data_5062 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignment for Unfolded HIV-1 protease tethered dimer ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhavesh Neel Sarovar . 2 Panchal Sanjay C . 3 Mittal Rohit . . 4 Hosur Ramkrishna V . stop_ _BMRB_accession_number 5062 _BMRB_flat_file_name bmr5062.str _Entry_type new _Submission_date 2001-06-19 _Accession_date 2001-06-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 190 '15N chemical shifts' 191 '13C chemical shifts' 569 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR Identification of local Structural Preferences in HIV-I Protease Tethered Heterodimer in 6 M Guanidine Hydrochloride ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21617172 _PubMed_ID 11741592 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhavesh Neel Sarovar . 2 Panchal Sanjay C . 3 Mittal Rohit . . 4 Hosur Ramkrishna V . stop_ _Journal_abbreviation "FEBS Lett." _Journal_volume 509 _Journal_issue 2 _Page_first 218 _Page_last 224 _Year 2001 loop_ _Keyword "HIV-1 protease" "denatured/unfolded protein" "Guanidine hydrochloride" "HNN" "HN(C)N" "residual structure" stop_ save_ ################################## # Molecular system description # ################################## save_system_HIV-1_protease _Saveframe_category molecular_system _Mol_system_name "HIV-1 protease tethered dimer" _Abbreviation_common "HIV-1 protease" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "HIV-1 protease" $HIV-1_protease stop_ _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1G6L ? "X-ray structure of C195A mutation" stop_ save_ ######################## # Monomeric polymers # ######################## save_HIV-1_protease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "HIV-1 protease" _Name_variant "C95M, C195A" _Abbreviation_common Protease _Molecular_mass 21971 _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Ambiguous_sequence_features ; Tethered linker. The HIV-1 protease tethered dimer is made up of two subunits covalently linked through a penta-peptide linker of amino acid sequence GGSSG. The residues in the first subunit are numbered 1 to 99 and second subunit are numbered 105 to 203. It is a C95M, C199A mutant. ; ############################## # Polymer residue sequence # ############################## _Residue_count 203 _Mol_residue_sequence ; PQVTLWQRPLVTIKIGGQLK EALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYD QILIEICAHKAIGTVLVGPT PVNIIGRNLLTQIGMTLNFG GSSGPQVTLWQRPLVTIKIG GQLKEALLDTGADDTVLEEM SLPGRWKPKMIGGIGGFIKV RQYDQILIEICAHKAIGTVL VGPTPVNIIGRNLLTQIGAT LNF ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 GLN 3 VAL 4 THR 5 LEU 6 TRP 7 GLN 8 ARG 9 PRO 10 LEU 11 VAL 12 THR 13 ILE 14 LYS 15 ILE 16 GLY 17 GLY 18 GLN 19 LEU 20 LYS 21 GLU 22 ALA 23 LEU 24 LEU 25 ASP 26 THR 27 GLY 28 ALA 29 ASP 30 ASP 31 THR 32 VAL 33 LEU 34 GLU 35 GLU 36 MET 37 SER 38 LEU 39 PRO 40 GLY 41 ARG 42 TRP 43 LYS 44 PRO 45 LYS 46 MET 47 ILE 48 GLY 49 GLY 50 ILE 51 GLY 52 GLY 53 PHE 54 ILE 55 LYS 56 VAL 57 ARG 58 GLN 59 TYR 60 ASP 61 GLN 62 ILE 63 LEU 64 ILE 65 GLU 66 ILE 67 CYS 68 ALA 69 HIS 70 LYS 71 ALA 72 ILE 73 GLY 74 THR 75 VAL 76 LEU 77 VAL 78 GLY 79 PRO 80 THR 81 PRO 82 VAL 83 ASN 84 ILE 85 ILE 86 GLY 87 ARG 88 ASN 89 LEU 90 LEU 91 THR 92 GLN 93 ILE 94 GLY 95 MET 96 THR 97 LEU 98 ASN 99 PHE 100 GLY 101 GLY 102 SER 103 SER 104 GLY 105 PRO 106 GLN 107 VAL 108 THR 109 LEU 110 TRP 111 GLN 112 ARG 113 PRO 114 LEU 115 VAL 116 THR 117 ILE 118 LYS 119 ILE 120 GLY 121 GLY 122 GLN 123 LEU 124 LYS 125 GLU 126 ALA 127 LEU 128 LEU 129 ASP 130 THR 131 GLY 132 ALA 133 ASP 134 ASP 135 THR 136 VAL 137 LEU 138 GLU 139 GLU 140 MET 141 SER 142 LEU 143 PRO 144 GLY 145 ARG 146 TRP 147 LYS 148 PRO 149 LYS 150 MET 151 ILE 152 GLY 153 GLY 154 ILE 155 GLY 156 GLY 157 PHE 158 ILE 159 LYS 160 VAL 161 ARG 162 GLN 163 TYR 164 ASP 165 GLN 166 ILE 167 LEU 168 ILE 169 GLU 170 ILE 171 CYS 172 ALA 173 HIS 174 LYS 175 ALA 176 ILE 177 GLY 178 THR 179 VAL 180 LEU 181 VAL 182 GLY 183 PRO 184 THR 185 PRO 186 VAL 187 ASN 188 ILE 189 ILE 190 GLY 191 ARG 192 ASN 193 LEU 194 LEU 195 THR 196 GLN 197 ILE 198 GLY 199 ALA 200 THR 201 LEU 202 ASN 203 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 4356 "Aspartic protease" 100.00 203 98.03 98.03 1.34e-107 PDB 1G6L "1.9a Crystal Structure Of Tethered Hiv-1 Protease" 100.00 203 98.52 98.52 1.82e-108 PDB 1LV1 "Crystal Structure Analysis Of The Non-Active Site Mutant Of Tethered Hiv-1 Protease To 2.1a Resolution" 100.00 203 99.01 99.01 3.66e-109 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _ATCC_number _Gene_mnemonic $HIV-1_protease HIV-1 11676 Viruses . Lentivirus Lentivirus 11676 gag-pol stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _ATCC_number _Vector_type _Vector_name $HIV-1_protease 'recombinant technology' "E. coli" Escherichia coli BL21(DE3) 37762 plasmid pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HIV-1_protease 1.2 mM "[U-95% 13C; U-90% 15N]" "guanidine hydrochloride" 6 M . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N TROSY HNN HN(C)N 2D 1H-15N TOCSY HNCA HN(CO)CA CBCANH CBCA(CO)NH ; _Details ; Two new pulse sequences HNN, HN(C)N were used to get HN, NH assignments in this poorly amide proton dispersed spectra in unfolded condition. ; save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 0.1 n/a temperature 305 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 TSP H 1 "methyl protons" ppm 0.00 external indirect cylindrical external parallel 1.0 DSS N 15 "methyl protons" ppm 0.00 external indirect cylindrical external parallel 0.10132905 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "HIV-1 protease" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 PRO CB C 37.23 0.10 1 2 1 PRO C C 176.69 0.10 1 3 1 PRO CA C 56.20 0.10 1 4 2 GLN H H 8.72 0.02 1 5 2 GLN CB C 33.57 0.10 1 6 2 GLN C C 176.05 0.10 1 7 2 GLN CA C 53.15 0.10 1 8 2 GLN N N 120.53 0.05 1 9 3 VAL H H 8.34 0.02 1 10 3 VAL CB C 33.92 0.10 1 11 3 VAL C C 176.23 0.10 1 12 3 VAL CA C 60.63 0.10 1 13 3 VAL N N 120.58 0.05 1 14 4 THR H H 8.39 0.02 1 15 4 THR CB C 70.02 0.10 1 16 4 THR C C 177.02 0.10 1 17 4 THR CA C 61.38 0.10 1 18 4 THR N N 118.98 0.05 1 19 5 LEU H H 8.61 0.03 1 20 5 LEU CB C 43.63 0.10 1 21 5 LEU C C 175.34 0.10 1 22 5 LEU CA C 52.84 0.10 1 23 5 LEU N N 122.41 0.10 1 24 6 TRP H H 8.45 0.02 1 25 6 TRP CB C 31.92 0.10 1 26 6 TRP C C 177.27 0.10 1 27 6 TRP CA C 57.65 0.10 1 28 6 TRP N N 121.84 0.05 1 29 7 GLN H H 8.53 0.02 1 30 7 GLN CB C 31.27 0.10 1 31 7 GLN C C 176.37 0.10 1 32 7 GLN CA C 52.68 0.10 1 33 7 GLN N N 120.64 0.05 1 34 8 ARG H H 7.98 0.02 1 35 8 ARG CB C 31.27 0.10 1 36 8 ARG CA C 59.21 0.10 1 37 8 ARG N N 126.14 0.05 1 38 9 PRO CB C 32.28 0.10 1 39 9 PRO C C 177.60 0.10 1 40 9 PRO CA C 62.93 0.10 1 41 10 LEU H H 8.75 0.02 1 42 10 LEU CB C 43.48 0.10 1 43 10 LEU C C 177.40 0.10 1 44 10 LEU CA C 55.95 0.10 1 45 10 LEU N N 122.83 0.05 1 46 11 VAL H H 8.22 0.02 1 47 11 VAL CB C 32.98 0.10 1 48 11 VAL C C 176.63 0.10 1 49 11 VAL CA C 61.85 0.10 1 50 11 VAL N N 122.22 0.05 1 51 12 THR H H 8.36 0.02 1 52 12 THR CB C 69.67 0.10 1 53 12 THR C C 174.88 0.10 1 54 12 THR CA C 61.23 0.10 1 55 12 THR N N 118.76 0.05 1 56 13 ILE H H 8.31 0.02 1 57 13 ILE CB C 38.92 0.10 1 58 13 ILE C C 176.36 0.10 1 59 13 ILE CA C 60.76 0.10 1 60 13 ILE N N 124.63 0.05 1 61 14 LYS H H 8.56 0.02 1 62 14 LYS CB C 33.33 0.10 1 63 14 LYS C C 175.79 0.10 1 64 14 LYS CA C 55.95 0.10 1 65 14 LYS N N 126.72 0.05 1 66 15 ILE H H 8.45 0.02 1 67 15 ILE CB C 38.57 0.10 1 68 15 ILE C C 177.27 0.10 1 69 15 ILE CA C 61.07 0.10 1 70 15 ILE N N 124.11 0.05 1 71 16 GLY H H 8.67 0.02 1 72 16 GLY C C 175.07 0.10 1 73 16 GLY CA C 45.07 0.10 1 74 16 GLY N N 114.21 0.05 1 75 17 GLY H H 8.49 0.02 1 76 17 GLY C C 174.69 0.10 1 77 17 GLY CA C 45.07 0.10 1 78 17 GLY N N 109.95 0.05 1 79 18 GLN H H 8.56 0.02 1 80 18 GLN CB C 29.83 0.10 1 81 18 GLN C C 176.63 0.10 1 82 18 GLN CA C 55.79 0.10 1 83 18 GLN N N 120.97 0.05 1 84 19 LEU H H 8.50 0.02 1 85 19 LEU CB C 42.06 0.10 1 86 19 LEU C C 175.14 0.10 1 87 19 LEU CA C 55.01 0.10 1 88 19 LEU N N 124.37 0.05 1 89 20 LYS H H 8.56 0.02 1 90 20 LYS CB C 33.33 0.10 1 91 20 LYS C C 176.39 0.10 1 92 20 LYS CA C 56.05 0.10 1 93 20 LYS N N 123.41 0.05 1 94 21 GLU H H 8.61 0.02 1 95 21 GLU CB C 30.53 0.10 1 96 21 GLU C C 175.01 0.10 1 97 21 GLU CA C 55.25 0.10 1 98 21 GLU N N 122.84 0.05 1 99 22 ALA H H 8.46 0.02 1 100 22 ALA CB C 19.69 0.10 1 101 22 ALA C C 176.53 0.10 1 102 22 ALA CA C 52.06 0.10 1 103 22 ALA N N 125.33 0.05 1 104 23 LEU H H 8.34 0.02 1 105 23 LEU CB C 43.33 0.10 1 106 23 LEU C C 176.50 0.10 1 107 23 LEU CA C 54.86 0.10 1 108 23 LEU N N 122.60 0.05 1 109 24 LEU H H 8.43 0.02 1 110 24 LEU CB C 42.53 0.10 1 111 24 LEU C C 177.60 0.10 1 112 24 LEU CA C 57.07 0.10 1 113 24 LEU N N 123.30 0.05 1 114 25 ASP H H 8.58 0.02 1 115 25 ASP CB C 40.02 0.10 1 116 25 ASP C C 176.95 0.10 1 117 25 ASP CA C 52.84 0.10 1 118 25 ASP N N 122.21 0.05 1 119 26 THR H H 8.30 0.02 1 120 26 THR CB C 70.02 0.10 1 121 26 THR C C 175.91 0.10 1 122 26 THR CA C 61.54 0.10 1 123 26 THR N N 114.21 0.05 1 124 27 GLY H H 8.69 0.02 1 125 27 GLY C C 174.88 0.10 1 126 27 GLY CA C 45.23 0.10 1 127 27 GLY N N 111.89 0.05 1 128 28 ALA H H 8.32 0.02 1 129 28 ALA CB C 20.04 0.10 1 130 28 ALA C C 174.29 0.10 1 131 28 ALA CA C 52.37 0.10 1 132 28 ALA N N 124.37 0.05 1 133 29 ASP H H 8.55 0.02 1 134 29 ASP CB C 39.36 0.10 1 135 29 ASP C C 176.56 0.10 1 136 29 ASP CA C 54.06 0.10 1 137 29 ASP N N 119.20 0.05 1 138 30 ASP H H 8.54 0.02 1 139 30 ASP CB C 39.36 0.10 1 140 30 ASP C C 177.02 0.10 1 141 30 ASP CA C 54.48 0.10 1 142 30 ASP N N 121.54 0.05 1 143 31 THR H H 8.33 0.02 1 144 31 THR CB C 70.02 0.10 1 145 31 THR C C 177.47 0.10 1 146 31 THR CA C 62.00 0.10 1 147 31 THR N N 114.66 0.05 1 148 32 VAL H H 8.26 0.02 1 149 32 VAL CB C 33.73 0.10 1 150 32 VAL C C 175.89 0.10 1 151 32 VAL CA C 61.18 0.10 1 152 32 VAL N N 122.99 0.05 1 153 33 LEU H H 8.42 0.02 1 154 33 LEU CB C 43.38 0.10 1 155 33 LEU C C 177.18 0.10 1 156 33 LEU CA C 55.17 0.10 1 157 33 LEU N N 126.49 0.05 1 158 34 GLU H H 8.57 0.02 1 159 34 GLU CB C 30.36 0.10 1 160 34 GLU C C 175.86 0.10 1 161 34 GLU CA C 54.70 0.10 1 162 34 GLU N N 122.56 0.10 1 163 35 GLU H H 8.43 0.03 1 164 35 GLU CB C 29.83 0.10 1 165 35 GLU C C 175.83 0.10 1 166 35 GLU CA C 55.79 0.10 1 167 35 GLU N N 121.03 0.05 1 168 36 MET H H 8.37 0.02 1 169 36 MET CB C 34.41 0.10 1 170 36 MET C C 176.12 0.10 1 171 36 MET CA C 54.86 0.10 1 172 36 MET N N 122.75 0.05 1 173 37 SER H H 8.55 0.02 1 174 37 SER CB C 65.07 0.10 1 175 37 SER C C 174.22 0.10 1 176 37 SER CA C 56.93 0.10 1 177 37 SER N N 121.82 0.05 1 178 38 LEU H H 8.47 0.02 1 179 38 LEU CB C 42.06 0.10 1 180 38 LEU CA C 54.86 0.10 1 181 38 LEU N N 127.21 0.05 1 182 39 PRO CB C 32.27 0.10 1 183 39 PRO C C 177.92 0.10 1 184 39 PRO CA C 63.09 0.10 1 185 40 GLY H H 8.59 0.02 1 186 40 GLY C C 178.18 0.10 1 187 40 GLY CA C 45.23 0.10 1 188 40 GLY N N 110.17 0.05 1 189 41 ARG H H 8.33 0.02 1 190 41 ARG CB C 30.88 0.10 1 191 41 ARG C C 177.86 0.10 1 192 41 ARG CA C 55.94 0.10 1 193 41 ARG N N 121.53 0.05 1 194 42 TRP H H 8.47 0.02 1 195 42 TRP CB C 29.83 0.10 1 196 42 TRP C C 176.17 0.10 1 197 42 TRP CA C 57.34 0.10 1 198 42 TRP N N 123.24 0.05 1 199 43 LYS H H 8.08 0.02 1 200 43 LYS CB C 32.63 0.10 1 201 43 LYS CA C 53.61 0.10 1 202 43 LYS N N 125.48 0.05 1 203 44 PRO CB C 30.18 0.10 1 204 44 PRO C C 174.69 0.10 1 205 44 PRO CA C 56.25 0.10 1 206 45 LYS H H 8.42 0.02 1 207 45 LYS CB C 30.53 0.10 1 208 45 LYS C C 176.62 0.10 1 209 45 LYS CA C 51.91 0.10 1 210 45 LYS N N 125.76 0.05 1 211 46 MET H H 8.31 0.02 1 212 46 MET CB C 32.98 0.10 1 213 46 MET C C 175.60 0.10 1 214 46 MET CA C 54.86 0.10 1 215 46 MET N N 122.10 0.05 1 216 47 ILE H H 8.38 0.03 1 217 47 ILE CB C 38.57 0.10 1 218 47 ILE C C 177.27 0.10 1 219 47 ILE CA C 61.07 0.10 1 220 47 ILE N N 123.28 0.10 1 221 48 GLY H H 8.67 0.10 1 222 48 GLY C C 174.94 0.10 1 223 48 GLY CA C 44.92 0.10 1 224 48 GLY N N 114.03 0.05 1 225 49 GLY H H 8.44 0.02 1 226 49 GLY C C 174.75 0.10 1 227 49 GLY CA C 44.92 0.10 1 228 49 GLY N N 109.80 0.05 1 229 50 ILE H H 8.29 0.02 1 230 50 ILE CB C 38.57 0.10 1 231 50 ILE C C 177.27 0.10 1 232 50 ILE CA C 61.23 0.10 1 233 50 ILE N N 120.51 0.05 1 234 51 GLY H H 8.65 0.02 1 235 51 GLY C C 174.94 0.10 1 236 51 GLY CA C 45.07 0.10 1 237 51 GLY N N 113.40 0.05 1 238 52 GLY H H 8.37 0.02 1 239 52 GLY C C 178.18 0.10 1 240 52 GLY CA C 45.07 0.10 1 241 52 GLY N N 109.76 0.05 1 242 53 PHE H H 8.33 0.02 1 243 53 PHE CB C 39.96 0.10 1 244 53 PHE C C 176.17 0.10 1 245 53 PHE CA C 55.95 0.10 1 246 53 PHE N N 121.30 0.05 1 247 54 ILE H H 8.28 0.02 1 248 54 ILE CB C 37.62 0.10 1 249 54 ILE C C 174.62 0.10 1 250 54 ILE CA C 60.61 0.10 1 251 54 ILE N N 123.52 0.05 1 252 55 LYS H H 8.53 0.02 1 253 55 LYS CB C 34.41 0.10 1 254 55 LYS C C 175.40 0.10 1 255 55 LYS CA C 54.70 0.10 1 256 55 LYS N N 126.97 0.05 1 257 56 VAL H H 8.26 0.02 1 258 56 VAL CB C 32.98 0.10 1 259 56 VAL C C 176.50 0.10 1 260 56 VAL CA C 60.92 0.10 1 261 56 VAL N N 122.76 0.05 1 262 57 ARG H H 8.60 0.02 1 263 57 ARG CB C 30.88 0.10 1 264 57 ARG C C 176.62 0.10 1 265 57 ARG CA C 56.10 0.10 1 266 57 ARG N N 125.51 0.05 1 267 58 GLN H H 8.54 0.03 1 268 58 GLN CB C 29.83 0.10 1 269 58 GLN C C 176.24 0.10 1 270 58 GLN CA C 55.79 0.10 1 271 58 GLN N N 122.58 0.10 1 272 59 TYR H H 8.38 0.03 1 273 59 TYR CB C 37.18 0.10 1 274 59 TYR C C 177.11 0.10 1 275 59 TYR CA C 57.50 0.10 1 276 59 TYR N N 121.56 0.05 1 277 60 ASP H H 8.39 0.02 1 278 60 ASP CB C 38.92 0.10 1 279 60 ASP C C 176.17 0.10 1 280 60 ASP CA C 54.23 0.10 1 281 60 ASP N N 122.49 0.05 1 282 61 GLN H H 8.59 0.02 1 283 61 GLN CB C 32.98 0.10 1 284 61 GLN C C 177.62 0.10 1 285 61 GLN CA C 58.43 0.10 1 286 61 GLN N N 123.08 0.05 1 287 62 ILE H H 8.57 0.02 1 288 62 ILE CB C 39.83 0.10 1 289 62 ILE C C 177.53 0.10 1 290 62 ILE CA C 60.10 0.10 1 291 62 ILE N N 125.63 0.05 1 292 63 LEU H H 8.25 0.02 1 293 63 LEU CB C 42.98 0.10 1 294 63 LEU C C 176.69 0.10 1 295 63 LEU CA C 56.85 0.10 1 296 63 LEU N N 121.47 0.05 1 297 64 ILE H H 8.48 0.02 1 298 64 ILE CB C 38.56 0.10 1 299 64 ILE C C 174.43 0.10 1 300 64 ILE CA C 61.23 0.10 1 301 64 ILE N N 117.85 0.05 1 302 65 GLU H H 8.32 0.02 1 303 65 GLU CB C 29.92 0.10 1 304 65 GLU C C 174.69 0.10 1 305 65 GLU CA C 57.38 0.10 1 306 65 GLU N N 124.22 0.05 1 307 66 ILE H H 8.44 0.02 1 308 66 ILE CB C 38.92 0.10 1 309 66 ILE C C 176.89 0.10 1 310 66 ILE CA C 55.79 0.10 1 311 66 ILE N N 125.90 0.05 1 312 67 CYS H H 8.39 0.02 1 313 67 CYS CB C 30.18 0.10 1 314 67 CYS C C 176.37 0.10 1 315 67 CYS CA C 59.91 0.10 1 316 67 CYS N N 123.76 0.05 1 317 68 ALA H H 8.34 0.02 1 318 68 ALA CB C 18.64 0.10 1 319 68 ALA C C 176.69 0.10 1 320 68 ALA CA C 55.32 0.10 1 321 68 ALA N N 122.45 0.05 1 322 69 HIS H H 8.51 0.02 1 323 69 HIS CB C 32.97 0.10 1 324 69 HIS C C 177.86 0.10 1 325 69 HIS CA C 54.70 0.10 1 326 69 HIS N N 125.72 0.05 1 327 70 LYS H H 8.36 0.02 1 328 70 LYS CB C 33.33 0.10 1 329 70 LYS C C 176.76 0.10 1 330 70 LYS CA C 56.05 0.10 1 331 70 LYS N N 123.35 0.05 1 332 71 ALA H H 8.61 0.02 1 333 71 ALA CB C 19.34 0.10 1 334 71 ALA C C 174.69 0.10 1 335 71 ALA CA C 52.06 0.10 1 336 71 ALA N N 126.94 0.05 1 337 72 ILE H H 8.31 0.02 1 338 72 ILE CB C 38.92 0.10 1 339 72 ILE C C 177.27 0.10 1 340 72 ILE CA C 61.07 0.10 1 341 72 ILE N N 121.16 0.05 1 342 73 GLY H H 8.65 0.02 1 343 73 GLY C C 174.62 0.10 1 344 73 GLY CA C 45.07 0.10 1 345 73 GLY N N 113.66 0.05 1 346 74 THR H H 8.22 0.02 1 347 74 THR CB C 70.02 0.10 1 348 74 THR C C 175.07 0.10 1 349 74 THR CA C 60.86 0.10 1 350 74 THR N N 115.02 0.05 1 351 75 VAL H H 8.35 0.02 1 352 75 VAL CB C 32.98 0.10 1 353 75 VAL C C 176.37 0.10 1 354 75 VAL CA C 62.00 0.10 1 355 75 VAL N N 122.39 0.05 1 356 76 LEU H H 8.54 0.02 1 357 76 LEU CB C 42.16 0.10 1 358 76 LEU C C 177.53 0.10 1 359 76 LEU CA C 54.86 0.10 1 360 76 LEU N N 127.27 0.05 1 361 77 VAL H H 8.23 0.02 1 362 77 VAL CB C 32.62 0.10 1 363 77 VAL C C 175.76 0.10 1 364 77 VAL CA C 61.84 0.10 1 365 77 VAL N N 121.51 0.05 1 366 78 GLY H H 8.49 0.02 1 367 78 GLY CA C 44.45 0.10 1 368 78 GLY N N 113.35 0.05 1 369 79 PRO CB C 43.11 0.10 1 370 79 PRO C C 175.18 0.10 1 371 79 PRO CA C 60.91 0.10 1 372 80 THR H H 8.19 0.02 1 373 80 THR CA C 56.72 0.10 1 374 80 THR N N 132.55 0.05 1 375 81 PRO CB C 29.82 0.10 1 376 81 PRO C C 176.86 0.10 1 377 81 PRO CA C 55.33 0.10 1 378 82 VAL H H 8.51 0.02 1 379 82 VAL CB C 33.58 0.10 1 380 82 VAL C C 176.18 0.10 1 381 82 VAL CA C 61.25 0.10 1 382 82 VAL N N 123.37 0.05 1 383 83 ASN H H 8.60 0.03 1 384 83 ASN CB C 39.82 0.10 1 385 83 ASN C C 175.11 0.10 1 386 83 ASN CA C 50.94 0.10 1 387 83 ASN N N 122.45 0.10 1 388 84 ILE H H 8.59 0.10 1 389 84 ILE CB C 39.70 0.10 1 390 84 ILE C C 176.26 0.10 1 391 84 ILE CA C 59.79 0.10 1 392 84 ILE N N 123.54 0.05 1 393 85 ILE H H 8.26 0.02 1 394 85 ILE CB C 38.21 0.10 1 395 85 ILE C C 177.27 0.10 1 396 85 ILE CA C 61.23 0.10 1 397 85 ILE N N 121.36 0.05 1 398 86 GLY H H 8.62 0.02 1 399 86 GLY C C 176.24 0.10 1 400 86 GLY CA C 45.23 0.10 1 401 86 GLY N N 113.80 0.05 1 402 87 ARG H H 8.40 0.02 1 403 87 ARG CB C 30.53 0.10 1 404 87 ARG C C 176.76 0.10 1 405 87 ARG CA C 55.79 0.10 1 406 87 ARG N N 121.49 0.05 1 407 88 ASN H H 8.30 0.02 1 408 88 ASN CB C 38.57 0.10 1 409 88 ASN C C 174.69 0.10 1 410 88 ASN CA C 55.07 0.10 1 411 88 ASN N N 122.54 0.10 1 412 89 LEU H H 8.47 0.02 1 413 89 LEU CB C 41.71 0.10 1 414 89 LEU C C 175.53 0.10 1 415 89 LEU CA C 54.86 0.10 1 416 89 LEU N N 125.76 0.05 1 417 90 LEU H H 8.35 0.02 1 418 90 LEU CB C 42.06 0.10 1 419 90 LEU C C 178.18 0.10 1 420 90 LEU CA C 61.07 0.10 1 421 90 LEU N N 123.06 0.05 1 422 91 THR H H 8.18 0.02 1 423 91 THR CB C 69.67 0.10 1 424 91 THR C C 177.86 0.10 1 425 91 THR CA C 61.54 0.10 1 426 91 THR N N 114.80 0.05 1 427 92 GLN H H 8.24 0.02 1 428 92 GLN CB C 28.92 0.10 1 429 92 GLN C C 176.56 0.10 1 430 92 GLN CA C 57.27 0.10 1 431 92 GLN N N 122.08 0.05 1 432 93 ILE H H 8.33 0.02 1 433 93 ILE CB C 38.56 0.10 1 434 93 ILE C C 177.27 0.10 1 435 93 ILE CA C 61.23 0.10 1 436 93 ILE N N 125.18 0.05 1 437 94 GLY H H 8.61 0.02 1 438 94 GLY C C 174.56 0.10 1 439 94 GLY CA C 45.23 0.10 1 440 94 GLY N N 113.56 0.05 1 441 95 MET H H 8.38 0.10 1 442 95 MET CB C 33.33 0.10 1 443 95 MET C C 176.95 0.10 1 444 95 MET CA C 55.48 0.10 1 445 95 MET N N 121.01 0.05 1 446 96 THR H H 8.38 0.02 1 447 96 THR CB C 69.67 0.10 1 448 96 THR C C 175.01 0.10 1 449 96 THR CA C 61.38 0.10 1 450 96 THR N N 116.24 0.05 1 451 97 LEU H H 8.41 0.02 1 452 97 LEU CB C 42.06 0.10 1 453 97 LEU C C 177.14 0.10 1 454 97 LEU CA C 54.86 0.10 1 455 97 LEU N N 125.04 0.05 1 456 98 ASN H H 8.49 0.02 1 457 98 ASN CB C 39.27 0.10 1 458 98 ASN C C 176.24 0.10 1 459 98 ASN CA C 52.68 0.10 1 460 98 ASN N N 120.18 0.05 1 461 99 PHE H H 8.41 0.02 1 462 99 PHE CB C 39.27 0.10 1 463 99 PHE C C 176.62 0.10 1 464 99 PHE CA C 57.65 0.10 1 465 99 PHE N N 122.08 0.05 1 466 100 GLY H H 8.64 0.02 1 467 100 GLY C C 175.14 0.10 1 468 100 GLY CA C 45.23 0.10 1 469 100 GLY N N 111.31 0.05 1 470 101 GLY H H 8.29 0.02 1 471 101 GLY C C 174.81 0.10 1 472 101 GLY CA C 45.23 0.10 1 473 101 GLY N N 109.85 0.05 1 474 102 SER H H 8.49 0.02 1 475 102 SER CB C 63.38 0.10 1 476 102 SER C C 175.20 0.10 1 477 102 SER CA C 57.96 0.10 1 478 102 SER N N 116.80 0.05 1 479 103 SER H H 8.59 0.02 1 480 103 SER CB C 63.73 0.10 1 481 103 SER C C 175.14 0.10 1 482 103 SER CA C 58.12 0.10 1 483 103 SER N N 118.48 0.05 1 484 104 GLY H H 8.44 0.02 1 485 104 GLY CA C 44.60 0.10 1 486 104 GLY N N 111.26 0.05 1 487 105 PRO CB C 39.83 0.10 1 488 105 PRO C C 176.69 0.10 1 489 105 PRO CA C 56.91 0.10 1 490 106 GLN H H 8.57 0.03 1 491 106 GLN CB C 32.98 0.10 1 492 106 GLN C C 175.40 0.10 1 493 106 GLN CA C 53.43 0.10 1 494 106 GLN N N 123.54 0.05 1 495 107 VAL H H 8.57 0.02 1 496 107 VAL CB C 34.41 0.10 1 497 107 VAL C C 176.23 0.10 1 498 107 VAL CA C 60.94 0.10 1 499 107 VAL N N 120.36 0.05 1 500 108 THR H H 8.39 0.02 1 501 108 THR CB C 70.02 0.10 1 502 108 THR C C 177.02 0.10 1 503 108 THR CA C 61.38 0.10 1 504 108 THR N N 119.16 0.05 1 505 109 LEU H H 8.61 0.02 1 506 109 LEU CB C 43.63 0.10 1 507 109 LEU C C 175.34 0.10 1 508 109 LEU CA C 52.84 0.10 1 509 109 LEU N N 122.41 0.05 1 510 110 TRP H H 8.45 0.02 1 511 110 TRP CB C 31.92 0.10 1 512 110 TRP C C 177.27 0.10 1 513 110 TRP CA C 57.65 0.10 1 514 110 TRP N N 121.84 0.05 1 515 111 GLN H H 8.53 0.02 1 516 111 GLN CB C 31.27 0.10 1 517 111 GLN C C 176.37 0.10 1 518 111 GLN CA C 52.68 0.10 1 519 111 GLN N N 120.64 0.05 1 520 112 ARG H H 7.98 0.02 1 521 112 ARG CB C 31.27 0.10 1 522 112 ARG CA C 59.21 0.10 1 523 112 ARG N N 126.14 0.05 1 524 113 PRO CB C 32.28 0.10 1 525 113 PRO C C 177.60 0.10 1 526 113 PRO CA C 62.93 0.10 1 527 114 LEU H H 8.75 0.02 1 528 114 LEU CB C 43.48 0.10 1 529 114 LEU C C 177.40 0.10 1 530 114 LEU CA C 55.95 0.10 1 531 114 LEU N N 122.83 0.05 1 532 115 VAL H H 8.22 0.02 1 533 115 VAL CB C 32.98 0.10 1 534 115 VAL C C 176.63 0.10 1 535 115 VAL CA C 61.85 0.10 1 536 115 VAL N N 122.22 0.05 1 537 116 THR H H 8.36 0.02 1 538 116 THR CB C 69.67 0.10 1 539 116 THR C C 174.88 0.10 1 540 116 THR CA C 61.23 0.10 1 541 116 THR N N 118.76 0.05 1 542 117 ILE H H 8.31 0.02 1 543 117 ILE CB C 38.92 0.10 1 544 117 ILE C C 176.36 0.10 1 545 117 ILE CA C 60.76 0.10 1 546 117 ILE N N 124.63 0.05 1 547 118 LYS H H 8.56 0.02 1 548 118 LYS CB C 33.33 0.10 1 549 118 LYS C C 175.79 0.10 1 550 118 LYS CA C 55.95 0.10 1 551 118 LYS N N 126.72 0.05 1 552 119 ILE H H 8.45 0.02 1 553 119 ILE CB C 38.57 0.10 1 554 119 ILE C C 177.27 0.10 1 555 119 ILE CA C 61.07 0.10 1 556 119 ILE N N 124.11 0.05 1 557 120 GLY H H 8.67 0.02 1 558 120 GLY C C 175.07 0.10 1 559 120 GLY CA C 45.07 0.10 1 560 120 GLY N N 114.21 0.05 1 561 121 GLY H H 8.49 0.02 1 562 121 GLY C C 174.69 0.10 1 563 121 GLY CA C 45.07 0.10 1 564 121 GLY N N 109.95 0.05 1 565 122 GLN H H 8.56 0.02 1 566 122 GLN CB C 29.83 0.10 1 567 122 GLN C C 176.63 0.10 1 568 122 GLN CA C 55.79 0.10 1 569 122 GLN N N 120.97 0.05 1 570 123 LEU H H 8.50 0.02 1 571 123 LEU CB C 42.06 0.10 1 572 123 LEU C C 175.14 0.10 1 573 123 LEU CA C 55.01 0.10 1 574 123 LEU N N 124.37 0.05 1 575 124 LYS H H 8.56 0.02 1 576 124 LYS CB C 33.33 0.10 1 577 124 LYS C C 176.39 0.10 1 578 124 LYS CA C 56.05 0.10 1 579 124 LYS N N 123.41 0.05 1 580 125 GLU H H 8.61 0.02 1 581 125 GLU CB C 30.53 0.10 1 582 125 GLU C C 175.01 0.10 1 583 125 GLU CA C 55.25 0.10 1 584 125 GLU N N 122.84 0.05 1 585 126 ALA H H 8.46 0.02 1 586 126 ALA CB C 19.69 0.10 1 587 126 ALA C C 176.53 0.10 1 588 126 ALA CA C 52.06 0.10 1 589 126 ALA N N 125.33 0.05 1 590 127 LEU H H 8.34 0.02 1 591 127 LEU CB C 43.33 0.10 1 592 127 LEU C C 176.50 0.10 1 593 127 LEU CA C 54.86 0.10 1 594 127 LEU N N 122.60 0.05 1 595 128 LEU H H 8.43 0.02 1 596 128 LEU CB C 42.53 0.10 1 597 128 LEU C C 177.60 0.10 1 598 128 LEU CA C 57.07 0.10 1 599 128 LEU N N 123.30 0.05 1 600 129 ASP H H 8.58 0.02 1 601 129 ASP CB C 40.02 0.10 1 602 129 ASP C C 176.95 0.10 1 603 129 ASP CA C 52.84 0.10 1 604 129 ASP N N 122.21 0.05 1 605 130 THR H H 8.30 0.02 1 606 130 THR CB C 70.02 0.10 1 607 130 THR C C 175.91 0.10 1 608 130 THR CA C 61.54 0.10 1 609 130 THR N N 114.21 0.05 1 610 131 GLY H H 8.69 0.02 1 611 131 GLY C C 174.88 0.10 1 612 131 GLY CA C 45.23 0.10 1 613 131 GLY N N 111.89 0.05 1 614 132 ALA H H 8.32 0.02 1 615 132 ALA CB C 20.04 0.10 1 616 132 ALA C C 174.29 0.10 1 617 132 ALA CA C 52.37 0.10 1 618 132 ALA N N 124.37 0.05 1 619 133 ASP H H 8.55 0.02 1 620 133 ASP CB C 39.36 0.10 1 621 133 ASP C C 176.56 0.10 1 622 133 ASP CA C 54.06 0.10 1 623 133 ASP N N 119.20 0.05 1 624 134 ASP H H 8.54 0.02 1 625 134 ASP CB C 39.36 0.10 1 626 134 ASP C C 177.02 0.10 1 627 134 ASP CA C 54.48 0.10 1 628 134 ASP N N 121.54 0.05 1 629 135 THR H H 8.33 0.02 1 630 135 THR CB C 70.02 0.10 1 631 135 THR C C 177.47 0.10 1 632 135 THR CA C 62.00 0.10 1 633 135 THR N N 114.66 0.05 1 634 136 VAL H H 8.26 0.02 1 635 136 VAL CB C 33.73 0.10 1 636 136 VAL C C 175.89 0.10 1 637 136 VAL CA C 61.18 0.10 1 638 136 VAL N N 122.99 0.05 1 639 137 LEU H H 8.42 0.02 1 640 137 LEU CB C 43.38 0.10 1 641 137 LEU C C 177.18 0.10 1 642 137 LEU CA C 55.17 0.10 1 643 137 LEU N N 126.49 0.05 1 644 138 GLU H H 8.57 0.02 1 645 138 GLU CB C 30.36 0.10 1 646 138 GLU C C 175.86 0.10 1 647 138 GLU CA C 54.70 0.10 1 648 138 GLU N N 122.56 0.05 1 649 139 GLU H H 8.43 0.02 1 650 139 GLU CB C 29.83 0.10 1 651 139 GLU C C 175.83 0.10 1 652 139 GLU CA C 55.79 0.10 1 653 139 GLU N N 121.03 0.05 1 654 140 MET H H 8.37 0.02 1 655 140 MET CB C 34.41 0.10 1 656 140 MET C C 176.12 0.10 1 657 140 MET CA C 54.86 0.10 1 658 140 MET N N 122.75 0.05 1 659 141 SER H H 8.55 0.02 1 660 141 SER CB C 65.07 0.10 1 661 141 SER C C 174.22 0.10 1 662 141 SER CA C 56.93 0.10 1 663 141 SER N N 121.82 0.05 1 664 142 LEU H H 8.47 0.02 1 665 142 LEU CB C 42.06 0.10 1 666 142 LEU CA C 54.86 0.10 1 667 142 LEU N N 127.21 0.05 1 668 143 PRO CB C 32.27 0.10 1 669 143 PRO C C 177.92 0.10 1 670 143 PRO CA C 63.09 0.10 1 671 144 GLY H H 8.59 0.02 1 672 144 GLY C C 178.18 0.10 1 673 144 GLY CA C 45.23 0.10 1 674 144 GLY N N 110.17 0.05 1 675 145 ARG H H 8.33 0.02 1 676 145 ARG CB C 30.88 0.10 1 677 145 ARG C C 177.86 0.10 1 678 145 ARG CA C 55.94 0.10 1 679 145 ARG N N 121.53 0.05 1 680 146 TRP H H 8.47 0.02 1 681 146 TRP CB C 29.83 0.10 1 682 146 TRP C C 176.17 0.10 1 683 146 TRP CA C 57.34 0.10 1 684 146 TRP N N 123.24 0.05 1 685 147 LYS H H 8.08 0.02 1 686 147 LYS CB C 32.63 0.10 1 687 147 LYS CA C 53.61 0.10 1 688 147 LYS N N 125.48 0.05 1 689 148 PRO CB C 30.18 0.10 1 690 148 PRO C C 174.69 0.10 1 691 148 PRO CA C 56.25 0.10 1 692 149 LYS CB C 30.53 0.10 1 693 149 LYS C C 176.62 0.10 1 694 149 LYS CA C 51.91 0.10 1 695 149 LYS N N 125.76 0.05 1 696 150 MET H H 8.31 0.02 1 697 150 MET CB C 32.98 0.10 1 698 150 MET C C 175.60 0.10 1 699 150 MET CA C 54.86 0.10 1 700 150 MET N N 122.10 0.05 1 701 151 ILE H H 8.38 0.02 1 702 151 ILE CB C 38.57 0.10 1 703 151 ILE C C 177.27 0.10 1 704 151 ILE CA C 61.07 0.10 1 705 151 ILE N N 123.28 0.05 1 706 152 GLY H H 8.67 0.02 1 707 152 GLY C C 174.94 0.10 1 708 152 GLY CA C 44.92 0.10 1 709 152 GLY N N 114.03 0.05 1 710 153 GLY H H 8.44 0.02 1 711 153 GLY C C 174.75 0.10 1 712 153 GLY CA C 44.92 0.10 1 713 153 GLY N N 109.80 0.05 1 714 154 ILE H H 8.29 0.02 1 715 154 ILE CB C 38.57 0.10 1 716 154 ILE C C 177.27 0.10 1 717 154 ILE CA C 61.23 0.10 1 718 154 ILE N N 120.51 0.05 1 719 155 GLY H H 8.65 0.02 1 720 155 GLY C C 174.94 0.10 1 721 155 GLY CA C 45.07 0.10 1 722 155 GLY N N 113.40 0.05 1 723 156 GLY H H 8.37 0.02 1 724 156 GLY C C 178.18 0.10 1 725 156 GLY CA C 45.07 0.10 1 726 156 GLY N N 109.76 0.05 1 727 157 PHE H H 8.33 0.02 1 728 157 PHE CB C 39.96 0.10 1 729 157 PHE C C 176.17 0.10 1 730 157 PHE CA C 55.95 0.10 1 731 157 PHE N N 121.30 0.05 1 732 158 ILE H H 8.28 0.02 1 733 158 ILE CB C 37.62 0.10 1 734 158 ILE C C 174.62 0.10 1 735 158 ILE CA C 60.61 0.10 1 736 158 ILE N N 123.52 0.05 1 737 159 LYS H H 8.53 0.02 1 738 159 LYS CB C 34.41 0.10 1 739 159 LYS C C 175.40 0.10 1 740 159 LYS CA C 54.70 0.10 1 741 159 LYS N N 126.97 0.05 1 742 160 VAL H H 8.26 0.02 1 743 160 VAL CB C 32.98 0.10 1 744 160 VAL C C 176.50 0.10 1 745 160 VAL CA C 60.92 0.10 1 746 160 VAL N N 122.76 0.05 1 747 161 ARG H H 8.60 0.02 1 748 161 ARG CB C 30.88 0.10 1 749 161 ARG C C 176.62 0.10 1 750 161 ARG CA C 56.10 0.10 1 751 161 ARG N N 125.51 0.05 1 752 162 GLN H H 8.54 0.02 1 753 162 GLN CB C 29.83 0.10 1 754 162 GLN C C 176.24 0.10 1 755 162 GLN CA C 55.79 0.10 1 756 162 GLN N N 122.58 0.05 1 757 163 TYR H H 8.38 0.02 1 758 163 TYR CB C 37.18 0.10 1 759 163 TYR C C 177.11 0.10 1 760 163 TYR CA C 57.50 0.10 1 761 163 TYR N N 121.56 0.05 1 762 164 ASP H H 8.39 0.02 1 763 164 ASP CB C 38.92 0.10 1 764 164 ASP C C 176.17 0.10 1 765 164 ASP CA C 54.23 0.10 1 766 164 ASP N N 122.49 0.05 1 767 165 GLN H H 8.59 0.02 1 768 165 GLN CB C 32.98 0.10 1 769 165 GLN C C 177.62 0.10 1 770 165 GLN CA C 58.43 0.10 1 771 165 GLN N N 123.08 0.05 1 772 166 ILE H H 8.57 0.02 1 773 166 ILE CB C 39.83 0.10 1 774 166 ILE C C 177.53 0.10 1 775 166 ILE CA C 60.10 0.10 1 776 166 ILE N N 125.63 0.05 1 777 167 LEU H H 8.25 0.02 1 778 167 LEU CB C 42.98 0.10 1 779 167 LEU C C 176.69 0.10 1 780 167 LEU CA C 56.85 0.10 1 781 167 LEU N N 121.47 0.05 1 782 168 ILE H H 8.48 0.02 1 783 168 ILE CB C 38.56 0.10 1 784 168 ILE C C 174.43 0.10 1 785 168 ILE CA C 61.23 0.10 1 786 168 ILE N N 117.85 0.05 1 787 169 GLU H H 8.32 0.10 1 788 169 GLU CB C 29.92 0.10 1 789 169 GLU C C 174.69 0.10 1 790 169 GLU CA C 57.38 0.10 1 791 169 GLU N N 124.22 0.05 1 792 170 ILE H H 8.44 0.02 1 793 170 ILE CB C 38.92 0.10 1 794 170 ILE C C 176.89 0.10 1 795 170 ILE CA C 55.79 0.10 1 796 170 ILE N N 125.90 0.05 1 797 171 CYS H H 8.39 0.02 1 798 171 CYS CB C 30.18 0.10 1 799 171 CYS C C 176.37 0.10 1 800 171 CYS CA C 59.91 0.10 1 801 171 CYS N N 123.76 0.05 1 802 172 ALA H H 8.34 0.02 1 803 172 ALA CB C 18.64 0.10 1 804 172 ALA C C 176.69 0.10 1 805 172 ALA CA C 55.32 0.10 1 806 172 ALA N N 122.45 0.05 1 807 173 HIS H H 8.51 0.02 1 808 173 HIS CB C 32.97 0.10 1 809 173 HIS C C 177.86 0.10 1 810 173 HIS CA C 54.70 0.10 1 811 173 HIS N N 125.72 0.05 1 812 174 LYS H H 8.36 0.02 1 813 174 LYS CB C 33.33 0.10 1 814 174 LYS C C 176.76 0.10 1 815 174 LYS CA C 56.05 0.10 1 816 174 LYS N N 123.35 0.05 1 817 175 ALA H H 8.61 0.02 1 818 175 ALA CB C 19.34 0.10 1 819 175 ALA C C 174.69 0.10 1 820 175 ALA CA C 52.06 0.10 1 821 175 ALA N N 126.94 0.05 1 822 176 ILE H H 8.31 0.02 1 823 176 ILE CB C 38.92 0.10 1 824 176 ILE C C 177.27 0.10 1 825 176 ILE CA C 61.07 0.10 1 826 176 ILE N N 121.16 0.05 1 827 177 GLY H H 8.65 0.02 1 828 177 GLY C C 174.62 0.10 1 829 177 GLY CA C 45.07 0.10 1 830 177 GLY N N 113.66 0.05 1 831 178 THR H H 8.22 0.02 1 832 178 THR CB C 70.02 0.10 1 833 178 THR C C 175.07 0.10 1 834 178 THR CA C 60.86 0.10 1 835 178 THR N N 115.02 0.05 1 836 179 VAL H H 8.35 0.02 1 837 179 VAL CB C 32.98 0.10 1 838 179 VAL C C 176.37 0.10 1 839 179 VAL CA C 62.00 0.10 1 840 179 VAL N N 122.39 0.05 1 841 180 LEU H H 8.54 0.02 1 842 180 LEU CB C 42.16 0.10 1 843 180 LEU C C 177.53 0.10 1 844 180 LEU CA C 54.86 0.10 1 845 180 LEU N N 127.27 0.05 1 846 181 VAL H H 8.23 0.02 1 847 181 VAL CB C 32.62 0.10 1 848 181 VAL C C 175.76 0.10 1 849 181 VAL CA C 61.84 0.10 1 850 181 VAL N N 121.51 0.05 1 851 182 GLY H H 8.49 0.02 1 852 182 GLY CA C 44.45 0.10 1 853 182 GLY N N 113.35 0.05 1 854 183 PRO CB C 43.11 0.10 1 855 183 PRO C C 175.18 0.10 1 856 183 PRO CA C 60.91 0.10 1 857 184 THR H H 8.19 0.02 1 858 184 THR CA C 56.72 0.10 1 859 184 THR N N 132.55 0.05 1 860 185 PRO CB C 29.82 0.10 1 861 185 PRO C C 176.86 0.10 1 862 185 PRO CA C 55.33 0.10 1 863 186 VAL H H 8.51 0.02 1 864 186 VAL CB C 33.58 0.10 1 865 186 VAL C C 176.18 0.10 1 866 186 VAL CA C 61.25 0.10 1 867 186 VAL N N 123.37 0.05 1 868 187 ASN H H 8.60 0.02 1 869 187 ASN CB C 39.82 0.10 1 870 187 ASN C C 175.11 0.10 1 871 187 ASN CA C 50.94 0.10 1 872 187 ASN N N 122.45 0.05 1 873 188 ILE H H 8.59 0.02 1 874 188 ILE CB C 39.70 0.10 1 875 188 ILE C C 176.26 0.10 1 876 188 ILE CA C 59.79 0.10 1 877 188 ILE N N 123.54 0.05 1 878 189 ILE H H 8.26 0.02 1 879 189 ILE CB C 38.21 0.10 1 880 189 ILE C C 177.27 0.10 1 881 189 ILE CA C 61.23 0.10 1 882 189 ILE N N 121.36 0.05 1 883 190 GLY H H 8.62 0.02 1 884 190 GLY C C 176.24 0.10 1 885 190 GLY CA C 45.23 0.10 1 886 190 GLY N N 113.80 0.05 1 887 191 ARG H H 8.40 0.02 1 888 191 ARG CB C 30.53 0.10 1 889 191 ARG C C 176.76 0.10 1 890 191 ARG CA C 55.79 0.10 1 891 191 ARG N N 121.49 0.05 1 892 192 ASN H H 8.30 0.02 1 893 192 ASN CB C 38.57 0.10 1 894 192 ASN C C 174.69 0.10 1 895 192 ASN CA C 55.07 0.10 1 896 192 ASN N N 122.54 0.05 1 897 193 LEU H H 8.47 0.02 1 898 193 LEU CB C 41.71 0.10 1 899 193 LEU C C 175.53 0.10 1 900 193 LEU CA C 54.86 0.10 1 901 193 LEU N N 125.76 0.05 1 902 194 LEU H H 8.35 0.02 1 903 194 LEU CB C 42.06 0.10 1 904 194 LEU C C 178.18 0.10 1 905 194 LEU CA C 61.07 0.10 1 906 194 LEU N N 123.06 0.05 1 907 195 THR H H 8.18 0.02 1 908 195 THR CB C 69.67 0.10 1 909 195 THR C C 177.86 0.10 1 910 195 THR CA C 61.54 0.10 1 911 195 THR N N 114.80 0.05 1 912 196 GLN H H 8.24 0.02 1 913 196 GLN CB C 28.92 0.10 1 914 196 GLN C C 176.56 0.10 1 915 196 GLN CA C 57.27 0.10 1 916 196 GLN N N 122.08 0.05 1 917 197 ILE H H 8.33 0.02 1 918 197 ILE CB C 38.56 0.10 1 919 197 ILE C C 177.27 0.10 1 920 197 ILE CA C 61.23 0.10 1 921 197 ILE N N 125.18 0.05 1 922 198 GLY H H 8.57 0.02 1 923 198 GLY C C 177.15 0.10 1 924 198 GLY CA C 45.23 0.10 1 925 198 GLY N N 113.66 0.05 1 926 199 ALA H H 8.54 0.02 1 927 199 ALA CB C 19.69 0.10 1 928 199 ALA C C 178.50 0.10 1 929 199 ALA CA C 55.17 0.10 1 930 199 ALA N N 124.13 0.05 1 931 200 THR H H 8.32 0.02 1 932 200 THR CB C 69.67 0.10 1 933 200 THR C C 175.01 0.10 1 934 200 THR CA C 61.54 0.10 1 935 200 THR N N 114.07 0.05 1 936 201 LEU H H 8.41 0.02 1 937 201 LEU CB C 42.06 0.10 1 938 201 LEU C C 177.14 0.10 1 939 201 LEU CA C 54.86 0.10 1 940 201 LEU N N 125.04 0.05 1 941 202 ASN H H 8.49 0.02 1 942 202 ASN CB C 39.27 0.10 1 943 202 ASN C C 176.24 0.10 1 944 202 ASN CA C 52.68 0.10 1 945 202 ASN N N 120.18 0.05 1 946 203 PHE H H 8.41 0.02 1 947 203 PHE CB C 39.27 0.10 1 948 203 PHE C C 176.62 0.10 1 949 203 PHE CA C 57.65 0.10 1 950 203 PHE N N 122.08 0.05 1 stop_ save_