H 4.93 0.02 1 907 . 160 ALA C C 175.18 0.2 1 908 . 160 ALA CA C 49.44 0.2 1 909 . 160 ALA CB C 21.42 0.2 1 910 . 160 ALA N N 126.85 0.2 1 911 . 161 TRP H H 9.23 0.02 1 912 . 161 TRP HA H 5.20 0.02 1 913 . 161 TRP C C 176.03 0.2 1 914 . 161 TRP CA C 55.17 0.2 1 915 . 161 TRP CB C 31.16 0.2 1 916 . 161 TRP N N 123.75 0.2 1 917 . 162 ARG H H 9.29 0.02 1 918 . 162 ARG HA H 5.38 0.02 1 919 . 162 ARG C C 175.25 0.2 1 920 . 162 ARG CA C 54.45 0.2 1 921 . 162 ARG CB C 33.06 0.2 1 922 . 162 ARG N N 122.19 0.2 1 923 . 163 GLY H H 9.03 0.02 1 924 . 163 GLY C C 172.31 0.2 1 925 . 163 GLY CA C 43.16 0.2 1 926 . 163 GLY N N 114.21 0.2 1 927 . 164 LYS H H 8.81 0.02 1 928 . 164 LYS HA H 5.02 0.02 1 929 . 164 LYS C C 175.58 0.2 1 930 . 164 LYS CA C 55.14 0.2 1 931 . 164 LYS CB C 34.02 0.2 1 932 . 164 LYS N N 122.56 0.2 1 933 . 165 GLY H H 7.72 0.02 1 934 . 165 GLY HA2 H 3.93 0.02 1 935 . 165 GLY HA3 H 4.17 0.02 1 936 . 165 GLY C C 170.69 0.2 1 937 . 165 GLY CA C 44.18 0.2 1 938 . 165 GLY N N 110.46 0.2 1 939 . 166 GLU H H 8.19 0.02 1 940 . 166 GLU HA H 4.51 0.02 1 941 . 166 GLU C C 175.23 0.2 1 942 . 166 GLU CA C 54.33 0.2 1 943 . 166 GLU CB C 29.26 0.2 1 944 . 166 GLU N N 117.87 0.2 1 945 . 167 GLY H H 8.54 0.02 1 946 . 167 GLY HA2 H 4.41 0.02 1 947 . 167 GLY C C 172.78 0.2 1 948 . 167 GLY CA C 44.00 0.2 1 949 . 167 GLY N N 110.18 0.2 1 950 . 168 LEU H H 7.67 0.02 1 951 . 168 LEU HA H 4.28 0.02 1 952 . 168 LEU CA C 51.73 0.2 1 953 . 168 LEU CB C 43.52 0.2 1 954 . 168 LEU N N 120.82 0.2 1 955 . 169 PRO C C 179.06 0.2 1 956 . 169 PRO CA C 65.44 0.2 1 957 . 169 PRO CB C 31.40 0.2 1 958 . 170 GLY H H 8.96 0.02 1 959 . 170 GLY HA2 H 3.74 0.02 1 960 . 170 GLY HA3 H 3.93 0.02 1 961 . 170 GLY C C 174.46 0.2 1 962 . 170 GLY CA C 45.64 0.2 1 963 . 170 GLY N N 105.33 0.2 1 964 . 171 MET H H 7.95 0.02 1 965 . 171 MET C C 179.05 0.2 1 966 . 171 MET CA C 56.16 0.2 1 967 . 171 MET CB C 33.06 0.2 1 968 . 171 MET N N 113.64 0.2 1 969 . 172 CYS H H 8.06 0.02 1 970 . 172 CYS HA H 5.01 0.02 1 971 . 172 CYS C C 173.97 0.2 1 972 . 172 CYS CA C 61.50 0.2 1 973 . 172 CYS CB C 28.55 0.2 1 974 . 172 CYS N N 116.66 0.2 1 975 . 173 GLY H H 9.44 0.02 1 976 . 173 GLY HA2 H 4.23 0.02 1 977 . 173 GLY HA3 H 4.82 0.2 1 978 . 173 GLY C C 172.62 0.2 1 979 . 173 GLY CA C 44.82 0.2 1 980 . 173 GLY N N 112.95 0.2 1 981 . 174 GLY H H 8.28 0.02 1 982 . 174 GLY HA2 H 4.02 0.02 1 983 . 174 GLY HA3 H 4.30 0.02 1 984 . 174 GLY C C 171.62 0.2 1 985 . 174 GLY CA C 44.56 0.2 1 986 . 174 GLY N N 110.20 0.2 1 987 . 175 ALA H H 8.09 0.02 1 988 . 175 ALA HA H 5.24 0.02 1 989 . 175 ALA C C 175.14 0.2 1 990 . 175 ALA CA C 49.87 0.2 1 991 . 175 ALA CB C 23.08 0.2 1 992 . 175 ALA N N 119.02 0.2 1 993 . 176 LEU H H 7.95 0.02 1 994 . 176 LEU HA H 4.26 0.02 1 995 . 176 LEU C C 176.29 0.2 1 996 . 176 LEU CA C 52.89 0.2 1 997 . 176 LEU CB C 37.34 0.2 1 998 . 176 LEU N N 125.20 0.2 1 999 . 177 VAL H H 9.45 0.02 1 1000 . 177 VAL C C 179.28 0.2 1 1001 . 177 VAL CA C 58.03 0.2 1 1002 . 177 VAL CB C 28.08 0.2 1 1003 . 177 VAL N N 130.05 0.2 1 1004 . 178 SER H H 8.72 0.02 1 1005 . 178 SER HA H 4.40 0.02 1 1006 . 178 SER C C 179.38 0.2 1 1007 . 178 SER CA C 61.14 0.2 1 1008 . 178 SER CB C 62.36 0.2 1 1009 . 178 SER N N 117.92 0.2 1 1010 . 179 SER H H 8.04 0.02 1 1011 . 179 SER HA H 4.36 0.02 1 1012 . 179 SER C C 175.88 0.2 1 1013 . 179 SER CA C 59.42 0.2 1 1014 . 179 SER CB C 63.49 0.2 1 1015 . 179 SER N N 119.91 0.2 1 1016 . 180 ASN H H 8.49 0.02 1 1017 . 180 ASN HA H 4.49 0.02 1 1018 . 180 ASN CA C 52.81 0.2 1 1019 . 180 ASN CB C 37.34 0.2 1 1020 . 180 ASN N N 119.39 0.2 1 1021 . 181 GLN C C 174.94 0.2 1 1022 . 181 GLN CA C 59.31 0.2 1 1023 . 182 SER H H 7.56 0.02 1 1024 . 182 SER HA H 4.10 0.02 1 1025 . 182 SER C C 175.20 0.2 1 1026 . 182 SER CA C 59.62 0.2 1 1027 . 182 SER CB C 64.21 0.2 1 1028 . 182 SER N N 119.17 0.2 1 1029 . 183 ILE H H 6.50 0.02 1 1030 . 183 ILE HA H 4.63 0.02 1 1031 . 183 ILE C C 175.20 0.2 1 1032 . 183 ILE CA C 59.97 0.2 1 1033 . 183 ILE CB C 35.44 0.2 1 1034 . 183 ILE N N 110.44 0.2 1 1035 . 184 GLN H H 7.83 0.02 1 1036 . 184 GLN HA H 3.79 0.02 1 1037 . 184 GLN C C 175.41 0.2 1 1038 . 184 GLN CA C 56.62 0.2 1 1039 . 184 GLN CB C 24.98 0.2 1 1040 . 184 GLN N N 116.60 0.2 1 1041 . 185 ASN H H 7.99 0.02 1 1042 . 185 ASN HA H 3.79 0.02 1 1043 . 185 ASN C C 171.22 0.2 1 1044 . 185 ASN CA C 55.56 0.2 1 1045 . 185 ASN CB C 36.87 0.2 1 1046 . 185 ASN N N 109.79 0.2 1 1047 . 186 ALA H H 5.79 0.02 1 1048 . 186 ALA HA H 4.12 0.02 1 1049 . 186 ALA C C 176.78 0.2 1 1050 . 186 ALA CA C 52.21 0.2 1 1051 . 186 ALA CB C 19.04 0.2 1 1052 . 186 ALA N N 110.04 0.2 1 1053 . 187 ILE H H 8.71 0.02 1 1054 . 187 ILE HA H 4.53 0.02 1 1055 . 187 ILE C C 175.42 0.2 1 1056 . 187 ILE CA C 61.49 0.2 1 1057 . 187 ILE CB C 37.11 0.2 1 1058 . 187 ILE N N 118.85 0.2 1 1059 . 188 LEU H H 9.95 0.02 1 1060 . 188 LEU HA H 5.51 0.02 1 1061 . 188 LEU C C 178.90 0.2 1 1062 . 188 LEU CA C 53.78 0.2 1 1063 . 188 LEU CB C 43.05 0.2 1 1064 . 188 LEU N N 123.93 0.2 1 1065 . 189 GLY H H 7.32 0.02 1 1066 . 189 GLY C C 171.06 0.2 1 1067 . 189 GLY CA C 45.32 0.2 1 1068 . 189 GLY N N 102.05 0.2 1 1069 . 190 ILE H H 7.93 0.02 1 1070 . 190 ILE HA H 5.25 0.02 1 1071 . 190 ILE C C 175.18 0.2 1 1072 . 190 ILE CA C 55.40 0.2 1 1073 . 190 ILE CB C 39.87 0.2 1 1074 . 190 ILE N N 118.40 0.2 1 1075 . 191 HIS H H 8.87 0.02 1 1076 . 191 HIS HA H 4.44 0.02 1 1077 . 191 HIS C C 175.60 0.2 1 1078 . 191 HIS CA C 58.96 0.2 1 1079 . 191 HIS CB C 32.33 0.2 1 1080 . 191 HIS N N 127.19 0.2 1 1081 . 192 VAL H H 8.78 0.02 1 1082 . 192 VAL HA H 3.99 0.02 1 1083 . 192 VAL C C 173.90 0.2 1 1084 . 192 VAL CA C 61.34 0.2 1 1085 . 192 VAL N N 119.03 0.2 1 1086 . 193 ALA H H 6.96 0.02 1 1087 . 193 ALA HA H 4.20 0.02 1 1088 . 193 ALA C C 175.22 0.2 1 1089 . 193 ALA CA C 52.30 0.2 1 1090 . 193 ALA CB C 21.18 0.2 1 1091 . 193 ALA N N 119.55 0.2 1 1092 . 194 GLY H H 7.92 0.02 1 1093 . 194 GLY HA2 H 5.09 0.02 5 1094 . 194 GLY HA3 H 5.00 0.02 5 1095 . 194 GLY C C 172.84 0.2 1 1096 . 194 GLY CA C 44.88 0.2 1 1097 . 194 GLY N N 107.32 0.2 1 1098 . 195 GLY H H 7.23 0.02 1 1099 . 195 GLY HA2 H 4.40 0.02 1 1100 . 195 GLY HA3 H 4.16 0.02 1 1101 . 195 GLY C C 174.21 0.02 1 1102 . 195 GLY CA C 44.54 0.2 1 1103 . 195 GLY N N 96.23 0.2 1 1104 . 196 ASN H H 9.26 0.02 1 1105 . 196 ASN HA H 4.49 0.02 1 1106 . 196 ASN C C 174.54 0.2 1 1107 . 196 ASN CA C 54.32 0.2 1 1108 . 196 ASN CB C 37.11 0.2 1 1109 . 196 ASN N N 120.63 0.2 1 1110 . 197 SER H H 8.65 0.02 1 1111 . 197 SER HA H 4.49 0.02 1 1112 . 197 SER C C 174.01 0.2 1 1113 . 197 SER CA C 59.75 0.2 1 1114 . 197 SER CB C 62.07 0.2 1 1115 . 197 SER N N 108.12 0.2 1 1116 . 198 ILE H H 7.81 0.02 1 1117 . 198 ILE HA H 4.77 0.02 1 1118 . 198 ILE C C 174.49 0.2 1 1119 . 198 ILE CA C 59.16 0.2 1 1120 . 198 ILE CB C 39.96 0.2 1 1121 . 198 ILE N N 120.25 0.2 1 1122 . 199 LEU H H 8.29 0.02 1 1123 . 199 LEU HA H 4.79 0.02 1 1124 . 199 LEU C C 175.72 0.2 1 1125 . 199 LEU CA C 53.12 0.2 1 1126 . 199 LEU CB C 41.87 0.2 1 1127 . 199 LEU N N 124.46 0.2 1 1128 . 200 VAL H H 8.92 0.02 1 1129 . 200 VAL HA H 5.10 0.02 1 1130 . 200 VAL C C 173.68 0.2 1 1131 . 200 VAL CA C 60.59 0.2 1 1132 . 200 VAL CB C 33.78 0.2 1 1133 . 200 VAL N N 123.99 0.2 1 1134 . 201 ALA H H 8.67 0.02 1 1135 . 201 ALA HA H 5.34 0.02 1 1136 . 201 ALA C C 176.52 0.2 1 1137 . 201 ALA CA C 49.34 0.2 1 1138 . 201 ALA CB C 21.18 0.2 1 1139 . 201 ALA N N 127.08 0.2 1 1140 . 202 LYS H H 8.70 0.02 1 1141 . 202 LYS HA H 3.93 0.02 1 1142 . 202 LYS C C 176.29 0.2 1 1143 . 202 LYS CA C 54.27 0.2 1 1144 . 202 LYS CB C 33.30 0.2 1 1145 . 202 LYS N N 124.00 0.2 1 1146 . 203 LEU H H 8.44 0.02 1 1147 . 203 LEU HA H 4.40 0.02 1 1148 . 203 LEU C C 176.08 0.2 1 1149 . 203 LEU CA C 56.56 0.2 1 1150 . 203 LEU CB C 41.62 0.2 1 1151 . 203 LEU N N 128.24 0.2 1 1152 . 204 VAL H H 7.95 0.02 1 1153 . 204 VAL HA H 4.10 0.02 1 1154 . 204 VAL C C 173.32 0.2 1 1155 . 204 VAL CA C 60.94 0.2 1 1156 . 204 VAL CB C 34.73 0.2 1 1157 . 204 VAL N N 129.08 0.2 1 1158 . 205 THR H H 7.65 0.02 1 1159 . 205 THR HA H 5.48 0.02 1 1160 . 205 THR C C 176.44 0.2 1 1161 . 205 THR CA C 57.50 0.2 1 1162 . 205 THR CB C 71.34 0.2 1 1163 . 205 THR N N 110.95 0.2 1 1164 . 206 GLN H H 8.80 0.02 1 1165 . 206 GLN HA H 4.40 0.02 1 1166 . 206 GLN C C 179.26 0.2 1 1167 . 206 GLN CA C 58.45 0.2 1 1168 . 206 GLN CB C 28.79 0.2 1 1169 . 206 GLN N N 117.99 0.2 1 1170 . 207 GLU H H 9.49 0.02 1 1171 . 207 GLU HA H 3.93 0.02 1 1172 . 207 GLU C C 179.18 0.2 1 1173 . 207 GLU CA C 60.34 0.2 1 1174 . 207 GLU CB C 27.36 0.2 1 1175 . 207 GLU N N 118.88 0.2 1 1176 . 208 MET H H 7.63 0.02 1 1177 . 208 MET HA H 4.00 0.02 1 1178 . 208 MET C C 176.99 0.2 1 1179 . 208 MET CA C 57.96 0.2 1 1180 . 208 MET CB C 30.45 0.2 1 1181 . 208 MET N N 117.77 0.2 1 1182 . 209 PHE H H 7.12 0.02 1 1183 . 209 PHE HA H 4.30 0.02 1 1184 . 209 PHE C C 176.93 0.2 1 1185 . 209 PHE CA C 57.33 0.2 1 1186 . 209 PHE CB C 37.11 0.2 1 1187 . 209 PHE N N 113.74 0.2 1 1188 . 210 GLN H H 7.48 0.02 1 1189 . 210 GLN HA H 4.07 0.02 1 1190 . 210 GLN C C 176.85 0.2 1 1191 . 210 GLN CA C 57.93 0.2 1 1192 . 210 GLN CB C 27.84 0.2 1 1193 . 210 GLN N N 119.32 0.2 1 1194 . 211 ASN H H 7.93 0.02 1 1195 . 211 ASN HA H 4.59 0.02 1 1196 . 211 ASN C C 176.11 0.2 1 1197 . 211 ASN CA C 54.02 0.2 1 1198 . 211 ASN CB C 38.06 0.2 1 1199 . 211 ASN N N 114.48 0.2 1 1200 . 212 ILE H H 7.15 0.02 1 1201 . 212 ILE HA H 3.55 0.02 1 1202 . 212 ILE C C 175.62 0.2 1 1203 . 212 ILE CA C 62.65 0.2 1 1204 . 212 ILE CB C 36.87 0.2 1 1205 . 212 ILE N N 115.26 0.2 1 1206 . 213 ASP H H 7.54 0.02 1 1207 . 213 ASP HA H 4.63 0.02 1 1208 . 213 ASP C C 175.67 0.2 1 1209 . 213 ASP CA C 53.94 0.2 1 1210 . 213 ASP CB C 40.43 0.2 1 1211 . 213 ASP N N 120.48 0.2 1 1212 . 214 LYS H H 7.73 0.02 1 1213 . 214 LYS HA H 4.26 0.02 1 1214 . 214 LYS C C 176.20 0.2 1 1215 . 214 LYS CA C 55.94 0.2 1 1216 . 214 LYS CB C 32.39 0.2 1 1217 . 214 LYS N N 120.74 0.2 1 1218 . 215 LYS H H 8.39 0.02 1 1219 . 215 LYS HA H 4.35 0.02 1 1220 . 215 LYS C C 176.35 0.2 1 1221 . 215 LYS CA C 55.83 0.2 1 1222 . 215 LYS CB C 32.11 0.2 1 1223 . 215 LYS N N 123.29 0.2 1 1224 . 216 ILE H H 8.29 0.02 1 1225 . 216 ILE HA H 4.20 0.02 1 1226 . 216 ILE C C 175.37 0.2 1 1227 . 216 ILE CA C 60.69 0.2 1 1228 . 216 ILE CB C 37.82 0.2 1 1229 . 216 ILE N N 123.37 0.2 1 1230 . 217 GLU H H 8.01 0.02 1 1231 . 217 GLU HA H 4.16 0.02 1 1232 . 217 GLU C C 175.39 0.2 1 1233 . 217 GLU CA C 57.21 0.2 1 1234 . 217 GLU CB C 30.21 0.2 1 1235 . 217 GLU N N 129.40 0.2 1 stop_ save_