data_6917 #Corrected using PDB structure: 2AV5A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 37 A CB 23.70 18.27 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 58 L N 114.96 129.64 # 99 V N 127.30 116.17 #120 R N 127.65 115.76 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A -0.84 -0.76 0.36 -0.27 0.09 # #bmr6917.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6917.str file): #HA CA CB CO N HN #N/A -0.80 -0.80 +0.36 -0.27 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.20 +/-0.22 +/-0.15 +/-0.47 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.962 0.993 0.857 0.756 0.709 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.993 1.030 0.737 2.261 0.301 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of Pyrococcus furiosus Pop5 (PF1378), an archaeal RNase P protein. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wilson Ross C. . 2 Foster Mark P. . stop_ _BMRB_accession_number 6917 _BMRB_flat_file_name bmr6917.str _Entry_type new _Submission_date 2005-12-05 _Accession_date 2005-12-06 _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 "13C chemical shifts" 306 "1H chemical shifts" 102 "15N chemical shifts" 102 stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_title ; Structure of Pfu Pop5, an archaeal RNase P protein ; _Citation_status published _Citation_type journal _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wilson Ross C. . 2 Bohlen C. J. . 3 Foster Mark P. . 4 Bell C E. . stop_ _Journal_abbreviation "Proc. Natl. Acad. Sci. U. S. A." _Journal_volume 103 _Journal_issue 4 _Page_first 873 _Page_last 878 _Year 2006 loop_ _Keyword "RNase P" Archaea stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "pop5 monomer" _Abbreviation_common "pop5 monomer" loop_ _Mol_system_component_name _Mol_label "pop5 monomer" $Pfu_pop5 stop_ _System_molecular_weight 13708 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_Pfu_pop5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Pfu pop5" _Molecular_mass 13708 _Mol_thiol_state "all free" _Details ; The protein studied included a C72S mutation that improved solubility. Also, the N-terminal Met was observed (via mass spectrometry) to have been removed during expression in E. coli. ; ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; MSERPKTLPPTLRDKKRYIA FKVISENQFNKDEIKEAIWN ACLRTLGELGTAKAKPWLIK FDETTQTGIIRSDRNHVYDV IFSLTLVSDINGNKAIIKVL GVSGTIKRLKRKFLSQFGWR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLU 4 ARG 5 PRO 6 LYS 7 THR 8 LEU 9 PRO 10 PRO 11 THR 12 LEU 13 ARG 14 ASP 15 LYS 16 LYS 17 ARG 18 TYR 19 ILE 20 ALA 21 PHE 22 LYS 23 VAL 24 ILE 25 SER 26 GLU 27 ASN 28 GLN 29 PHE 30 ASN 31 LYS 32 ASP 33 GLU 34 ILE 35 LYS 36 GLU 37 ALA 38 ILE 39 TRP 40 ASN 41 ALA 42 CYS 43 LEU 44 ARG 45 THR 46 LEU 47 GLY 48 GLU 49 LEU 50 GLY 51 THR 52 ALA 53 LYS 54 ALA 55 LYS 56 PRO 57 TRP 58 LEU 59 ILE 60 LYS 61 PHE 62 ASP 63 GLU 64 THR 65 THR 66 GLN 67 THR 68 GLY 69 ILE 70 ILE 71 ARG 72 SER 73 ASP 74 ARG 75 ASN 76 HIS 77 VAL 78 TYR 79 ASP 80 VAL 81 ILE 82 PHE 83 SER 84 LEU 85 THR 86 LEU 87 VAL 88 SER 89 ASP 90 ILE 91 ASN 92 GLY 93 ASN 94 LYS 95 ALA 96 ILE 97 ILE 98 LYS 99 VAL 100 LEU 101 GLY 102 VAL 103 SER 104 GLY 105 THR 106 ILE 107 LYS 108 ARG 109 LEU 110 LYS 111 ARG 112 LYS 113 PHE 114 LEU 115 SER 116 GLN 117 PHE 118 GLY 119 TRP 120 ARG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Pfu_pop5 "Pyrococcus furiosus" 2261 Archaea "Not applicable" Pyrococcus furiosus "DSM 3638" 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 $Pfu_pop5 "recombinant technology" "E. coli" Escherichia coli BL21-DE3 ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details "Pfu Pop5 in Acetate buffer with sodium azide as a preservative." loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pfu_pop5 0.3 mM "[U-95% 13C; U-95% 15N]" "Sodium Acetate" 10 mM ? "Potassium Chloride" 0.5 mM ? "Sodium Azide" 0.05 mM ? stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model "Avance DRX" _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H15N HSQC 1H1513C HNCO 1H1513C HNCA 1H1513C HNCACB 1H1513C CBCACONH ; save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label $sample_1 save_ save_1H1513C_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name 1H1513C_HNCO _Sample_label $sample_1 save_ save_1H1513C_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name 1H1513C_HNCA _Sample_label $sample_1 save_ save_1H1513C_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name 1H1513C_HNCACB _Sample_label $sample_1 save_ save_1H1513C_CBCACONH _Saveframe_category NMR_applied_experiment _Experiment_name 1H1513C_CBCACONH _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 pH temperature 328 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 direct internal ? ? ? 1.0 TSP C 13 "methyl protons" ppm 0 indirect internal ? ? ? 0.251449530 TSP N 15 "methyl protons" ppm 0 indirect internal ? ? ? 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "pop5 monomer" 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 4 6 LYS H H 8.23 . 1 5 6 LYS C C 176.73 . 1 6 6 LYS CA C 56.26 . 1 7 6 LYS CB C 32.91 . 1 9 7 THR H H 7.82 . 1 10 7 THR C C 174.00 . 1 11 7 THR CA C 61.23 . 1 12 7 THR CB C 69.87 . 1 13 7 THR N N 114.87 . 1 14 8 LEU H H 8.10 . 1 15 8 LEU CA C 52.63 . 1 16 8 LEU CB C 41.53 . 1 17 8 LEU N N 126.03 . 1 21 11 THR H H 7.83 . 1 26 12 LEU H H 7.92 . 1 30 17 ARG CA C 53.38 . 1 31 18 TYR H H 8.48 . 1 32 18 TYR C C 173.88 . 1 33 18 TYR CA C 56.61 . 1 34 18 TYR CB C 41.84 . 1 35 18 TYR N N 116.99 . 1 36 19 ILE H H 9.41 . 1 37 19 ILE C C 175.85 . 1 38 19 ILE CA C 59.80 . 1 39 19 ILE CB C 41.67 . 1 40 19 ILE N N 121.16 . 1 41 20 ALA H H 8.58 . 1 42 20 ALA C C 176.60 . 1 43 20 ALA CA C 49.46 . 1 44 20 ALA CB C 20.19 . 1 45 20 ALA N N 128.66 . 1 46 21 PHE H H 8.46 . 1 47 21 PHE C C 170.63 . 1 48 21 PHE CA C 55.60 . 1 49 21 PHE CB C 42.73 . 1 50 21 PHE N N 119.15 . 1 51 22 LYS H H 8.97 . 1 52 22 LYS C C 174.49 . 1 53 22 LYS CA C 53.79 . 1 54 22 LYS CB C 37.63 . 1 55 22 LYS N N 120.76 . 1 56 23 VAL H H 8.86 . 1 57 23 VAL C C 175.17 . 1 58 23 VAL CA C 61.91 . 1 59 23 VAL CB C 32.61 . 1 60 23 VAL N N 126.56 . 1 61 24 ILE H H 9.23 . 1 62 24 ILE C C 175.58 . 1 63 24 ILE CA C 60.46 . 1 64 24 ILE CB C 37.51 . 1 65 24 ILE N N 129.24 . 1 66 25 SER H H 8.12 . 1 67 25 SER C C 173.39 . 1 68 25 SER CA C 57.56 . 1 69 25 SER CB C 64.28 . 1 70 25 SER N N 121.25 . 1 71 26 GLU H H 8.53 . 1 72 26 GLU C C 176.46 . 1 73 26 GLU CA C 57.39 . 1 74 26 GLU CB C 29.46 . 1 75 26 GLU N N 122.30 . 1 76 27 ASN H H 8.08 . 1 77 27 ASN C C 172.59 . 1 78 27 ASN CA C 52.19 . 1 79 27 ASN CB C 40.89 . 1 80 27 ASN N N 117.82 . 1 81 28 GLN H H 7.79 . 1 82 28 GLN C C 174.93 . 1 83 28 GLN CA C 54.88 . 1 84 28 GLN CB C 29.69 . 1 85 28 GLN N N 119.37 . 1 86 29 PHE H H 8.28 . 1 87 29 PHE C C 176.16 . 1 88 29 PHE CA C 57.88 . 1 89 29 PHE CB C 41.76 . 1 90 29 PHE N N 121.78 . 1 91 30 ASN H H 9.17 . 1 92 30 ASN C C 176.22 . 1 93 30 ASN CA C 50.84 . 1 94 30 ASN CB C 40.22 . 1 95 30 ASN N N 118.24 . 1 96 31 LYS H H 9.06 . 1 97 31 LYS C C 177.15 . 1 98 31 LYS CA C 59.62 . 1 99 31 LYS CB C 31.62 . 1 100 31 LYS N N 116.75 . 1 101 32 ASP H H 7.97 . 1 102 32 ASP C C 178.88 . 1 103 32 ASP CA C 57.65 . 1 104 32 ASP CB C 39.83 . 1 105 32 ASP N N 121.00 . 1 106 33 GLU H H 8.01 . 1 107 33 GLU C C 179.95 . 1 108 33 GLU CA C 58.48 . 1 109 33 GLU CB C 29.57 . 1 110 33 GLU N N 120.69 . 1 111 34 ILE H H 7.42 . 1 112 34 ILE C C 176.84 . 1 113 34 ILE CA C 60.44 . 1 114 34 ILE CB C 34.19 . 1 115 34 ILE N N 118.61 . 1 116 35 LYS H H 7.97 . 1 117 35 LYS C C 178.62 . 1 118 35 LYS CA C 60.41 . 1 119 35 LYS CB C 32.06 . 1 120 35 LYS N N 121.53 . 1 121 36 GLU H H 7.38 . 1 122 36 GLU C C 178.04 . 1 123 36 GLU CA C 58.72 . 1 124 36 GLU CB C 29.12 . 1 125 36 GLU N N 116.97 . 1 126 37 ALA H H 7.74 . 1 127 37 ALA C C 180.92 . 1 128 37 ALA CA C 54.79 . 1 129 37 ALA CB C 23.66 . 1 130 37 ALA N N 121.27 . 1 131 38 ILE H H 8.05 . 1 132 38 ILE C C 177.12 . 1 133 38 ILE CA C 64.98 . 1 134 38 ILE CB C 37.48 . 1 135 38 ILE N N 116.99 . 1 136 39 TRP H H 7.60 . 1 137 39 TRP C C 177.83 . 1 138 39 TRP CA C 60.73 . 1 139 39 TRP CB C 28.94 . 1 140 39 TRP N N 120.69 . 1 141 40 ASN H H 8.56 . 1 142 40 ASN C C 177.68 . 1 143 40 ASN CA C 56.12 . 1 144 40 ASN CB C 38.14 . 1 145 40 ASN N N 114.88 . 1 146 41 ALA H H 7.99 . 1 147 41 ALA C C 180.98 . 1 148 41 ALA CA C 54.93 . 1 149 41 ALA CB C 17.57 . 1 150 41 ALA N N 122.28 . 1 151 42 CYS H H 7.52 . 1 152 42 CYS C C 176.29 . 1 153 42 CYS CA C 63.12 . 1 154 42 CYS CB C 26.45 . 1 155 42 CYS N N 117.53 . 1 156 43 LEU H H 8.29 . 1 157 43 LEU C C 180.45 . 1 158 43 LEU CA C 58.27 . 1 160 43 LEU N N 122.13 . 1 161 44 ARG H H 7.76 . 1 162 44 ARG C C 177.54 . 1 163 44 ARG CA C 58.71 . 1 164 44 ARG CB C 30.35 . 1 165 44 ARG N N 116.07 . 1 166 45 THR H H 7.24 . 1 167 45 THR C C 175.28 . 1 168 45 THR CA C 64.80 . 1 169 45 THR CB C 69.21 . 1 170 45 THR N N 112.86 . 1 171 46 LEU H H 8.88 . 1 172 46 LEU C C 179.11 . 1 173 46 LEU CA C 54.58 . 1 175 46 LEU N N 119.10 . 1 176 47 GLY H H 7.17 . 1 177 47 GLY C C 174.59 . 1 178 47 GLY CA C 43.88 . 1 179 47 GLY N N 105.60 . 1 180 48 GLU H H 8.87 . 1 181 48 GLU C C 179.12 . 1 182 48 GLU CA C 60.51 . 1 183 48 GLU CB C 29.36 . 1 184 48 GLU N N 121.95 . 1 185 49 LEU H H 8.39 . 1 186 49 LEU C C 179.76 . 1 187 49 LEU CA C 57.55 . 1 188 49 LEU CB C 40.91 . 1 189 49 LEU N N 120.19 . 1 190 50 GLY H H 7.67 . 1 191 50 GLY C C 176.74 . 1 192 50 GLY CA C 47.20 . 1 193 50 GLY N N 105.26 . 1 194 51 THR H H 7.70 . 1 196 51 THR CA C 68.18 . 1 197 51 THR CB C 67.73 . 1 198 51 THR N N 119.40 . 1 199 52 ALA H H 7.57 . 1 204 53 LYS H H 7.33 . 1 205 53 LYS C C 177.45 . 1 206 53 LYS CA C 57.95 . 1 209 54 ALA H H 7.37 . 1 210 54 ALA C C 176.31 . 1 211 54 ALA CA C 53.87 . 1 212 54 ALA CB C 18.88 . 1 213 54 ALA N N 119.12 . 1 214 55 LYS H H 7.97 . 1 215 55 LYS CA C 56.24 . 1 216 55 LYS CB C 31.25 . 1 217 55 LYS N N 112.18 . 1 218 57 TRP C C 176.19 . 1 219 57 TRP CA C 58.11 . 1 220 58 LEU H H 7.26 . 1 221 58 LEU C C 174.46 . 1 222 58 LEU CA C 56.96 . 1 223 58 LEU CB C 41.58 . 1 224 58 LEU N N 114.96 . 1 225 59 ILE H H 8.53 . 1 226 59 ILE C C 176.39 . 1 227 59 ILE CA C 61.46 . 1 228 59 ILE CB C 37.64 . 1 229 59 ILE N N 128.15 . 1 230 60 LYS H H 7.21 . 1 231 60 LYS C C 173.63 . 1 232 60 LYS CA C 55.69 . 1 233 60 LYS CB C 36.17 . 1 234 60 LYS N N 115.77 . 1 235 61 PHE H H 8.91 . 1 236 61 PHE C C 172.57 . 1 237 61 PHE CA C 56.58 . 1 238 61 PHE CB C 43.30 . 1 239 61 PHE N N 125.94 . 1 240 62 ASP H H 9.07 . 1 241 62 ASP C C 175.58 . 1 242 62 ASP CA C 52.31 . 1 243 62 ASP CB C 42.00 . 1 244 62 ASP N N 127.25 . 1 245 63 GLU H H 8.96 . 1 246 63 GLU C C 178.92 . 1 247 63 GLU CA C 58.75 . 1 248 63 GLU CB C 29.18 . 1 249 63 GLU N N 125.95 . 1 250 64 THR H H 7.94 . 1 251 64 THR C C 175.93 . 1 252 64 THR CA C 66.37 . 1 254 64 THR N N 114.34 . 1 255 65 THR H H 6.93 . 1 256 65 THR C C 174.33 . 1 257 65 THR CA C 61.45 . 1 258 65 THR CB C 70.45 . 1 259 65 THR N N 106.86 . 1 260 66 GLN H H 7.97 . 1 261 66 GLN C C 174.37 . 1 262 66 GLN CA C 56.15 . 1 263 66 GLN CB C 26.43 . 1 264 66 GLN N N 118.08 . 1 265 67 THR H H 6.82 . 1 266 67 THR C C 173.71 . 1 267 67 THR CA C 57.72 . 1 268 67 THR CB C 72.88 . 1 269 67 THR N N 104.80 . 1 270 68 GLY H H 7.33 . 1 271 68 GLY C C 170.67 . 1 272 68 GLY CA C 46.89 . 1 273 68 GLY N N 103.48 . 1 274 69 ILE H H 8.08 . 1 275 69 ILE C C 175.56 . 1 276 69 ILE CA C 60.19 . 1 277 69 ILE CB C 42.78 . 1 278 69 ILE N N 114.44 . 1 279 70 ILE H H 9.41 . 1 280 70 ILE C C 174.55 . 1 281 70 ILE CA C 59.05 . 1 282 70 ILE CB C 42.63 . 1 283 70 ILE N N 127.53 . 1 284 71 ARG H H 9.55 . 1 285 71 ARG C C 174.19 . 1 286 71 ARG CA C 54.47 . 1 287 71 ARG CB C 33.96 . 1 288 71 ARG N N 128.19 . 1 289 72 SER H H 8.46 . 1 290 72 SER C C 173.92 . 1 291 72 SER CA C 56.86 . 1 292 72 SER CB C 67.30 . 1 293 72 SER N N 118.06 . 1 294 73 ASP H H 8.61 . 1 295 73 ASP C C 178.90 . 1 296 73 ASP CA C 55.09 . 1 297 73 ASP CB C 43.95 . 1 298 73 ASP N N 121.75 . 1 299 74 ARG H H 8.48 . 1 300 74 ARG C C 176.45 . 1 301 74 ARG CA C 59.15 . 1 302 74 ARG CB C 29.14 . 1 303 74 ARG N N 124.27 . 1 304 75 ASN H H 8.54 . 1 305 75 ASN C C 175.61 . 1 306 75 ASN CA C 54.34 . 1 307 75 ASN CB C 38.00 . 1 308 75 ASN N N 115.93 . 1 309 76 HIS H H 7.56 . 1 310 76 HIS C C 174.88 . 1 311 76 HIS CA C 55.92 . 1 312 76 HIS CB C 30.51 . 1 313 76 HIS N N 114.03 . 1 314 77 VAL H H 7.19 . 1 315 77 VAL C C 176.42 . 1 316 77 VAL CA C 65.54 . 1 317 77 VAL CB C 30.89 . 1 318 77 VAL N N 121.23 . 1 319 78 TYR H H 8.04 . 1 320 78 TYR C C 177.67 . 1 321 78 TYR CA C 61.83 . 1 322 78 TYR CB C 36.49 . 1 323 78 TYR N N 118.89 . 1 324 79 ASP H H 7.54 . 1 325 79 ASP C C 179.06 . 1 326 79 ASP CA C 57.09 . 1 327 79 ASP CB C 40.41 . 1 328 79 ASP N N 120.70 . 1 329 80 VAL H H 7.61 . 1 330 80 VAL C C 177.46 . 1 331 80 VAL CA C 66.56 . 1 332 80 VAL CB C 30.91 . 1 333 80 VAL N N 121.25 . 1 334 81 ILE H H 8.12 . 1 335 81 ILE C C 177.85 . 1 336 81 ILE CA C 67.04 . 1 337 81 ILE CB C 37.70 . 1 338 81 ILE N N 119.43 . 1 339 82 PHE H H 8.43 . 1 340 82 PHE C C 178.04 . 1 341 82 PHE CA C 60.78 . 1 342 82 PHE CB C 38.38 . 1 343 82 PHE N N 120.18 . 1 344 83 SER H H 7.49 . 1 345 83 SER C C 176.56 . 1 346 83 SER CA C 62.70 . 1 347 83 SER CB C 62.94 . 1 348 83 SER N N 113.87 . 1 349 84 LEU H H 7.84 . 1 350 84 LEU C C 179.55 . 1 351 84 LEU CA C 57.07 . 1 352 84 LEU CB C 40.19 . 1 353 84 LEU N N 118.61 . 1 354 85 THR H H 7.91 . 1 355 85 THR C C 174.68 . 1 356 85 THR CA C 64.51 . 1 357 85 THR CB C 69.35 . 1 358 85 THR N N 111.67 . 1 359 86 LEU H H 6.76 . 1 360 86 LEU C C 177.85 . 1 361 86 LEU CA C 54.61 . 1 362 86 LEU CB C 41.78 . 1 363 86 LEU N N 118.84 . 1 364 87 VAL H H 6.90 . 1 365 87 VAL C C 176.24 . 1 366 87 VAL CA C 64.35 . 1 367 87 VAL CB C 31.50 . 1 368 87 VAL N N 120.65 . 1 369 88 SER H H 8.78 . 1 370 88 SER C C 174.80 . 1 371 88 SER CA C 58.03 . 1 373 88 SER N N 120.64 . 1 374 89 ASP H H 7.62 . 1 375 89 ASP C C 174.03 . 1 376 89 ASP CA C 53.60 . 1 377 89 ASP CB C 44.44 . 1 378 89 ASP N N 121.80 . 1 379 90 ILE H H 8.62 . 1 380 90 ILE C C 175.79 . 1 381 90 ILE CA C 61.32 . 1 382 90 ILE CB C 39.20 . 1 383 90 ILE N N 120.71 . 1 384 91 ASN H H 9.02 . 1 385 91 ASN C C 174.68 . 1 386 91 ASN CA C 53.79 . 1 387 91 ASN CB C 37.30 . 1 388 91 ASN N N 126.06 . 1 389 92 GLY H H 8.66 . 1 390 92 GLY C C 174.18 . 1 391 92 GLY CA C 45.27 . 1 392 92 GLY N N 104.23 . 1 393 93 ASN H H 7.71 . 1 394 93 ASN C C 174.36 . 1 395 93 ASN CA C 51.68 . 1 396 93 ASN CB C 40.67 . 1 397 93 ASN N N 118.38 . 1 398 94 LYS H H 8.72 . 1 399 94 LYS C C 176.26 . 1 400 94 LYS CA C 57.80 . 1 401 94 LYS CB C 31.73 . 1 402 94 LYS N N 124.82 . 1 403 95 ALA H H 7.79 . 1 404 95 ALA C C 173.52 . 1 405 95 ALA CA C 51.71 . 1 406 95 ALA CB C 21.83 . 1 407 95 ALA N N 127.64 . 1 408 96 ILE H H 7.86 . 1 409 96 ILE C C 174.93 . 1 410 96 ILE CA C 58.86 . 1 411 96 ILE CB C 41.93 . 1 412 96 ILE N N 112.75 . 1 413 97 ILE H H 9.31 . 1 415 97 ILE CA C 60.36 . 1 417 97 ILE N N 123.82 . 1 418 98 LYS H H 8.97 . 1 419 98 LYS C C 176.00 . 1 423 99 VAL H H 8.70 . 1 424 99 VAL C C 175.91 . 1 425 99 VAL CA C 63.59 . 1 427 99 VAL N N 127.30 . 1 428 100 LEU H H 8.73 . 1 430 100 LEU CA C 55.11 . 1 432 100 LEU N N 128.18 . 1 433 101 GLY H H 6.63 . 1 436 102 VAL C C 175.48 . 1 437 103 SER H H 8.71 . 1 438 103 SER C C 171.79 . 1 439 103 SER CA C 57.56 . 1 440 103 SER N N 117.03 . 1 441 104 GLY H H 7.04 . 1 442 104 GLY CA C 43.43 . 1 443 104 GLY N N 118.79 . 1 444 106 ILE C C 177.49 . 1 445 106 ILE CA C 64.82 . 1 446 106 ILE CB C 41.22 . 1 447 107 LYS H H 8.18 . 1 448 107 LYS C C 178.88 . 1 449 107 LYS CA C 60.11 . 1 450 107 LYS CB C 32.02 . 1 451 107 LYS N N 120.18 . 1 452 108 ARG H H 7.30 . 1 453 108 ARG C C 177.88 . 1 454 108 ARG CA C 58.77 . 1 455 108 ARG CB C 29.58 . 1 456 108 ARG N N 117.50 . 1 457 109 LEU H H 7.49 . 1 459 109 LEU CA C 57.72 . 1 460 109 LEU CB C 43.12 . 1 461 109 LEU N N 119.30 . 1 462 110 LYS H H 8.31 . 1 463 110 LYS C C 178.11 . 1 464 110 LYS CA C 60.05 . 1 465 110 LYS CB C 32.06 . 1 467 111 ARG H H 7.44 . 1 468 111 ARG C C 178.40 . 1 469 111 ARG CA C 58.55 . 1 471 111 ARG N N 116.87 . 1 472 112 LYS H H 7.98 . 1 473 112 LYS C C 177.92 . 1 474 112 LYS CA C 57.93 . 1 475 112 LYS CB C 32.35 . 1 476 112 LYS N N 115.37 . 1 477 113 PHE H H 7.54 . 1 478 113 PHE CA C 58.09 . 1 479 113 PHE CB C 41.36 . 1 480 113 PHE N N 111.69 . 1 481 114 LEU C C 178.87 . 1 482 114 LEU CA C 54.68 . 1 484 115 SER H H 8.10 . 1 485 115 SER C C 178.12 . 1 486 115 SER CA C 61.52 . 1 487 115 SER N N 121.85 . 1 488 116 GLN H H 8.73 . 1 490 116 GLN CA C 57.25 . 1 491 116 GLN CB C 27.43 . 1 492 116 GLN N N 121.25 . 1 493 117 PHE H H 7.50 . 1 498 118 GLY H H 7.75 . 1 502 119 TRP H H 7.33 . 1 507 120 ARG H H 8.02 . 1 stop_ save_