data_25247 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift 1H, 13C, 15N Assignments of FliG bound to unlabeled FliF C-terminal peptide ; _BMRB_accession_number 25247 _BMRB_flat_file_name bmr25247.str _Entry_type original _Submission_date 2014-09-24 _Accession_date 2014-09-24 _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 Levenson Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 273 "13C chemical shifts" 557 "15N chemical shifts" 273 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-11 original BMRB . stop_ _Original_release_date 2014-09-25 save_ ############################# # Citation for this entry # ############################# save_Biochemistry_2 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28089452 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lynch Michael J. . 2 Levenson Robert . . 3 Kim Eun A. . 4 Sircar Ria . . 5 Blair David F. . 6 Dahlquist Frederick W. . 7 Crane Brian R. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 25 _Journal_issue 2 _Journal_ISSN 1878-4186 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 317 _Page_last 328 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'FliFc-FliG complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FliFc $FliFc FliG $FliG stop_ _System_molecular_weight 43300 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details '15N,13C,2H uniformly-labeled FliG bound to unlabeled peptide corresponding to C-terminal region of FliF, forming a heterodimer.' save_ ######################## # Monomeric polymers # ######################## save_FliFc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FliFc _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 38 _Mol_residue_sequence ; VSPEEKELLELLEELENIFS RSPSDIAEIVRLWFFERG ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 SER 3 PRO 4 GLU 5 GLU 6 LYS 7 GLU 8 LEU 9 LEU 10 GLU 11 LEU 12 LEU 13 GLU 14 GLU 15 LEU 16 GLU 17 ASN 18 ILE 19 PHE 20 SER 21 ARG 22 SER 23 PRO 24 SER 25 ASP 26 ILE 27 ALA 28 GLU 29 ILE 30 VAL 31 ARG 32 LEU 33 TRP 34 PHE 35 PHE 36 GLU 37 ARG 38 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_FliG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FliG _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 342 _Mol_residue_sequence ; MHHHQHHMPEKKIDGRRKAA VLLVALGPEKAAQVMKHLDE ETVEQLVVEIANIGRVTPEE KKQVLEEFLSLAKAKEMISE GGIEYAKKVLEKAFGPERAR KIIERLTSSLQVKPFSFVRD TDPVQLVNFLQSEHPQTIAV VLSYLDPPVAAQILGALPEE LQTEVLKRIALLERTSPEVV KEIERNLEKKISGFVSRTFS KVGGIDTAAEIMNNLDRTTE KKIMDKLVQENPELADEIRR RMFVFEDILKLDDRSIQLVL REVDTRDLALALKGASDELK EKIFKNMSKRAAALLKDELE YMGPVRLKDVEEAQQKIINI IRRLEEAGEIVIARGGGEEL IM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 MET 2 -5 HIS 3 -4 HIS 4 -3 HIS 5 -2 GLN 6 -1 HIS 7 0 HIS 8 1 MET 9 2 PRO 10 3 GLU 11 4 LYS 12 5 LYS 13 6 ILE 14 7 ASP 15 8 GLY 16 9 ARG 17 10 ARG 18 11 LYS 19 12 ALA 20 13 ALA 21 14 VAL 22 15 LEU 23 16 LEU 24 17 VAL 25 18 ALA 26 19 LEU 27 20 GLY 28 21 PRO 29 22 GLU 30 23 LYS 31 24 ALA 32 25 ALA 33 26 GLN 34 27 VAL 35 28 MET 36 29 LYS 37 30 HIS 38 31 LEU 39 32 ASP 40 33 GLU 41 34 GLU 42 35 THR 43 36 VAL 44 37 GLU 45 38 GLN 46 39 LEU 47 40 VAL 48 41 VAL 49 42 GLU 50 43 ILE 51 44 ALA 52 45 ASN 53 46 ILE 54 47 GLY 55 48 ARG 56 49 VAL 57 50 THR 58 51 PRO 59 52 GLU 60 53 GLU 61 54 LYS 62 55 LYS 63 56 GLN 64 57 VAL 65 58 LEU 66 59 GLU 67 60 GLU 68 61 PHE 69 62 LEU 70 63 SER 71 64 LEU 72 65 ALA 73 66 LYS 74 67 ALA 75 68 LYS 76 69 GLU 77 70 MET 78 71 ILE 79 72 SER 80 73 GLU 81 74 GLY 82 75 GLY 83 76 ILE 84 77 GLU 85 78 TYR 86 79 ALA 87 80 LYS 88 81 LYS 89 82 VAL 90 83 LEU 91 84 GLU 92 85 LYS 93 86 ALA 94 87 PHE 95 88 GLY 96 89 PRO 97 90 GLU 98 91 ARG 99 92 ALA 100 93 ARG 101 94 LYS 102 95 ILE 103 96 ILE 104 97 GLU 105 98 ARG 106 99 LEU 107 100 THR 108 101 SER 109 102 SER 110 103 LEU 111 104 GLN 112 105 VAL 113 106 LYS 114 107 PRO 115 108 PHE 116 109 SER 117 110 PHE 118 111 VAL 119 112 ARG 120 113 ASP 121 114 THR 122 115 ASP 123 116 PRO 124 117 VAL 125 118 GLN 126 119 LEU 127 120 VAL 128 121 ASN 129 122 PHE 130 123 LEU 131 124 GLN 132 125 SER 133 126 GLU 134 127 HIS 135 128 PRO 136 129 GLN 137 130 THR 138 131 ILE 139 132 ALA 140 133 VAL 141 134 VAL 142 135 LEU 143 136 SER 144 137 TYR 145 138 LEU 146 139 ASP 147 140 PRO 148 141 PRO 149 142 VAL 150 143 ALA 151 144 ALA 152 145 GLN 153 146 ILE 154 147 LEU 155 148 GLY 156 149 ALA 157 150 LEU 158 151 PRO 159 152 GLU 160 153 GLU 161 154 LEU 162 155 GLN 163 156 THR 164 157 GLU 165 158 VAL 166 159 LEU 167 160 LYS 168 161 ARG 169 162 ILE 170 163 ALA 171 164 LEU 172 165 LEU 173 166 GLU 174 167 ARG 175 168 THR 176 169 SER 177 170 PRO 178 171 GLU 179 172 VAL 180 173 VAL 181 174 LYS 182 175 GLU 183 176 ILE 184 177 GLU 185 178 ARG 186 179 ASN 187 180 LEU 188 181 GLU 189 182 LYS 190 183 LYS 191 184 ILE 192 185 SER 193 186 GLY 194 187 PHE 195 188 VAL 196 189 SER 197 190 ARG 198 191 THR 199 192 PHE 200 193 SER 201 194 LYS 202 195 VAL 203 196 GLY 204 197 GLY 205 198 ILE 206 199 ASP 207 200 THR 208 201 ALA 209 202 ALA 210 203 GLU 211 204 ILE 212 205 MET 213 206 ASN 214 207 ASN 215 208 LEU 216 209 ASP 217 210 ARG 218 211 THR 219 212 THR 220 213 GLU 221 214 LYS 222 215 LYS 223 216 ILE 224 217 MET 225 218 ASP 226 219 LYS 227 220 LEU 228 221 VAL 229 222 GLN 230 223 GLU 231 224 ASN 232 225 PRO 233 226 GLU 234 227 LEU 235 228 ALA 236 229 ASP 237 230 GLU 238 231 ILE 239 232 ARG 240 233 ARG 241 234 ARG 242 235 MET 243 236 PHE 244 237 VAL 245 238 PHE 246 239 GLU 247 240 ASP 248 241 ILE 249 242 LEU 250 243 LYS 251 244 LEU 252 245 ASP 253 246 ASP 254 247 ARG 255 248 SER 256 249 ILE 257 250 GLN 258 251 LEU 259 252 VAL 260 253 LEU 261 254 ARG 262 255 GLU 263 256 VAL 264 257 ASP 265 258 THR 266 259 ARG 267 260 ASP 268 261 LEU 269 262 ALA 270 263 LEU 271 264 ALA 272 265 LEU 273 266 LYS 274 267 GLY 275 268 ALA 276 269 SER 277 270 ASP 278 271 GLU 279 272 LEU 280 273 LYS 281 274 GLU 282 275 LYS 283 276 ILE 284 277 PHE 285 278 LYS 286 279 ASN 287 280 MET 288 281 SER 289 282 LYS 290 283 ARG 291 284 ALA 292 285 ALA 293 286 ALA 294 287 LEU 295 288 LEU 296 289 LYS 297 290 ASP 298 291 GLU 299 292 LEU 300 293 GLU 301 294 TYR 302 295 MET 303 296 GLY 304 297 PRO 305 298 VAL 306 299 ARG 307 300 LEU 308 301 LYS 309 302 ASP 310 303 VAL 311 304 GLU 312 305 GLU 313 306 ALA 314 307 GLN 315 308 GLN 316 309 LYS 317 310 ILE 318 311 ILE 319 312 ASN 320 313 ILE 321 314 ILE 322 315 ARG 323 316 ARG 324 317 LEU 325 318 GLU 326 319 GLU 327 320 ALA 328 321 GLY 329 322 GLU 330 323 ILE 331 324 VAL 332 325 ILE 333 326 ALA 334 327 ARG 335 328 GLY 336 329 GLY 337 330 GLY 338 331 GLU 339 332 GLU 340 333 LEU 341 334 ILE 342 335 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FliFc 'Thermotoga maritima' 2336 Bacteria . Thermotoga maritima $FliG 'Thermotoga maritima' 2336 Bacteria . Thermotoga maritima 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 _Details $FliFc 'obtained from a vendor' . . . . . Synthesized $FliG 'recombinant technology' . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_FliG-FliFc _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FliFc 350 mM 'natural abundance' $FliG 350 mM '[U-13C; U-15N; U-2H]' 'Sodium phosphate' 50 mM 'natural abundance' NaCl 100 mM 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ 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 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $FliG-FliFc save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $FliG-FliFc save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $FliG-FliFc save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $FliG-FliFc save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $FliG-FliFc save_ ####################### # Sample conditions # ####################### save_Sodium_Phosphate _Saveframe_category sample_conditions _Details '50 mM Sodium phosphate, 100 mM NaCl, 1 mM EDTA, pH 6.5' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 6.5 . pH pressure 1 . atm temperature 313 . 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 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 external 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_ _Software_label $ANSIG stop_ loop_ _Experiment_label '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(COCA)CB' stop_ loop_ _Sample_label $FliG-FliFc stop_ _Sample_conditions_label $Sodium_Phosphate _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FliG _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 11 18 LYS CA C 57.47 0.1 1 2 11 18 LYS CB C 27.40 0.1 1 3 12 19 ALA H H 7.625 0.02 1 4 12 19 ALA CA C 52.38 0.1 1 5 12 19 ALA CB C 16.29 0.1 1 6 12 19 ALA N N 118.01 0.1 1 7 13 20 ALA H H 7.699 0.02 1 8 13 20 ALA CA C 52.51 0.1 1 9 13 20 ALA CB C 15.68 0.1 1 10 13 20 ALA N N 119.13 0.1 1 11 14 21 VAL H H 8.742 0.02 1 12 14 21 VAL CA C 64.00 0.1 1 13 14 21 VAL CB C 27.93 0.1 1 14 14 21 VAL N N 118.56 0.1 1 15 15 22 LEU H H 8.155 0.02 1 16 15 22 LEU CA C 54.89 0.1 1 17 15 22 LEU CB C 38.62 0.1 1 18 15 22 LEU N N 120.86 0.1 1 19 16 23 LEU H H 7.854 0.02 1 20 16 23 LEU CA C 55.09 0.1 1 21 16 23 LEU CB C 36.92 0.1 1 22 16 23 LEU N N 117.15 0.1 1 23 17 24 VAL H H 8.578 0.02 1 24 17 24 VAL CA C 63.27 0.1 1 25 17 24 VAL CB C 28.00 0.1 1 26 17 24 VAL N N 122.63 0.1 1 27 18 25 ALA H H 8.226 0.02 1 28 18 25 ALA CA C 51.47 0.1 1 29 18 25 ALA CB C 13.71 0.1 1 30 18 25 ALA N N 123.94 0.1 1 31 19 26 LEU H H 7.458 0.02 1 32 19 26 LEU CA C 53.61 0.1 1 33 19 26 LEU CB C 39.65 0.1 1 34 19 26 LEU N N 116.58 0.1 1 35 20 27 GLY H H 7.146 0.02 1 36 20 27 GLY CA C 40.87 0.1 1 37 20 27 GLY N N 107.87 0.1 1 38 22 29 GLU CA C 56.98 0.1 1 39 22 29 GLU CB C 25.80 0.1 1 40 23 30 LYS H H 8.308 0.02 1 41 23 30 LYS CA C 56.51 0.1 1 42 23 30 LYS CB C 29.58 0.1 1 43 23 30 LYS N N 120.56 0.1 1 44 24 31 ALA H H 8.896 0.02 1 45 24 31 ALA CA C 52.72 0.1 1 46 24 31 ALA CB C 15.34 0.1 1 47 24 31 ALA N N 121.34 0.1 1 48 25 32 ALA H H 7.662 0.02 1 49 25 32 ALA CA C 52.30 0.1 1 50 25 32 ALA CB C 14.55 0.1 1 51 25 32 ALA N N 118.89 0.1 1 52 26 33 GLN H H 7.263 0.02 1 53 26 33 GLN CA C 55.32 0.1 1 54 26 33 GLN CB C 25.26 0.1 1 55 26 33 GLN N N 115.94 0.1 1 56 27 34 VAL H H 7.713 0.02 1 57 27 34 VAL CA C 63.83 0.1 1 58 27 34 VAL CB C 28.38 0.1 1 59 27 34 VAL N N 119.28 0.1 1 60 28 35 MET H H 8.347 0.02 1 61 28 35 MET CA C 56.61 0.1 1 62 28 35 MET CB C 29.89 0.1 1 63 28 35 MET N N 116.24 0.1 1 64 29 36 LYS H H 7.019 0.02 1 65 29 36 LYS CA C 55.13 0.1 1 66 29 36 LYS CB C 28.58 0.1 1 67 29 36 LYS N N 117.09 0.1 1 68 30 37 HIS H H 7.406 0.02 1 69 30 37 HIS CA C 53.59 0.1 1 70 30 37 HIS CB C 27.25 0.1 1 71 30 37 HIS N N 115.98 0.1 1 72 31 38 LEU H H 7.339 0.02 1 73 31 38 LEU CA C 49.94 0.1 1 74 31 38 LEU CB C 41.32 0.1 1 75 31 38 LEU N N 120.31 0.1 1 76 32 39 ASP H H 8.038 0.02 1 77 32 39 ASP CA C 50.39 0.1 1 78 32 39 ASP CB C 38.75 0.1 1 79 32 39 ASP N N 118.67 0.1 1 80 33 40 GLU H H 8.688 0.02 1 81 33 40 GLU CA C 57.34 0.1 1 82 33 40 GLU CB C 26.34 0.1 1 83 33 40 GLU N N 120.66 0.1 1 84 34 41 GLU H H 8.468 0.02 1 85 34 41 GLU CA C 56.75 0.1 1 86 34 41 GLU CB C 25.98 0.1 1 87 34 41 GLU N N 119.56 0.1 1 88 35 42 THR H H 7.763 0.02 1 89 35 42 THR CA C 63.65 0.1 1 90 35 42 THR CB C 64.34 0.1 1 91 35 42 THR N N 119.21 0.1 1 92 36 43 VAL H H 8.072 0.02 1 93 36 43 VAL CA C 65.12 0.1 1 94 36 43 VAL CB C 28.35 0.1 1 95 36 43 VAL N N 121.79 0.1 1 96 37 44 GLU H H 7.978 0.02 1 97 37 44 GLU CA C 56.68 0.1 1 98 37 44 GLU CB C 26.00 0.1 1 99 37 44 GLU N N 117.44 0.1 1 100 38 45 GLN H H 7.292 0.02 1 101 38 45 GLN CA C 55.43 0.1 1 102 38 45 GLN CB C 26.21 0.1 1 103 38 45 GLN N N 115.63 0.1 1 104 39 46 LEU H H 8.528 0.02 1 105 39 46 LEU CA C 55.13 0.1 1 106 39 46 LEU CB C 38.86 0.1 1 107 39 46 LEU N N 123.00 0.1 1 108 40 47 VAL H H 8.594 0.02 1 109 40 47 VAL CA C 64.02 0.1 1 110 40 47 VAL CB C 28.12 0.1 1 111 40 47 VAL N N 118.53 0.1 1 112 41 48 VAL H H 6.963 0.02 1 113 41 48 VAL CA C 63.23 0.1 1 114 41 48 VAL CB C 28.44 0.1 1 115 41 48 VAL N N 121.05 0.1 1 116 42 49 GLU H H 7.751 0.02 1 117 42 49 GLU CA C 55.96 0.1 1 118 42 49 GLU CB C 25.85 0.1 1 119 42 49 GLU N N 120.95 0.1 1 120 43 50 ILE H H 8.555 0.02 1 121 43 50 ILE CA C 62.86 0.1 1 122 43 50 ILE CB C 35.46 0.1 1 123 43 50 ILE N N 118.74 0.1 1 124 44 51 ALA H H 7.758 0.02 1 125 44 51 ALA CA C 51.63 0.1 1 126 44 51 ALA CB C 14.80 0.1 1 127 44 51 ALA N N 122.41 0.1 1 128 45 52 ASN H H 7.447 0.02 1 129 45 52 ASN CA C 49.90 0.1 1 130 45 52 ASN CB C 36.54 0.1 1 131 45 52 ASN N N 114.89 0.1 1 132 46 53 ILE H H 7.193 0.02 1 133 46 53 ILE CA C 60.10 0.1 1 134 46 53 ILE CB C 35.68 0.1 1 135 46 53 ILE N N 121.96 0.1 1 136 47 54 GLY H H 8.198 0.02 1 137 47 54 GLY CA C 42.70 0.1 1 138 47 54 GLY N N 110.30 0.1 1 139 48 55 ARG H H 8.129 0.02 1 140 48 55 ARG CA C 53.15 0.1 1 141 48 55 ARG CB C 27.02 0.1 1 142 48 55 ARG N N 124.33 0.1 1 143 49 56 VAL H H 8.285 0.02 1 144 49 56 VAL CA C 58.16 0.1 1 145 49 56 VAL CB C 29.74 0.1 1 146 49 56 VAL N N 127.08 0.1 1 147 50 57 THR H H 8.908 0.02 1 148 50 57 THR CA C 57.41 0.1 1 149 50 57 THR CB C 65.80 0.1 1 150 50 57 THR N N 121.11 0.1 1 151 51 58 PRO CA C 62.53 0.1 1 152 51 58 PRO CB C 28.25 0.1 1 153 52 59 GLU H H 8.563 0.02 1 154 52 59 GLU CA C 57.45 0.1 1 155 52 59 GLU CB C 25.44 0.1 1 156 52 59 GLU N N 116.70 0.1 1 157 53 60 GLU H H 7.738 0.02 1 158 53 60 GLU CA C 56.35 0.1 1 159 53 60 GLU CB C 26.03 0.1 1 160 53 60 GLU N N 122.72 0.1 1 161 54 61 LYS H H 7.962 0.02 1 162 54 61 LYS CA C 57.76 0.1 1 163 54 61 LYS CB C 29.52 0.1 1 164 54 61 LYS N N 118.75 0.1 1 165 55 62 LYS H H 8.285 0.02 1 166 55 62 LYS CA C 57.53 0.1 1 167 55 62 LYS CB C 29.24 0.1 1 168 55 62 LYS N N 117.93 0.1 1 169 56 63 GLN H H 7.742 0.02 1 170 56 63 GLN CA C 56.26 0.1 1 171 56 63 GLN CB C 25.19 0.1 1 172 56 63 GLN N N 117.87 0.1 1 173 57 64 VAL H H 8.233 0.02 1 174 57 64 VAL CA C 64.29 0.1 1 175 57 64 VAL CB C 28.51 0.1 1 176 57 64 VAL N N 121.08 0.1 1 177 58 65 LEU H H 8.496 0.02 1 178 58 65 LEU CA C 55.68 0.1 1 179 58 65 LEU CB C 38.49 0.1 1 180 58 65 LEU N N 120.39 0.1 1 181 59 66 GLU H H 8.816 0.02 1 182 59 66 GLU CA C 57.40 0.1 1 183 59 66 GLU CB C 26.29 0.1 1 184 59 66 GLU N N 118.65 0.1 1 185 60 67 GLU H H 8.008 0.02 1 186 60 67 GLU CA C 57.26 0.1 1 187 60 67 GLU CB C 26.02 0.1 1 188 60 67 GLU N N 121.75 0.1 1 189 61 68 PHE H H 9.231 0.02 1 190 61 68 PHE CA C 59.47 0.1 1 191 61 68 PHE CB C 36.15 0.1 1 192 61 68 PHE N N 119.98 0.1 1 193 62 69 LEU H H 8.708 0.02 1 194 62 69 LEU CA C 54.89 0.1 1 195 62 69 LEU CB C 37.91 0.1 1 196 62 69 LEU N N 118.88 0.1 1 197 63 70 SER H H 7.787 0.02 1 198 63 70 SER CA C 59.44 0.1 1 199 63 70 SER N N 116.21 0.1 1 200 64 71 LEU H H 7.711 0.02 1 201 64 71 LEU CA C 54.94 0.1 1 202 64 71 LEU CB C 38.54 0.1 1 203 64 71 LEU N N 122.42 0.1 1 204 65 72 ALA H H 8.617 0.02 1 205 65 72 ALA CA C 52.07 0.1 1 206 65 72 ALA CB C 14.09 0.1 1 207 65 72 ALA N N 121.82 0.1 1 208 66 73 LYS H H 8.092 0.02 1 209 66 73 LYS CA C 55.49 0.1 1 210 66 73 LYS CB C 27.90 0.1 1 211 66 73 LYS N N 118.90 0.1 1 212 67 74 ALA H H 7.771 0.02 1 213 67 74 ALA CA C 52.39 0.1 1 214 67 74 ALA CB C 15.35 0.1 1 215 67 74 ALA N N 121.81 0.1 1 216 68 75 LYS H H 8.221 0.02 1 217 68 75 LYS CA C 56.99 0.1 1 218 68 75 LYS CB C 28.42 0.1 1 219 68 75 LYS N N 118.37 0.1 1 220 69 76 GLU H H 7.695 0.02 1 221 69 76 GLU CA C 56.34 0.1 1 222 69 76 GLU CB C 26.21 0.1 1 223 69 76 GLU N N 120.67 0.1 1 224 70 77 MET H H 8.031 0.02 1 225 70 77 MET CA C 56.14 0.1 1 226 70 77 MET CB C 30.43 0.1 1 227 70 77 MET N N 118.42 0.1 1 228 71 78 ILE H H 8.330 0.02 1 229 71 78 ILE CA C 62.77 0.1 1 230 71 78 ILE CB C 34.46 0.1 1 231 71 78 ILE N N 120.72 0.1 1 232 72 79 SER H H 7.976 0.02 1 233 72 79 SER CA C 58.72 0.1 1 234 72 79 SER CB C 60.32 0.1 1 235 72 79 SER N N 116.74 0.1 1 236 73 80 GLU H H 7.660 0.02 1 237 73 80 GLU CA C 54.28 0.1 1 238 73 80 GLU CB C 26.72 0.1 1 239 73 80 GLU N N 119.23 0.1 1 240 74 81 GLY H H 8.008 0.02 1 241 74 81 GLY CA C 42.36 0.1 1 242 74 81 GLY N N 105.86 0.1 1 243 75 82 GLY H H 8.314 0.02 1 244 75 82 GLY CA C 42.55 0.1 1 245 75 82 GLY N N 112.17 0.1 1 246 76 83 ILE H H 8.182 0.02 1 247 76 83 ILE CA C 62.06 0.1 1 248 76 83 ILE CB C 34.53 0.1 1 249 76 83 ILE N N 120.51 0.1 1 250 77 84 GLU H H 8.471 0.02 1 251 77 84 GLU CA C 56.71 0.1 1 252 77 84 GLU CB C 25.31 0.1 1 253 77 84 GLU N N 119.87 0.1 1 254 78 85 TYR H H 7.586 0.02 1 255 78 85 TYR CA C 57.28 0.1 1 256 78 85 TYR CB C 34.99 0.1 1 257 78 85 TYR N N 120.40 0.1 1 258 79 86 ALA H H 7.922 0.02 1 259 79 86 ALA CA C 51.85 0.1 1 260 79 86 ALA CB C 16.04 0.1 1 261 79 86 ALA N N 121.17 0.1 1 262 80 87 LYS H H 8.443 0.02 1 263 80 87 LYS CA C 57.75 0.1 1 264 80 87 LYS CB C 29.02 0.1 1 265 80 87 LYS N N 117.25 0.1 1 266 81 88 LYS H H 7.298 0.02 1 267 81 88 LYS CA C 56.27 0.1 1 268 81 88 LYS CB C 28.64 0.1 1 269 81 88 LYS N N 118.04 0.1 1 270 82 89 VAL H H 7.598 0.02 1 271 82 89 VAL CA C 63.20 0.1 1 272 82 89 VAL CB C 28.52 0.1 1 273 82 89 VAL N N 119.74 0.1 1 274 83 90 LEU H H 8.390 0.02 1 275 83 90 LEU CA C 54.51 0.1 1 276 83 90 LEU CB C 39.04 0.1 1 277 83 90 LEU N N 119.59 0.1 1 278 84 91 GLU H H 8.654 0.02 1 279 84 91 GLU CA C 56.66 0.1 1 280 84 91 GLU CB C 25.75 0.1 1 281 84 91 GLU N N 120.98 0.1 1 282 85 92 LYS H H 7.294 0.02 1 283 85 92 LYS CA C 55.77 0.1 1 284 85 92 LYS CB C 28.65 0.1 1 285 85 92 LYS N N 119.66 0.1 1 286 86 93 ALA H H 7.169 0.02 1 287 86 93 ALA CA C 51.22 0.1 1 288 86 93 ALA CB C 15.50 0.1 1 289 86 93 ALA N N 118.88 0.1 1 290 87 94 PHE H H 8.366 0.02 1 291 87 94 PHE CA C 54.01 0.1 1 292 87 94 PHE CB C 38.65 0.1 1 293 87 94 PHE N N 112.61 0.1 1 294 88 95 GLY H H 7.785 0.02 1 295 88 95 GLY CA C 41.38 0.1 1 296 88 95 GLY N N 110.96 0.1 1 297 90 97 GLU CA C 56.91 0.1 1 298 90 97 GLU CB C 25.91 0.1 1 299 91 98 ARG H H 8.773 0.02 1 300 91 98 ARG CA C 55.98 0.1 1 301 91 98 ARG CB C 26.09 0.1 1 302 91 98 ARG N N 120.21 0.1 1 303 92 99 ALA H H 7.976 0.02 1 304 92 99 ALA CA C 52.94 0.1 1 305 92 99 ALA CB C 16.12 0.1 1 306 92 99 ALA N N 118.83 0.1 1 307 93 100 ARG H H 7.572 0.02 1 308 93 100 ARG CA C 56.66 0.1 1 309 93 100 ARG CB C 26.20 0.1 1 310 93 100 ARG N N 116.13 0.1 1 311 94 101 LYS H H 7.406 0.02 1 312 94 101 LYS CA C 55.84 0.1 1 313 94 101 LYS CB C 28.63 0.1 1 314 94 101 LYS N N 119.03 0.1 1 315 95 102 ILE H H 8.110 0.02 1 316 95 102 ILE CA C 62.61 0.1 1 317 95 102 ILE CB C 34.49 0.1 1 318 95 102 ILE N N 120.40 0.1 1 319 96 103 ILE H H 7.997 0.02 1 320 96 103 ILE CA C 61.26 0.1 1 321 96 103 ILE CB C 33.12 0.1 1 322 96 103 ILE N N 119.00 0.1 1 323 97 104 GLU H H 8.191 0.02 1 324 97 104 GLU CA C 56.77 0.1 1 325 97 104 GLU CB C 26.16 0.1 1 326 97 104 GLU N N 121.98 0.1 1 327 113 120 ASP CA C 51.78 0.1 1 328 113 120 ASP CB C 38.15 0.1 1 329 114 121 THR H H 7.436 0.02 1 330 114 121 THR CA C 59.18 0.1 1 331 114 121 THR CB C 66.67 0.1 1 332 114 121 THR N N 114.23 0.1 1 333 115 122 ASP H H 8.190 0.02 1 334 115 122 ASP CA C 48.97 0.1 1 335 115 122 ASP CB C 38.94 0.1 1 336 115 122 ASP N N 125.49 0.1 1 337 116 123 PRO CA C 62.27 0.1 1 338 116 123 PRO CB C 28.99 0.1 1 339 117 124 VAL H H 7.804 0.02 1 340 117 124 VAL CA C 63.03 0.1 1 341 117 124 VAL CB C 27.91 0.1 1 342 117 124 VAL N N 118.39 0.1 1 343 118 125 GLN H H 7.617 0.02 1 344 118 125 GLN CA C 55.36 0.1 1 345 118 125 GLN CB C 25.04 0.1 1 346 118 125 GLN N N 119.24 0.1 1 347 119 126 LEU H H 7.902 0.02 1 348 119 126 LEU CA C 54.91 0.1 1 349 119 126 LEU CB C 38.32 0.1 1 350 119 126 LEU N N 120.16 0.1 1 351 120 127 VAL H H 8.088 0.02 1 352 120 127 VAL CA C 64.56 0.1 1 353 120 127 VAL CB C 28.10 0.1 1 354 120 127 VAL N N 120.08 0.1 1 355 121 128 ASN H H 7.603 0.02 1 356 121 128 ASN CA C 53.29 0.1 1 357 121 128 ASN CB C 35.39 0.1 1 358 121 128 ASN N N 117.05 0.1 1 359 122 129 PHE H H 7.715 0.02 1 360 122 129 PHE CA C 56.90 0.1 1 361 122 129 PHE N N 119.42 0.1 1 362 123 130 LEU H H 8.372 0.02 1 363 123 130 LEU CA C 53.67 0.1 1 364 123 130 LEU CB C 38.49 0.1 1 365 123 130 LEU N N 117.32 0.1 1 366 124 131 GLN H H 7.849 0.02 1 367 124 131 GLN CA C 55.70 0.1 1 368 124 131 GLN CB C 24.44 0.1 1 369 124 131 GLN N N 113.35 0.1 1 370 125 132 SER H H 7.081 0.02 1 371 125 132 SER CA C 54.94 0.1 1 372 125 132 SER N N 112.22 0.1 1 373 126 133 GLU H H 7.417 0.02 1 374 126 133 GLU CA C 51.49 0.1 1 375 126 133 GLU CB C 27.59 0.1 1 376 126 133 GLU N N 121.76 0.1 1 377 127 134 HIS H H 8.706 0.02 1 378 127 134 HIS CA C 53.00 0.1 1 379 127 134 HIS CB C 28.43 0.1 1 380 127 134 HIS N N 121.09 0.1 1 381 129 136 GLN H H 11.304 0.02 1 382 129 136 GLN CA C 56.37 0.1 1 383 129 136 GLN CB C 25.69 0.1 1 384 129 136 GLN N N 121.56 0.1 1 385 130 137 THR H H 7.491 0.02 1 386 130 137 THR CA C 63.43 0.1 1 387 130 137 THR CB C 65.25 0.1 1 388 130 137 THR N N 117.07 0.1 1 389 131 138 ILE H H 7.909 0.02 1 390 131 138 ILE CA C 63.02 0.1 1 391 131 138 ILE CB C 34.23 0.1 1 392 131 138 ILE N N 120.09 0.1 1 393 132 139 ALA H H 8.223 0.02 1 394 132 139 ALA CA C 52.16 0.1 1 395 132 139 ALA CB C 15.79 0.1 1 396 132 139 ALA N N 119.32 0.1 1 397 133 140 VAL H H 7.401 0.02 1 398 133 140 VAL CA C 64.45 0.1 1 399 133 140 VAL CB C 28.55 0.1 1 400 133 140 VAL N N 118.79 0.1 1 401 134 141 VAL H H 7.711 0.02 1 402 134 141 VAL CA C 64.69 0.1 1 403 134 141 VAL CB C 27.68 0.1 1 404 134 141 VAL N N 117.75 0.1 1 405 135 142 LEU H H 8.476 0.02 1 406 135 142 LEU CA C 55.06 0.1 1 407 135 142 LEU CB C 37.27 0.1 1 408 135 142 LEU N N 115.08 0.1 1 409 136 143 SER H H 7.542 0.02 1 410 136 143 SER CA C 59.32 0.1 1 411 136 143 SER CB C 60.59 0.1 1 412 136 143 SER N N 113.72 0.1 1 413 137 144 TYR H H 7.637 0.02 1 414 137 144 TYR CA C 56.71 0.1 1 415 137 144 TYR CB C 36.70 0.1 1 416 137 144 TYR N N 120.50 0.1 1 417 138 145 LEU H H 7.048 0.02 1 418 138 145 LEU CA C 50.44 0.1 1 419 138 145 LEU CB C 40.31 0.1 1 420 138 145 LEU N N 119.04 0.1 1 421 139 146 ASP H H 8.511 0.02 1 422 139 146 ASP CA C 50.36 0.1 1 423 139 146 ASP CB C 37.59 0.1 1 424 139 146 ASP N N 122.71 0.1 1 425 141 148 PRO CA C 63.48 0.1 1 426 142 149 VAL H H 7.181 0.02 1 427 142 149 VAL CA C 62.26 0.1 1 428 142 149 VAL CB C 28.35 0.1 1 429 142 149 VAL N N 118.83 0.1 1 430 143 150 ALA H H 8.137 0.02 1 431 143 150 ALA CA C 52.35 0.1 1 432 143 150 ALA CB C 15.69 0.1 1 433 143 150 ALA N N 122.08 0.1 1 434 144 151 ALA H H 8.508 0.02 1 435 144 151 ALA CA C 52.07 0.1 1 436 144 151 ALA CB C 16.02 0.1 1 437 144 151 ALA N N 117.87 0.1 1 438 145 152 GLN H H 7.304 0.02 1 439 145 152 GLN CA C 55.85 0.1 1 440 145 152 GLN CB C 24.99 0.1 1 441 145 152 GLN N N 118.97 0.1 1 442 146 153 ILE H H 7.655 0.02 1 443 146 153 ILE CA C 61.15 0.1 1 444 146 153 ILE CB C 33.54 0.1 1 445 146 153 ILE N N 118.97 0.1 1 446 147 154 LEU H H 8.617 0.02 1 447 147 154 LEU CA C 55.51 0.1 1 448 147 154 LEU CB C 38.75 0.1 1 449 147 154 LEU N N 120.17 0.1 1 450 148 155 GLY H H 8.055 0.02 1 451 148 155 GLY CA C 43.09 0.1 1 452 148 155 GLY N N 121.32 0.1 1 453 149 156 ALA H H 7.347 0.02 1 454 149 156 ALA CA C 48.58 0.1 1 455 149 156 ALA CB C 16.87 0.1 1 456 149 156 ALA N N 121.68 0.1 1 457 150 157 LEU H H 7.277 0.02 1 458 150 157 LEU CA C 50.30 0.1 1 459 150 157 LEU CB C 37.19 0.1 1 460 150 157 LEU N N 120.58 0.1 1 461 151 158 PRO CA C 60.29 0.1 1 462 151 158 PRO CB C 29.08 0.1 1 463 152 159 GLU H H 8.675 0.02 1 464 152 159 GLU CA C 57.17 0.1 1 465 152 159 GLU CB C 26.50 0.1 1 466 152 159 GLU N N 124.90 0.1 1 467 153 160 GLU H H 9.392 0.02 1 468 153 160 GLU CA C 56.02 0.1 1 469 153 160 GLU CB C 25.25 0.1 1 470 153 160 GLU N N 117.40 0.1 1 471 154 161 LEU H H 7.736 0.02 1 472 154 161 LEU CA C 52.39 0.1 1 473 154 161 LEU CB C 40.93 0.1 1 474 154 161 LEU N N 118.94 0.1 1 475 155 162 GLN H H 7.405 0.02 1 476 155 162 GLN CA C 58.02 0.1 1 477 155 162 GLN CB C 25.42 0.1 1 478 155 162 GLN N N 117.36 0.1 1 479 156 163 THR H H 7.891 0.02 1 480 156 163 THR CA C 64.26 0.1 1 481 156 163 THR N N 112.49 0.1 1 482 157 164 GLU H H 7.570 0.02 1 483 157 164 GLU CA C 55.92 0.1 1 484 157 164 GLU CB C 25.93 0.1 1 485 157 164 GLU N N 122.23 0.1 1 486 158 165 VAL H H 8.273 0.02 1 487 158 165 VAL CA C 63.98 0.1 1 488 158 165 VAL CB C 27.92 0.1 1 489 158 165 VAL N N 117.28 0.1 1 490 159 166 LEU H H 7.695 0.02 1 491 159 166 LEU CA C 54.32 0.1 1 492 159 166 LEU CB C 37.37 0.1 1 493 159 166 LEU N N 121.33 0.1 1 494 160 167 LYS H H 8.474 0.02 1 495 160 167 LYS CA C 57.16 0.1 1 496 160 167 LYS CB C 28.34 0.1 1 497 160 167 LYS N N 118.64 0.1 1 498 161 168 ARG H H 7.834 0.02 1 499 161 168 ARG CA C 55.61 0.1 1 500 161 168 ARG CB C 26.08 0.1 1 501 161 168 ARG N N 116.10 0.1 1 502 162 169 ILE H H 8.445 0.02 1 503 162 169 ILE CA C 63.32 0.1 1 504 162 169 ILE CB C 34.97 0.1 1 505 162 169 ILE N N 121.41 0.1 1 506 163 170 ALA H H 7.898 0.02 1 507 163 170 ALA CA C 51.60 0.1 1 508 163 170 ALA CB C 15.19 0.1 1 509 163 170 ALA N N 121.88 0.1 1 510 164 171 LEU H H 7.817 0.02 1 511 164 171 LEU CA C 52.28 0.1 1 512 164 171 LEU CB C 38.63 0.1 1 513 164 171 LEU N N 114.01 0.1 1 514 165 172 LEU H H 7.622 0.02 1 515 165 172 LEU CA C 55.40 0.1 1 516 165 172 LEU CB C 38.56 0.1 1 517 165 172 LEU N N 125.47 0.1 1 518 166 173 GLU H H 7.318 0.02 1 519 166 173 GLU CA C 55.09 0.1 1 520 166 173 GLU CB C 26.68 0.1 1 521 166 173 GLU N N 115.38 0.1 1 522 167 174 ARG H H 7.635 0.02 1 523 167 174 ARG CA C 52.26 0.1 1 524 167 174 ARG CB C 27.07 0.1 1 525 167 174 ARG N N 117.39 0.1 1 526 168 175 THR H H 7.314 0.02 1 527 168 175 THR CA C 59.82 0.1 1 528 168 175 THR N N 118.17 0.1 1 529 169 176 SER H H 7.733 0.02 1 530 169 176 SER CA C 54.08 0.1 1 531 169 176 SER N N 121.45 0.1 1 532 172 179 VAL CA C 62.52 0.1 1 533 173 180 VAL H H 7.158 0.02 1 534 173 180 VAL CA C 64.22 0.1 1 535 173 180 VAL CB C 28.44 0.1 1 536 173 180 VAL N N 119.68 0.1 1 537 174 181 LYS H H 8.226 0.02 1 538 174 181 LYS CA C 55.83 0.1 1 539 174 181 LYS CB C 28.43 0.1 1 540 174 181 LYS N N 118.66 0.1 1 541 175 182 GLU H H 7.404 0.02 1 542 175 182 GLU CA C 56.24 0.1 1 543 175 182 GLU CB C 25.81 0.1 1 544 175 182 GLU N N 119.59 0.1 1 545 176 183 ILE H H 7.609 0.02 1 546 176 183 ILE CA C 62.30 0.1 1 547 176 183 ILE CB C 34.99 0.1 1 548 176 183 ILE N N 120.95 0.1 1 549 177 184 GLU H H 8.613 0.02 1 550 177 184 GLU CA C 57.59 0.1 1 551 177 184 GLU CB C 26.42 0.1 1 552 177 184 GLU N N 119.67 0.1 1 553 178 185 ARG H H 8.147 0.02 1 554 178 185 ARG CA C 56.34 0.1 1 555 178 185 ARG CB C 26.64 0.1 1 556 178 185 ARG N N 118.17 0.1 1 557 179 186 ASN H H 7.679 0.02 1 558 179 186 ASN CA C 53.04 0.1 1 559 179 186 ASN CB C 35.68 0.1 1 560 179 186 ASN N N 118.34 0.1 1 561 180 187 LEU H H 8.273 0.02 1 562 180 187 LEU CA C 54.66 0.1 1 563 180 187 LEU CB C 38.41 0.1 1 564 180 187 LEU N N 121.64 0.1 1 565 181 188 GLU H H 7.925 0.02 1 566 181 188 GLU CA C 56.09 0.1 1 567 181 188 GLU CB C 26.27 0.1 1 568 181 188 GLU N N 118.39 0.1 1 569 182 189 LYS H H 7.126 0.02 1 570 182 189 LYS CA C 54.22 0.1 1 571 182 189 LYS N N 114.95 0.1 1 572 183 190 LYS H H 7.482 0.02 1 573 183 190 LYS CA C 54.48 0.1 1 574 183 190 LYS N N 117.75 0.1 1 575 184 191 ILE H H 7.992 0.02 1 576 184 191 ILE CA C 56.70 0.1 1 577 184 191 ILE CB C 35.26 0.1 1 578 184 191 ILE N N 118.99 0.1 1 579 194 201 LYS CA C 53.22 0.1 1 580 194 201 LYS CB C 29.75 0.1 1 581 195 202 VAL H H 8.086 0.02 1 582 195 202 VAL CA C 58.19 0.1 1 583 195 202 VAL CB C 30.19 0.1 1 584 195 202 VAL N N 122.66 0.1 1 585 196 203 GLY H H 8.447 0.02 1 586 196 203 GLY CA C 42.15 0.1 1 587 196 203 GLY N N 110.31 0.1 1 588 197 204 GLY H H 7.893 0.02 1 589 197 204 GLY CA C 41.29 0.1 1 590 197 204 GLY N N 106.96 0.1 1 591 198 205 ILE H H 8.613 0.02 1 592 198 205 ILE CA C 61.68 0.1 1 593 198 205 ILE CB C 33.52 0.1 1 594 198 205 ILE N N 121.44 0.1 1 595 199 206 ASP H H 8.382 0.02 1 596 199 206 ASP CA C 55.17 0.1 1 597 199 206 ASP CB C 36.61 0.1 1 598 199 206 ASP N N 119.54 0.1 1 599 200 207 THR H H 7.573 0.02 1 600 200 207 THR CA C 63.87 0.1 1 601 200 207 THR CB C 65.57 0.1 1 602 200 207 THR N N 118.53 0.1 1 603 201 208 ALA H H 8.069 0.02 1 604 201 208 ALA CA C 52.48 0.1 1 605 201 208 ALA CB C 14.51 0.1 1 606 201 208 ALA N N 122.65 0.1 1 607 202 209 ALA H H 8.523 0.02 1 608 202 209 ALA CA C 52.22 0.1 1 609 202 209 ALA CB C 15.62 0.1 1 610 202 209 ALA N N 119.53 0.1 1 611 203 210 GLU H H 7.957 0.02 1 612 203 210 GLU CA C 56.26 0.1 1 613 203 210 GLU CB C 25.87 0.1 1 614 203 210 GLU N N 117.39 0.1 1 615 204 211 ILE H H 8.103 0.02 1 616 204 211 ILE CA C 63.78 0.1 1 617 204 211 ILE CB C 34.20 0.1 1 618 204 211 ILE N N 120.87 0.1 1 619 205 212 MET H H 8.084 0.02 1 620 205 212 MET CA C 55.51 0.1 1 621 205 212 MET CB C 29.39 0.1 1 622 205 212 MET N N 118.53 0.1 1 623 206 213 ASN H H 8.043 0.02 1 624 206 213 ASN CA C 51.63 0.1 1 625 206 213 ASN CB C 35.84 0.1 1 626 206 213 ASN N N 116.48 0.1 1 627 207 214 ASN H H 7.671 0.02 1 628 207 214 ASN CA C 51.44 0.1 1 629 207 214 ASN CB C 39.20 0.1 1 630 207 214 ASN N N 116.58 0.1 1 631 208 215 LEU H H 7.153 0.02 1 632 208 215 LEU CA C 51.49 0.1 1 633 208 215 LEU CB C 41.19 0.1 1 634 208 215 LEU N N 121.99 0.1 1 635 209 216 ASP H H 8.164 0.02 1 636 209 216 ASP CA C 51.23 0.1 1 637 209 216 ASP CB C 38.45 0.1 1 638 209 216 ASP N N 119.80 0.1 1 639 210 217 ARG H H 8.700 0.02 1 640 210 217 ARG CA C 56.07 0.1 1 641 210 217 ARG CB C 26.63 0.1 1 642 210 217 ARG N N 121.71 0.1 1 643 211 218 THR H H 8.210 0.02 1 644 211 218 THR CA C 63.68 0.1 1 645 211 218 THR CB C 65.16 0.1 1 646 211 218 THR N N 115.77 0.1 1 647 212 219 THR H H 8.027 0.02 1 648 212 219 THR CA C 63.84 0.1 1 649 212 219 THR CB C 64.81 0.1 1 650 212 219 THR N N 121.86 0.1 1 651 213 220 GLU H H 8.443 0.02 1 652 213 220 GLU CA C 57.72 0.1 1 653 213 220 GLU CB C 25.07 0.1 1 654 213 220 GLU N N 121.89 0.1 1 655 214 221 LYS H H 7.762 0.02 1 656 214 221 LYS CA C 56.31 0.1 1 657 214 221 LYS CB C 28.83 0.1 1 658 214 221 LYS N N 118.29 0.1 1 659 215 222 LYS H H 7.490 0.02 1 660 215 222 LYS CA C 56.72 0.1 1 661 215 222 LYS CB C 28.99 0.1 1 662 215 222 LYS N N 118.74 0.1 1 663 216 223 ILE H H 7.852 0.02 1 664 216 223 ILE CA C 61.73 0.1 1 665 216 223 ILE CB C 35.22 0.1 1 666 216 223 ILE N N 119.40 0.1 1 667 217 224 MET H H 8.590 0.02 1 668 217 224 MET CA C 54.51 0.1 1 669 217 224 MET CB C 27.34 0.1 1 670 217 224 MET N N 119.44 0.1 1 671 218 225 ASP H H 8.646 0.02 1 672 218 225 ASP CA C 54.38 0.1 1 673 218 225 ASP CB C 37.07 0.1 1 674 218 225 ASP N N 118.56 0.1 1 675 219 226 LYS H H 7.238 0.02 1 676 219 226 LYS CA C 55.88 0.1 1 677 219 226 LYS CB C 28.88 0.1 1 678 219 226 LYS N N 119.94 0.1 1 679 220 227 LEU H H 8.732 0.02 1 680 220 227 LEU CA C 55.12 0.1 1 681 220 227 LEU CB C 38.59 0.1 1 682 220 227 LEU N N 121.91 0.1 1 683 221 228 VAL H H 8.641 0.02 1 684 221 228 VAL CA C 63.28 0.1 1 685 221 228 VAL CB C 28.14 0.1 1 686 221 228 VAL N N 118.49 0.1 1 687 222 229 GLN H H 6.907 0.02 1 688 222 229 GLN CA C 55.00 0.1 1 689 222 229 GLN CB C 25.75 0.1 1 690 222 229 GLN N N 115.34 0.1 1 691 223 230 GLU H H 7.699 0.02 1 692 223 230 GLU CA C 54.99 0.1 1 693 223 230 GLU CB C 28.35 0.1 1 694 223 230 GLU N N 116.55 0.1 1 695 224 231 ASN H H 8.956 0.02 1 696 224 231 ASN CA C 48.62 0.1 1 697 224 231 ASN CB C 36.08 0.1 1 698 224 231 ASN N N 116.36 0.1 1 699 225 232 PRO CA C 62.55 0.1 1 700 225 232 PRO CB C 27.88 0.1 1 701 226 233 GLU H H 8.481 0.02 1 702 226 233 GLU CA C 56.94 0.1 1 703 226 233 GLU CB C 25.48 0.1 1 704 226 233 GLU N N 118.71 0.1 1 705 227 234 LEU H H 7.364 0.02 1 706 227 234 LEU CA C 53.98 0.1 1 707 227 234 LEU CB C 38.90 0.1 1 708 227 234 LEU N N 122.45 0.1 1 709 228 235 ALA H H 8.053 0.02 1 710 228 235 ALA CA C 52.56 0.1 1 711 228 235 ALA CB C 15.44 0.1 1 712 228 235 ALA N N 119.99 0.1 1 713 229 236 ASP H H 7.865 0.02 1 714 229 236 ASP CA C 54.49 0.1 1 715 229 236 ASP CB C 38.27 0.1 1 716 229 236 ASP N N 116.52 0.1 1 717 230 237 GLU H H 7.599 0.02 1 718 230 237 GLU CA C 56.53 0.1 1 719 230 237 GLU CB C 26.30 0.1 1 720 230 237 GLU N N 119.54 0.1 1 721 231 238 ILE H H 8.037 0.02 1 722 231 238 ILE CA C 62.77 0.1 1 723 231 238 ILE CB C 35.04 0.1 1 724 231 238 ILE N N 118.49 0.1 1 725 232 239 ARG H H 8.426 0.02 1 726 232 239 ARG CA C 56.51 0.1 1 727 232 239 ARG CB C 26.45 0.1 1 728 232 239 ARG N N 119.58 0.1 1 729 233 240 ARG H H 8.003 0.02 1 730 233 240 ARG CA C 56.02 0.1 1 731 233 240 ARG CB C 27.00 0.1 1 732 233 240 ARG N N 117.68 0.1 1 733 234 241 ARG H H 7.306 0.02 1 734 234 241 ARG CA C 51.98 0.1 1 735 234 241 ARG CB C 26.33 0.1 1 736 234 241 ARG N N 116.57 0.1 1 737 235 242 MET H H 7.559 0.02 1 738 235 242 MET CA C 54.81 0.1 1 739 235 242 MET CB C 31.65 0.1 1 740 235 242 MET N N 119.59 0.1 1 741 236 243 PHE H H 7.324 0.02 1 742 236 243 PHE CA C 55.61 0.1 1 743 236 243 PHE CB C 37.55 0.1 1 744 236 243 PHE N N 120.24 0.1 1 745 237 244 VAL H H 8.470 0.02 1 746 237 244 VAL CA C 56.19 0.1 1 747 237 244 VAL CB C 30.36 0.1 1 748 237 244 VAL N N 122.90 0.1 1 749 238 245 PHE H H 8.880 0.02 1 750 238 245 PHE CA C 60.90 0.1 1 751 238 245 PHE CB C 36.12 0.1 1 752 238 245 PHE N N 123.54 0.1 1 753 239 246 GLU H H 8.275 0.02 1 754 239 246 GLU CA C 55.66 0.1 1 755 239 246 GLU CB C 25.01 0.1 1 756 239 246 GLU N N 111.96 0.1 1 757 240 247 ASP H H 7.952 0.02 1 758 240 247 ASP CA C 53.89 0.1 1 759 240 247 ASP CB C 36.16 0.1 1 760 240 247 ASP N N 121.13 0.1 1 761 241 248 ILE H H 7.746 0.02 1 762 241 248 ILE CA C 62.53 0.1 1 763 241 248 ILE CB C 33.92 0.1 1 764 241 248 ILE N N 122.56 0.1 1 765 242 249 LEU H H 7.214 0.02 1 766 242 249 LEU CA C 54.43 0.1 1 767 242 249 LEU CB C 39.14 0.1 1 768 242 249 LEU N N 116.92 0.1 1 769 243 250 LYS H H 7.654 0.02 1 770 243 250 LYS CA C 53.71 0.1 1 771 243 250 LYS CB C 29.43 0.1 1 772 243 250 LYS N N 116.19 0.1 1 773 244 251 LEU H H 7.478 0.02 1 774 244 251 LEU CA C 51.84 0.1 1 775 244 251 LEU CB C 38.95 0.1 1 776 244 251 LEU N N 120.88 0.1 1 777 245 252 ASP H H 8.019 0.02 1 778 245 252 ASP CA C 49.81 0.1 1 779 245 252 ASP CB C 38.45 0.1 1 780 245 252 ASP N N 118.50 0.1 1 781 246 253 ASP H H 8.251 0.02 1 782 246 253 ASP CA C 55.64 0.1 1 783 246 253 ASP CB C 37.89 0.1 1 784 246 253 ASP N N 120.56 0.1 1 785 247 254 ARG H H 8.192 0.02 1 786 247 254 ARG CA C 56.53 0.1 1 787 247 254 ARG CB C 25.73 0.1 1 788 247 254 ARG N N 119.73 0.1 1 789 248 255 SER H H 7.981 0.02 1 790 248 255 SER CA C 59.94 0.1 1 791 248 255 SER N N 116.41 0.1 1 792 249 256 ILE H H 7.928 0.02 1 793 249 256 ILE CA C 61.74 0.1 1 794 249 256 ILE CB C 33.00 0.1 1 795 249 256 ILE N N 121.37 0.1 1 796 250 257 GLN H H 8.195 0.02 1 797 250 257 GLN CA C 57.05 0.1 1 798 250 257 GLN CB C 24.15 0.1 1 799 250 257 GLN N N 118.67 0.1 1 800 251 258 LEU H H 7.614 0.02 1 801 251 258 LEU CA C 55.28 0.1 1 802 251 258 LEU CB C 38.43 0.1 1 803 251 258 LEU N N 119.85 0.1 1 804 252 259 VAL H H 7.664 0.02 1 805 252 259 VAL CA C 63.25 0.1 1 806 252 259 VAL CB C 28.47 0.1 1 807 252 259 VAL N N 120.32 0.1 1 808 253 260 LEU H H 8.251 0.02 1 809 253 260 LEU CA C 54.03 0.1 1 810 253 260 LEU CB C 37.74 0.1 1 811 253 260 LEU N N 116.11 0.1 1 812 254 261 ARG H H 7.253 0.02 1 813 254 261 ARG CA C 55.45 0.1 1 814 254 261 ARG CB C 27.19 0.1 1 815 254 261 ARG N N 116.93 0.1 1 816 255 262 GLU H H 7.562 0.02 1 817 255 262 GLU CA C 52.88 0.1 1 818 255 262 GLU CB C 28.45 0.1 1 819 255 262 GLU N N 115.40 0.1 1 820 256 263 VAL H H 7.114 0.02 1 821 256 263 VAL CA C 57.92 0.1 1 822 256 263 VAL CB C 30.40 0.1 1 823 256 263 VAL N N 118.04 0.1 1 824 257 264 ASP H H 9.165 0.02 1 825 257 264 ASP CA C 51.03 0.1 1 826 257 264 ASP CB C 39.67 0.1 1 827 257 264 ASP N N 128.48 0.1 1 828 258 265 THR H H 8.447 0.02 1 829 258 265 THR CA C 64.00 0.1 1 830 258 265 THR CB C 65.53 0.1 1 831 258 265 THR N N 120.81 0.1 1 832 259 266 ARG H H 8.513 0.02 1 833 259 266 ARG CA C 56.58 0.1 1 834 259 266 ARG CB C 25.94 0.1 1 835 259 266 ARG N N 121.39 0.1 1 836 260 267 ASP H H 7.073 0.02 1 837 260 267 ASP CA C 54.26 0.1 1 838 260 267 ASP CB C 37.65 0.1 1 839 260 267 ASP N N 117.96 0.1 1 840 261 268 LEU H H 7.795 0.02 1 841 261 268 LEU CA C 54.60 0.1 1 842 261 268 LEU CB C 38.44 0.1 1 843 261 268 LEU N N 119.68 0.1 1 844 262 269 ALA H H 8.170 0.02 1 845 262 269 ALA CA C 52.48 0.1 1 846 262 269 ALA CB C 14.97 0.1 1 847 262 269 ALA N N 119.68 0.1 1 848 263 270 LEU H H 7.422 0.02 1 849 263 270 LEU CA C 54.99 0.1 1 850 263 270 LEU CB C 39.57 0.1 1 851 263 270 LEU N N 115.58 0.1 1 852 264 271 ALA H H 7.960 0.02 1 853 264 271 ALA CA C 51.59 0.1 1 854 264 271 ALA CB C 15.98 0.1 1 855 264 271 ALA N N 117.37 0.1 1 856 265 272 LEU CA C 51.54 0.1 1 857 266 273 LYS H H 8.049 0.02 1 858 266 273 LYS CA C 52.78 0.1 1 859 266 273 LYS N N 114.97 0.1 1 860 267 274 GLY CA C 41.97 0.1 1 861 268 275 ALA H H 7.353 0.02 1 862 268 275 ALA CA C 47.71 0.1 1 863 268 275 ALA CB C 19.72 0.1 1 864 268 275 ALA N N 123.48 0.1 1 865 269 276 SER H H 9.584 0.02 1 866 269 276 SER CA C 55.39 0.1 1 867 269 276 SER CB C 61.44 0.1 1 868 269 276 SER N N 119.06 0.1 1 869 270 277 ASP H H 8.821 0.02 1 870 270 277 ASP CA C 55.04 0.1 1 871 270 277 ASP CB C 36.92 0.1 1 872 270 277 ASP N N 122.07 0.1 1 873 271 278 GLU H H 8.774 0.02 1 874 271 278 GLU CA C 57.08 0.1 1 875 271 278 GLU CB C 25.56 0.1 1 876 271 278 GLU N N 119.57 0.1 1 877 272 279 LEU H H 8.009 0.02 1 878 272 279 LEU CA C 55.25 0.1 1 879 272 279 LEU CB C 37.27 0.1 1 880 272 279 LEU N N 123.72 0.1 1 881 273 280 LYS H H 8.068 0.02 1 882 273 280 LYS CA C 58.22 0.1 1 883 273 280 LYS CB C 28.54 0.1 1 884 273 280 LYS N N 118.11 0.1 1 885 274 281 GLU H H 7.896 0.02 1 886 274 281 GLU CA C 56.44 0.1 1 887 274 281 GLU CB C 25.98 0.1 1 888 274 281 GLU N N 115.91 0.1 1 889 275 282 LYS H H 7.423 0.02 1 890 275 282 LYS CA C 55.51 0.1 1 891 275 282 LYS CB C 29.24 0.1 1 892 275 282 LYS N N 120.46 0.1 1 893 276 283 ILE H H 7.590 0.02 1 894 276 283 ILE CA C 60.45 0.1 1 895 276 283 ILE CB C 32.33 0.1 1 896 276 283 ILE N N 118.79 0.1 1 897 277 284 PHE H H 8.701 0.02 1 898 277 284 PHE CA C 56.90 0.1 1 899 277 284 PHE CB C 34.92 0.1 1 900 277 284 PHE N N 118.17 0.1 1 901 278 285 LYS H H 8.015 0.02 1 902 278 285 LYS CA C 55.26 0.1 1 903 278 285 LYS CB C 28.31 0.1 1 904 278 285 LYS N N 115.80 0.1 1 905 279 286 ASN H H 7.455 0.02 1 906 279 286 ASN CA C 51.54 0.1 1 907 279 286 ASN CB C 38.45 0.1 1 908 279 286 ASN N N 118.09 0.1 1 909 280 287 MET H H 7.230 0.02 1 910 280 287 MET CA C 51.83 0.1 1 911 280 287 MET CB C 34.24 0.1 1 912 280 287 MET N N 118.00 0.1 1 913 281 288 SER H H 8.515 0.02 1 914 281 288 SER CA C 55.01 0.1 1 915 281 288 SER CB C 61.35 0.1 1 916 281 288 SER N N 117.37 0.1 1 917 283 290 ARG CA C 55.83 0.1 1 918 283 290 ARG CB C 26.52 0.1 1 919 284 291 ALA H H 7.658 0.02 1 920 284 291 ALA CA C 52.07 0.1 1 921 284 291 ALA CB C 15.41 0.1 1 922 284 291 ALA N N 122.75 0.1 1 923 285 292 ALA H H 8.754 0.02 1 924 285 292 ALA CA C 52.12 0.1 1 925 285 292 ALA CB C 15.03 0.1 1 926 285 292 ALA N N 121.78 0.1 1 927 286 293 ALA H H 7.604 0.02 1 928 286 293 ALA CA C 52.13 0.1 1 929 286 293 ALA CB C 14.67 0.1 1 930 286 293 ALA N N 120.66 0.1 1 931 287 294 LEU H H 7.593 0.02 1 932 287 294 LEU CA C 54.74 0.1 1 933 287 294 LEU CB C 38.36 0.1 1 934 287 294 LEU N N 118.74 0.1 1 935 288 295 LEU H H 7.932 0.02 1 936 288 295 LEU CA C 54.72 0.1 1 937 288 295 LEU CB C 38.05 0.1 1 938 288 295 LEU N N 121.99 0.1 1 939 289 296 LYS H H 8.384 0.02 1 940 289 296 LYS CA C 57.67 0.1 1 941 289 296 LYS CB C 28.66 0.1 1 942 289 296 LYS N N 119.65 0.1 1 943 290 297 ASP H H 7.607 0.02 1 944 290 297 ASP CA C 54.50 0.1 1 945 290 297 ASP CB C 37.25 0.1 1 946 290 297 ASP N N 119.63 0.1 1 947 291 298 GLU H H 7.928 0.02 1 948 291 298 GLU CA C 56.24 0.1 1 949 291 298 GLU CB C 25.95 0.1 1 950 291 298 GLU N N 121.23 0.1 1 951 292 299 LEU H H 8.282 0.02 1 952 292 299 LEU CA C 55.20 0.1 1 953 292 299 LEU CB C 38.98 0.1 1 954 292 299 LEU N N 117.49 0.1 1 955 293 300 GLU H H 7.777 0.02 1 956 293 300 GLU CA C 55.55 0.1 1 957 293 300 GLU CB C 26.12 0.1 1 958 293 300 GLU N N 119.01 0.1 1 959 294 301 TYR H H 7.775 0.02 1 960 294 301 TYR CA C 55.20 0.1 1 961 294 301 TYR CB C 34.88 0.1 1 962 294 301 TYR N N 116.66 0.1 1 963 295 302 MET H H 7.512 0.02 1 964 295 302 MET CA C 55.00 0.1 1 965 295 302 MET CB C 30.41 0.1 1 966 295 302 MET N N 120.56 0.1 1 967 296 303 GLY H H 7.967 0.02 1 968 296 303 GLY CA C 41.36 0.1 1 969 296 303 GLY N N 109.49 0.1 1 970 297 304 PRO CA C 60.26 0.1 1 971 297 304 PRO CB C 28.36 0.1 1 972 298 305 VAL H H 8.028 0.02 1 973 298 305 VAL CA C 56.76 0.1 1 974 298 305 VAL CB C 31.60 0.1 1 975 298 305 VAL N N 118.34 0.1 1 976 299 306 ARG H H 8.739 0.02 1 977 299 306 ARG CA C 52.33 0.1 1 978 299 306 ARG CB C 27.29 0.1 1 979 299 306 ARG N N 123.77 0.1 1 980 301 308 LYS CA C 55.96 0.1 1 981 301 308 LYS CB C 28.86 0.1 1 982 302 309 ASP H H 7.062 0.02 1 983 302 309 ASP CA C 54.23 0.1 1 984 302 309 ASP CB C 37.37 0.1 1 985 302 309 ASP N N 118.17 0.1 1 986 303 310 VAL H H 7.304 0.02 1 987 303 310 VAL CA C 63.28 0.1 1 988 303 310 VAL CB C 28.93 0.1 1 989 303 310 VAL N N 123.07 0.1 1 990 304 311 GLU H H 8.278 0.02 1 991 304 311 GLU CA C 56.76 0.1 1 992 304 311 GLU CB C 26.15 0.1 1 993 304 311 GLU N N 119.13 0.1 1 994 305 312 GLU H H 8.019 0.02 1 995 305 312 GLU CA C 56.58 0.1 1 996 305 312 GLU CB C 26.11 0.1 1 997 305 312 GLU N N 119.28 0.1 1 998 306 313 ALA H H 7.526 0.02 1 999 306 313 ALA CA C 52.64 0.1 1 1000 306 313 ALA CB C 15.67 0.1 1 1001 306 313 ALA N N 123.69 0.1 1 1002 307 314 GLN H H 8.093 0.02 1 1003 307 314 GLN CA C 56.47 0.1 1 1004 307 314 GLN CB C 24.01 0.1 1 1005 307 314 GLN N N 115.94 0.1 1 1006 308 315 GLN H H 8.295 0.02 1 1007 308 315 GLN CA C 55.50 0.1 1 1008 308 315 GLN CB C 24.48 0.1 1 1009 308 315 GLN N N 118.07 0.1 1 1010 309 316 LYS H H 7.948 0.02 1 1011 309 316 LYS CA C 57.15 0.1 1 1012 309 316 LYS CB C 29.03 0.1 1 1013 309 316 LYS N N 121.05 0.1 1 1014 310 317 ILE H H 7.514 0.02 1 1015 310 317 ILE CA C 62.66 0.1 1 1016 310 317 ILE CB C 34.30 0.1 1 1017 310 317 ILE N N 119.77 0.1 1 1018 311 318 ILE H H 8.513 0.02 1 1019 311 318 ILE CA C 62.87 0.1 1 1020 311 318 ILE CB C 34.29 0.1 1 1021 311 318 ILE N N 122.06 0.1 1 1022 312 319 ASN H H 8.362 0.02 1 1023 312 319 ASN CA C 53.49 0.1 1 1024 312 319 ASN CB C 34.77 0.1 1 1025 312 319 ASN N N 118.56 0.1 1 1026 313 320 ILE H H 7.549 0.02 1 1027 313 320 ILE CA C 62.69 0.1 1 1028 313 320 ILE CB C 34.65 0.1 1 1029 313 320 ILE N N 123.27 0.1 1 1030 314 321 ILE CA C 63.28 0.1 1 1031 314 321 ILE CB C 33.92 0.1 1 1032 315 322 ARG H H 8.409 0.02 1 1033 315 322 ARG CA C 56.08 0.1 1 1034 315 322 ARG CB C 26.09 0.1 1 1035 315 322 ARG N N 117.74 0.1 1 1036 316 323 ARG H H 7.838 0.02 1 1037 316 323 ARG CA C 56.46 0.1 1 1038 316 323 ARG CB C 26.18 0.1 1 1039 316 323 ARG N N 121.17 0.1 1 1040 317 324 LEU H H 8.261 0.02 1 1041 317 324 LEU CA C 54.87 0.1 1 1042 317 324 LEU CB C 38.49 0.1 1 1043 317 324 LEU N N 121.55 0.1 1 1044 318 325 GLU H H 8.578 0.02 1 1045 318 325 GLU CA C 56.24 0.1 1 1046 318 325 GLU CB C 25.90 0.1 1 1047 318 325 GLU N N 123.26 0.1 1 1048 319 326 GLU H H 8.375 0.02 1 1049 319 326 GLU CA C 56.36 0.1 1 1050 319 326 GLU CB C 25.89 0.1 1 1051 319 326 GLU N N 123.27 0.1 1 1052 320 327 ALA H H 7.624 0.02 1 1053 320 327 ALA CA C 49.43 0.1 1 1054 320 327 ALA CB C 16.16 0.1 1 1055 320 327 ALA N N 118.58 0.1 1 1056 321 328 GLY H H 7.831 0.02 1 1057 321 328 GLY CA C 42.23 0.1 1 1058 321 328 GLY N N 106.88 0.1 1 1059 322 329 GLU H H 7.959 0.02 1 1060 322 329 GLU CA C 54.74 0.1 1 1061 322 329 GLU CB C 27.83 0.1 1 1062 322 329 GLU N N 118.09 0.1 1 1063 323 330 ILE H H 6.784 0.02 1 1064 323 330 ILE CA C 56.24 0.1 1 1065 323 330 ILE CB C 38.21 0.1 1 1066 323 330 ILE N N 110.63 0.1 1 1067 324 331 VAL H H 8.049 0.02 1 1068 324 331 VAL CA C 58.45 0.1 1 1069 324 331 VAL CB C 30.56 0.1 1 1070 324 331 VAL N N 123.26 0.1 1 1071 325 332 ILE H H 8.621 0.02 1 1072 325 332 ILE CA C 57.84 0.1 1 1073 325 332 ILE CB C 35.02 0.1 1 1074 325 332 ILE N N 127.29 0.1 1 1075 326 333 ALA H H 8.312 0.02 1 1076 326 333 ALA CA C 49.29 0.1 1 1077 326 333 ALA CB C 15.55 0.1 1 1078 326 333 ALA N N 130.29 0.1 1 1079 327 334 ARG H H 8.225 0.02 1 1080 327 334 ARG CA C 52.94 0.1 1 1081 327 334 ARG CB C 27.80 0.1 1 1082 327 334 ARG N N 122.14 0.1 1 1083 330 337 GLY CA C 42.29 0.1 1 1084 331 338 GLU H H 8.305 0.02 1 1085 331 338 GLU CA C 53.77 0.1 1 1086 331 338 GLU CB C 26.82 0.1 1 1087 331 338 GLU N N 121.15 0.1 1 1088 332 339 GLU H H 8.365 0.02 1 1089 332 339 GLU CA C 53.58 0.1 1 1090 332 339 GLU CB C 26.79 0.1 1 1091 332 339 GLU N N 121.92 0.1 1 1092 333 340 LEU H H 8.070 0.02 1 1093 333 340 LEU CA C 52.04 0.1 1 1094 333 340 LEU CB C 38.86 0.1 1 1095 333 340 LEU N N 123.91 0.1 1 1096 334 341 ILE H H 7.978 0.02 1 1097 334 341 ILE CA C 58.07 0.1 1 1098 334 341 ILE CB C 34.99 0.1 1 1099 334 341 ILE N N 123.36 0.1 1 1100 335 342 MET H H 7.803 0.02 1 1101 335 342 MET CA C 54.04 0.1 1 1102 335 342 MET CB C 30.82 0.1 1 1103 335 342 MET N N 130.00 0.1 1 stop_ save_