data_16837 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HAV 3C C24S ; _BMRB_accession_number 16837 _BMRB_flat_file_name bmr16837.str _Entry_type original _Submission_date 2010-04-06 _Accession_date 2010-04-06 _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 Blaum Baerbel S. . 2 Winfried Wuensche . . 3 Andrew Benie J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 157 "13C chemical shifts" 494 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-22 update BMRB 'update entry citation' 2011-12-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Functional binding of hexanucleotides to 3C protease of hepatitis A virus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22156376 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blaum Barbel S. . 2 Wunsche Winfried . . 3 Benie Andrew J. . 4 Kusov Yuri . . 5 Peters Hannelore . . 6 Gauss-Muller Verena . . 7 Peters Thomas . . 8 Sczakiel Georg . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_name_full 'Nucleic acids research' _Journal_volume 40 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3042 _Page_last 3055 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HAV 3C C24S' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HAV 3C C24S' $HAV_3C_protease_C24S stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HAV_3C_protease_C24S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HAV_3C_protease_C24S _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'viral protease' stop_ _Details . ############################## # 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 2015-06-13 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 1HAV "Hepatitis A Virus 3c Proteinase" 100.00 217 100.00 100.00 1.92e-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 2.90e-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 2.00e-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 2.00e-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 1.61e-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 1.61e-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 1.61e-153 DBJ BAA35102 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.70e-141 DBJ BAA35103 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.75e-141 DBJ BAA35104 "polyprotein [Hepatitis A virus]" 100.00 2216 99.08 99.08 5.77e-140 DBJ BAA35105 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.87e-141 DBJ BAA35106 "polyprotein [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.67e-141 EMBL CAA33491 "unnamed protein product, partial [Hepatitis A virus]" 100.00 891 99.08 99.54 9.49e-148 EMBL CAA50195 "viral polyprotein, partial [Hepatitis A virus]" 100.00 746 98.62 99.08 3.43e-148 EMBL CAA53024 "unnamed protein product [Hepatitis A virus]" 100.00 2218 98.62 99.08 6.07e-140 EMBL CAA53025 "unnamed protein product [Hepatitis A virus]" 100.00 2227 99.08 99.08 1.69e-140 EMBL CAA53026 "unnamed protein product [Hepatitis A virus]" 100.00 2227 99.54 99.54 3.36e-141 GB AAA45465 "polyprotein a (alt.) [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.87e-141 GB AAA45466 "polyprotein b (alt.) [Hepatitis A virus]" 100.00 2225 99.54 99.54 2.62e-141 GB AAA45467 "viral protein [Hepatitis A virus]" 100.00 2226 99.08 99.54 1.17e-140 GB AAA45468 "viral protein [Hepatitis A virus]" 100.00 2226 99.08 99.54 1.04e-140 GB AAA45469 "viral protein [Hepatitis A virus]" 100.00 2226 98.62 99.08 2.63e-140 PIR GNNYHB "genome polyprotein - human hepatitis A virus (strain MBB) [Human hepatitis A virus]" 100.00 2227 99.54 99.54 3.36e-141 REF NP_041007 "hypothetical protein HAVgp1 [Hepatitis A virus]" 100.00 2227 99.54 99.54 2.87e-141 REF NP_041008 "hypothetical protein HAVgp2 [Hepatitis A virus]" 100.00 2225 99.54 99.54 2.62e-141 REF NP_740558 "3C mature peptide [Hepatitis A virus]" 100.00 219 99.54 99.54 1.09e-156 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 3.36e-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 8.46e-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 2.90e-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 2.87e-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 2.67e-141 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HAV_3C_protease_C24S 'Hepatitis A virus' 12092 Virus . Hepatovirus . 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 $HAV_3C_protease_C24S 'recombinant technology' . Escherichia coli . ptac5SOD 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 $HAV_3C_protease_C24S 0.2 mM '[U-100% 13C; U-100% 15N; U-75% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 200 . mM pH 7.4 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details "CA, CB, C' and N shifts corrected using CheckShift server" 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 C 13 'methyl carbons' ppm 0.00 na direct . . . 1.00 water H 1 protons ppm 4.7 internal direct . . . 1.00 ammonia N 15 nitrogen ppm 0.00 na direct . . . 1.00 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HN(CA)CO' '3D HNCACB' '3D HN(CO)CACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HAV 3C C24S' _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 2 2 THR H H 8.0960 . 1 2 2 2 THR CA C 66.71 . 1 3 2 2 THR CB C 68.62 . 1 4 2 2 THR N N 117.71 . 1 5 3 3 LEU H H 7.9640 . 1 6 3 3 LEU C C 179.89 . 1 7 3 3 LEU CA C 57.86 . 1 8 3 3 LEU CB C 40.85 . 1 9 3 3 LEU N N 119.40 . 1 10 4 4 GLU H H 7.6740 . 1 11 4 4 GLU C C 179.62 . 1 12 4 4 GLU CA C 59.41 . 1 13 4 4 GLU CB C 29.31 . 1 14 4 4 GLU N N 121.33 . 1 15 5 5 ILE H H 7.4910 . 1 16 5 5 ILE C C 178.66 . 1 17 5 5 ILE CA C 62.00 . 1 18 5 5 ILE CB C 34.92 . 1 19 5 5 ILE N N 120.31 . 1 20 6 6 ALA H H 8.8650 . 1 21 6 6 ALA C C 179.74 . 1 22 6 6 ALA CA C 55.76 . 1 23 6 6 ALA CB C 18.03 . 1 24 6 6 ALA N N 121.88 . 1 25 7 7 GLY H H 7.6690 . 1 26 7 7 GLY C C 176.32 . 1 27 7 7 GLY CA C 47.38 . 1 28 7 7 GLY N N 104.16 . 1 29 8 8 LEU H H 7.1850 . 1 30 8 8 LEU C C 180.29 . 1 31 8 8 LEU CA C 58.01 . 1 32 8 8 LEU CB C 41.19 . 1 33 8 8 LEU N N 122.14 . 1 34 9 9 VAL H H 8.0910 . 1 35 9 9 VAL C C 178.31 . 1 36 9 9 VAL CA C 66.97 . 1 37 9 9 VAL CB C 31.35 . 1 38 9 9 VAL N N 118.44 . 1 39 10 10 ARG H H 8.4150 . 1 40 10 10 ARG C C 179.32 . 1 41 10 10 ARG CA C 60.14 . 1 42 10 10 ARG CB C 28.99 . 1 43 10 10 ARG N N 116.89 . 1 44 11 11 LYS H H 7.1550 . 1 45 11 11 LYS C C 176.74 . 1 46 11 11 LYS CA C 58.67 . 1 47 11 11 LYS CB C 31.75 . 1 48 11 11 LYS N N 115.76 . 1 49 12 12 ASN H H 7.4470 . 1 50 12 12 ASN C C 174.29 . 1 51 12 12 ASN CA C 52.84 . 1 52 12 12 ASN CB C 38.77 . 1 53 12 12 ASN N N 118.78 . 1 54 13 13 LEU H H 7.3880 . 1 55 13 13 LEU C C 177.39 . 1 56 13 13 LEU CA C 56.22 . 1 57 13 13 LEU CB C 43.09 . 1 58 13 13 LEU N N 125.22 . 1 59 14 14 VAL H H 9.0320 . 1 60 14 14 VAL C C 175.62 . 1 61 14 14 VAL CA C 59.14 . 1 62 14 14 VAL CB C 34.69 . 1 63 14 14 VAL N N 117.39 . 1 64 15 15 GLN H H 7.5960 . 1 65 15 15 GLN C C 174.56 . 1 66 15 15 GLN CA C 57.14 . 1 67 15 15 GLN CB C 31.41 . 1 68 15 15 GLN N N 117.98 . 1 69 16 16 PHE H H 9.0980 . 1 70 16 16 PHE C C 174.31 . 1 71 16 16 PHE CA C 57.17 . 1 72 16 16 PHE CB C 42.71 . 1 73 16 16 PHE N N 123.67 . 1 74 17 17 GLY H H 8.5370 . 1 75 17 17 GLY C C 169.75 . 1 76 17 17 GLY CA C 44.56 . 1 77 17 17 GLY N N 119.29 . 1 78 18 18 VAL H H 7.9580 . 1 79 18 18 VAL C C 175.52 . 1 80 18 18 VAL CA C 59.32 . 1 81 18 18 VAL CB C 35.37 . 1 82 18 18 VAL N N 112.25 . 1 83 19 19 GLY H H 8.7450 . 1 84 19 19 GLY C C 172.56 . 1 85 19 19 GLY CA C 46.15 . 1 86 19 19 GLY N N 109.96 . 1 87 20 20 GLU H H 8.2980 . 1 88 20 20 GLU C C 178.18 . 1 89 20 20 GLU CA C 55.49 . 1 90 20 20 GLU CB C 31.46 . 1 91 20 20 GLU N N 120.53 . 1 92 22 22 ASN C C 175.34 . 1 93 22 22 ASN CA C 54.57 . 1 94 22 22 ASN CB C 37.53 . 1 95 23 23 GLY H H 7.7620 . 1 96 23 23 GLY C C 174.01 . 1 97 23 23 GLY CA C 44.93 . 1 98 23 23 GLY N N 107.44 . 1 99 24 24 SER H H 7.8810 . 1 100 24 24 SER C C 173.23 . 1 101 24 24 SER CA C 58.19 . 1 102 24 24 SER CB C 64.04 . 1 103 24 24 SER N N 116.04 . 1 104 25 25 VAL H H 7.7710 . 1 105 25 25 VAL C C 174.64 . 1 106 25 25 VAL CA C 61.83 . 1 107 25 25 VAL CB C 32.32 . 1 108 25 25 VAL N N 122.09 . 1 109 26 26 ARG H H 8.0880 . 1 110 26 26 ARG C C 174.60 . 1 111 26 26 ARG CA C 54.54 . 1 112 26 26 ARG CB C 30.60 . 1 113 26 26 ARG N N 127.86 . 1 114 27 27 TRP H H 8.3830 . 1 115 27 27 TRP C C 177.24 . 1 116 27 27 TRP CA C 57.78 . 1 117 27 27 TRP CB C 28.25 . 1 118 27 27 TRP N N 128.09 . 1 119 29 29 MET C C 173.63 . 1 120 29 29 MET CA C 56.80 . 1 121 29 29 MET CB C 29.60 . 1 122 30 30 ASN H H 8.3550 . 1 123 30 30 ASN C C 171.93 . 1 124 30 30 ASN CA C 53.47 . 1 125 30 30 ASN CB C 42.26 . 1 126 30 30 ASN N N 119.11 . 1 127 31 31 ALA H H 8.9520 . 1 128 31 31 ALA C C 174.56 . 1 129 31 31 ALA CA C 51.61 . 1 130 31 31 ALA CB C 23.05 . 1 131 31 31 ALA N N 117.14 . 1 132 32 32 LEU H H 8.2580 . 1 133 32 32 LEU C C 176.24 . 1 134 32 32 LEU CA C 53.10 . 1 135 32 32 LEU CB C 45.28 . 1 136 32 32 LEU N N 119.99 . 1 137 33 33 GLY H H 8.7740 . 1 138 33 33 GLY C C 174.04 . 1 139 33 33 GLY CA C 44.73 . 1 140 33 33 GLY N N 116.75 . 1 141 34 34 VAL H H 8.5990 . 1 142 34 34 VAL C C 174.20 . 1 143 34 34 VAL CA C 61.74 . 1 144 34 34 VAL CB C 32.52 . 1 145 34 34 VAL N N 117.18 . 1 146 35 35 LYS H H 6.6060 . 1 147 35 35 LYS C C 174.21 . 1 148 35 35 LYS CA C 57.62 . 1 149 35 35 LYS CB C 32.89 . 1 150 35 35 LYS N N 113.44 . 1 151 36 36 ASP H H 8.9230 . 1 152 36 36 ASP C C 173.11 . 1 153 36 36 ASP CA C 57.53 . 1 154 36 36 ASP CB C 39.25 . 1 155 36 36 ASP N N 123.11 . 1 156 37 37 ASP H H 8.8000 . 1 157 37 37 ASP C C 174.00 . 1 158 37 37 ASP CA C 52.06 . 1 159 37 37 ASP CB C 38.23 . 1 160 37 37 ASP N N 122.06 . 1 161 38 38 TRP H H 8.6340 . 1 162 38 38 TRP C C 177.00 . 1 163 38 38 TRP CA C 57.45 . 1 164 38 38 TRP CB C 31.13 . 1 165 38 38 TRP N N 117.17 . 1 166 39 39 LEU H H 9.4360 . 1 167 39 39 LEU C C 176.17 . 1 168 39 39 LEU CA C 54.54 . 1 169 39 39 LEU CB C 45.52 . 1 170 39 39 LEU N N 119.64 . 1 171 40 40 LEU H H 8.9070 . 1 172 40 40 LEU CA C 53.78 . 1 173 40 40 LEU CB C 43.89 . 1 174 40 40 LEU N N 119.51 . 1 175 49 49 GLU C C 177.03 . 1 176 49 49 GLU CA C 55.17 . 1 177 49 49 GLU CB C 29.24 . 1 178 50 50 LYS H H 8.6220 . 1 179 50 50 LYS C C 176.92 . 1 180 50 50 LYS CA C 57.82 . 1 181 50 50 LYS CB C 31.92 . 1 182 50 50 LYS N N 125.51 . 1 183 51 51 ASP H H 8.7410 . 1 184 51 51 ASP C C 177.99 . 1 185 51 51 ASP CA C 55.54 . 1 186 51 51 ASP CB C 39.47 . 1 187 51 51 ASP N N 120.26 . 1 188 52 52 TYR H H 7.3850 . 1 189 52 52 TYR C C 176.97 . 1 190 52 52 TYR CA C 60.75 . 1 191 52 52 TYR CB C 37.56 . 1 192 52 52 TYR N N 117.53 . 1 193 53 53 GLU H H 8.4240 . 1 194 53 53 GLU C C 177.34 . 1 195 53 53 GLU CA C 59.17 . 1 196 53 53 GLU CB C 28.32 . 1 197 53 53 GLU N N 119.08 . 1 198 55 55 MET H H 7.6040 . 1 199 55 55 MET C C 174.35 . 1 200 55 55 MET CA C 56.39 . 1 201 55 55 MET CB C 33.94 . 1 202 55 55 MET N N 120.40 . 1 203 56 56 GLU H H 8.5430 . 1 204 56 56 GLU C C 175.11 . 1 205 56 56 GLU CA C 55.13 . 1 206 56 56 GLU CB C 31.59 . 1 207 56 56 GLU N N 120.53 . 1 208 57 57 PHE H H 8.7100 . 1 209 57 57 PHE C C 174.25 . 1 210 57 57 PHE CA C 52.65 . 1 211 57 57 PHE CB C 39.33 . 1 212 57 57 PHE N N 121.98 . 1 213 58 58 TYR H H 7.9900 . 1 214 58 58 TYR C C 174.06 . 1 215 58 58 TYR CA C 56.73 . 1 216 58 58 TYR CB C 43.23 . 1 217 58 58 TYR N N 118.72 . 1 218 59 59 PHE H H 9.1350 . 1 219 59 59 PHE C C 175.88 . 1 220 59 59 PHE CA C 55.90 . 1 221 59 59 PHE CB C 42.48 . 1 222 59 59 PHE N N 115.60 . 1 223 60 60 ASN H H 8.8900 . 1 224 60 60 ASN C C 175.74 . 1 225 60 60 ASN CA C 52.30 . 1 226 60 60 ASN CB C 38.94 . 1 227 60 60 ASN N N 121.06 . 1 228 61 61 ARG H H 8.8770 . 1 229 61 61 ARG C C 176.59 . 1 230 61 61 ARG CA C 54.76 . 1 231 61 61 ARG CB C 31.49 . 1 232 61 61 ARG N N 127.32 . 1 233 62 62 GLY C C 175.14 . 1 234 62 62 GLY CA C 47.52 . 1 235 63 63 GLY H H 8.2320 . 1 236 63 63 GLY C C 174.05 . 1 237 63 63 GLY CA C 45.40 . 1 238 63 63 GLY N N 107.78 . 1 239 64 64 THR H H 7.2520 . 1 240 64 64 THR C C 172.09 . 1 241 64 64 THR CA C 62.17 . 1 242 64 64 THR CB C 70.24 . 1 243 64 64 THR N N 117.58 . 1 244 65 65 TYR H H 8.2030 . 1 245 65 65 TYR C C 175.49 . 1 246 65 65 TYR CA C 54.68 . 1 247 65 65 TYR CB C 37.77 . 1 248 65 65 TYR N N 124.14 . 1 249 66 66 TYR H H 9.2450 . 1 250 66 66 TYR CA C 57.86 . 1 251 66 66 TYR CB C 41.10 . 1 252 66 66 TYR N N 122.81 . 1 253 67 67 SER H H 8.6340 . 1 254 67 67 SER C C 173.69 . 1 255 67 67 SER CA C 56.95 . 1 256 67 67 SER CB C 67.05 . 1 257 67 67 SER N N 116.44 . 1 258 68 68 ILE H H 8.7420 . 1 259 68 68 ILE C C 172.37 . 1 260 68 68 ILE CA C 60.20 . 1 261 68 68 ILE CB C 41.39 . 1 262 68 68 ILE N N 120.85 . 1 263 69 69 SER H H 8.1710 . 1 264 69 69 SER C C 176.48 . 1 265 69 69 SER CA C 59.24 . 1 266 69 69 SER CB C 63.01 . 1 267 69 69 SER N N 121.20 . 1 268 70 70 ALA H H 8.2020 . 1 269 70 70 ALA C C 179.26 . 1 270 70 70 ALA CA C 55.49 . 1 271 70 70 ALA CB C 18.62 . 1 272 70 70 ALA N N 129.02 . 1 273 71 71 GLY H H 7.8450 . 1 274 71 71 GLY C C 174.73 . 1 275 71 71 GLY CA C 46.12 . 1 276 71 71 GLY N N 101.65 . 1 277 72 72 ASN H H 7.7380 . 1 278 72 72 ASN C C 175.13 . 1 279 72 72 ASN CA C 53.09 . 1 280 72 72 ASN CB C 39.74 . 1 281 72 72 ASN N N 116.45 . 1 282 73 73 VAL H H 6.8480 . 1 283 73 73 VAL C C 175.32 . 1 284 73 73 VAL CA C 61.26 . 1 285 73 73 VAL CB C 32.73 . 1 286 73 73 VAL N N 114.93 . 1 287 74 74 VAL H H 7.7420 . 1 288 74 74 VAL C C 174.54 . 1 289 74 74 VAL CA C 62.88 . 1 290 74 74 VAL CB C 32.74 . 1 291 74 74 VAL N N 125.07 . 1 292 75 75 ILE H H 8.3150 . 1 293 75 75 ILE C C 176.58 . 1 294 75 75 ILE CA C 59.96 . 1 295 75 75 ILE CB C 39.50 . 1 296 75 75 ILE N N 126.57 . 1 297 76 76 GLN H H 9.6870 . 1 298 76 76 GLN C C 174.51 . 1 299 76 76 GLN CA C 54.22 . 1 300 76 76 GLN CB C 32.21 . 1 301 76 76 GLN N N 127.85 . 1 302 77 77 SER H H 8.4790 . 1 303 77 77 SER C C 175.36 . 1 304 77 77 SER CA C 58.56 . 1 305 77 77 SER CB C 64.18 . 1 306 77 77 SER N N 119.10 . 1 307 79 79 ASP C C 176.57 . 1 308 79 79 ASP CA C 55.81 . 1 309 79 79 ASP CB C 31.18 . 1 310 80 80 VAL H H 9.0120 . 1 311 80 80 VAL C C 175.83 . 1 312 80 80 VAL CA C 54.86 . 1 313 80 80 VAL CB C 33.65 . 1 314 80 80 VAL N N 120.69 . 1 315 81 81 GLY H H 8.5040 . 1 316 81 81 GLY C C 171.51 . 1 317 81 81 GLY CA C 44.30 . 1 318 81 81 GLY N N 109.69 . 1 319 87 87 LEU C C 175.74 . 1 320 87 87 LEU CA C 54.24 . 1 321 87 87 LEU CB C 43.65 . 1 322 88 88 MET H H 9.7960 . 1 323 88 88 MET C C 173.43 . 1 324 88 88 MET CA C 54.47 . 1 325 88 88 MET CB C 37.15 . 1 326 88 88 MET N N 123.47 . 1 327 89 89 LYS H H 8.6500 . 1 328 89 89 LYS C C 176.55 . 1 329 89 89 LYS CA C 54.98 . 1 330 89 89 LYS CB C 33.29 . 1 331 89 89 LYS N N 130.62 . 1 332 90 90 VAL H H 8.4840 . 1 333 90 90 VAL C C 173.94 . 1 334 90 90 VAL CA C 59.36 . 1 335 90 90 VAL CB C 31.73 . 1 336 90 90 VAL N N 126.47 . 1 337 94 94 PRO C C 176.89 . 1 338 94 94 PRO CA C 63.23 . 1 339 94 94 PRO CB C 30.97 . 1 340 95 95 LYS H H 7.6050 . 1 341 95 95 LYS C C 178.39 . 1 342 95 95 LYS CA C 57.51 . 1 343 95 95 LYS CB C 33.26 . 1 344 95 95 LYS N N 120.36 . 1 345 96 96 PHE H H 9.4700 . 1 346 96 96 PHE C C 176.95 . 1 347 96 96 PHE CA C 58.13 . 1 348 96 96 PHE CB C 40.18 . 1 349 96 96 PHE N N 121.94 . 1 350 97 97 ARG H H 8.5390 . 1 351 97 97 ARG C C 175.82 . 1 352 97 97 ARG CA C 56.74 . 1 353 97 97 ARG CB C 30.17 . 1 354 97 97 ARG N N 124.17 . 1 355 98 98 ASP H H 8.3930 . 1 356 98 98 ASP C C 178.47 . 1 357 98 98 ASP CA C 54.10 . 1 358 98 98 ASP CB C 39.77 . 1 359 98 98 ASP N N 123.57 . 1 360 99 99 ILE H H 8.8120 . 1 361 99 99 ILE C C 178.06 . 1 362 99 99 ILE CA C 61.47 . 1 363 99 99 ILE CB C 38.45 . 1 364 99 99 ILE N N 122.10 . 1 365 100 100 THR H H 8.8140 . 1 366 100 100 THR C C 177.19 . 1 367 100 100 THR CA C 65.99 . 1 368 100 100 THR CB C 69.34 . 1 369 100 100 THR N N 116.84 . 1 370 101 101 GLN H H 8.2440 . 1 371 101 101 GLN C C 176.32 . 1 372 101 101 GLN CA C 56.87 . 1 373 101 101 GLN CB C 27.05 . 1 374 101 101 GLN N N 115.95 . 1 375 102 102 HIS H H 7.8730 . 1 376 102 102 HIS C C 175.63 . 1 377 102 102 HIS CA C 56.79 . 1 378 102 102 HIS CB C 29.17 . 1 379 102 102 HIS N N 116.53 . 1 380 103 103 PHE H H 7.4930 . 1 381 103 103 PHE C C 176.57 . 1 382 103 103 PHE CA C 58.42 . 1 383 103 103 PHE CB C 39.46 . 1 384 103 103 PHE N N 119.59 . 1 385 104 104 ILE H H 8.6050 . 1 386 104 104 ILE C C 174.41 . 1 387 104 104 ILE CA C 60.89 . 1 388 104 104 ILE CB C 39.89 . 1 389 104 104 ILE N N 123.56 . 1 390 105 105 LYS H H 8.9420 . 1 391 105 105 LYS C C 179.54 . 1 392 105 105 LYS CA C 56.69 . 1 393 105 105 LYS CB C 32.36 . 1 394 105 105 LYS N N 126.74 . 1 395 106 106 LYS H H 10.1510 . 1 396 106 106 LYS C C 180.04 . 1 397 106 106 LYS CA C 60.73 . 1 398 106 106 LYS CB C 31.55 . 1 399 106 106 LYS N N 126.26 . 1 400 107 107 GLY H H 9.2530 . 1 401 107 107 GLY C C 174.56 . 1 402 107 107 GLY CA C 46.24 . 1 403 107 107 GLY N N 104.70 . 1 404 108 108 ASP H H 7.9110 . 1 405 108 108 ASP C C 177.20 . 1 406 108 108 ASP CA C 54.86 . 1 407 108 108 ASP CB C 42.21 . 1 408 108 108 ASP N N 117.36 . 1 409 109 109 VAL H H 7.2530 . 1 410 109 109 VAL C C 174.82 . 1 411 109 109 VAL CA C 69.45 . 1 412 109 109 VAL CB C 30.23 . 1 413 109 109 VAL N N 122.95 . 1 414 110 110 PRO C C 178.64 . 1 415 110 110 PRO CA C 65.91 . 1 416 110 110 PRO CB C 31.06 . 1 417 111 111 ARG H H 7.9080 . 1 418 111 111 ARG C C 176.55 . 1 419 111 111 ARG CA C 57.83 . 1 420 111 111 ARG CB C 30.09 . 1 421 111 111 ARG N N 113.50 . 1 422 112 112 ALA H H 7.8420 . 1 423 112 112 ALA C C 178.09 . 1 424 112 112 ALA CA C 51.94 . 1 425 112 112 ALA CB C 21.11 . 1 426 112 112 ALA N N 119.68 . 1 427 113 113 LEU H H 6.8800 . 1 428 113 113 LEU C C 176.95 . 1 429 113 113 LEU CA C 56.16 . 1 430 113 113 LEU CB C 42.68 . 1 431 113 113 LEU N N 118.06 . 1 432 114 114 ASN H H 9.7240 . 1 433 114 114 ASN C C 173.45 . 1 434 114 114 ASN CA C 55.38 . 1 435 114 114 ASN CB C 37.40 . 1 436 114 114 ASN N N 115.53 . 1 437 115 115 ARG H H 7.2140 . 1 438 115 115 ARG C C 176.20 . 1 439 115 115 ARG CA C 53.27 . 1 440 115 115 ARG CB C 31.99 . 1 441 115 115 ARG N N 115.62 . 1 442 116 116 LEU H H 8.2550 . 1 443 116 116 LEU C C 177.51 . 1 444 116 116 LEU CA C 55.95 . 1 445 116 116 LEU CB C 40.83 . 1 446 116 116 LEU N N 120.06 . 1 447 117 117 ALA H H 7.1900 . 1 448 117 117 ALA C C 174.59 . 1 449 117 117 ALA CA C 52.01 . 1 450 117 117 ALA CB C 24.17 . 1 451 117 117 ALA N N 121.50 . 1 452 118 118 THR H H 8.5870 . 1 453 118 118 THR C C 172.53 . 1 454 118 118 THR CA C 61.94 . 1 455 118 118 THR CB C 71.65 . 1 456 118 118 THR N N 115.95 . 1 457 119 119 LEU H H 9.6150 . 1 458 119 119 LEU C C 173.95 . 1 459 119 119 LEU CA C 54.57 . 1 460 119 119 LEU CB C 40.88 . 1 461 119 119 LEU N N 130.81 . 1 462 120 120 VAL H H 9.0890 . 1 463 120 120 VAL C C 174.33 . 1 464 120 120 VAL CA C 61.89 . 1 465 120 120 VAL CB C 31.05 . 1 466 120 120 VAL N N 129.70 . 1 467 121 121 THR H H 7.9140 . 1 468 121 121 THR C C 173.38 . 1 469 121 121 THR CA C 59.19 . 1 470 121 121 THR CB C 69.31 . 1 471 121 121 THR N N 118.07 . 1 472 122 122 THR H H 8.5180 . 1 473 122 122 THR C C 173.35 . 1 474 122 122 THR CA C 61.45 . 1 475 122 122 THR CB C 71.58 . 1 476 122 122 THR N N 115.65 . 1 477 123 123 VAL H H 7.7810 . 1 478 123 123 VAL C C 176.52 . 1 479 123 123 VAL CA C 62.56 . 1 480 123 123 VAL CB C 33.06 . 1 481 123 123 VAL N N 117.66 . 1 482 124 124 ASN C C 175.36 . 1 483 124 124 ASN CA C 54.39 . 1 484 124 124 ASN CB C 37.40 . 1 485 125 125 GLY H H 8.0200 . 1 486 125 125 GLY C C 174.58 . 1 487 125 125 GLY CA C 45.37 . 1 488 125 125 GLY N N 102.99 . 1 489 126 126 THR H H 7.8430 . 1 490 126 126 THR C C 172.32 . 1 491 126 126 THR CA C 61.01 . 1 492 126 126 THR CB C 69.88 . 1 493 126 126 THR N N 120.82 . 1 494 131 131 SER C C 174.26 . 1 495 131 131 SER CA C 59.63 . 1 496 131 131 SER CB C 62.95 . 1 497 132 132 GLU H H 8.2930 . 1 498 132 132 GLU C C 177.24 . 1 499 132 132 GLU CA C 56.42 . 1 500 132 132 GLU CB C 28.89 . 1 501 132 132 GLU N N 123.50 . 1 502 133 133 GLY H H 8.2280 . 1 503 133 133 GLY C C 168.77 . 1 504 133 133 GLY CA C 45.42 . 1 505 133 133 GLY N N 107.59 . 1 506 134 134 PRO C C 180.01 . 1 507 134 134 PRO CA C 62.35 . 1 508 134 134 PRO CB C 30.89 . 1 509 135 135 LEU H H 7.3670 . 1 510 135 135 LEU C C 178.35 . 1 511 135 135 LEU CA C 56.47 . 1 512 135 135 LEU CB C 44.35 . 1 513 135 135 LEU N N 123.62 . 1 514 136 136 LYS H H 8.3310 . 1 515 136 136 LYS C C 175.18 . 1 516 136 136 LYS CA C 54.82 . 1 517 136 136 LYS CB C 35.62 . 1 518 136 136 LYS N N 119.05 . 1 519 137 137 MET H H 8.3590 . 1 520 137 137 MET C C 175.12 . 1 521 137 137 MET CA C 54.78 . 1 522 137 137 MET CB C 33.72 . 1 523 137 137 MET N N 120.88 . 1 524 138 138 GLU C C 173.72 . 1 525 138 138 GLU CA C 55.50 . 1 526 138 138 GLU CB C 37.03 . 1 527 139 139 GLU H H 7.0790 . 1 528 139 139 GLU C C 176.64 . 1 529 139 139 GLU CA C 53.60 . 1 530 139 139 GLU CB C 33.70 . 1 531 139 139 GLU N N 114.89 . 1 532 140 140 LYS H H 8.6760 . 1 533 140 140 LYS C C 177.53 . 1 534 140 140 LYS CA C 55.50 . 1 535 140 140 LYS CB C 42.09 . 1 536 140 140 LYS N N 119.70 . 1 537 141 141 ALA H H 8.9050 . 1 538 141 141 ALA C C 174.29 . 1 539 141 141 ALA CA C 51.70 . 1 540 141 141 ALA CB C 24.31 . 1 541 141 141 ALA N N 124.76 . 1 542 142 142 THR H H 8.8310 . 1 543 142 142 THR C C 173.02 . 1 544 142 142 THR CA C 61.96 . 1 545 142 142 THR CB C 71.11 . 1 546 142 142 THR N N 115.61 . 1 547 143 143 TYR H H 9.7290 . 1 548 143 143 TYR C C 173.89 . 1 549 143 143 TYR CA C 54.56 . 1 550 143 143 TYR CB C 40.80 . 1 551 143 143 TYR N N 131.35 . 1 552 149 149 ASP C C 177.33 . 1 553 149 149 ASP CA C 53.58 . 1 554 149 149 ASP CB C 39.82 . 1 555 150 150 GLY H H 7.8690 . 1 556 150 150 GLY C C 174.79 . 1 557 150 150 GLY CA C 45.63 . 1 558 150 150 GLY N N 107.80 . 1 559 151 151 THR H H 7.9070 . 1 560 151 151 THR C C 173.65 . 1 561 151 151 THR CA C 62.37 . 1 562 151 151 THR CB C 70.61 . 1 563 151 151 THR N N 113.96 . 1 564 152 152 THR H H 7.9990 . 1 565 152 152 THR C C 174.70 . 1 566 152 152 THR CA C 60.35 . 1 567 152 152 THR CB C 71.60 . 1 568 152 152 THR N N 109.37 . 1 569 153 153 VAL H H 8.6030 . 1 570 153 153 VAL C C 173.15 . 1 571 153 153 VAL CA C 60.35 . 1 572 153 153 VAL CB C 34.65 . 1 573 153 153 VAL N N 119.50 . 1 574 154 154 ASP H H 7.9810 . 1 575 154 154 ASP C C 175.31 . 1 576 154 154 ASP CA C 54.19 . 1 577 154 154 ASP CB C 41.12 . 1 578 154 154 ASP N N 124.87 . 1 579 155 155 LEU H H 8.7300 . 1 580 155 155 LEU C C 174.99 . 1 581 155 155 LEU CA C 54.03 . 1 582 155 155 LEU CB C 42.77 . 1 583 155 155 LEU N N 125.86 . 1 584 156 156 THR H H 8.7070 . 1 585 156 156 THR CA C 59.36 . 1 586 156 156 THR CB C 62.80 . 1 587 156 156 THR N N 124.67 . 1 588 157 157 VAL CA C 59.86 . 1 589 157 157 VAL CB C 40.47 . 1 590 158 158 ASP H H 8.1570 . 1 591 158 158 ASP CA C 54.13 . 1 592 158 158 ASP CB C 42.32 . 1 593 158 158 ASP N N 124.83 . 1 594 159 159 GLN H H 8.7810 . 1 595 159 159 GLN CA C 61.38 . 1 596 159 159 GLN CB C 33.91 . 1 597 159 159 GLN N N 124.00 . 1 598 160 160 ALA H H 8.5250 . 1 599 160 160 ALA CA C 50.03 . 1 600 160 160 ALA CB C 21.69 . 1 601 160 160 ALA N N 127.27 . 1 602 161 161 TRP C C 176.40 . 1 603 161 161 TRP CA C 56.02 . 1 604 161 161 TRP CB C 31.47 . 1 605 162 162 ARG H H 9.1100 . 1 606 162 162 ARG C C 175.44 . 1 607 162 162 ARG CA C 55.22 . 1 608 162 162 ARG CB C 33.38 . 1 609 162 162 ARG N N 121.98 . 1 610 163 163 GLY H H 8.8340 . 1 611 163 163 GLY C C 172.53 . 1 612 163 163 GLY CA C 43.80 . 1 613 163 163 GLY N N 113.77 . 1 614 164 164 LYS H H 8.6780 . 1 615 164 164 LYS C C 175.78 . 1 616 164 164 LYS CA C 56.06 . 1 617 164 164 LYS CB C 34.26 . 1 618 164 164 LYS N N 122.77 . 1 619 165 165 GLY H H 7.5650 . 1 620 165 165 GLY C C 170.86 . 1 621 165 165 GLY CA C 44.88 . 1 622 165 165 GLY N N 110.61 . 1 623 166 166 GLU H H 8.0060 . 1 624 166 166 GLU C C 175.39 . 1 625 166 166 GLU CA C 55.03 . 1 626 166 166 GLU CB C 29.92 . 1 627 166 166 GLU N N 117.83 . 1 628 167 167 GLY H H 8.3600 . 1 629 167 167 GLY C C 172.93 . 1 630 167 167 GLY CA C 44.69 . 1 631 167 167 GLY N N 110.16 . 1 632 168 168 LEU H H 7.5130 . 1 633 168 168 LEU C C 177.49 . 1 634 168 168 LEU CA C 52.56 . 1 635 168 168 LEU CB C 43.70 . 1 636 168 168 LEU N N 120.78 . 1 637 170 170 GLY C C 174.65 . 1 638 170 170 GLY CA C 46.38 . 1 639 171 171 MET H H 7.8240 . 1 640 171 171 MET C C 179.15 . 1 641 171 171 MET CA C 56.98 . 1 642 171 171 MET CB C 33.71 . 1 643 171 171 MET N N 113.67 . 1 644 172 172 CYS H H 7.8460 . 1 645 172 172 CYS C C 174.08 . 1 646 172 172 CYS CA C 62.26 . 1 647 172 172 CYS CB C 28.86 . 1 648 172 172 CYS N N 117.20 . 1 649 173 173 GLY H H 9.3390 . 1 650 173 173 GLY C C 173.03 . 1 651 173 173 GLY CA C 45.59 . 1 652 173 173 GLY N N 113.09 . 1 653 174 174 GLY H H 7.0590 . 1 654 174 174 GLY C C 171.74 . 1 655 174 174 GLY CA C 45.23 . 1 656 174 174 GLY N N 98.20 . 1 657 175 175 ALA H H 7.9200 . 1 658 175 175 ALA C C 174.75 . 1 659 175 175 ALA CA C 50.54 . 1 660 175 175 ALA CB C 23.21 . 1 661 175 175 ALA N N 118.77 . 1 662 176 176 LEU H H 7.8160 . 1 663 176 176 LEU C C 174.72 . 1 664 176 176 LEU CA C 53.64 . 1 665 176 176 LEU CB C 44.45 . 1 666 176 176 LEU N N 125.23 . 1 667 177 177 VAL H H 9.0650 . 1 668 177 177 VAL C C 176.33 . 1 669 177 177 VAL CA C 61.39 . 1 670 177 177 VAL CB C 34.04 . 1 671 177 177 VAL N N 126.39 . 1 672 178 178 SER H H 8.4960 . 1 673 178 178 SER C C 175.31 . 1 674 178 178 SER CA C 59.76 . 1 675 178 178 SER CB C 64.53 . 1 676 178 178 SER N N 119.96 . 1 677 179 179 SER H H 7.8580 . 1 678 179 179 SER C C 174.22 . 1 679 179 179 SER CA C 60.09 . 1 680 179 179 SER CB C 63.61 . 1 681 179 179 SER N N 119.74 . 1 682 180 180 ASN H H 8.2370 . 1 683 180 180 ASN C C 176.39 . 1 684 180 180 ASN CA C 53.51 . 1 685 180 180 ASN CB C 37.69 . 1 686 180 180 ASN N N 119.53 . 1 687 186 186 ALA C C 177.03 . 1 688 186 186 ALA CA C 53.01 . 1 689 186 186 ALA CB C 19.75 . 1 690 187 187 ILE H H 8.5090 . 1 691 187 187 ILE C C 176.23 . 1 692 187 187 ILE CA C 62.56 . 1 693 187 187 ILE CB C 37.63 . 1 694 187 187 ILE N N 119.09 . 1 695 188 188 LEU H H 9.0080 . 1 696 188 188 LEU C C 179.06 . 1 697 188 188 LEU CA C 54.63 . 1 698 188 188 LEU CB C 41.84 . 1 699 188 188 LEU N N 123.30 . 1 700 189 189 GLY H H 7.1660 . 1 701 189 189 GLY C C 171.35 . 1 702 189 189 GLY CA C 46.12 . 1 703 189 189 GLY N N 102.14 . 1 704 190 190 ILE H H 7.7790 . 1 705 190 190 ILE C C 175.38 . 1 706 190 190 ILE CA C 56.21 . 1 707 190 190 ILE CB C 40.31 . 1 708 190 190 ILE N N 118.35 . 1 709 191 191 HIS H H 8.7220 . 1 710 191 191 HIS C C 175.71 . 1 711 191 191 HIS CA C 59.55 . 1 712 191 191 HIS CB C 32.87 . 1 713 191 191 HIS N N 127.16 . 1 714 193 193 ALA C C 174.76 . 1 715 193 193 ALA CA C 52.89 . 1 716 193 193 ALA CB C 21.54 . 1 717 194 194 GLY H H 8.1160 . 1 718 194 194 GLY C C 172.87 . 1 719 194 194 GLY CA C 45.66 . 1 720 194 194 GLY N N 107.19 . 1 721 195 195 GLY H H 8.1410 . 1 722 195 195 GLY C C 174.32 . 1 723 195 195 GLY CA C 45.35 . 1 724 195 195 GLY N N 110.28 . 1 725 196 196 ASN CA C 58.87 . 1 726 196 196 ASN CB C 39.58 . 1 727 197 197 SER H H 8.6140 . 1 728 197 197 SER CA C 58.93 . 1 729 197 197 SER CB C 63.14 . 1 730 197 197 SER N N 123.05 . 1 731 198 198 ILE H H 8.6880 . 1 732 198 198 ILE CA C 54.60 . 1 733 198 198 ILE CB C 33.81 . 1 734 198 198 ILE N N 120.49 . 1 735 202 202 LYS C C 176.49 . 1 736 202 202 LYS CA C 55.48 . 1 737 202 202 LYS CB C 34.47 . 1 738 203 203 LEU H H 8.2460 . 1 739 203 203 LEU C C 175.86 . 1 740 203 203 LEU CA C 57.33 . 1 741 203 203 LEU CB C 41.59 . 1 742 203 203 LEU N N 128.67 . 1 743 204 204 VAL H H 7.8180 . 1 744 204 204 VAL C C 173.55 . 1 745 204 204 VAL CA C 61.71 . 1 746 204 204 VAL CB C 34.94 . 1 747 204 204 VAL N N 128.99 . 1 748 205 205 THR H H 7.4270 . 1 749 205 205 THR C C 176.67 . 1 750 205 205 THR CA C 58.18 . 1 751 205 205 THR CB C 71.56 . 1 752 205 205 THR N N 110.72 . 1 753 206 206 GLN H H 8.6500 . 1 754 206 206 GLN C C 179.44 . 1 755 206 206 GLN CA C 59.27 . 1 756 206 206 GLN CB C 29.22 . 1 757 206 206 GLN N N 117.84 . 1 758 207 207 GLU H H 9.3250 . 1 759 207 207 GLU C C 179.35 . 1 760 207 207 GLU CA C 61.05 . 1 761 207 207 GLU CB C 27.84 . 1 762 207 207 GLU N N 118.84 . 1 763 208 208 MET H H 7.4950 . 1 764 208 208 MET C C 177.14 . 1 765 208 208 MET CA C 58.77 . 1 766 208 208 MET CB C 30.91 . 1 767 208 208 MET N N 117.81 . 1 768 209 209 PHE H H 6.9610 . 1 769 209 209 PHE C C 177.13 . 1 770 209 209 PHE CA C 58.24 . 1 771 209 209 PHE CB C 37.20 . 1 772 209 209 PHE N N 113.73 . 1 773 210 210 GLN H H 7.3210 . 1 774 210 210 GLN C C 177.00 . 1 775 210 210 GLN CA C 58.65 . 1 776 210 210 GLN CB C 28.31 . 1 777 210 210 GLN N N 119.39 . 1 778 211 211 ASN H H 7.8130 . 1 779 211 211 ASN C C 176.23 . 1 780 211 211 ASN CA C 54.67 . 1 781 211 211 ASN CB C 38.47 . 1 782 211 211 ASN N N 114.63 . 1 783 212 212 ILE H H 7.0000 . 1 784 212 212 ILE C C 175.76 . 1 785 212 212 ILE CA C 63.51 . 1 786 212 212 ILE CB C 37.12 . 1 787 212 212 ILE N N 115.86 . 1 788 213 213 ASP H H 7.3950 . 1 789 213 213 ASP C C 175.91 . 1 790 213 213 ASP CA C 54.94 . 1 791 213 213 ASP CB C 40.91 . 1 792 213 213 ASP N N 120.44 . 1 793 214 214 LYS H H 7.5690 . 1 794 214 214 LYS CA C 56.63 . 1 795 214 214 LYS CB C 32.82 . 1 796 214 214 LYS N N 120.65 . 1 797 215 215 LYS H H 8.2410 . 1 798 215 215 LYS CA C 56.66 . 1 799 215 215 LYS CB C 32.55 . 1 800 215 215 LYS N N 123.76 . 1 801 216 216 ILE H H 8.1590 . 1 802 216 216 ILE CA C 61.45 . 1 803 216 216 ILE CB C 38.19 . 1 804 216 216 ILE N N 125.90 . 1 805 217 217 GLU H H 7.8580 . 1 806 217 217 GLU CA C 58.20 . 1 807 217 217 GLU CB C 31.03 . 1 808 217 217 GLU N N 129.95 . 1 stop_ save_