data_18421 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Capsid protein from Equine Infectious Anemia Virus ; _BMRB_accession_number 18421 _BMRB_flat_file_name bmr18421.str _Entry_type original _Submission_date 2012-04-24 _Accession_date 2012-04-24 _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 Chen Kang . . 2 Tjandra Nico . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 "13C chemical shifts" 588 "15N chemical shifts" 185 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-24 update BMRB 'update entry citation' 2012-09-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_eiavCA _Saveframe_category entry_citation _Citation_full . _Citation_title 'The maturational refolding of the -hairpin motif of equine infectious anemia virus capsid protein extends its helix 1 at capsid assembly locus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23184932 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chen Kang . . 2 Piszczek Grzegorz . . 3 Carter Carol . . 4 Tjandra Nico . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1511 _Page_last 1520 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'eiavCA monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label eiavCA $eiavCA stop_ _System_molecular_weight 26000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_eiavCA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common eiavCA _Molecular_mass . _Mol_thiol_state 'free and disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 230 _Mol_residue_sequence ; PIMIDGAGNRNFRPLTPRGY TTWVNTIQTNGLLNEASQNL FGILSVDCTSEEMNAFLDVV PGQAGQKQILLDAIDKIADD WDNRHPLPNAPLVAPPQGPI PMTARFIRGLGVPRERQMEP AFDQFRQTYRQWIIEAMSEG IKVMIGKPKAQNIRQGAKEP YPEFVDRLLSQIKSEGHPQE ISKFLTDTLTIQNANEECRN AMRHLRPEDTLEEKMYACRD IGTTKQKMML ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 ILE 3 MET 4 ILE 5 ASP 6 GLY 7 ALA 8 GLY 9 ASN 10 ARG 11 ASN 12 PHE 13 ARG 14 PRO 15 LEU 16 THR 17 PRO 18 ARG 19 GLY 20 TYR 21 THR 22 THR 23 TRP 24 VAL 25 ASN 26 THR 27 ILE 28 GLN 29 THR 30 ASN 31 GLY 32 LEU 33 LEU 34 ASN 35 GLU 36 ALA 37 SER 38 GLN 39 ASN 40 LEU 41 PHE 42 GLY 43 ILE 44 LEU 45 SER 46 VAL 47 ASP 48 CYS 49 THR 50 SER 51 GLU 52 GLU 53 MET 54 ASN 55 ALA 56 PHE 57 LEU 58 ASP 59 VAL 60 VAL 61 PRO 62 GLY 63 GLN 64 ALA 65 GLY 66 GLN 67 LYS 68 GLN 69 ILE 70 LEU 71 LEU 72 ASP 73 ALA 74 ILE 75 ASP 76 LYS 77 ILE 78 ALA 79 ASP 80 ASP 81 TRP 82 ASP 83 ASN 84 ARG 85 HIS 86 PRO 87 LEU 88 PRO 89 ASN 90 ALA 91 PRO 92 LEU 93 VAL 94 ALA 95 PRO 96 PRO 97 GLN 98 GLY 99 PRO 100 ILE 101 PRO 102 MET 103 THR 104 ALA 105 ARG 106 PHE 107 ILE 108 ARG 109 GLY 110 LEU 111 GLY 112 VAL 113 PRO 114 ARG 115 GLU 116 ARG 117 GLN 118 MET 119 GLU 120 PRO 121 ALA 122 PHE 123 ASP 124 GLN 125 PHE 126 ARG 127 GLN 128 THR 129 TYR 130 ARG 131 GLN 132 TRP 133 ILE 134 ILE 135 GLU 136 ALA 137 MET 138 SER 139 GLU 140 GLY 141 ILE 142 LYS 143 VAL 144 MET 145 ILE 146 GLY 147 LYS 148 PRO 149 LYS 150 ALA 151 GLN 152 ASN 153 ILE 154 ARG 155 GLN 156 GLY 157 ALA 158 LYS 159 GLU 160 PRO 161 TYR 162 PRO 163 GLU 164 PHE 165 VAL 166 ASP 167 ARG 168 LEU 169 LEU 170 SER 171 GLN 172 ILE 173 LYS 174 SER 175 GLU 176 GLY 177 HIS 178 PRO 179 GLN 180 GLU 181 ILE 182 SER 183 LYS 184 PHE 185 LEU 186 THR 187 ASP 188 THR 189 LEU 190 THR 191 ILE 192 GLN 193 ASN 194 ALA 195 ASN 196 GLU 197 GLU 198 CYS 199 ARG 200 ASN 201 ALA 202 MET 203 ARG 204 HIS 205 LEU 206 ARG 207 PRO 208 GLU 209 ASP 210 THR 211 LEU 212 GLU 213 GLU 214 LYS 215 MET 216 TYR 217 ALA 218 CYS 219 ARG 220 ASP 221 ILE 222 GLY 223 THR 224 THR 225 LYS 226 GLN 227 LYS 228 MET 229 MET 230 LEU 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 18815 his-eiav-ca 99.57 237 100.00 100.00 5.72e-169 PDB 1EIA "X-Ray Crystal Structure Of Equine Infectious Anemia Virus (Eiav) Capsid Protein P26" 90.00 207 100.00 100.00 2.12e-151 PDB 2EIA "X-Ray Crystal Structure Of Equine Infectious Anemia Virus (Eiav) Capsid Protein P26" 89.57 206 100.00 100.00 9.65e-151 DBJ BAB12103 "gag polyprotein [Equine infectious anemia virus]" 100.00 488 98.70 99.57 1.15e-165 DBJ BAB12109 "gag polyprotein [Equine infectious anemia virus]" 100.00 488 97.83 99.13 3.53e-164 GB AAA43003 "gag protein [Equine infectious anemia virus]" 100.00 486 100.00 100.00 1.87e-167 GB AAA43010 "gag protein, partial [Equine infectious anemia virus]" 100.00 365 100.00 100.00 1.68e-169 GB AAA43011 "gag [Equine infectious anemia virus]" 100.00 512 100.00 100.00 1.66e-166 GB AAB59861 "gag protein [Equine infectious anemia virus]" 100.00 486 100.00 100.00 1.87e-167 GB AAC03760 "gag polyprotein [Equine infectious anemia virus]" 100.00 486 100.00 100.00 1.87e-167 REF NP_056901 "gag protein [Equine infectious anemia virus]" 100.00 486 100.00 100.00 1.87e-167 SP P69730 "RecName: Full=Gag polyprotein; Contains: RecName: Full=Matrix protein p15; Short=MA; Contains: RecName: Full=Capsid protein p26" 100.00 486 100.00 100.00 1.87e-167 SP P69731 "RecName: Full=Gag polyprotein; Contains: RecName: Full=Matrix protein p15; Short=MA; Contains: RecName: Full=Capsid protein p26" 100.00 486 100.00 100.00 1.87e-167 SP P69732 "RecName: Full=Gag polyprotein; Contains: RecName: Full=Matrix protein p15; Short=MA; Contains: RecName: Full=Capsid protein p26" 100.00 486 100.00 100.00 1.87e-167 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $eiavCA 'equine infectious anemia virus' 11665 Viruses . Lentivirus 'equine infectious anemia virus' 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 $eiavCA 'recombinant technology' . Escherichia coli . pET 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 $eiavCA 0.15 mM '[U-13C; U-15N; U-2H]' NaCl 50 mM '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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HMQC-NOE-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HMQC-NOE-HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 0.05 . M pH 6.7 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCACB' '3D HN(CO)CACB' '3D 1H-15N NOESY' '3D HMQC-NOE-HSQC' 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 eiavCA _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 4 4 ILE H H 8.541 . 1 2 4 4 ILE C C 176.7 . 1 3 4 4 ILE CA C 59.98 . 1 4 4 4 ILE CB C 38.23 . 1 5 4 4 ILE N N 124.9 . 1 6 5 5 ASP H H 8.377 . 1 7 5 5 ASP C C 178.4 . 1 8 5 5 ASP CA C 52.38 . 1 9 5 5 ASP CB C 40.91 . 1 10 5 5 ASP N N 127.2 . 1 11 6 6 GLY H H 8.538 . 1 12 6 6 GLY C C 174.4 . 1 13 6 6 GLY CA C 46.11 . 1 14 6 6 GLY N N 105.2 . 1 15 7 7 ALA H H 8.014 . 1 16 7 7 ALA C C 177.6 . 1 17 7 7 ALA CA C 50.81 . 1 18 7 7 ALA CB C 18.51 . 1 19 7 7 ALA N N 122.2 . 1 20 8 8 GLY H H 7.995 . 1 21 8 8 GLY C C 174.8 . 1 22 8 8 GLY CA C 44.74 . 1 23 8 8 GLY N N 107.3 . 1 24 9 9 ASN H H 8.708 . 1 25 9 9 ASN C C 174.9 . 1 26 9 9 ASN CA C 53.20 . 1 27 9 9 ASN CB C 37.99 . 1 28 9 9 ASN N N 120.6 . 1 29 10 10 ARG H H 8.683 . 1 30 10 10 ARG C C 175.7 . 1 31 10 10 ARG CA C 54.93 . 1 32 10 10 ARG CB C 31.51 . 1 33 10 10 ARG N N 121.0 . 1 34 11 11 ASN H H 8.982 . 1 35 11 11 ASN C C 172.9 . 1 36 11 11 ASN CA C 51.99 . 1 37 11 11 ASN CB C 41.87 . 1 38 11 11 ASN N N 120.7 . 1 39 12 12 PHE H H 9.053 . 1 40 12 12 PHE C C 174.5 . 1 41 12 12 PHE CA C 57.55 . 1 42 12 12 PHE CB C 40.34 . 1 43 12 12 PHE N N 122.9 . 1 44 13 13 ARG H H 7.701 . 1 45 13 13 ARG C C 172.0 . 1 46 13 13 ARG CA C 51.45 . 1 47 13 13 ARG CB C 30.76 . 1 48 13 13 ARG N N 128.1 . 1 49 14 14 PRO C C 177.5 . 1 50 14 14 PRO CA C 61.66 . 1 51 14 14 PRO CB C 31.31 . 1 52 15 15 LEU H H 8.926 . 1 53 15 15 LEU C C 177.2 . 1 54 15 15 LEU CA C 55.09 . 1 55 15 15 LEU CB C 41.21 . 1 56 15 15 LEU N N 123.1 . 1 57 16 16 THR H H 7.958 . 1 58 16 16 THR C C 174.0 . 1 59 16 16 THR CA C 59.62 . 1 60 16 16 THR CB C 68.34 . 1 61 16 16 THR N N 115.1 . 1 62 22 22 THR C C 177.1 . 1 63 22 22 THR CA C 66.49 . 1 64 22 22 THR CB C 67.89 . 1 65 23 23 TRP H H 8.129 . 1 66 23 23 TRP C C 175.8 . 1 67 23 23 TRP CA C 59.64 . 1 68 23 23 TRP N N 125.7 . 1 69 24 24 VAL H H 8.541 . 1 70 24 24 VAL C C 178.4 . 1 71 24 24 VAL CA C 66.68 . 1 72 24 24 VAL CB C 30.87 . 1 73 24 24 VAL N N 117.2 . 1 74 25 25 ASN H H 8.584 . 1 75 25 25 ASN C C 178.5 . 1 76 25 25 ASN CA C 55.89 . 1 77 25 25 ASN CB C 37.56 . 1 78 25 25 ASN N N 116.8 . 1 79 26 26 THR H H 8.094 . 1 80 26 26 THR C C 176.3 . 1 81 26 26 THR CA C 66.97 . 1 82 26 26 THR CB C 67.69 . 1 83 26 26 THR N N 118.3 . 1 84 27 27 ILE H H 7.896 . 1 85 27 27 ILE C C 179.3 . 1 86 27 27 ILE CA C 62.62 . 1 87 27 27 ILE CB C 35.25 . 1 88 27 27 ILE N N 121.9 . 1 89 28 28 GLN H H 8.380 . 1 90 28 28 GLN C C 177.9 . 1 91 28 28 GLN CA C 58.55 . 1 92 28 28 GLN CB C 27.94 . 1 93 28 28 GLN N N 120.1 . 1 94 29 29 THR H H 7.671 . 1 95 29 29 THR C C 175.4 . 1 96 29 29 THR CA C 64.88 . 1 97 29 29 THR CB C 69.10 . 1 98 29 29 THR N N 111.3 . 1 99 30 30 ASN H H 8.081 . 1 100 30 30 ASN C C 175.5 . 1 101 30 30 ASN CA C 54.44 . 1 102 30 30 ASN CB C 40.59 . 1 103 30 30 ASN N N 116.0 . 1 104 31 31 GLY H H 7.799 . 1 105 31 31 GLY C C 172.5 . 1 106 31 31 GLY CA C 43.37 . 1 107 31 31 GLY N N 108.6 . 1 108 32 32 LEU H H 8.093 . 1 109 32 32 LEU C C 175.8 . 1 110 32 32 LEU CA C 57.09 . 1 111 32 32 LEU CB C 42.43 . 1 112 32 32 LEU N N 121.3 . 1 113 33 33 LEU H H 8.166 . 1 114 33 33 LEU C C 174.6 . 1 115 33 33 LEU CA C 51.17 . 1 116 33 33 LEU CB C 38.06 . 1 117 33 33 LEU N N 114.1 . 1 118 34 34 ASN H H 7.561 . 1 119 34 34 ASN C C 174.6 . 1 120 34 34 ASN CA C 52.81 . 1 121 34 34 ASN CB C 43.29 . 1 122 34 34 ASN N N 119.5 . 1 123 35 35 GLU H H 9.825 . 1 124 35 35 GLU C C 177.2 . 1 125 35 35 GLU CA C 60.25 . 1 126 35 35 GLU CB C 28.63 . 1 127 35 35 GLU N N 127.5 . 1 128 36 36 ALA H H 8.580 . 1 129 36 36 ALA C C 181.6 . 1 130 36 36 ALA CA C 54.88 . 1 131 36 36 ALA CB C 17.04 . 1 132 36 36 ALA N N 121.9 . 1 133 37 37 SER H H 7.330 . 1 134 37 37 SER C C 175.7 . 1 135 37 37 SER N N 117.2 . 1 136 38 38 GLN H H 8.341 . 1 137 38 38 GLN C C 178.2 . 1 138 38 38 GLN CA C 58.52 . 1 139 38 38 GLN CB C 28.92 . 1 140 38 38 GLN N N 123.4 . 1 141 39 39 ASN H H 8.706 . 1 142 39 39 ASN C C 178.2 . 1 143 39 39 ASN CA C 55.63 . 1 144 39 39 ASN CB C 37.70 . 1 145 39 39 ASN N N 118.7 . 1 146 40 40 LEU H H 7.898 . 1 147 40 40 LEU C C 178.3 . 1 148 40 40 LEU CA C 57.23 . 1 149 40 40 LEU CB C 40.56 . 1 150 40 40 LEU N N 120.0 . 1 151 41 41 PHE H H 9.043 . 1 152 41 41 PHE C C 179.3 . 1 153 41 41 PHE CA C 62.11 . 1 154 41 41 PHE CB C 37.77 . 1 155 41 41 PHE N N 118.9 . 1 156 42 42 GLY H H 8.526 . 1 157 42 42 GLY C C 175.4 . 1 158 42 42 GLY CA C 47.03 . 1 159 42 42 GLY N N 107.0 . 1 160 43 43 ILE H H 7.432 . 1 161 45 45 SER H H 7.529 . 1 162 51 51 GLU C C 179.7 . 1 163 51 51 GLU CA C 59.02 . 1 164 51 51 GLU CB C 28.32 . 1 165 52 52 GLU H H 7.855 . 1 166 52 52 GLU C C 179.2 . 1 167 52 52 GLU CA C 58.75 . 1 168 52 52 GLU CB C 29.95 . 1 169 52 52 GLU N N 119.6 . 1 170 54 54 ASN C C 177.9 . 1 171 54 54 ASN CA C 56.12 . 1 172 55 55 ALA H H 7.934 . 1 173 55 55 ALA C C 180.8 . 1 174 55 55 ALA CA C 54.94 . 1 175 55 55 ALA N N 124.0 . 1 176 56 56 PHE H H 7.885 . 1 177 56 56 PHE C C 179.2 . 1 178 56 56 PHE CA C 61.28 . 1 179 56 56 PHE CB C 37.08 . 1 180 56 56 PHE N N 116.2 . 1 181 57 57 LEU H H 7.552 . 1 182 57 57 LEU C C 178.5 . 1 183 57 57 LEU CA C 56.78 . 1 184 57 57 LEU CB C 39.87 . 1 185 57 57 LEU N N 116.5 . 1 186 58 58 ASP H H 8.122 . 1 187 58 58 ASP C C 178.0 . 1 188 58 58 ASP CA C 55.99 . 1 189 58 58 ASP CB C 40.74 . 1 190 58 58 ASP N N 118.0 . 1 191 59 59 VAL H H 7.416 . 1 192 59 59 VAL C C 175.6 . 1 193 59 59 VAL CA C 61.83 . 1 194 59 59 VAL CB C 31.09 . 1 195 59 59 VAL N N 112.3 . 1 196 60 60 VAL H H 7.270 . 1 197 60 60 VAL C C 174.4 . 1 198 60 60 VAL CA C 60.28 . 1 199 60 60 VAL CB C 31.62 . 1 200 60 60 VAL N N 121.3 . 1 201 61 61 PRO C C 176.9 . 1 202 61 61 PRO CA C 61.77 . 1 203 61 61 PRO CB C 30.76 . 1 204 62 62 GLY H H 8.471 . 1 205 62 62 GLY C C 174.5 . 1 206 62 62 GLY CA C 45.91 . 1 207 62 62 GLY N N 109.4 . 1 208 63 63 GLN H H 8.490 . 1 209 63 63 GLN C C 176.3 . 1 210 63 63 GLN CA C 55.23 . 1 211 63 63 GLN CB C 26.53 . 1 212 63 63 GLN N N 117.7 . 1 213 64 64 ALA H H 8.305 . 1 214 64 64 ALA CA C 54.56 . 1 215 64 64 ALA CB C 17.67 . 1 216 64 64 ALA N N 121.1 . 1 217 65 65 GLY C C 176.6 . 1 218 65 65 GLY CA C 46.15 . 1 219 66 66 GLN H H 7.979 . 1 220 66 66 GLN C C 177.8 . 1 221 66 66 GLN CA C 59.37 . 1 222 66 66 GLN CB C 27.90 . 1 223 66 66 GLN N N 120.8 . 1 224 67 67 LYS H H 8.441 . 1 225 67 67 LYS C C 177.6 . 1 226 67 67 LYS CA C 59.41 . 1 227 67 67 LYS CB C 31.38 . 1 228 67 67 LYS N N 118.8 . 1 229 68 68 GLN H H 7.882 . 1 230 68 68 GLN C C 177.6 . 1 231 68 68 GLN CA C 58.13 . 1 232 68 68 GLN CB C 27.43 . 1 233 68 68 GLN N N 117.7 . 1 234 69 69 ILE H H 7.363 . 1 235 69 69 ILE C C 179.1 . 1 236 69 69 ILE CA C 64.44 . 1 237 69 69 ILE CB C 37.26 . 1 238 69 69 ILE N N 118.5 . 1 239 70 70 LEU H H 7.837 . 1 240 70 70 LEU C C 177.9 . 1 241 70 70 LEU CA C 57.85 . 1 242 70 70 LEU CB C 40.72 . 1 243 70 70 LEU N N 120.3 . 1 244 71 71 LEU H H 8.752 . 1 245 71 71 LEU C C 179.7 . 1 246 71 71 LEU CA C 57.96 . 1 247 71 71 LEU CB C 39.45 . 1 248 71 71 LEU N N 119.2 . 1 249 72 72 ASP H H 8.661 . 1 250 72 72 ASP C C 179.0 . 1 251 72 72 ASP CA C 56.88 . 1 252 72 72 ASP CB C 39.34 . 1 253 72 72 ASP N N 119.5 . 1 254 73 73 ALA H H 7.804 . 1 255 73 73 ALA C C 180.8 . 1 256 73 73 ALA CA C 54.73 . 1 257 73 73 ALA CB C 17.18 . 1 258 73 73 ALA N N 122.9 . 1 259 74 74 ILE H H 8.429 . 1 260 74 74 ILE C C 177.4 . 1 261 74 74 ILE CA C 65.71 . 1 262 74 74 ILE CB C 37.10 . 1 263 74 74 ILE N N 120.6 . 1 264 75 75 ASP H H 8.464 . 1 265 75 75 ASP C C 178.3 . 1 266 75 75 ASP CA C 57.16 . 1 267 75 75 ASP CB C 39.14 . 1 268 75 75 ASP N N 119.6 . 1 269 76 76 LYS H H 7.513 . 1 270 76 76 LYS C C 179.5 . 1 271 76 76 LYS CA C 59.03 . 1 272 76 76 LYS CB C 31.42 . 1 273 76 76 LYS N N 118.9 . 1 274 77 77 ILE H H 7.293 . 1 275 77 77 ILE C C 178.4 . 1 276 77 77 ILE CA C 64.79 . 1 277 77 77 ILE CB C 37.75 . 1 278 77 77 ILE N N 122.8 . 1 279 78 78 ALA H H 8.486 . 1 280 78 78 ALA C C 178.9 . 1 281 78 78 ALA CA C 53.91 . 1 282 78 78 ALA CB C 18.60 . 1 283 78 78 ALA N N 124.3 . 1 284 79 79 ASP H H 8.383 . 1 285 79 79 ASP C C 179.2 . 1 286 79 79 ASP CA C 56.93 . 1 287 79 79 ASP CB C 39.67 . 1 288 79 79 ASP N N 118.3 . 1 289 80 80 ASP H H 7.693 . 1 290 80 80 ASP C C 177.9 . 1 291 80 80 ASP CA C 57.10 . 1 292 80 80 ASP CB C 40.84 . 1 293 80 80 ASP N N 120.3 . 1 294 81 81 TRP H H 8.436 . 1 295 81 81 TRP C C 180.2 . 1 296 81 81 TRP CA C 61.59 . 1 297 81 81 TRP CB C 27.70 . 1 298 81 81 TRP N N 120.6 . 1 299 82 82 ASP H H 8.539 . 1 300 82 82 ASP C C 178.8 . 1 301 82 82 ASP CA C 57.22 . 1 302 82 82 ASP CB C 39.19 . 1 303 82 82 ASP N N 119.9 . 1 304 83 83 ASN H H 8.182 . 1 305 83 83 ASN C C 177.2 . 1 306 83 83 ASN CA C 55.54 . 1 307 83 83 ASN CB C 38.11 . 1 308 83 83 ASN N N 118.6 . 1 309 84 84 ARG H H 7.615 . 1 310 84 84 ARG C C 175.5 . 1 311 84 84 ARG CA C 56.33 . 1 312 84 84 ARG CB C 29.64 . 1 313 84 84 ARG N N 116.1 . 1 314 85 85 HIS H H 7.592 . 1 315 85 85 HIS C C 179.8 . 1 316 85 85 HIS CA C 52.59 . 1 317 85 85 HIS CB C 26.77 . 1 318 85 85 HIS N N 117.3 . 1 319 86 86 PRO C C 177.9 . 1 320 86 86 PRO CA C 63.50 . 1 321 86 86 PRO CB C 31.43 . 1 322 87 87 LEU H H 8.471 . 1 323 87 87 LEU C C 174.0 . 1 324 87 87 LEU CA C 52.08 . 1 325 87 87 LEU CB C 42.23 . 1 326 87 87 LEU N N 124.6 . 1 327 88 88 PRO C C 177.1 . 1 328 88 88 PRO CA C 63.03 . 1 329 88 88 PRO CB C 31.15 . 1 330 89 89 ASN H H 8.752 . 1 331 89 89 ASN C C 174.7 . 1 332 89 89 ASN CA C 52.85 . 1 333 89 89 ASN CB C 37.23 . 1 334 89 89 ASN N N 116.0 . 1 335 90 90 ALA H H 7.719 . 1 336 90 90 ALA C C 175.5 . 1 337 90 90 ALA CA C 50.63 . 1 338 90 90 ALA CB C 17.17 . 1 339 90 90 ALA N N 122.8 . 1 340 91 91 PRO C C 174.8 . 1 341 91 91 PRO CA C 61.81 . 1 342 91 91 PRO CB C 31.73 . 1 343 92 92 LEU H H 8.393 . 1 344 92 92 LEU C C 178.1 . 1 345 92 92 LEU CA C 54.97 . 1 346 92 92 LEU CB C 41.99 . 1 347 92 92 LEU N N 115.5 . 1 348 93 93 VAL H H 7.439 . 1 349 93 93 VAL C C 175.0 . 1 350 93 93 VAL CA C 59.36 . 1 351 93 93 VAL CB C 33.80 . 1 352 93 93 VAL N N 115.7 . 1 353 94 94 ALA H H 8.281 . 1 354 94 94 ALA C C 173.8 . 1 355 94 94 ALA CA C 49.81 . 1 356 94 94 ALA CB C 16.29 . 1 357 94 94 ALA N N 128.1 . 1 358 96 96 PRO C C 176.1 . 1 359 96 96 PRO CA C 63.84 . 1 360 96 96 PRO CB C 31.00 . 1 361 97 97 GLN H H 7.259 . 1 362 97 97 GLN C C 175.3 . 1 363 97 97 GLN CA C 53.66 . 1 364 97 97 GLN CB C 31.33 . 1 365 97 97 GLN N N 112.7 . 1 366 98 98 GLY H H 8.700 . 1 367 98 98 GLY C C 180.9 . 1 368 98 98 GLY CA C 44.23 . 1 369 98 98 GLY N N 108.5 . 1 370 99 99 PRO C C 177.5 . 1 371 99 99 PRO CA C 62.69 . 1 372 99 99 PRO CB C 32.45 . 1 373 100 100 ILE H H 9.455 . 1 374 100 100 ILE C C 173.9 . 1 375 100 100 ILE CA C 63.78 . 1 376 100 100 ILE CB C 35.98 . 1 377 100 100 ILE N N 127.0 . 1 378 101 101 PRO C C 176.4 . 1 379 101 101 PRO CA C 62.58 . 1 380 101 101 PRO CB C 31.51 . 1 381 102 102 MET H H 8.827 . 1 382 102 102 MET C C 176.2 . 1 383 102 102 MET CA C 54.68 . 1 384 102 102 MET CB C 29.92 . 1 385 102 102 MET N N 125.1 . 1 386 103 103 THR H H 8.095 . 1 387 103 103 THR C C 174.6 . 1 388 103 103 THR CA C 58.65 . 1 389 103 103 THR CB C 70.05 . 1 390 103 103 THR N N 116.0 . 1 391 104 104 ALA H H 10.28 . 1 392 104 104 ALA C C 179.6 . 1 393 104 104 ALA CA C 55.79 . 1 394 104 104 ALA CB C 18.23 . 1 395 104 104 ALA N N 124.6 . 1 396 105 105 ARG H H 8.745 . 1 397 105 105 ARG C C 177.1 . 1 398 105 105 ARG CA C 59.60 . 1 399 105 105 ARG CB C 29.07 . 1 400 105 105 ARG N N 116.0 . 1 401 106 106 PHE H H 7.206 . 1 402 106 106 PHE C C 180.9 . 1 403 106 106 PHE CA C 56.22 . 1 404 106 106 PHE CB C 36.35 . 1 405 106 106 PHE N N 115.1 . 1 406 107 107 ILE H H 8.583 . 1 407 107 107 ILE C C 175.8 . 1 408 107 107 ILE CA C 66.71 . 1 409 107 107 ILE CB C 36.97 . 1 410 107 107 ILE N N 125.2 . 1 411 108 108 ARG H H 7.290 . 1 412 108 108 ARG C C 175.1 . 1 413 108 108 ARG CA C 55.73 . 1 414 108 108 ARG CB C 30.19 . 1 415 108 108 ARG N N 113.7 . 1 416 109 109 GLY H H 7.931 . 1 417 109 109 GLY C C 174.4 . 1 418 109 109 GLY CA C 44.88 . 1 419 109 109 GLY N N 104.5 . 1 420 110 110 LEU H H 8.236 . 1 421 110 110 LEU C C 175.9 . 1 422 110 110 LEU CA C 55.03 . 1 423 110 110 LEU CB C 39.00 . 1 424 110 110 LEU N N 124.9 . 1 425 111 111 GLY H H 8.546 . 1 426 111 111 GLY C C 174.3 . 1 427 111 111 GLY CA C 45.25 . 1 428 111 111 GLY N N 108.7 . 1 429 112 112 VAL H H 7.144 . 1 430 112 112 VAL C C 174.0 . 1 431 112 112 VAL CA C 57.94 . 1 432 112 112 VAL CB C 31.48 . 1 433 112 112 VAL N N 118.7 . 1 434 113 113 PRO C C 177.5 . 1 435 113 113 PRO CA C 62.53 . 1 436 113 113 PRO CB C 31.95 . 1 437 114 114 ARG H H 8.943 . 1 438 114 114 ARG C C 177.9 . 1 439 114 114 ARG CA C 59.83 . 1 440 114 114 ARG CB C 28.97 . 1 441 114 114 ARG N N 125.2 . 1 442 115 115 GLU H H 9.336 . 1 443 115 115 GLU C C 180.0 . 1 444 115 115 GLU CA C 59.86 . 1 445 115 115 GLU CB C 27.53 . 1 446 115 115 GLU N N 115.6 . 1 447 116 116 ARG H H 6.936 . 1 448 116 116 ARG C C 178.0 . 1 449 116 116 ARG CA C 58.19 . 1 450 116 116 ARG CB C 27.50 . 1 451 116 116 ARG N N 114.6 . 1 452 117 117 GLN H H 7.174 . 1 453 117 117 GLN C C 176.1 . 1 454 117 117 GLN CA C 56.72 . 1 455 117 117 GLN CB C 26.30 . 1 456 117 117 GLN N N 116.2 . 1 457 118 118 MET H H 6.810 . 1 458 118 118 MET C C 176.2 . 1 459 118 118 MET CA C 54.89 . 1 460 118 118 MET CB C 32.81 . 1 461 118 118 MET N N 113.4 . 1 462 119 119 GLU H H 6.879 . 1 463 119 119 GLU C C 176.9 . 1 464 119 119 GLU CA C 54.72 . 1 465 119 119 GLU CB C 28.69 . 1 466 119 119 GLU N N 117.9 . 1 467 120 120 PRO C C 179.2 . 1 468 121 121 ALA H H 7.948 . 1 469 121 121 ALA C C 178.0 . 1 470 121 121 ALA CA C 53.82 . 1 471 121 121 ALA CB C 17.92 . 1 472 121 121 ALA N N 116.3 . 1 473 122 122 PHE H H 8.195 . 1 474 122 122 PHE C C 178.0 . 1 475 122 122 PHE CA C 56.80 . 1 476 122 122 PHE CB C 39.72 . 1 477 122 122 PHE N N 118.1 . 1 478 123 123 ASP H H 8.248 . 1 479 123 123 ASP C C 178.3 . 1 480 123 123 ASP CA C 58.17 . 1 481 123 123 ASP CB C 38.50 . 1 482 123 123 ASP N N 125.1 . 1 483 124 124 GLN H H 8.936 . 1 484 124 124 GLN C C 178.1 . 1 485 124 124 GLN CA C 57.42 . 1 486 124 124 GLN N N 114.1 . 1 487 125 125 PHE H H 7.670 . 1 488 125 125 PHE C C 176.1 . 1 489 125 125 PHE CA C 59.97 . 1 490 125 125 PHE N N 121.9 . 1 491 127 127 GLN C C 179.6 . 1 492 127 127 GLN CA C 58.49 . 1 493 127 127 GLN CB C 27.40 . 1 494 128 128 THR H H 7.072 . 1 495 128 128 THR CA C 66.19 . 1 496 128 128 THR N N 117.5 . 1 497 129 129 TYR H H 7.905 . 1 498 134 134 ILE C C 179.1 . 1 499 134 134 ILE CA C 66.65 . 1 500 135 135 GLU H H 8.722 . 1 501 135 135 GLU C C 179.5 . 1 502 135 135 GLU CA C 58.85 . 1 503 135 135 GLU CB C 28.28 . 1 504 135 135 GLU N N 120.9 . 1 505 136 136 ALA H H 9.177 . 1 506 136 136 ALA C C 180.2 . 1 507 136 136 ALA CA C 54.64 . 1 508 136 136 ALA CB C 19.28 . 1 509 136 136 ALA N N 124.1 . 1 510 137 137 MET H H 8.699 . 1 511 137 137 MET C C 177.7 . 1 512 137 137 MET CA C 59.92 . 1 513 137 137 MET CB C 31.95 . 1 514 137 137 MET N N 118.0 . 1 515 138 138 SER H H 7.882 . 1 516 138 138 SER C C 177.3 . 1 517 138 138 SER CA C 62.25 . 1 518 138 138 SER CB C 63.24 . 1 519 138 138 SER N N 116.1 . 1 520 139 139 GLU H H 8.134 . 1 521 139 139 GLU C C 179.3 . 1 522 139 139 GLU CA C 58.37 . 1 523 139 139 GLU CB C 28.08 . 1 524 139 139 GLU N N 121.9 . 1 525 140 140 GLY H H 8.869 . 1 526 140 140 GLY C C 175.2 . 1 527 140 140 GLY CA C 47.25 . 1 528 140 140 GLY N N 108.1 . 1 529 141 141 ILE H H 8.600 . 1 530 141 141 ILE C C 177.8 . 1 531 141 141 ILE CA C 65.85 . 1 532 141 141 ILE CB C 37.66 . 1 533 141 141 ILE N N 123.1 . 1 534 142 142 LYS H H 7.305 . 1 535 142 142 LYS C C 179.9 . 1 536 142 142 LYS CA C 59.37 . 1 537 142 142 LYS CB C 31.24 . 1 538 142 142 LYS N N 117.7 . 1 539 143 143 VAL H H 7.829 . 1 540 143 143 VAL C C 178.5 . 1 541 143 143 VAL CA C 64.99 . 1 542 143 143 VAL CB C 31.00 . 1 543 143 143 VAL N N 119.0 . 1 544 144 144 MET H H 7.883 . 1 545 144 144 MET C C 178.8 . 1 546 144 144 MET CA C 56.13 . 1 547 144 144 MET CB C 30.48 . 1 548 144 144 MET N N 117.8 . 1 549 145 145 ILE H H 7.960 . 1 550 145 145 ILE C C 177.5 . 1 551 145 145 ILE CA C 62.70 . 1 552 145 145 ILE CB C 37.24 . 1 553 145 145 ILE N N 118.4 . 1 554 146 146 GLY H H 7.826 . 1 555 146 146 GLY C C 174.0 . 1 556 146 146 GLY CA C 44.79 . 1 557 146 146 GLY N N 108.6 . 1 558 147 147 LYS H H 7.789 . 1 559 147 147 LYS C C 174.5 . 1 560 147 147 LYS CA C 53.89 . 1 561 147 147 LYS CB C 31.24 . 1 562 147 147 LYS N N 121.8 . 1 563 148 148 PRO C C 175.9 . 1 564 148 148 PRO CA C 62.89 . 1 565 148 148 PRO CB C 31.25 . 1 566 149 149 LYS H H 8.008 . 1 567 149 149 LYS C C 178.4 . 1 568 149 149 LYS CA C 54.49 . 1 569 149 149 LYS CB C 34.32 . 1 570 149 149 LYS N N 118.8 . 1 571 150 150 ALA H H 10.32 . 1 572 150 150 ALA C C 177.8 . 1 573 150 150 ALA CA C 55.85 . 1 574 150 150 ALA CB C 17.95 . 1 575 150 150 ALA N N 127.3 . 1 576 151 151 GLN H H 8.810 . 1 577 151 151 GLN C C 176.4 . 1 578 151 151 GLN CA C 58.85 . 1 579 151 151 GLN CB C 27.00 . 1 580 151 151 GLN N N 110.8 . 1 581 152 152 ASN H H 8.005 . 1 582 152 152 ASN C C 175.0 . 1 583 152 152 ASN CA C 52.40 . 1 584 152 152 ASN CB C 38.88 . 1 585 152 152 ASN N N 114.7 . 1 586 153 153 ILE H H 7.674 . 1 587 153 153 ILE C C 174.1 . 1 588 153 153 ILE CA C 60.04 . 1 589 153 153 ILE CB C 33.69 . 1 590 153 153 ILE N N 123.3 . 1 591 154 154 ARG H H 8.310 . 1 592 154 154 ARG C C 175.6 . 1 593 154 154 ARG CA C 53.71 . 1 594 154 154 ARG CB C 32.19 . 1 595 154 154 ARG N N 125.8 . 1 596 155 155 GLN H H 7.478 . 1 597 155 155 GLN C C 177.1 . 1 598 155 155 GLN CA C 54.73 . 1 599 155 155 GLN CB C 26.64 . 1 600 155 155 GLN N N 125.8 . 1 601 156 156 GLY H H 9.798 . 1 602 156 156 GLY C C 175.5 . 1 603 156 156 GLY CA C 44.77 . 1 604 156 156 GLY N N 116.3 . 1 605 157 157 ALA H H 8.955 . 1 606 157 157 ALA C C 178.4 . 1 607 157 157 ALA CA C 55.45 . 1 608 157 157 ALA CB C 18.04 . 1 609 157 157 ALA N N 125.8 . 1 610 158 158 LYS H H 8.575 . 1 611 158 158 LYS C C 175.4 . 1 612 158 158 LYS CA C 53.29 . 1 613 158 158 LYS CB C 31.20 . 1 614 158 158 LYS N N 113.6 . 1 615 159 159 GLU H H 6.911 . 1 616 159 159 GLU C C 174.3 . 1 617 159 159 GLU CA C 52.78 . 1 618 159 159 GLU CB C 31.33 . 1 619 159 159 GLU N N 124.5 . 1 620 160 160 PRO C C 176.6 . 1 621 160 160 PRO CA C 62.58 . 1 622 160 160 PRO CB C 31.09 . 1 623 161 161 TYR H H 8.673 . 1 624 161 161 TYR C C 174.1 . 1 625 161 161 TYR CA C 58.41 . 1 626 161 161 TYR CB C 38.47 . 1 627 161 161 TYR N N 125.2 . 1 628 162 162 PRO C C 178.8 . 1 629 162 162 PRO CA C 65.91 . 1 630 162 162 PRO CB C 30.22 . 1 631 163 163 GLU H H 6.899 . 1 632 163 163 GLU C C 179.1 . 1 633 163 163 GLU CA C 58.54 . 1 634 163 163 GLU CB C 28.64 . 1 635 163 163 GLU N N 114.9 . 1 636 164 164 PHE H H 7.343 . 1 637 164 164 PHE C C 175.7 . 1 638 164 164 PHE CA C 58.81 . 1 639 164 164 PHE CB C 37.73 . 1 640 164 164 PHE N N 122.7 . 1 641 165 165 VAL H H 8.201 . 1 642 165 165 VAL C C 177.2 . 1 643 165 165 VAL CA C 66.24 . 1 644 165 165 VAL CB C 30.12 . 1 645 165 165 VAL N N 119.5 . 1 646 166 166 ASP H H 7.513 . 1 647 166 166 ASP C C 179.3 . 1 648 166 166 ASP CA C 57.35 . 1 649 166 166 ASP CB C 40.27 . 1 650 166 166 ASP N N 117.6 . 1 651 167 167 ARG H H 7.541 . 1 652 167 167 ARG C C 179.5 . 1 653 167 167 ARG CA C 59.25 . 1 654 167 167 ARG CB C 29.16 . 1 655 167 167 ARG N N 119.2 . 1 656 168 168 LEU H H 8.462 . 1 657 168 168 LEU C C 178.3 . 1 658 168 168 LEU CA C 57.86 . 1 659 168 168 LEU CB C 40.76 . 1 660 168 168 LEU N N 122.7 . 1 661 169 169 LEU H H 9.137 . 1 662 169 169 LEU C C 180.6 . 1 663 169 169 LEU CA C 58.21 . 1 664 169 169 LEU CB C 39.13 . 1 665 169 169 LEU N N 118.9 . 1 666 170 170 SER H H 7.921 . 1 667 170 170 SER C C 177.1 . 1 668 170 170 SER CA C 61.52 . 1 669 170 170 SER CB C 62.46 . 1 670 170 170 SER N N 114.1 . 1 671 171 171 GLN H H 7.550 . 1 672 171 171 GLN C C 178.9 . 1 673 171 171 GLN CA C 57.52 . 1 674 171 171 GLN CB C 26.58 . 1 675 171 171 GLN N N 122.0 . 1 676 172 172 ILE H H 8.771 . 1 677 172 172 ILE C C 179.7 . 1 678 172 172 ILE CA C 66.30 . 1 679 172 172 ILE CB C 37.81 . 1 680 172 172 ILE N N 120.1 . 1 681 173 173 LYS H H 8.370 . 1 682 173 173 LYS C C 179.3 . 1 683 173 173 LYS CA C 59.27 . 1 684 173 173 LYS CB C 31.25 . 1 685 173 173 LYS N N 120.1 . 1 686 174 174 SER H H 7.810 . 1 687 174 174 SER C C 175.2 . 1 688 174 174 SER CA C 60.38 . 1 689 174 174 SER CB C 62.58 . 1 690 174 174 SER N N 115.0 . 1 691 175 175 GLU H H 7.381 . 1 692 175 175 GLU C C 178.0 . 1 693 175 175 GLU CA C 56.87 . 1 694 175 175 GLU CB C 29.62 . 1 695 175 175 GLU N N 119.9 . 1 696 176 176 GLY H H 7.384 . 1 697 176 176 GLY C C 174.8 . 1 698 176 176 GLY CA C 47.19 . 1 699 176 176 GLY N N 106.0 . 1 700 177 177 HIS H H 8.539 . 1 701 177 177 HIS C C 174.5 . 1 702 177 177 HIS CA C 54.60 . 1 703 177 177 HIS CB C 30.09 . 1 704 177 177 HIS N N 119.2 . 1 705 178 178 PRO C C 177.9 . 1 706 179 179 GLN H H 9.043 . 1 707 179 179 GLN C C 177.7 . 1 708 179 179 GLN CA C 59.27 . 1 709 179 179 GLN CB C 27.68 . 1 710 179 179 GLN N N 123.6 . 1 711 180 180 GLU H H 9.721 . 1 712 180 180 GLU C C 179.4 . 1 713 180 180 GLU CA C 59.41 . 1 714 180 180 GLU CB C 27.62 . 1 715 180 180 GLU N N 117.8 . 1 716 181 181 ILE H H 7.181 . 1 717 181 181 ILE C C 177.5 . 1 718 181 181 ILE CA C 62.25 . 1 719 181 181 ILE CB C 36.59 . 1 720 181 181 ILE N N 120.4 . 1 721 182 182 SER H H 8.561 . 1 722 182 182 SER C C 177.9 . 1 723 182 182 SER CA C 62.24 . 1 724 182 182 SER N N 116.5 . 1 725 183 183 LYS H H 8.330 . 1 726 183 183 LYS C C 176.8 . 1 727 183 183 LYS CA C 59.41 . 1 728 183 183 LYS CB C 31.30 . 1 729 183 183 LYS N N 123.6 . 1 730 184 184 PHE H H 7.406 . 1 731 184 184 PHE C C 179.3 . 1 732 184 184 PHE CA C 60.89 . 1 733 184 184 PHE CB C 38.51 . 1 734 184 184 PHE N N 119.9 . 1 735 185 185 LEU H H 8.910 . 1 736 185 185 LEU C C 178.1 . 1 737 185 185 LEU CA C 57.15 . 1 738 185 185 LEU CB C 41.63 . 1 739 185 185 LEU N N 120.2 . 1 740 186 186 THR H H 8.141 . 1 741 186 186 THR C C 176.1 . 1 742 186 186 THR CA C 67.32 . 1 743 186 186 THR CB C 67.91 . 1 744 186 186 THR N N 116.4 . 1 745 187 187 ASP H H 8.815 . 1 746 187 187 ASP C C 176.4 . 1 747 187 187 ASP CA C 57.18 . 1 748 187 187 ASP CB C 39.21 . 1 749 187 187 ASP N N 122.9 . 1 750 188 188 THR H H 7.565 . 1 751 188 188 THR C C 178.7 . 1 752 188 188 THR CA C 64.12 . 1 753 188 188 THR CB C 69.09 . 1 754 188 188 THR N N 105.2 . 1 755 189 189 LEU H H 8.753 . 1 756 189 189 LEU C C 179.0 . 1 757 189 189 LEU CA C 58.28 . 1 758 189 189 LEU CB C 40.38 . 1 759 189 189 LEU N N 122.2 . 1 760 190 190 THR H H 7.281 . 1 761 190 190 THR C C 175.9 . 1 762 190 190 THR CA C 64.02 . 1 763 190 190 THR CB C 68.25 . 1 764 190 190 THR N N 105.7 . 1 765 191 191 ILE H H 6.739 . 1 766 191 191 ILE C C 176.7 . 1 767 191 191 ILE CA C 62.48 . 1 768 191 191 ILE CB C 38.44 . 1 769 191 191 ILE N N 117.0 . 1 770 192 192 GLN H H 8.322 . 1 771 192 192 GLN C C 176.9 . 1 772 192 192 GLN CA C 58.40 . 1 773 192 192 GLN CB C 28.95 . 1 774 192 192 GLN N N 114.1 . 1 775 193 193 ASN H H 8.061 . 1 776 193 193 ASN C C 175.0 . 1 777 193 193 ASN CA C 51.91 . 1 778 193 193 ASN CB C 35.83 . 1 779 193 193 ASN N N 114.3 . 1 780 194 194 ALA H H 7.014 . 1 781 194 194 ALA C C 175.9 . 1 782 194 194 ALA CA C 51.22 . 1 783 194 194 ALA CB C 18.67 . 1 784 194 194 ALA N N 123.3 . 1 785 195 195 ASN H H 9.032 . 1 786 195 195 ASN C C 174.6 . 1 787 195 195 ASN CA C 51.33 . 1 788 195 195 ASN CB C 36.34 . 1 789 195 195 ASN N N 118.8 . 1 790 196 196 GLU H H 8.360 . 1 791 196 196 GLU C C 178.5 . 1 792 196 196 GLU CA C 60.12 . 1 793 196 196 GLU CB C 29.04 . 1 794 196 196 GLU N N 118.0 . 1 795 197 197 GLU H H 8.271 . 1 796 197 197 GLU C C 179.6 . 1 797 197 197 GLU CA C 59.29 . 1 798 197 197 GLU CB C 28.82 . 1 799 197 197 GLU N N 118.6 . 1 800 198 198 CYS H H 8.907 . 1 801 198 198 CYS C C 176.5 . 1 802 198 198 CYS CA C 56.63 . 1 803 198 198 CYS CB C 34.98 . 1 804 198 198 CYS N N 119.8 . 1 805 199 199 ARG H H 9.242 . 1 806 199 199 ARG C C 180.8 . 1 807 199 199 ARG CA C 60.79 . 1 808 199 199 ARG CB C 28.70 . 1 809 199 199 ARG N N 120.0 . 1 810 200 200 ASN H H 7.942 . 1 811 200 200 ASN C C 177.8 . 1 812 200 200 ASN CA C 55.98 . 1 813 200 200 ASN CB C 37.67 . 1 814 200 200 ASN N N 116.2 . 1 815 201 201 ALA H H 7.730 . 1 816 201 201 ALA C C 178.3 . 1 817 201 201 ALA CA C 53.75 . 1 818 201 201 ALA CB C 17.41 . 1 819 201 201 ALA N N 123.7 . 1 820 202 202 MET H H 7.568 . 1 821 202 202 MET C C 177.1 . 1 822 202 202 MET CA C 55.46 . 1 823 202 202 MET CB C 33.32 . 1 824 202 202 MET N N 114.4 . 1 825 203 203 ARG H H 7.232 . 1 826 203 203 ARG C C 176.1 . 1 827 203 203 ARG CA C 58.75 . 1 828 203 203 ARG CB C 28.86 . 1 829 203 203 ARG N N 118.7 . 1 830 204 204 HIS H H 8.906 . 1 831 204 204 HIS C C 175.1 . 1 832 204 204 HIS CA C 55.78 . 1 833 204 204 HIS CB C 29.26 . 1 834 204 204 HIS N N 116.1 . 1 835 205 205 LEU H H 7.785 . 1 836 205 205 LEU C C 175.8 . 1 837 205 205 LEU CA C 53.08 . 1 838 205 205 LEU CB C 42.27 . 1 839 205 205 LEU N N 122.0 . 1 840 206 206 ARG H H 9.499 . 1 841 206 206 ARG C C 175.4 . 1 842 206 206 ARG CA C 52.44 . 1 843 206 206 ARG CB C 29.48 . 1 844 206 206 ARG N N 120.8 . 1 845 207 207 PRO C C 177.2 . 1 846 207 207 PRO CA C 65.70 . 1 847 207 207 PRO CB C 30.70 . 1 848 208 208 GLU H H 8.833 . 1 849 208 208 GLU C C 177.6 . 1 850 208 208 GLU CA C 57.17 . 1 851 208 208 GLU CB C 27.63 . 1 852 208 208 GLU N N 110.5 . 1 853 209 209 ASP H H 7.718 . 1 854 209 209 ASP C C 175.6 . 1 855 209 209 ASP CA C 55.81 . 1 856 209 209 ASP CB C 40.65 . 1 857 209 209 ASP N N 121.3 . 1 858 210 210 THR H H 8.357 . 1 859 210 210 THR C C 175.9 . 1 860 210 210 THR CA C 61.67 . 1 861 210 210 THR CB C 70.55 . 1 862 210 210 THR N N 108.8 . 1 863 211 211 LEU H H 8.707 . 1 864 211 211 LEU C C 179.3 . 1 865 211 211 LEU CA C 57.11 . 1 866 211 211 LEU CB C 40.62 . 1 867 211 211 LEU N N 121.3 . 1 868 212 212 GLU H H 8.753 . 1 869 212 212 GLU C C 179.6 . 1 870 212 212 GLU CA C 60.36 . 1 871 212 212 GLU CB C 27.95 . 1 872 212 212 GLU N N 117.0 . 1 873 213 213 GLU H H 7.840 . 1 874 213 213 GLU C C 179.6 . 1 875 213 213 GLU CA C 59.12 . 1 876 213 213 GLU CB C 28.92 . 1 877 213 213 GLU N N 120.4 . 1 878 214 214 LYS H H 7.730 . 1 879 214 214 LYS C C 176.8 . 1 880 214 214 LYS CA C 59.91 . 1 881 214 214 LYS CB C 31.70 . 1 882 214 214 LYS N N 122.9 . 1 883 215 215 MET H H 8.820 . 1 884 215 215 MET C C 179.5 . 1 885 215 215 MET CA C 58.48 . 1 886 215 215 MET CB C 31.94 . 1 887 215 215 MET N N 114.4 . 1 888 216 216 TYR H H 8.083 . 1 889 216 216 TYR C C 178.8 . 1 890 216 216 TYR CA C 60.82 . 1 891 216 216 TYR CB C 37.43 . 1 892 216 216 TYR N N 118.6 . 1 893 217 217 ALA H H 7.817 . 1 894 217 217 ALA C C 179.2 . 1 895 217 217 ALA CA C 54.42 . 1 896 217 217 ALA CB C 16.95 . 1 897 217 217 ALA N N 121.1 . 1 898 218 218 CYS H H 7.030 . 1 899 218 218 CYS C C 174.5 . 1 900 218 218 CYS CA C 54.84 . 1 901 218 218 CYS CB C 39.06 . 1 902 218 218 CYS N N 110.9 . 1 903 219 219 ARG H H 7.190 . 1 904 219 219 ARG C C 175.9 . 1 905 219 219 ARG CA C 58.12 . 1 906 219 219 ARG CB C 28.50 . 1 907 219 219 ARG N N 120.4 . 1 908 220 220 ASP H H 8.527 . 1 909 220 220 ASP C C 176.3 . 1 910 220 220 ASP CA C 53.78 . 1 911 220 220 ASP CB C 40.44 . 1 912 220 220 ASP N N 118.6 . 1 913 221 221 ILE H H 7.510 . 1 914 221 221 ILE C C 177.1 . 1 915 221 221 ILE CA C 60.97 . 1 916 221 221 ILE CB C 36.70 . 1 917 221 221 ILE N N 121.3 . 1 918 222 222 GLY H H 8.837 . 1 919 222 222 GLY C C 174.4 . 1 920 222 222 GLY CA C 45.06 . 1 921 222 222 GLY N N 114.1 . 1 922 223 223 THR H H 7.806 . 1 923 223 223 THR C C 175.0 . 1 924 223 223 THR CA C 61.23 . 1 925 223 223 THR CB C 69.68 . 1 926 223 223 THR N N 112.3 . 1 927 224 224 THR H H 8.253 . 1 928 224 224 THR C C 174.7 . 1 929 224 224 THR CA C 62.08 . 1 930 224 224 THR CB C 69.28 . 1 931 224 224 THR N N 116.3 . 1 932 225 225 LYS H H 8.335 . 1 933 225 225 LYS C C 176.6 . 1 934 225 225 LYS CA C 56.09 . 1 935 225 225 LYS CB C 31.89 . 1 936 225 225 LYS N N 123.6 . 1 937 226 226 GLN H H 8.293 . 1 938 226 226 GLN C C 176.0 . 1 939 226 226 GLN CA C 55.59 . 1 940 226 226 GLN CB C 28.58 . 1 941 226 226 GLN N N 121.3 . 1 942 227 227 LYS H H 8.340 . 1 943 227 227 LYS C C 176.4 . 1 944 227 227 LYS CA C 56.06 . 1 945 227 227 LYS CB C 32.04 . 1 946 227 227 LYS N N 122.8 . 1 947 228 228 MET H H 8.344 . 1 948 228 228 MET C C 175.8 . 1 949 228 228 MET CA C 54.99 . 1 950 228 228 MET CB C 32.04 . 1 951 228 228 MET N N 121.5 . 1 952 229 229 MET H H 8.315 . 1 953 229 229 MET C C 174.9 . 1 954 229 229 MET CA C 54.84 . 1 955 229 229 MET CB C 31.92 . 1 956 229 229 MET N N 122.2 . 1 957 230 230 LEU H H 7.806 . 1 958 230 230 LEU C C 172.9 . 1 959 230 230 LEU CA C 56.32 . 1 960 230 230 LEU CB C 42.34 . 1 961 230 230 LEU N N 129.1 . 1 stop_ save_