data_18170 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of human CXCR1 in phospholipid bilayers ; _BMRB_accession_number 18170 _BMRB_flat_file_name bmr18170.str _Entry_type original _Submission_date 2011-12-31 _Accession_date 2011-12-31 _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 Park 'Sang Ho' . . 2 Das Bibhuti B. . 3 Casagrande Fabio . . 4 Nothnagel Henry . . 5 Chu Mignon . . 6 Kiefer Hans . . 7 Maier Klaus . . 8 'De Angelis' Anna . . 9 Marassi Francesca M. . 10 Opella Stanley J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 816 "15N chemical shifts" 298 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-13 update BMRB 'update entry citation' 2012-10-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the chemokine receptor CXCR1 in phospholipid bilayers.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23086146 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Park 'Sang Ho' . . 2 Das Bibhuti B. . 3 Casagrande Fabio . . 4 Tian Ye . . 5 Nothnagel Henry J. . 6 Chu Mignon . . 7 Kiefer Hans . . 8 Maier Klaus . . 9 'De Angelis' Anna A. . 10 Marassi Francesca M. . 11 Opella Stanley J. . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 491 _Journal_issue 7426 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 779 _Page_last 783 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'human CXCR1 in phospholipid bilayers' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human CXCR1 in phospholipid bilayers' $cxcr1 4-TRIFLUOROMETHYLANILINE $ANI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cxcr1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 33726.656 _Mol_thiol_state 'disulfide bound and not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 309 _Mol_residue_sequence ; MPPADEDYSPCMLETETLNK YVVIIAYALVFLLSLLGNSL VMLVILYSRVGRSVTDVYLL NLALADLLFALTLPIWAASK VNGWIFGTFLCKVVSLLKEV NFYSGILLLACISVDRYLAI VHATRTLTQKRHLVKFVCLG CWGLSMNLSLPFFLFRQAYH PNNSSPVCYEVLGNDTAKWR MVLRILPHTFGFIVPLFVML FCYGFTLRTLFKAHMGQKHR AMRVIFAVVLIFLLCWLPYN LVLLADTLMRTQVIQESCER RNNIGRALDATEILGFLHSC LNPIIYAFIGQNFRHGFLKI LAMHGLVSK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 20 MET 2 21 PRO 3 22 PRO 4 23 ALA 5 24 ASP 6 25 GLU 7 26 ASP 8 27 TYR 9 28 SER 10 29 PRO 11 30 CYS 12 31 MET 13 32 LEU 14 33 GLU 15 34 THR 16 35 GLU 17 36 THR 18 37 LEU 19 38 ASN 20 39 LYS 21 40 TYR 22 41 VAL 23 42 VAL 24 43 ILE 25 44 ILE 26 45 ALA 27 46 TYR 28 47 ALA 29 48 LEU 30 49 VAL 31 50 PHE 32 51 LEU 33 52 LEU 34 53 SER 35 54 LEU 36 55 LEU 37 56 GLY 38 57 ASN 39 58 SER 40 59 LEU 41 60 VAL 42 61 MET 43 62 LEU 44 63 VAL 45 64 ILE 46 65 LEU 47 66 TYR 48 67 SER 49 68 ARG 50 69 VAL 51 70 GLY 52 71 ARG 53 72 SER 54 73 VAL 55 74 THR 56 75 ASP 57 76 VAL 58 77 TYR 59 78 LEU 60 79 LEU 61 80 ASN 62 81 LEU 63 82 ALA 64 83 LEU 65 84 ALA 66 85 ASP 67 86 LEU 68 87 LEU 69 88 PHE 70 89 ALA 71 90 LEU 72 91 THR 73 92 LEU 74 93 PRO 75 94 ILE 76 95 TRP 77 96 ALA 78 97 ALA 79 98 SER 80 99 LYS 81 100 VAL 82 101 ASN 83 102 GLY 84 103 TRP 85 104 ILE 86 105 PHE 87 106 GLY 88 107 THR 89 108 PHE 90 109 LEU 91 110 CYS 92 111 LYS 93 112 VAL 94 113 VAL 95 114 SER 96 115 LEU 97 116 LEU 98 117 LYS 99 118 GLU 100 119 VAL 101 120 ASN 102 121 PHE 103 122 TYR 104 123 SER 105 124 GLY 106 125 ILE 107 126 LEU 108 127 LEU 109 128 LEU 110 129 ALA 111 130 CYS 112 131 ILE 113 132 SER 114 133 VAL 115 134 ASP 116 135 ARG 117 136 TYR 118 137 LEU 119 138 ALA 120 139 ILE 121 140 VAL 122 141 HIS 123 142 ALA 124 143 THR 125 144 ARG 126 145 THR 127 146 LEU 128 147 THR 129 148 GLN 130 149 LYS 131 150 ARG 132 151 HIS 133 152 LEU 134 153 VAL 135 154 LYS 136 155 PHE 137 156 VAL 138 157 CYS 139 158 LEU 140 159 GLY 141 160 CYS 142 161 TRP 143 162 GLY 144 163 LEU 145 164 SER 146 165 MET 147 166 ASN 148 167 LEU 149 168 SER 150 169 LEU 151 170 PRO 152 171 PHE 153 172 PHE 154 173 LEU 155 174 PHE 156 175 ARG 157 176 GLN 158 177 ALA 159 178 TYR 160 179 HIS 161 180 PRO 162 181 ASN 163 182 ASN 164 183 SER 165 184 SER 166 185 PRO 167 186 VAL 168 187 CYS 169 188 TYR 170 189 GLU 171 190 VAL 172 191 LEU 173 192 GLY 174 193 ASN 175 194 ASP 176 195 THR 177 196 ALA 178 197 LYS 179 198 TRP 180 199 ARG 181 200 MET 182 201 VAL 183 202 LEU 184 203 ARG 185 204 ILE 186 205 LEU 187 206 PRO 188 207 HIS 189 208 THR 190 209 PHE 191 210 GLY 192 211 PHE 193 212 ILE 194 213 VAL 195 214 PRO 196 215 LEU 197 216 PHE 198 217 VAL 199 218 MET 200 219 LEU 201 220 PHE 202 221 CYS 203 222 TYR 204 223 GLY 205 224 PHE 206 225 THR 207 226 LEU 208 227 ARG 209 228 THR 210 229 LEU 211 230 PHE 212 231 LYS 213 232 ALA 214 233 HIS 215 234 MET 216 235 GLY 217 236 GLN 218 237 LYS 219 238 HIS 220 239 ARG 221 240 ALA 222 241 MET 223 242 ARG 224 243 VAL 225 244 ILE 226 245 PHE 227 246 ALA 228 247 VAL 229 248 VAL 230 249 LEU 231 250 ILE 232 251 PHE 233 252 LEU 234 253 LEU 235 254 CYS 236 255 TRP 237 256 LEU 238 257 PRO 239 258 TYR 240 259 ASN 241 260 LEU 242 261 VAL 243 262 LEU 244 263 LEU 245 264 ALA 246 265 ASP 247 266 THR 248 267 LEU 249 268 MET 250 269 ARG 251 270 THR 252 271 GLN 253 272 VAL 254 273 ILE 255 274 GLN 256 275 GLU 257 276 SER 258 277 CYS 259 278 GLU 260 279 ARG 261 280 ARG 262 281 ASN 263 282 ASN 264 283 ILE 265 284 GLY 266 285 ARG 267 286 ALA 268 287 LEU 269 288 ASP 270 289 ALA 271 290 THR 272 291 GLU 273 292 ILE 274 293 LEU 275 294 GLY 276 295 PHE 277 296 LEU 278 297 HIS 279 298 SER 280 299 CYS 281 300 LEU 282 301 ASN 283 302 PRO 284 303 ILE 285 304 ILE 286 305 TYR 287 306 ALA 288 307 PHE 289 308 ILE 290 309 GLY 291 310 GLN 292 311 ASN 293 312 PHE 294 313 ARG 295 314 HIS 296 315 GLY 297 316 PHE 298 317 LEU 299 318 LYS 300 319 ILE 301 320 LEU 302 321 ALA 303 322 MET 304 323 HIS 305 324 GLY 306 325 LEU 307 326 VAL 308 327 SER 309 328 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2LNL "Structure Of Human Cxcr1 In Phospholipid Bilayers" 95.79 296 100.00 100.00 0.00e+00 DBJ BAG35550 "unnamed protein product [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 DBJ BAG74111 "interleukin 8 receptor, alpha [synthetic construct]" 100.00 350 100.00 100.00 0.00e+00 EMBL CAA46688 "High affinity interleukin-8 receptor [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 EMBL CAB37671 "interleukin-8 receptor type A [Gorilla gorilla]" 100.00 350 97.09 97.41 0.00e+00 EMBL CAB37850 "interleukin-8 receptor type A [Pan troglodytes]" 100.00 350 98.71 98.71 0.00e+00 EMBL CAG46791 "IL8RA [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 EMBL CAG46826 "IL8RA [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 GB AAA59159 "IL-8 receptor [Homo sapiens]" 100.00 350 99.68 100.00 0.00e+00 GB AAA59160 "interleukin 8 receptor alpha [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 GB AAA64378 "interleukin-8 receptor type A [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 GB AAB25879 "interleukin-8 receptor type 1, IL8R1 [human, neutrophils, Peptide, 350 aa]" 100.00 350 99.68 100.00 0.00e+00 GB AAB59436 "interleukin 8 receptor alpha [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 REF NP_000625 "C-X-C chemokine receptor type 1 [Homo sapiens]" 100.00 350 100.00 100.00 0.00e+00 REF NP_001035537 "C-X-C chemokine receptor type 1 [Pan troglodytes]" 100.00 350 98.71 98.71 0.00e+00 REF XP_004033238 "PREDICTED: c-X-C chemokine receptor type 1 isoform 1 [Gorilla gorilla gorilla]" 100.00 350 97.41 97.73 0.00e+00 REF XP_004033239 "PREDICTED: c-X-C chemokine receptor type 1 isoform 2 [Gorilla gorilla gorilla]" 100.00 350 97.41 97.73 0.00e+00 SP P25024 "RecName: Full=C-X-C chemokine receptor type 1; Short=CXC-R1; Short=CXCR-1; AltName: Full=CDw128a; AltName: Full=High affinity i" 100.00 350 100.00 100.00 0.00e+00 SP P55919 "RecName: Full=C-X-C chemokine receptor type 1; Short=CXC-R1; Short=CXCR-1; AltName: Full=High affinity interleukin-8 receptor A" 100.00 350 97.09 97.41 0.00e+00 SP P55920 "RecName: Full=C-X-C chemokine receptor type 1; Short=CXC-R1; Short=CXCR-1; AltName: Full=High affinity interleukin-8 receptor A" 100.00 350 98.71 98.71 0.00e+00 stop_ save_ ############# # Ligands # ############# save_ANI _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 4-(trifluoromethyl)aniline _BMRB_code ANI _PDB_code ANI _Molecular_mass 161.124 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? F1 F1 F . 0 . ? F2 F2 F . 0 . ? F3 F3 F . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N C1 ? ? SING N HN1 ? ? SING N HN2 ? ? DOUB C1 C2 ? ? SING C1 C6 ? ? SING C2 C3 ? ? SING C2 H2 ? ? DOUB C3 C4 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 C7 ? ? DOUB C5 C6 ? ? SING C5 H5 ? ? SING C6 H6 ? ? SING C7 F1 ? ? SING C7 F2 ? ? SING C7 F3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cxcr1 Human 9606 Eukaryota Metazoa Homo sapiens 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 $cxcr1 'recombinant technology' . Escherichia coli . pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type membrane _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cxcr1 . mg 2 4 '[U-100% 13C; U-100% 15N]' H2O 100 % . . 'natural abundance' HEPES 20 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name NCACX _Sample_label $sample_1 save_ save_SLF_2 _Saveframe_category NMR_applied_experiment _Experiment_name SLF _Sample_label $sample_1 save_ save_PDSD_3 _Saveframe_category NMR_applied_experiment _Experiment_name PDSD _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 7 . pH pressure 1 . atm temperature 273 . 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 'solid CH' ppm 0.00 external direct . . . 1 'liquid anhydrous ammonia' N 15 nitrogen ppm 0.00 external direct . . . 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label NCACX SLF PDSD stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'human CXCR1 in phospholipid bilayers' _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 20 1 MET C C 176.7 0.3 1 2 20 1 MET CA C 58.2 0.4 1 3 20 1 MET CB C 31.8 0.4 1 4 20 1 MET N N 119.9 0.5 1 5 21 2 PRO N N 145 0.5 1 6 23 4 ALA C C 178.6 0.3 1 7 23 4 ALA CA C 53.4 0.4 1 8 23 4 ALA CB C 18.2 0.4 1 9 23 4 ALA N N 124.4 0.5 1 10 24 5 ASP C C 177.4 0.3 1 11 24 5 ASP CA C 53.1 0.4 1 12 24 5 ASP CB C 39.5 0.4 1 13 24 5 ASP N N 124.2 0.5 1 14 25 6 GLU C C 176.2 0.3 1 15 25 6 GLU CA C 57.9 0.4 1 16 25 6 GLU N N 123.8 0.5 1 17 26 7 ASP C C 177.4 0.3 1 18 26 7 ASP CA C 54.2 0.4 1 19 26 7 ASP CB C 39.2 0.4 1 20 26 7 ASP N N 120.4 0.5 1 21 27 8 TYR C C 176.5 0.3 1 22 27 8 TYR CA C 57.25 0.4 1 23 27 8 TYR CB C 37.25 0.4 1 24 27 8 TYR N N 123 0.5 1 25 28 9 SER C C 173 0.3 1 26 28 9 SER CA C 57.5 0.4 1 27 28 9 SER CB C 63 0.4 1 28 28 9 SER N N 120.4 0.5 1 29 29 10 PRO N N 133 0.5 1 30 30 11 CYS C C 177.5 0.3 1 31 30 11 CYS CA C 56 0.4 1 32 30 11 CYS CB C 40.3 0.4 1 33 30 11 CYS N N 122.7 0.5 1 34 31 12 MET C C 173.2 0.3 1 35 31 12 MET CA C 58.15 0.4 1 36 31 12 MET CB C 31.1 0.4 1 37 31 12 MET N N 117.9 0.5 1 38 32 13 LEU C C 173.5 0.3 1 39 32 13 LEU CA C 53.78 0.4 1 40 32 13 LEU CB C 39.66 0.4 1 41 32 13 LEU N N 125.3 0.5 1 42 33 14 GLU C C 173.2 0.3 1 43 33 14 GLU CA C 55.9 0.4 1 44 33 14 GLU CB C 31 0.4 1 45 33 14 GLU N N 129.9 0.5 1 46 34 15 THR C C 172.5 0.3 1 47 34 15 THR CA C 63.5 0.4 1 48 34 15 THR CB C 67.2 0.4 1 49 34 15 THR N N 113.9 0.5 1 50 35 16 GLU C C 169.5 0.3 1 51 35 16 GLU CA C 55.84 0.4 1 52 35 16 GLU CB C 28.12 0.4 1 53 35 16 GLU N N 125.3 0.5 1 54 36 17 THR C C 174.2 0.3 1 55 36 17 THR CA C 65 0.4 1 56 36 17 THR N N 106.7 0.5 1 57 37 18 LEU C C 177.5 0.3 1 58 37 18 LEU CA C 56.4 0.4 1 59 37 18 LEU CB C 39.8 0.4 1 60 37 18 LEU N N 120.1 0.5 1 61 38 19 ASN C C 177.6 0.3 1 62 38 19 ASN CA C 55.9 0.4 1 63 38 19 ASN CB C 40.87 0.4 1 64 38 19 ASN N N 118.4 0.5 1 65 39 20 LYS C C 174.3 0.3 1 66 39 20 LYS CA C 56.7 0.4 1 67 39 20 LYS CB C 29.9 0.4 1 68 39 20 LYS N N 121.5 0.5 1 69 40 21 TYR C C 176.8 0.3 1 70 40 21 TYR CA C 58.2 0.4 1 71 40 21 TYR CB C 40 0.4 1 72 40 21 TYR N N 120.1 0.5 1 73 41 22 VAL C C 176 0.3 1 74 41 22 VAL CA C 65 0.4 1 75 41 22 VAL CB C 29.75 0.4 1 76 41 22 VAL N N 120.7 0.5 1 77 42 23 VAL C C 176.2 0.3 1 78 42 23 VAL CA C 65.56 0.4 1 79 42 23 VAL CB C 29.7 0.4 1 80 42 23 VAL N N 121.2 0.5 1 81 43 24 ILE C C 177 0.3 1 82 43 24 ILE CA C 64.3 0.4 1 83 43 24 ILE CB C 36.6 0.4 1 84 43 24 ILE N N 120.9 0.5 1 85 44 25 ILE C C 175 0.3 1 86 44 25 ILE CA C 59.7 0.4 1 87 44 25 ILE CB C 37 0.4 1 88 44 25 ILE N N 120.5 0.5 1 89 45 26 ALA C C 175.7 0.3 1 90 45 26 ALA CA C 52.7 0.4 1 91 45 26 ALA CB C 16.6 0.4 1 92 45 26 ALA N N 121.6 0.5 1 93 46 27 TYR C C 175.4 0.3 1 94 46 27 TYR CA C 58.53 0.4 1 95 46 27 TYR CB C 39.85 0.4 1 96 46 27 TYR N N 120.4 0.5 1 97 47 28 ALA C C 174.8 0.3 1 98 47 28 ALA CA C 53.8 0.4 1 99 47 28 ALA CB C 15.53 0.4 1 100 47 28 ALA N N 124.7 0.5 1 101 48 29 LEU C C 177.4 0.3 1 102 48 29 LEU CA C 56.86 0.4 1 103 48 29 LEU N N 117.7 0.5 1 104 49 30 VAL C C 181.1 0.3 1 105 49 30 VAL CA C 67.8 0.4 1 106 49 30 VAL CB C 29.9 0.4 1 107 49 30 VAL N N 118.4 0.5 1 108 50 31 PHE C C 171.9 0.3 1 109 50 31 PHE CA C 61.6 0.4 1 110 50 31 PHE CB C 42.62 0.4 1 111 50 31 PHE N N 124.7 0.5 1 112 51 32 LEU C C 176.6 0.3 1 113 51 32 LEU CA C 55.85 0.4 1 114 51 32 LEU CB C 40.22 0.4 1 115 51 32 LEU N N 125.6 0.5 1 116 52 33 LEU C C 173.7 0.3 1 117 52 33 LEU CA C 56.3 0.4 1 118 52 33 LEU CB C 39.2 0.4 1 119 52 33 LEU N N 122.8 0.5 1 120 53 34 SER C C 173 0.3 1 121 53 34 SER CA C 58.2 0.4 1 122 53 34 SER N N 118.7 0.5 1 123 54 35 LEU C C 176.8 0.3 1 124 54 35 LEU CA C 56.4 0.4 1 125 54 35 LEU CB C 40 0.4 1 126 54 35 LEU N N 123.5 0.5 1 127 55 36 LEU C C 177.2 0.3 1 128 55 36 LEU CA C 56 0.4 1 129 55 36 LEU CB C 40 0.4 1 130 55 36 LEU N N 124.6 0.5 1 131 56 37 GLY C C 174.8 0.3 1 132 56 37 GLY CA C 47.4 0.4 1 133 56 37 GLY N N 109.6 0.5 1 134 57 38 ASN C C 176.9 0.3 1 135 57 38 ASN CA C 55.7 0.4 1 136 57 38 ASN CB C 39.3 0.4 1 137 57 38 ASN N N 118.2 0.5 1 138 58 39 SER C C 180.1 0.3 1 139 58 39 SER CA C 59.9 0.4 1 140 58 39 SER CB C 63.3 0.4 1 141 58 39 SER N N 111.3 0.5 1 142 59 40 LEU C C 177.4 0.3 1 143 59 40 LEU CA C 56.15 0.4 1 144 59 40 LEU CB C 41 0.4 1 145 59 40 LEU N N 121.1 0.5 1 146 60 41 VAL C C 175.2 0.3 1 147 60 41 VAL CA C 65.4 0.4 1 148 60 41 VAL CB C 29.5 0.4 1 149 60 41 VAL N N 119.3 0.5 1 150 61 42 MET C C 176.5 0.3 1 151 61 42 MET CA C 55.84 0.4 1 152 61 42 MET N N 118.9 0.5 1 153 62 43 LEU C C 177.7 0.3 1 154 62 43 LEU CA C 56.16 0.4 1 155 62 43 LEU CB C 39.11 0.4 1 156 62 43 LEU N N 122.1 0.5 1 157 63 44 VAL CA C 64.85 0.4 1 158 63 44 VAL CB C 29.6 0.4 1 159 63 44 VAL N N 121.1 0.5 1 160 64 45 ILE C C 175.1 0.3 1 161 64 45 ILE CA C 64.4 0.4 1 162 64 45 ILE CB C 36.6 0.4 1 163 64 45 ILE N N 121 0.5 1 164 65 46 LEU C C 173.8 0.3 1 165 65 46 LEU CA C 56.2 0.4 1 166 65 46 LEU CB C 39.3 0.4 1 167 65 46 LEU N N 119 0.5 1 168 66 47 TYR C C 176.7 0.3 1 169 66 47 TYR CA C 58.34 0.4 1 170 66 47 TYR CB C 40 0.4 1 171 66 47 TYR N N 120.2 0.5 1 172 67 48 SER C C 175.4 0.3 1 173 67 48 SER CA C 60 0.4 1 174 67 48 SER CB C 62 0.4 1 175 67 48 SER N N 116.7 0.5 1 176 68 49 ARG C C 175.3 0.3 1 177 68 49 ARG CA C 60.4 0.4 1 178 68 49 ARG N N 121.5 0.5 1 179 69 50 VAL C C 174.6 0.3 1 180 69 50 VAL CA C 65.8 0.4 1 181 69 50 VAL CB C 29.85 0.4 1 182 69 50 VAL N N 120.6 0.5 1 183 70 51 GLY C C 174.4 0.3 1 184 70 51 GLY CA C 41.7 0.4 1 185 70 51 GLY N N 110.7 0.5 1 186 71 52 ARG C C 176.5 0.3 1 187 71 52 ARG CA C 56.8 0.4 1 188 71 52 ARG CB C 29.9 0.4 1 189 71 52 ARG N N 122.9 0.5 1 190 72 53 SER C C 174.3 0.3 1 191 72 53 SER CA C 57.8 0.4 1 192 72 53 SER N N 117.3 0.5 1 193 73 54 VAL C C 175.7 0.3 1 194 73 54 VAL CA C 66.1 0.4 1 195 73 54 VAL CB C 29.65 0.4 1 196 73 54 VAL N N 120.4 0.5 1 197 74 55 THR C C 175.8 0.3 1 198 74 55 THR CA C 64 0.4 1 199 74 55 THR N N 117.3 0.5 1 200 75 56 ASP C C 176.5 0.3 1 201 75 56 ASP CA C 56 0.4 1 202 75 56 ASP CB C 40.3 0.4 1 203 75 56 ASP N N 122.9 0.5 1 204 76 57 VAL C C 175.6 0.3 1 205 76 57 VAL CA C 66.4 0.4 1 206 76 57 VAL CB C 30.4 0.4 1 207 76 57 VAL N N 120.8 0.5 1 208 77 58 TYR C C 175.7 0.3 1 209 77 58 TYR CA C 60.56 0.4 1 210 77 58 TYR CB C 37 0.4 1 211 77 58 TYR N N 123.8 0.5 1 212 78 59 LEU C C 176.5 0.3 1 213 78 59 LEU CA C 55.9 0.4 1 214 78 59 LEU CB C 40 0.4 1 215 78 59 LEU N N 121 0.5 1 216 79 60 LEU C C 176 0.3 1 217 79 60 LEU CA C 55.8 0.4 1 218 79 60 LEU CB C 40.24 0.4 1 219 79 60 LEU N N 126.2 0.5 1 220 80 61 ASN C C 178.1 0.3 1 221 80 61 ASN CA C 56.5 0.4 1 222 80 61 ASN CB C 39.1 0.4 1 223 80 61 ASN N N 121.3 0.5 1 224 81 62 LEU C C 176.3 0.3 1 225 81 62 LEU CA C 56 0.4 1 226 81 62 LEU CB C 38.1 0.4 1 227 81 62 LEU N N 124.1 0.5 1 228 82 63 ALA C C 177.5 0.3 1 229 82 63 ALA CA C 53.4 0.4 1 230 82 63 ALA CB C 18.3 0.4 1 231 82 63 ALA N N 124.7 0.5 1 232 83 64 LEU C C 176.5 0.3 1 233 83 64 LEU CA C 55.9 0.4 1 234 83 64 LEU CB C 40.2 0.4 1 235 83 64 LEU N N 121.4 0.5 1 236 84 65 ALA C C 176.6 0.3 1 237 84 65 ALA CA C 54.4 0.4 1 238 84 65 ALA CB C 16.6 0.4 1 239 84 65 ALA N N 123.9 0.5 1 240 85 66 ASP C C 178.4 0.3 1 241 85 66 ASP CA C 56.33 0.4 1 242 85 66 ASP CB C 39.85 0.4 1 243 85 66 ASP N N 120.3 0.5 1 244 86 67 LEU C C 173.6 0.3 1 245 86 67 LEU CA C 56.3 0.4 1 246 86 67 LEU CB C 39.5 0.4 1 247 86 67 LEU N N 122.7 0.5 1 248 87 68 LEU C C 175.6 0.3 1 249 87 68 LEU CA C 56.15 0.4 1 250 87 68 LEU CB C 40 0.4 1 251 87 68 LEU N N 122 0.5 1 252 88 69 PHE C C 173.9 0.3 1 253 88 69 PHE CA C 55.9 0.4 1 254 88 69 PHE CB C 40.4 0.4 1 255 88 69 PHE N N 119.2 0.5 1 256 89 70 ALA C C 172.9 0.3 1 257 89 70 ALA CA C 53.1 0.4 1 258 89 70 ALA CB C 17 0.4 1 259 89 70 ALA N N 126.6 0.5 1 260 90 71 LEU C C 172.5 0.3 1 261 90 71 LEU CA C 56.5 0.4 1 262 90 71 LEU CB C 39.9 0.4 1 263 90 71 LEU N N 119.7 0.5 1 264 91 72 THR C C 176.4 0.3 1 265 91 72 THR CA C 60 0.4 1 266 91 72 THR CB C 69.5 0.4 1 267 91 72 THR N N 115.3 0.5 1 268 92 73 LEU C C 175.4 0.3 1 269 92 73 LEU CA C 55.6 0.4 1 270 92 73 LEU CB C 40.8 0.4 1 271 92 73 LEU N N 123 0.5 1 272 94 75 ILE C C 176.8 0.3 1 273 94 75 ILE CA C 64.3 0.4 1 274 94 75 ILE CB C 36.6 0.4 1 275 94 75 ILE N N 121 0.5 1 276 95 76 TRP C C 176.7 0.3 1 277 95 76 TRP CA C 58.1 0.4 1 278 95 76 TRP CB C 29 0.4 1 279 95 76 TRP N N 120.5 0.5 1 280 96 77 ALA C C 178.3 0.3 1 281 96 77 ALA CA C 52.4 0.4 1 282 96 77 ALA CB C 20.4 0.4 1 283 96 77 ALA N N 126.3 0.5 1 284 97 78 ALA C C 178 0.3 1 285 97 78 ALA CA C 53.6 0.4 1 286 97 78 ALA CB C 16.7 0.4 1 287 97 78 ALA N N 123.2 0.5 1 288 98 79 SER CA C 63 0.4 1 289 98 79 SER N N 109.4 0.5 1 290 99 80 LYS C C 177.3 0.3 1 291 99 80 LYS CA C 56.1 0.4 1 292 99 80 LYS CB C 30.7 0.4 1 293 99 80 LYS N N 121.5 0.5 1 294 100 81 VAL C C 176.3 0.3 1 295 100 81 VAL CA C 64.9 0.4 1 296 100 81 VAL CB C 29.85 0.4 1 297 100 81 VAL N N 121.2 0.5 1 298 101 82 ASN C C 173.8 0.3 1 299 101 82 ASN CA C 52.3 0.4 1 300 101 82 ASN CB C 39.7 0.4 1 301 101 82 ASN N N 116.7 0.5 1 302 102 83 GLY C C 174.6 0.3 1 303 102 83 GLY CA C 45.9 0.4 1 304 102 83 GLY N N 109.5 0.5 1 305 103 84 TRP C C 173.9 0.3 1 306 103 84 TRP CA C 58 0.4 1 307 103 84 TRP CB C 31 0.4 1 308 103 84 TRP N N 117.7 0.5 1 309 104 85 ILE C C 175.7 0.3 1 310 104 85 ILE CA C 60.4 0.4 1 311 104 85 ILE CB C 35.6 0.4 1 312 104 85 ILE N N 124.3 0.5 1 313 105 86 PHE C C 177.2 0.3 1 314 105 86 PHE CA C 55.7 0.4 1 315 105 86 PHE CB C 40.5 0.4 1 316 105 86 PHE N N 121.1 0.5 1 317 106 87 GLY C C 174.5 0.3 1 318 106 87 GLY CA C 41.9 0.4 1 319 106 87 GLY N N 110 0.5 1 320 107 88 THR C C 173.5 0.3 1 321 107 88 THR CA C 60.5 0.4 1 322 107 88 THR CB C 69.7 0.4 1 323 107 88 THR N N 114.7 0.5 1 324 108 89 PHE C C 173.5 0.3 1 325 108 89 PHE CA C 60 0.4 1 326 108 89 PHE CB C 37.03 0.4 1 327 108 89 PHE N N 124.2 0.5 1 328 109 90 LEU C C 176 0.3 1 329 109 90 LEU CA C 55.5 0.4 1 330 109 90 LEU CB C 40.9 0.4 1 331 109 90 LEU N N 123.2 0.5 1 332 110 91 CYS C C 176.7 0.3 1 333 110 91 CYS CA C 55.7 0.4 1 334 110 91 CYS CB C 39.4 0.4 1 335 110 91 CYS N N 117.6 0.5 1 336 111 92 LYS C C 176.4 0.3 1 337 111 92 LYS CA C 57.3 0.4 1 338 111 92 LYS CB C 30 0.4 1 339 111 92 LYS N N 121.6 0.5 1 340 112 93 VAL C C 174.1 0.3 1 341 112 93 VAL CA C 68 0.4 1 342 112 93 VAL N N 123.6 0.5 1 343 113 94 VAL C C 169.6 0.3 1 344 113 94 VAL CA C 68.8 0.4 1 345 113 94 VAL N N 127.8 0.5 1 346 114 95 SER C C 175.2 0.3 1 347 114 95 SER CA C 60.2 0.4 1 348 114 95 SER CB C 61.89 0.4 1 349 114 95 SER N N 117.5 0.5 1 350 115 96 LEU C C 173.7 0.3 1 351 115 96 LEU CA C 55.9 0.4 1 352 115 96 LEU CB C 40.6 0.4 1 353 115 96 LEU N N 120 0.5 1 354 116 97 LEU C C 177.8 0.3 1 355 116 97 LEU CA C 55.9 0.4 1 356 116 97 LEU CB C 40.25 0.4 1 357 116 97 LEU N N 126 0.5 1 358 117 98 LYS C C 173.2 0.3 1 359 117 98 LYS CA C 57 0.4 1 360 117 98 LYS CB C 29.8 0.4 1 361 117 98 LYS N N 120.9 0.5 1 362 118 99 GLU C C 177.1 0.3 1 363 118 99 GLU CA C 55.3 0.4 1 364 118 99 GLU CB C 28 0.4 1 365 118 99 GLU N N 118.9 0.5 1 366 119 100 VAL C C 173.6 0.3 1 367 119 100 VAL CA C 65.33 0.4 1 368 119 100 VAL CB C 29.25 0.4 1 369 119 100 VAL N N 123.4 0.5 1 370 120 101 ASN C C 174.5 0.3 1 371 120 101 ASN CA C 55.8 0.4 1 372 120 101 ASN CB C 38.9 0.4 1 373 120 101 ASN N N 120.3 0.5 1 374 121 102 PHE C C 175.5 0.3 1 375 121 102 PHE CA C 60.5 0.4 1 376 121 102 PHE CB C 37 0.4 1 377 121 102 PHE N N 123.6 0.5 1 378 122 103 TYR C C 176.1 0.3 1 379 122 103 TYR CA C 60.9 0.4 1 380 122 103 TYR CB C 37.3 0.4 1 381 122 103 TYR N N 120.5 0.5 1 382 123 104 SER C C 173.9 0.3 1 383 123 104 SER CA C 57.74 0.4 1 384 123 104 SER CB C 59.87 0.4 1 385 123 104 SER N N 124.6 0.5 1 386 124 105 GLY C C 171 0.3 1 387 124 105 GLY CA C 42.75 0.4 1 388 124 105 GLY N N 107.7 0.5 1 389 125 106 ILE C C 175.2 0.3 1 390 125 106 ILE CA C 62.95 0.4 1 391 125 106 ILE CB C 36.96 0.4 1 392 125 106 ILE N N 119.5 0.5 1 393 126 107 LEU C C 173.6 0.3 1 394 126 107 LEU CA C 56.25 0.4 1 395 126 107 LEU N N 122.3 0.5 1 396 127 108 LEU C C 176.1 0.3 1 397 127 108 LEU CA C 55.22 0.4 1 398 127 108 LEU CB C 41.67 0.4 1 399 127 108 LEU N N 126.5 0.5 1 400 128 109 LEU C C 175.6 0.3 1 401 128 109 LEU CA C 57.17 0.4 1 402 128 109 LEU CB C 40.3 0.4 1 403 128 109 LEU N N 121 0.5 1 404 129 110 ALA C C 176 0.3 1 405 129 110 ALA CA C 52.97 0.4 1 406 129 110 ALA CB C 17 0.4 1 407 129 110 ALA N N 125.8 0.5 1 408 130 111 CYS C C 177 0.3 1 409 130 111 CYS CA C 62.07 0.4 1 410 130 111 CYS CB C 29.88 0.4 1 411 130 111 CYS N N 120.3 0.5 1 412 131 112 ILE C C 174 0.3 1 413 131 112 ILE CA C 63.08 0.4 1 414 131 112 ILE CB C 36.22 0.4 1 415 131 112 ILE N N 121.3 0.5 1 416 132 113 SER C C 175.1 0.3 1 417 132 113 SER CA C 63.99 0.4 1 418 132 113 SER CB C 66.12 0.4 1 419 132 113 SER N N 117.7 0.5 1 420 133 114 VAL C C 177.7 0.3 1 421 133 114 VAL CA C 68.05 0.4 1 422 133 114 VAL N N 129.8 0.5 1 423 134 115 ASP C C 174.1 0.3 1 424 134 115 ASP CA C 57.5 0.4 1 425 134 115 ASP CB C 40.4 0.4 1 426 134 115 ASP N N 124 0.5 1 427 135 116 ARG C C 174.4 0.3 1 428 135 116 ARG CA C 58.42 0.4 1 429 135 116 ARG CB C 30.7 0.4 1 430 135 116 ARG N N 124.2 0.5 1 431 136 117 TYR C C 176.4 0.3 1 432 136 117 TYR CA C 60.25 0.4 1 433 136 117 TYR CB C 37.35 0.4 1 434 136 117 TYR N N 121 0.5 1 435 137 118 LEU C C 173.7 0.3 1 436 137 118 LEU CA C 54.87 0.4 1 437 137 118 LEU CB C 41.67 0.4 1 438 137 118 LEU N N 121.4 0.5 1 439 138 119 ALA C C 176.1 0.3 1 440 138 119 ALA CA C 52.86 0.4 1 441 138 119 ALA CB C 17.27 0.4 1 442 138 119 ALA N N 125.8 0.5 1 443 139 120 ILE C C 175.7 0.3 1 444 139 120 ILE CA C 60 0.4 1 445 139 120 ILE N N 120 0.5 1 446 140 121 VAL C C 173.9 0.3 1 447 140 121 VAL CA C 61.92 0.4 1 448 140 121 VAL CB C 30.9 0.4 1 449 140 121 VAL N N 118.7 0.5 1 450 141 122 HIS C C 177.9 0.3 1 451 141 122 HIS CA C 58.86 0.4 1 452 141 122 HIS CB C 30.09 0.4 1 453 141 122 HIS N N 117.2 0.5 1 454 142 123 ALA C C 174.6 0.3 1 455 142 123 ALA CA C 53.17 0.4 1 456 142 123 ALA CB C 16.58 0.4 1 457 142 123 ALA N N 121.2 0.5 1 458 143 124 THR C C 177 0.3 1 459 143 124 THR CA C 62.52 0.4 1 460 143 124 THR N N 118 0.5 1 461 144 125 ARG CA C 57.25 0.4 1 462 144 125 ARG CB C 30.34 0.4 1 463 145 126 THR C C 177 0.3 1 464 145 126 THR CA C 62.37 0.4 1 465 145 126 THR N N 119.7 0.5 1 466 146 127 LEU C C 173.2 0.3 1 467 146 127 LEU CA C 55.79 0.4 1 468 146 127 LEU CB C 40.57 0.4 1 469 146 127 LEU N N 127.9 0.5 1 470 147 128 THR C C 177.7 0.3 1 471 147 128 THR CA C 62.05 0.4 1 472 147 128 THR CB C 68.57 0.4 1 473 147 128 THR N N 124 0.5 1 474 148 129 GLN C C 176.7 0.3 1 475 148 129 GLN CA C 53.47 0.4 1 476 148 129 GLN CB C 29.31 0.4 1 477 148 129 GLN N N 122.8 0.5 1 478 149 130 LYS C C 175.9 0.3 1 479 149 130 LYS CA C 59.44 0.4 1 480 149 130 LYS N N 120.9 0.5 1 481 150 131 ARG C C 177.5 0.3 1 482 150 131 ARG CA C 56.7 0.4 1 483 150 131 ARG CB C 31.15 0.4 1 484 150 131 ARG N N 122.2 0.5 1 485 151 132 HIS C C 177.8 0.3 1 486 151 132 HIS CA C 59.13 0.4 1 487 151 132 HIS CB C 29.4 0.4 1 488 151 132 HIS N N 117.3 0.5 1 489 152 133 LEU C C 176.8 0.3 1 490 152 133 LEU CA C 56.15 0.4 1 491 152 133 LEU CB C 39.81 0.4 1 492 152 133 LEU N N 120.4 0.5 1 493 153 134 VAL C C 174.3 0.3 1 494 153 134 VAL CA C 61.24 0.4 1 495 153 134 VAL N N 121.5 0.5 1 496 154 135 LYS C C 175.3 0.3 1 497 154 135 LYS CA C 59 0.4 1 498 154 135 LYS N N 117 0.5 1 499 155 136 PHE C C 176.6 0.3 1 500 155 136 PHE CA C 61.2 0.4 1 501 155 136 PHE N N 121.1 0.5 1 502 156 137 VAL C C 177.7 0.3 1 503 156 137 VAL CA C 62.17 0.4 1 504 156 137 VAL CB C 33.4 0.4 1 505 156 137 VAL N N 123.8 0.5 1 506 157 138 CYS CA C 58.26 0.4 1 507 158 139 LEU C C 175.5 0.3 1 508 158 139 LEU CA C 55.75 0.4 1 509 158 139 LEU N N 122.9 0.5 1 510 159 140 GLY C C 176.2 0.3 1 511 159 140 GLY CA C 44.75 0.4 1 512 159 140 GLY N N 104.9 0.5 1 513 160 141 CYS C C 177 0.3 1 514 160 141 CYS CA C 59 0.4 1 515 160 141 CYS N N 113.6 0.5 1 516 161 142 TRP C C 174.9 0.3 1 517 161 142 TRP CA C 55.88 0.4 1 518 161 142 TRP N N 119 0.5 1 519 162 143 GLY C C 173.6 0.3 1 520 162 143 GLY CA C 45.1 0.4 1 521 162 143 GLY N N 108.3 0.5 1 522 163 144 LEU C C 173.5 0.3 1 523 163 144 LEU CA C 55.8 0.4 1 524 163 144 LEU CB C 39.85 0.4 1 525 163 144 LEU N N 120.2 0.5 1 526 164 145 SER C C 175 0.3 1 527 164 145 SER CA C 55.6 0.4 1 528 164 145 SER CB C 65.66 0.4 1 529 164 145 SER N N 117.2 0.5 1 530 165 146 MET C C 175.5 0.3 1 531 165 146 MET CA C 57.6 0.4 1 532 165 146 MET CB C 30 0.4 1 533 165 146 MET N N 121.2 0.5 1 534 166 147 ASN C C 176.5 0.3 1 535 166 147 ASN CA C 56.08 0.4 1 536 166 147 ASN CB C 38.94 0.4 1 537 166 147 ASN N N 120.2 0.5 1 538 167 148 LEU C C 171.9 0.3 1 539 167 148 LEU CA C 54.62 0.4 1 540 167 148 LEU CB C 30.03 0.4 1 541 167 148 LEU N N 123.2 0.5 1 542 168 149 SER C C 175.6 0.3 1 543 168 149 SER CA C 60.31 0.4 1 544 168 149 SER N N 123.3 0.5 1 545 169 150 LEU C C 176.6 0.3 1 546 169 150 LEU CA C 54.2 0.4 1 547 169 150 LEU N N 120.4 0.5 1 548 171 152 PHE C C 173.6 0.3 1 549 171 152 PHE CA C 61.7 0.4 1 550 171 152 PHE N N 118.6 0.5 1 551 172 153 PHE C C 174.2 0.3 1 552 172 153 PHE CA C 59.5 0.4 1 553 172 153 PHE CB C 42 0.4 1 554 172 153 PHE N N 116.3 0.5 1 555 173 154 LEU C C 177.3 0.3 1 556 173 154 LEU CA C 54.73 0.4 1 557 173 154 LEU CB C 37.23 0.4 1 558 173 154 LEU N N 120.4 0.5 1 559 174 155 PHE C C 177 0.3 1 560 174 155 PHE CA C 59 0.4 1 561 174 155 PHE CB C 43.22 0.4 1 562 174 155 PHE N N 121.2 0.5 1 563 175 156 ARG C C 178.4 0.3 1 564 175 156 ARG CA C 56.2 0.4 1 565 175 156 ARG N N 118.5 0.5 1 566 176 157 GLN C C 178 0.3 1 567 176 157 GLN CA C 56.2 0.4 1 568 176 157 GLN N N 122.1 0.5 1 569 177 158 ALA C C 176.9 0.3 1 570 177 158 ALA CA C 54.3 0.4 1 571 177 158 ALA CB C 16.87 0.4 1 572 177 158 ALA N N 123.2 0.5 1 573 178 159 TYR C C 174.8 0.3 1 574 178 159 TYR CA C 56.6 0.4 1 575 178 159 TYR CB C 39.9 0.4 1 576 178 159 TYR N N 120.7 0.5 1 577 179 160 HIS C C 176.6 0.3 1 578 179 160 HIS CA C 58.22 0.4 1 579 179 160 HIS CB C 31.56 0.4 1 580 179 160 HIS N N 119.6 0.5 1 581 181 162 ASN C C 172.5 0.3 1 582 181 162 ASN CA C 56.15 0.4 1 583 181 162 ASN CB C 36.5 0.4 1 584 181 162 ASN N N 119.2 0.5 1 585 182 163 ASN C C 175.8 0.3 1 586 182 163 ASN CA C 55.5 0.4 1 587 182 163 ASN N N 114.1 0.5 1 588 183 164 SER C C 175.6 0.3 1 589 183 164 SER CA C 55.4 0.4 1 590 183 164 SER CB C 63.8 0.4 1 591 183 164 SER N N 117.2 0.5 1 592 184 165 SER C C 175 0.3 1 593 184 165 SER CA C 55.5 0.4 1 594 184 165 SER CB C 63.8 0.4 1 595 184 165 SER N N 117 0.5 1 596 186 167 VAL C C 175.3 0.3 1 597 186 167 VAL CA C 65.29 0.4 1 598 186 167 VAL CB C 30.12 0.4 1 599 186 167 VAL N N 119.5 0.5 1 600 187 168 CYS C C 176.3 0.3 1 601 187 168 CYS CA C 56 0.4 1 602 187 168 CYS CB C 40 0.4 1 603 187 168 CYS N N 116.5 0.5 1 604 188 169 TYR C C 176.5 0.3 1 605 188 169 TYR CA C 55.86 0.4 1 606 188 169 TYR CB C 40.24 0.4 1 607 188 169 TYR N N 121.3 0.5 1 608 189 170 GLU C C 175.5 0.3 1 609 189 170 GLU CA C 57.9 0.4 1 610 189 170 GLU CB C 31.84 0.4 1 611 189 170 GLU N N 122 0.5 1 612 190 171 VAL C C 172.8 0.3 1 613 190 171 VAL CA C 65.67 0.4 1 614 190 171 VAL CB C 29.2 0.4 1 615 190 171 VAL N N 123.5 0.5 1 616 191 172 LEU CA C 55.5 0.4 1 617 191 172 LEU N N 129.9 0.5 1 618 192 173 GLY C C 173.5 0.3 1 619 192 173 GLY CA C 44.87 0.4 1 620 192 173 GLY N N 107.5 0.5 1 621 193 174 ASN CA C 52.8 0.4 1 622 193 174 ASN CB C 39.56 0.4 1 623 193 174 ASN N N 116.6 0.5 1 624 194 175 ASP C C 172.8 0.3 1 625 194 175 ASP CA C 53.9 0.4 1 626 194 175 ASP CB C 39.7 0.4 1 627 194 175 ASP N N 123.1 0.5 1 628 195 176 THR C C 175.5 0.3 1 629 195 176 THR CA C 63 0.4 1 630 195 176 THR N N 118.8 0.5 1 631 196 177 ALA C C 173 0.3 1 632 196 177 ALA CA C 53.8 0.4 1 633 196 177 ALA CB C 17.24 0.4 1 634 196 177 ALA N N 123.3 0.5 1 635 197 178 LYS C C 175 0.3 1 636 197 178 LYS CA C 56.9 0.4 1 637 197 178 LYS CB C 29.9 0.4 1 638 197 178 LYS N N 121.7 0.5 1 639 198 179 TRP C C 177.6 0.3 1 640 198 179 TRP CA C 59.3 0.4 1 641 198 179 TRP CB C 29.7 0.4 1 642 198 179 TRP N N 120.7 0.5 1 643 199 180 ARG C C 178.1 0.3 1 644 199 180 ARG CA C 55.95 0.4 1 645 199 180 ARG CB C 31.06 0.4 1 646 199 180 ARG N N 123.5 0.5 1 647 200 181 MET C C 175.4 0.3 1 648 200 181 MET CA C 58.1 0.4 1 649 200 181 MET CB C 31.1 0.4 1 650 200 181 MET N N 119.9 0.5 1 651 201 182 VAL C C 174.9 0.3 1 652 201 182 VAL CA C 65.7 0.4 1 653 201 182 VAL CB C 29.18 0.4 1 654 201 182 VAL N N 123.7 0.5 1 655 202 183 LEU C C 172.7 0.3 1 656 202 183 LEU CA C 54.8 0.4 1 657 202 183 LEU N N 124 0.5 1 658 203 184 ARG C C 176.2 0.3 1 659 203 184 ARG CA C 55.8 0.4 1 660 203 184 ARG CB C 31.26 0.4 1 661 203 184 ARG N N 124 0.5 1 662 204 185 ILE C C 176 0.3 1 663 204 185 ILE CA C 64.7 0.4 1 664 204 185 ILE CB C 36.4 0.4 1 665 204 185 ILE N N 120.5 0.5 1 666 205 186 LEU C C 176 0.3 1 667 205 186 LEU CA C 55 0.4 1 668 205 186 LEU N N 123.4 0.5 1 669 206 187 PRO CA C 62.5 0.4 1 670 206 187 PRO N N 138.7 0.5 1 671 207 188 HIS C C 175.2 0.3 1 672 207 188 HIS CA C 53.11 0.4 1 673 207 188 HIS CB C 30 0.4 1 674 207 188 HIS N N 113.5 0.5 1 675 208 189 THR C C 178 0.3 1 676 208 189 THR CA C 62.85 0.4 1 677 208 189 THR N N 122.1 0.5 1 678 209 190 PHE C C 175.4 0.3 1 679 209 190 PHE CA C 59.85 0.4 1 680 209 190 PHE N N 117.5 0.5 1 681 210 191 GLY C C 174.1 0.3 1 682 210 191 GLY CA C 45 0.4 1 683 210 191 GLY N N 111.7 0.5 1 684 211 192 PHE C C 175 0.3 1 685 211 192 PHE CA C 55.95 0.4 1 686 211 192 PHE N N 120.9 0.5 1 687 212 193 ILE C C 175.9 0.3 1 688 212 193 ILE CA C 64.44 0.4 1 689 212 193 ILE CB C 36.6 0.4 1 690 212 193 ILE N N 120.1 0.5 1 691 213 194 VAL C C 175.3 0.3 1 692 213 194 VAL CA C 65.75 0.4 1 693 213 194 VAL CB C 29.68 0.4 1 694 213 194 VAL N N 123.4 0.5 1 695 215 196 LEU C C 177.2 0.3 1 696 215 196 LEU CA C 55.7 0.4 1 697 215 196 LEU CB C 40.15 0.4 1 698 215 196 LEU N N 125.3 0.5 1 699 216 197 PHE C C 179.2 0.3 1 700 216 197 PHE CA C 60.65 0.4 1 701 216 197 PHE CB C 37 0.4 1 702 216 197 PHE N N 123.8 0.5 1 703 217 198 VAL C C 175.4 0.3 1 704 217 198 VAL CA C 65.66 0.4 1 705 217 198 VAL CB C 29.92 0.4 1 706 217 198 VAL N N 118.5 0.5 1 707 218 199 MET C C 174.4 0.3 1 708 218 199 MET CA C 55 0.4 1 709 218 199 MET CB C 31.65 0.4 1 710 218 199 MET N N 118.3 0.5 1 711 219 200 LEU C C 177.6 0.3 1 712 219 200 LEU CA C 55.8 0.4 1 713 219 200 LEU CB C 40.81 0.4 1 714 219 200 LEU N N 120.5 0.5 1 715 220 201 PHE C C 176 0.3 1 716 220 201 PHE CA C 61.17 0.4 1 717 220 201 PHE N N 124.7 0.5 1 718 221 202 CYS C C 176 0.3 1 719 221 202 CYS CA C 61.87 0.4 1 720 221 202 CYS N N 117.8 0.5 1 721 222 203 TYR C C 178.4 0.3 1 722 222 203 TYR CA C 57.5 0.4 1 723 222 203 TYR CB C 37.15 0.4 1 724 222 203 TYR N N 122 0.5 1 725 223 204 GLY C C 174.5 0.3 1 726 223 204 GLY CA C 41.7 0.4 1 727 223 204 GLY N N 110.3 0.5 1 728 224 205 PHE C C 176.5 0.3 1 729 224 205 PHE CA C 62.3 0.4 1 730 224 205 PHE CB C 36.9 0.4 1 731 224 205 PHE N N 120.1 0.5 1 732 225 206 THR C C 175 0.3 1 733 225 206 THR CA C 64.65 0.4 1 734 225 206 THR N N 118.5 0.5 1 735 226 207 LEU C C 177.2 0.3 1 736 226 207 LEU CA C 55.9 0.4 1 737 226 207 LEU CB C 39.4 0.4 1 738 226 207 LEU N N 122.9 0.5 1 739 227 208 ARG C C 177.2 0.3 1 740 227 208 ARG CA C 54.6 0.4 1 741 227 208 ARG CB C 28.5 0.4 1 742 227 208 ARG N N 121 0.5 1 743 228 209 THR C C 176.9 0.3 1 744 228 209 THR CA C 64.75 0.4 1 745 228 209 THR CB C 66.56 0.4 1 746 228 209 THR N N 119.6 0.5 1 747 229 210 LEU C C 177.8 0.3 1 748 229 210 LEU CA C 55.7 0.4 1 749 229 210 LEU CB C 40.26 0.4 1 750 229 210 LEU N N 125.6 0.5 1 751 230 211 PHE C C 176.9 0.3 1 752 230 211 PHE CA C 58.77 0.4 1 753 230 211 PHE CB C 41.94 0.4 1 754 230 211 PHE N N 121.9 0.5 1 755 231 212 LYS C C 174.9 0.3 1 756 231 212 LYS CA C 56 0.4 1 757 231 212 LYS CB C 30.9 0.4 1 758 231 212 LYS N N 121.6 0.5 1 759 232 213 ALA C C 176.9 0.3 1 760 232 213 ALA CA C 54 0.4 1 761 232 213 ALA CB C 21.83 0.4 1 762 232 213 ALA N N 123.5 0.5 1 763 233 214 HIS C C 176.1 0.3 1 764 233 214 HIS CA C 55.7 0.4 1 765 233 214 HIS CB C 29.06 0.4 1 766 233 214 HIS N N 123.5 0.5 1 767 234 215 MET C C 176.7 0.3 1 768 234 215 MET CA C 58 0.4 1 769 234 215 MET CB C 31.81 0.4 1 770 234 215 MET N N 120 0.5 1 771 235 216 GLY C C 173.3 0.3 1 772 235 216 GLY CA C 42.8 0.4 1 773 235 216 GLY N N 109.6 0.5 1 774 236 217 GLN C C 173.1 0.3 1 775 236 217 GLN CA C 55 0.4 1 776 236 217 GLN CB C 25.4 0.4 1 777 236 217 GLN N N 116.8 0.5 1 778 237 218 LYS C C 178.1 0.3 1 779 237 218 LYS CA C 56 0.4 1 780 237 218 LYS CB C 31.11 0.4 1 781 237 218 LYS N N 123.2 0.5 1 782 238 219 HIS C C 177 0.3 1 783 238 219 HIS CA C 54.72 0.4 1 784 238 219 HIS CB C 30 0.4 1 785 238 219 HIS N N 123.6 0.5 1 786 239 220 ARG C C 176.6 0.3 1 787 239 220 ARG CA C 55.65 0.4 1 788 239 220 ARG CB C 31.1 0.4 1 789 239 220 ARG N N 122.1 0.5 1 790 240 221 ALA C C 175.9 0.3 1 791 240 221 ALA CA C 52.8 0.4 1 792 240 221 ALA CB C 16.7 0.4 1 793 240 221 ALA N N 121.8 0.5 1 794 241 222 MET C C 175.6 0.3 1 795 241 222 MET CA C 58.1 0.4 1 796 241 222 MET CB C 31.81 0.4 1 797 241 222 MET N N 120.2 0.5 1 798 242 223 ARG C C 177.4 0.3 1 799 242 223 ARG CA C 56 0.4 1 800 242 223 ARG CB C 30.91 0.4 1 801 242 223 ARG N N 121.2 0.5 1 802 243 224 VAL C C 175.6 0.3 1 803 243 224 VAL CA C 65.47 0.4 1 804 243 224 VAL CB C 29.4 0.4 1 805 243 224 VAL N N 119.7 0.5 1 806 244 225 ILE C C 175.5 0.3 1 807 244 225 ILE CA C 64.6 0.4 1 808 244 225 ILE CB C 36.8 0.4 1 809 244 225 ILE N N 120.9 0.5 1 810 245 226 PHE C C 175.1 0.3 1 811 245 226 PHE CA C 60.2 0.4 1 812 245 226 PHE CB C 39.77 0.4 1 813 245 226 PHE N N 117.2 0.5 1 814 246 227 ALA C C 177.7 0.3 1 815 246 227 ALA CA C 53.2 0.4 1 816 246 227 ALA CB C 16.88 0.4 1 817 246 227 ALA N N 122.3 0.5 1 818 247 228 VAL C C 175 0.3 1 819 247 228 VAL CA C 66.45 0.4 1 820 247 228 VAL CB C 29.55 0.4 1 821 247 228 VAL N N 121 0.5 1 822 248 229 VAL C C 177.2 0.3 1 823 248 229 VAL CA C 64.86 0.4 1 824 248 229 VAL CB C 30.14 0.4 1 825 248 229 VAL N N 122.3 0.5 1 826 249 230 LEU C C 176.4 0.3 1 827 249 230 LEU CA C 56.18 0.4 1 828 249 230 LEU CB C 40.65 0.4 1 829 249 230 LEU N N 119.3 0.5 1 830 250 231 ILE C C 176.9 0.3 1 831 250 231 ILE CA C 64.2 0.4 1 832 250 231 ILE CB C 36.7 0.4 1 833 250 231 ILE N N 121.2 0.5 1 834 251 232 PHE C C 177.1 0.3 1 835 251 232 PHE CA C 59.8 0.4 1 836 251 232 PHE N N 125.1 0.5 1 837 252 233 LEU C C 176.7 0.3 1 838 252 233 LEU CA C 56 0.4 1 839 252 233 LEU CB C 40.7 0.4 1 840 252 233 LEU N N 118.8 0.5 1 841 253 234 LEU C C 176.7 0.3 1 842 253 234 LEU CA C 56.22 0.4 1 843 253 234 LEU CB C 40 0.4 1 844 253 234 LEU N N 121.8 0.5 1 845 254 235 CYS C C 176.8 0.3 1 846 254 235 CYS CA C 58.3 0.4 1 847 254 235 CYS CB C 28.04 0.4 1 848 254 235 CYS N N 119.8 0.5 1 849 255 236 TRP C C 178.4 0.3 1 850 255 236 TRP CA C 56.94 0.4 1 851 255 236 TRP CB C 29.85 0.4 1 852 255 236 TRP N N 121.3 0.5 1 853 256 237 LEU C C 177.7 0.3 1 854 256 237 LEU CA C 55.84 0.4 1 855 256 237 LEU CB C 40 0.4 1 856 256 237 LEU N N 124.9 0.5 1 857 258 239 TYR C C 179 0.3 1 858 258 239 TYR CA C 58.33 0.4 1 859 258 239 TYR CB C 42.07 0.4 1 860 258 239 TYR N N 124.9 0.5 1 861 259 240 ASN C C 173 0.3 1 862 259 240 ASN CA C 53.9 0.4 1 863 259 240 ASN CB C 37.62 0.4 1 864 259 240 ASN N N 123 0.5 1 865 260 241 LEU C C 175.3 0.3 1 866 260 241 LEU CA C 56.19 0.4 1 867 260 241 LEU CB C 39.06 0.4 1 868 260 241 LEU N N 121.8 0.5 1 869 261 242 VAL C C 175 0.3 1 870 261 242 VAL CA C 65.2 0.4 1 871 261 242 VAL CB C 29.62 0.4 1 872 261 242 VAL N N 118.6 0.5 1 873 262 243 LEU C C 176.6 0.3 1 874 262 243 LEU CA C 56 0.4 1 875 262 243 LEU CB C 40.07 0.4 1 876 262 243 LEU N N 121.8 0.5 1 877 263 244 LEU C C 176 0.3 1 878 263 244 LEU CA C 55.6 0.4 1 879 263 244 LEU CB C 40.62 0.4 1 880 263 244 LEU N N 123.5 0.5 1 881 264 245 ALA C C 174.4 0.3 1 882 264 245 ALA CA C 53.3 0.4 1 883 264 245 ALA CB C 15.82 0.4 1 884 264 245 ALA N N 122.2 0.5 1 885 265 246 ASP C C 171.6 0.3 1 886 265 246 ASP CA C 56.3 0.4 1 887 265 246 ASP N N 126.5 0.5 1 888 266 247 THR C C 175.3 0.3 1 889 266 247 THR CA C 60.3 0.4 1 890 266 247 THR N N 120.7 0.5 1 891 267 248 LEU C C 176.1 0.3 1 892 267 248 LEU CA C 55.95 0.4 1 893 267 248 LEU CB C 40.13 0.4 1 894 267 248 LEU N N 121.6 0.5 1 895 268 249 MET C C 176.8 0.3 1 896 268 249 MET CA C 58.2 0.4 1 897 268 249 MET CB C 31.9 0.4 1 898 268 249 MET N N 120.2 0.5 1 899 269 250 ARG C C 175.5 0.3 1 900 269 250 ARG CA C 57 0.4 1 901 269 250 ARG CB C 29.7 0.4 1 902 269 250 ARG N N 116.7 0.5 1 903 270 251 THR C C 175.7 0.3 1 904 270 251 THR CA C 64 0.4 1 905 270 251 THR N N 117.1 0.5 1 906 271 252 GLN C C 176 0.3 1 907 271 252 GLN CA C 57.4 0.4 1 908 271 252 GLN N N 122.8 0.5 1 909 272 253 VAL C C 176 0.3 1 910 272 253 VAL CA C 63.67 0.4 1 911 272 253 VAL CB C 35.31 0.4 1 912 272 253 VAL N N 121.3 0.5 1 913 273 254 ILE C C 178.3 0.3 1 914 273 254 ILE CA C 64 0.4 1 915 273 254 ILE CB C 36 0.4 1 916 273 254 ILE N N 123.3 0.5 1 917 274 255 GLN C C 176 0.3 1 918 274 255 GLN CA C 56.95 0.4 1 919 274 255 GLN N N 123.4 0.5 1 920 275 256 GLU C C 177.2 0.3 1 921 275 256 GLU CA C 55.73 0.4 1 922 275 256 GLU CB C 29.13 0.4 1 923 275 256 GLU N N 123.6 0.5 1 924 276 257 SER CA C 61.3 0.4 1 925 276 257 SER CB C 63.34 0.4 1 926 276 257 SER N N 116.4 0.5 1 927 277 258 CYS C C 175.6 0.3 1 928 277 258 CYS CA C 55.3 0.4 1 929 277 258 CYS CB C 39.7 0.4 1 930 277 258 CYS N N 117.2 0.5 1 931 278 259 GLU C C 175.2 0.3 1 932 278 259 GLU CA C 58.2 0.4 1 933 278 259 GLU CB C 28.89 0.4 1 934 278 259 GLU N N 120.9 0.5 1 935 279 260 ARG C C 176.6 0.3 1 936 279 260 ARG CA C 56.2 0.4 1 937 279 260 ARG CB C 29.5 0.4 1 938 279 260 ARG N N 123 0.5 1 939 280 261 ARG C C 176.3 0.3 1 940 280 261 ARG CA C 55.87 0.4 1 941 280 261 ARG CB C 28.25 0.4 1 942 280 261 ARG N N 124 0.5 1 943 281 262 ASN C C 174.6 0.3 1 944 281 262 ASN CA C 51.88 0.4 1 945 281 262 ASN CB C 37.7 0.4 1 946 281 262 ASN N N 121.1 0.5 1 947 282 263 ASN C C 176.6 0.3 1 948 282 263 ASN CA C 55.8 0.4 1 949 282 263 ASN CB C 39 0.4 1 950 282 263 ASN N N 121.6 0.5 1 951 283 264 ILE C C 175.2 0.3 1 952 283 264 ILE CA C 64.5 0.4 1 953 283 264 ILE CB C 36.6 0.4 1 954 283 264 ILE N N 120.8 0.5 1 955 284 265 GLY C C 176.8 0.3 1 956 284 265 GLY CA C 41.4 0.4 1 957 284 265 GLY N N 110.5 0.5 1 958 286 267 ALA C C 178.5 0.3 1 959 286 267 ALA CA C 53.84 0.4 1 960 286 267 ALA CB C 16.63 0.4 1 961 286 267 ALA N N 122.8 0.5 1 962 287 268 LEU C C 175.8 0.3 1 963 287 268 LEU CA C 56.15 0.4 1 964 287 268 LEU CB C 40.2 0.4 1 965 287 268 LEU N N 125.5 0.5 1 966 288 269 ASP C C 176.5 0.3 1 967 288 269 ASP CA C 56.25 0.4 1 968 288 269 ASP N N 116.8 0.5 1 969 289 270 ALA C C 177.5 0.3 1 970 289 270 ALA CA C 53.25 0.4 1 971 289 270 ALA CB C 16.9 0.4 1 972 289 270 ALA N N 124.6 0.5 1 973 290 271 THR C C 177 0.3 1 974 290 271 THR CA C 64.1 0.4 1 975 290 271 THR N N 114.9 0.5 1 976 291 272 GLU C C 177 0.3 1 977 291 272 GLU CA C 57.5 0.4 1 978 291 272 GLU CB C 29.7 0.4 1 979 291 272 GLU N N 120.8 0.5 1 980 292 273 ILE C C 176 0.3 1 981 292 273 ILE CA C 64.3 0.4 1 982 292 273 ILE CB C 36.64 0.4 1 983 292 273 ILE N N 121.3 0.5 1 984 293 274 LEU C C 175.1 0.3 1 985 293 274 LEU CA C 55.6 0.4 1 986 293 274 LEU CB C 39.44 0.4 1 987 293 274 LEU N N 122.7 0.5 1 988 294 275 GLY C C 173.8 0.3 1 989 294 275 GLY CA C 45.03 0.4 1 990 294 275 GLY N N 108.5 0.5 1 991 295 276 PHE C C 177.5 0.3 1 992 295 276 PHE CA C 58.5 0.4 1 993 295 276 PHE N N 121.6 0.5 1 994 296 277 LEU C C 175.3 0.3 1 995 296 277 LEU CA C 55.9 0.4 1 996 296 277 LEU CB C 40 0.4 1 997 296 277 LEU N N 120.9 0.5 1 998 297 278 HIS C C 176.6 0.3 1 999 297 278 HIS CA C 57.7 0.4 1 1000 297 278 HIS CB C 30.13 0.4 1 1001 297 278 HIS N N 120.6 0.5 1 1002 298 279 SER C C 177.7 0.3 1 1003 298 279 SER CA C 62.58 0.4 1 1004 298 279 SER CB C 64.53 0.4 1 1005 298 279 SER N N 122.5 0.5 1 1006 299 280 CYS C C 177.3 0.3 1 1007 299 280 CYS CA C 59.2 0.4 1 1008 299 280 CYS CB C 27.36 0.4 1 1009 299 280 CYS N N 121.6 0.5 1 1010 300 281 LEU C C 179 0.3 1 1011 300 281 LEU CA C 54.96 0.4 1 1012 300 281 LEU CB C 40.74 0.4 1 1013 300 281 LEU N N 121.3 0.5 1 1014 301 282 ASN C C 176.6 0.3 1 1015 301 282 ASN CA C 53.3 0.4 1 1016 301 282 ASN CB C 36.76 0.4 1 1017 301 282 ASN N N 119 0.5 1 1018 302 283 PRO CA C 58.86 0.4 1 1019 303 284 ILE C C 173.7 0.3 1 1020 303 284 ILE CA C 66.5 0.4 1 1021 303 284 ILE CB C 36.65 0.4 1 1022 303 284 ILE N N 120.9 0.5 1 1023 304 285 ILE C C 175.9 0.3 1 1024 304 285 ILE CA C 65.8 0.4 1 1025 304 285 ILE CB C 36.33 0.4 1 1026 304 285 ILE N N 120.4 0.5 1 1027 305 286 TYR C C 174.8 0.3 1 1028 305 286 TYR CA C 56.7 0.4 1 1029 305 286 TYR CB C 37.9 0.4 1 1030 305 286 TYR N N 120.3 0.5 1 1031 306 287 ALA C C 172 0.3 1 1032 306 287 ALA CA C 54.35 0.4 1 1033 306 287 ALA CB C 16.4 0.4 1 1034 306 287 ALA N N 123.3 0.5 1 1035 307 288 PHE C C 175.9 0.3 1 1036 307 288 PHE CA C 60.25 0.4 1 1037 307 288 PHE CB C 40.2 0.4 1 1038 307 288 PHE N N 120.4 0.5 1 1039 308 289 ILE C C 177.2 0.3 1 1040 308 289 ILE CA C 64.55 0.4 1 1041 308 289 ILE CB C 36.6 0.4 1 1042 308 289 ILE N N 120.7 0.5 1 1043 309 290 GLY C C 174 0.3 1 1044 309 290 GLY CA C 41.6 0.4 1 1045 309 290 GLY N N 111.3 0.5 1 1046 310 291 GLN C C 176.2 0.3 1 1047 310 291 GLN CA C 57.8 0.4 1 1048 310 291 GLN CB C 31.9 0.4 1 1049 310 291 GLN N N 119.4 0.5 1 1050 311 292 ASN C C 175.6 0.3 1 1051 311 292 ASN CA C 55.5 0.4 1 1052 311 292 ASN CB C 38.8 0.4 1 1053 311 292 ASN N N 120.1 0.5 1 1054 312 293 PHE C C 175.4 0.3 1 1055 312 293 PHE CA C 58.3 0.4 1 1056 312 293 PHE CB C 36.8 0.4 1 1057 312 293 PHE N N 120.7 0.5 1 1058 313 294 ARG C C 174.5 0.3 1 1059 313 294 ARG CA C 56 0.4 1 1060 313 294 ARG CB C 29.3 0.4 1 1061 313 294 ARG N N 123 0.5 1 1062 314 295 HIS C C 176.3 0.3 1 1063 314 295 HIS CA C 58.6 0.4 1 1064 314 295 HIS CB C 29.9 0.4 1 1065 314 295 HIS N N 122.1 0.5 1 1066 315 296 GLY C C 174.1 0.3 1 1067 315 296 GLY CA C 47.2 0.4 1 1068 315 296 GLY N N 109.7 0.5 1 1069 316 297 PHE C C 176.2 0.3 1 1070 316 297 PHE CA C 58.2 0.4 1 1071 316 297 PHE N N 123.6 0.5 1 1072 317 298 LEU C C 176.6 0.3 1 1073 317 298 LEU CA C 55.7 0.4 1 1074 317 298 LEU CB C 40.2 0.4 1 1075 317 298 LEU N N 122 0.5 1 1076 318 299 LYS C C 177.5 0.3 1 1077 318 299 LYS CA C 56.2 0.4 1 1078 318 299 LYS CB C 30 0.4 1 1079 318 299 LYS N N 121.8 0.5 1 1080 319 300 ILE C C 176 0.3 1 1081 319 300 ILE CA C 65.2 0.4 1 1082 319 300 ILE CB C 36.4 0.4 1 1083 319 300 ILE N N 120.6 0.5 1 1084 320 301 LEU C C 176.8 0.3 1 1085 320 301 LEU CA C 56.2 0.4 1 1086 320 301 LEU CB C 40 0.4 1 1087 320 301 LEU N N 121.9 0.5 1 1088 321 302 ALA C C 177.1 0.3 1 1089 321 302 ALA CA C 55 0.4 1 1090 321 302 ALA CB C 18 0.4 1 1091 321 302 ALA N N 123 0.5 1 1092 322 303 MET C C 173.3 0.3 1 1093 322 303 MET CA C 56.1 0.4 1 1094 322 303 MET N N 120.4 0.5 1 1095 323 304 HIS C C 173.2 0.3 1 1096 323 304 HIS CA C 57 0.4 1 1097 323 304 HIS CB C 29.7 0.4 1 1098 323 304 HIS N N 120.7 0.5 1 1099 324 305 GLY C C 173.8 0.3 1 1100 324 305 GLY CA C 45.23 0.4 1 1101 324 305 GLY N N 108.6 0.5 1 1102 325 306 LEU C C 177.6 0.3 1 1103 325 306 LEU CA C 53.9 0.4 1 1104 325 306 LEU CB C 39.6 0.4 1 1105 325 306 LEU N N 123.7 0.5 1 1106 326 307 VAL C C 175.4 0.3 1 1107 326 307 VAL CA C 63 0.4 1 1108 326 307 VAL CB C 30.55 0.4 1 1109 326 307 VAL N N 119.7 0.5 1 1110 327 308 SER C C 175.3 0.3 1 1111 327 308 SER CA C 59.7 0.4 1 1112 327 308 SER N N 116.8 0.5 1 1113 328 309 LYS CA C 56.64 0.4 1 1114 328 309 LYS N N 121.4 0.5 1 stop_ save_