data_18020 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments of Apo Human Integrin Alpha1 I-domain ; _BMRB_accession_number 18020 _BMRB_flat_file_name bmr18020.str _Entry_type original _Submission_date 2011-10-25 _Accession_date 2011-10-25 _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 Chin Yanni K. . 2 Headey Stephen J. . 3 McEwan Paul A. . 4 Emsley Jonas K. . 5 Simpson Jamie S. . 6 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 176 "13C chemical shifts" 538 "15N chemical shifts" 176 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-14 update BMRB 'update entry citation' 2013-02-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18021 'Mg2+ bound Alpha1 I-domain' stop_ save_ ############################# # Citation for this entry # ############################# save_Citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Assignments of human integrin 1I domain in the apo and Mg+ bound states.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23339031 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chin 'Yanni K-Y' . . 2 Headey Stephen . . 3 Mohanty Biswaranjan . . 4 Emsley Jonas . . 5 Simpson Jamie S. . 6 Scanlon Martin J. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 8 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 117 _Page_last 121 _Year 2014 _Details . loop_ _Keyword 'I domain' Integrin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Apo alpha1 I-domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '1 I-domain' $Integrin_Alpha1_I-domain stop_ _System_molecular_weight 21485 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Integrin_Alpha1_I-domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Integrin_Alpha1_I-domain _Molecular_mass 21485 _Mol_thiol_state 'all free' loop_ _Biological_function 'Responsible for the binding of collagen' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 192 _Mol_residue_sequence ; STQLDIVIVLDGSNSIYPWD SVTAFLNDLLERMDIGPKQT QVGIVQYGENVTHEFNLNKY SSTEEVLVAAKKIVQRGGRQ TMTALGIDTARKEAFTEARG ARRGVKKVMVIVTDGESHDN HRLKKVIQDCEDENIQRFSI AILGSYNRGNLSTEKFVEEI KSIASEPTEKHFFNVSDELA LVTIVKTLGERI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 140 SER 2 141 THR 3 142 GLN 4 143 LEU 5 144 ASP 6 145 ILE 7 146 VAL 8 147 ILE 9 148 VAL 10 149 LEU 11 150 ASP 12 151 GLY 13 152 SER 14 153 ASN 15 154 SER 16 155 ILE 17 156 TYR 18 157 PRO 19 158 TRP 20 159 ASP 21 160 SER 22 161 VAL 23 162 THR 24 163 ALA 25 164 PHE 26 165 LEU 27 166 ASN 28 167 ASP 29 168 LEU 30 169 LEU 31 170 GLU 32 171 ARG 33 172 MET 34 173 ASP 35 174 ILE 36 175 GLY 37 176 PRO 38 177 LYS 39 178 GLN 40 179 THR 41 180 GLN 42 181 VAL 43 182 GLY 44 183 ILE 45 184 VAL 46 185 GLN 47 186 TYR 48 187 GLY 49 188 GLU 50 189 ASN 51 190 VAL 52 191 THR 53 192 HIS 54 193 GLU 55 194 PHE 56 195 ASN 57 196 LEU 58 197 ASN 59 198 LYS 60 199 TYR 61 200 SER 62 201 SER 63 202 THR 64 203 GLU 65 204 GLU 66 205 VAL 67 206 LEU 68 207 VAL 69 208 ALA 70 209 ALA 71 210 LYS 72 211 LYS 73 212 ILE 74 213 VAL 75 214 GLN 76 215 ARG 77 216 GLY 78 217 GLY 79 218 ARG 80 219 GLN 81 220 THR 82 221 MET 83 222 THR 84 223 ALA 85 224 LEU 86 225 GLY 87 226 ILE 88 227 ASP 89 228 THR 90 229 ALA 91 230 ARG 92 231 LYS 93 232 GLU 94 233 ALA 95 234 PHE 96 235 THR 97 236 GLU 98 237 ALA 99 238 ARG 100 239 GLY 101 240 ALA 102 241 ARG 103 242 ARG 104 243 GLY 105 244 VAL 106 245 LYS 107 246 LYS 108 247 VAL 109 248 MET 110 249 VAL 111 250 ILE 112 251 VAL 113 252 THR 114 253 ASP 115 254 GLY 116 255 GLU 117 256 SER 118 257 HIS 119 258 ASP 120 259 ASN 121 260 HIS 122 261 ARG 123 262 LEU 124 263 LYS 125 264 LYS 126 265 VAL 127 266 ILE 128 267 GLN 129 268 ASP 130 269 CYS 131 270 GLU 132 271 ASP 133 272 GLU 134 273 ASN 135 274 ILE 136 275 GLN 137 276 ARG 138 277 PHE 139 278 SER 140 279 ILE 141 280 ALA 142 281 ILE 143 282 LEU 144 283 GLY 145 284 SER 146 285 TYR 147 286 ASN 148 287 ARG 149 288 GLY 150 289 ASN 151 290 LEU 152 291 SER 153 292 THR 154 293 GLU 155 294 LYS 156 295 PHE 157 296 VAL 158 297 GLU 159 298 GLU 160 299 ILE 161 300 LYS 162 301 SER 163 302 ILE 164 303 ALA 165 304 SER 166 305 GLU 167 306 PRO 168 307 THR 169 308 GLU 170 309 LYS 171 310 HIS 172 311 PHE 173 312 PHE 174 313 ASN 175 314 VAL 176 315 SER 177 316 ASP 178 317 GLU 179 318 LEU 180 319 ALA 181 320 LEU 182 321 VAL 183 322 THR 184 323 ILE 185 324 VAL 186 325 LYS 187 326 THR 188 327 LEU 189 328 GLY 190 329 GLU 191 330 ARG 192 331 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-03 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18021 Integrin_Alpha1_I-domain 100.00 192 100.00 100.00 3.97e-137 BMRB 18942 entity_1 100.00 192 100.00 100.00 3.97e-137 PDB 1PT6 "I Domain From Human Integrin Alpha1-beta1" 100.00 213 98.96 99.48 1.09e-135 PDB 1QC5 "I Domain From Integrin Alpha1-beta1" 100.00 192 99.48 100.00 1.34e-136 PDB 1QCY "The Crystal Structure Of The I-domain Of Human Integrin Alpha1beta1" 99.48 193 98.43 98.95 5.03e-134 PDB 2M32 "Alpha-1 Integrin I-domain In Complex With Glogen Triple Helical Peptide" 100.00 192 100.00 100.00 3.97e-137 PDB 4A0Q "Activated Conformation Of Integrin Alpha1 I-Domain Mutant" 100.00 201 98.96 98.96 7.78e-136 DBJ BAG62150 "unnamed protein product [Homo sapiens]" 100.00 1173 100.00 100.00 1.13e-125 GB AAI37122 "Integrin, alpha 1 [Homo sapiens]" 100.00 1179 100.00 100.00 1.18e-125 GB AAI37123 "Integrin, alpha 1 [Homo sapiens]" 100.00 1179 100.00 100.00 1.18e-125 GB EAW54866 "hCG2002731, isoform CRA_c [Homo sapiens]" 100.00 766 100.00 100.00 2.61e-129 GB EAW54867 "hCG2002731, isoform CRA_d [Homo sapiens]" 100.00 768 100.00 100.00 3.36e-129 GB EAW54868 "hCG2002731, isoform CRA_e [Homo sapiens]" 100.00 1177 100.00 100.00 1.02e-125 REF NP_852478 "integrin alpha-1 precursor [Homo sapiens]" 100.00 1179 100.00 100.00 1.18e-125 REF XP_001094788 "PREDICTED: integrin alpha-1 [Macaca mulatta]" 100.00 1179 100.00 100.00 1.57e-125 REF XP_002815595 "PREDICTED: integrin alpha-1 [Pongo abelii]" 100.00 1179 99.48 100.00 7.65e-125 REF XP_003276564 "PREDICTED: integrin alpha-1 [Nomascus leucogenys]" 100.00 1179 99.48 100.00 5.71e-125 REF XP_003827398 "PREDICTED: integrin alpha-1 [Pan paniscus]" 100.00 1179 100.00 100.00 1.22e-125 SP P56199 "RecName: Full=Integrin alpha-1; AltName: Full=CD49 antigen-like family member A; AltName: Full=Laminin and collagen receptor; A" 100.00 1179 100.00 100.00 1.18e-125 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Integrin_Alpha1_I-domain 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 $Integrin_Alpha1_I-domain 'recombinant technology' . Escherichia coli 'BL21 CODON+ RP (DE3)' p28a+ stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_1H_13C_15N_Alpha1I _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Integrin_Alpha1_I-domain 0.4 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $1H_13C_15N_Alpha1I save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $1H_13C_15N_Alpha1I save_ ####################### # Sample conditions # ####################### save_Apo_Condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 298 . 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 water C 13 protons ppm 4.7546646 na indirect . . . 0.251449530 water H 1 protons ppm 4.7546646 internal direct . . . 1.000000000 water N 15 protons ppm 4.7546646 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCO' '3D HNCACB' '3D HCACO' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $1H_13C_15N_Alpha1I stop_ _Sample_conditions_label $Apo_Condition _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name '1 I-domain' _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 1 1 SER C C 174.58 . . 2 1 1 SER CA C 58.347 . . 3 1 1 SER CB C 63.523 . . 4 2 2 THR H H 8.12 . . 5 2 2 THR C C 174.53 . . 6 2 2 THR CA C 61.711 . . 7 2 2 THR CB C 69.556 . . 8 2 2 THR N N 115.89 . . 9 3 3 GLN H H 8.22 . . 10 3 3 GLN C C 174.48 . . 11 3 3 GLN CA C 56.107 . . 12 3 3 GLN CB C 29.554 . . 13 3 3 GLN N N 122.91 . . 14 4 4 LEU H H 6.937 . . 15 4 4 LEU C C 174.805 . . 16 4 4 LEU CA C 54.124 . . 17 4 4 LEU CB C 46.538 . . 18 4 4 LEU N N 121.62 . . 19 5 5 ASP H H 8.87 . . 20 5 5 ASP C C 173.499 . . 21 5 5 ASP CA C 54.038 . . 22 5 5 ASP CB C 42.055 . . 23 5 5 ASP N N 126.22 . . 24 6 6 ILE H H 8.926 . . 25 6 6 ILE C C 174.187 . . 26 6 6 ILE CA C 59.038 . . 27 6 6 ILE CB C 40.244 . . 28 6 6 ILE N N 123.06 . . 29 7 7 VAL H H 8.94 . . 30 7 7 VAL C C 175.535 . . 31 7 7 VAL CA C 59.469 . . 32 7 7 VAL CB C 34.037 . . 33 7 7 VAL N N 124.49 . . 34 8 8 ILE H H 8.45 . . 35 8 8 ILE C C 173.429 . . 36 8 8 ILE CA C 59.469 . . 37 8 8 ILE CB C 38.003 . . 38 8 8 ILE N N 127.64 . . 39 9 9 VAL H H 9.65 . . 40 9 9 VAL C C 173.907 . . 41 9 9 VAL CA C 61.538 . . 42 9 9 VAL CB C 31.882 . . 43 9 9 VAL N N 129.97 . . 44 10 10 LEU H H 9.14 . . 45 10 10 LEU C C 174.089 . . 46 10 10 LEU CA C 53.262 . . 47 10 10 LEU CB C 45.417 . . 48 10 10 LEU N N 125.13 . . 49 11 11 ASP H H 7.96 . . 50 11 11 ASP C C 175.254 . . 51 11 11 ASP CA C 52.815 . . 52 11 11 ASP CB C 42.039 . . 53 11 11 ASP N N 127.48 . . 54 12 12 GLY H H 8.347 . . 55 12 12 GLY C C 175.43 . . 56 12 12 GLY CA C 45.046 . . 57 12 12 GLY N N 112.59 . . 58 13 13 SER H H 8.299 . . 59 13 13 SER CA C 59.247 . . 60 13 13 SER CB C 63.925 . . 61 13 13 SER N N 113.82 . . 62 14 14 ASN C C 175.27 . . 63 14 14 ASN CA C 55.56 . . 64 14 14 ASN CB C 38.597 . . 65 15 15 SER H H 7.73 . . 66 15 15 SER C C 174.61 . . 67 15 15 SER CA C 59.846 . . 68 15 15 SER CB C 61.495 . . 69 15 15 SER N N 112.74 . . 70 16 16 ILE H H 7.09 . . 71 16 16 ILE C C 175.94 . . 72 16 16 ILE CA C 62.088 . . 73 16 16 ILE N N 123.63 . . 74 17 17 TYR H H 9.31 . . 75 17 17 TYR CA C 55.372 . . 76 17 17 TYR N N 128.22 . . 77 18 18 PRO C C 177.86 . . 78 18 18 PRO CA C 61.612 . . 79 18 18 PRO CB C 33.102 . . 80 19 19 TRP H H 9.32 . . 81 19 19 TRP C C 177.11 . . 82 19 19 TRP CA C 58.99 . . 83 19 19 TRP CB C 29.235 . . 84 19 19 TRP N N 126.28 . . 85 20 20 ASP H H 8.425 . . 86 20 20 ASP C C 178.2 . . 87 20 20 ASP CA C 55.48 . . 88 20 20 ASP CB C 39.632 . . 89 20 20 ASP N N 113.68 . . 90 21 21 SER H H 7.46 . . 91 21 21 SER C C 176.32 . . 92 21 21 SER CA C 62.001 . . 93 21 21 SER CB C 62.927 . . 94 21 21 SER N N 115.04 . . 95 22 22 VAL H H 7.343 . . 96 22 22 VAL C C 178.119 . . 97 22 22 VAL CA C 65.552 . . 98 22 22 VAL CB C 29.916 . . 99 22 22 VAL N N 124.44 . . 100 23 23 THR H H 7.529 . . 101 23 23 THR C C 177.82 . . 102 23 23 THR CA C 65.674 . . 103 23 23 THR CB C 67.505 . . 104 23 23 THR N N 110.58 . . 105 24 24 ALA H H 7.85 . . 106 24 24 ALA C C 178.69 . . 107 24 24 ALA CA C 55.011 . . 108 24 24 ALA CB C 17.802 . . 109 24 24 ALA N N 124.77 . . 110 25 25 PHE H H 7.06 . . 111 25 25 PHE C C 175.26 . . 112 25 25 PHE CA C 60.418 . . 113 25 25 PHE CB C 38.597 . . 114 25 25 PHE N N 118.41 . . 115 26 26 LEU H H 7.87 . . 116 26 26 LEU C C 177.97 . . 117 26 26 LEU CA C 57.078 . . 118 26 26 LEU CB C 41.862 . . 119 26 26 LEU N N 115.99 . . 120 27 27 ASN H H 8.02 . . 121 27 27 ASN C C 175.7 . . 122 27 27 ASN CA C 57.309 . . 123 27 27 ASN CB C 40.218 . . 124 27 27 ASN N N 115.26 . . 125 28 28 ASP H H 8.23 . . 126 28 28 ASP C C 178.18 . . 127 28 28 ASP CA C 56.356 . . 128 28 28 ASP CB C 39.473 . . 129 28 28 ASP N N 117.3 . . 130 29 29 LEU H H 7.93 . . 131 29 29 LEU C C 177.83 . . 132 29 29 LEU CA C 57.152 . . 133 29 29 LEU CB C 42.34 . . 134 29 29 LEU N N 119.11 . . 135 30 30 LEU H H 7.92 . . 136 30 30 LEU C C 179.21 . . 137 30 30 LEU CA C 56.834 . . 138 30 30 LEU CB C 40.827 . . 139 30 30 LEU N N 115.63 . . 140 31 31 GLU H H 8.15 . . 141 31 31 GLU C C 176.98 . . 142 31 31 GLU CA C 58.427 . . 143 31 31 GLU CB C 28.722 . . 144 31 31 GLU N N 114.89 . . 145 32 32 ARG H H 6.73 . . 146 32 32 ARG C C 176.39 . . 147 32 32 ARG CA C 55.286 . . 148 32 32 ARG CB C 29.957 . . 149 32 32 ARG N N 113.96 . . 150 33 33 MET H H 7.636 . . 151 33 33 MET C C 174.83 . . 152 33 33 MET CA C 55.399 . . 153 33 33 MET CB C 33.978 . . 154 33 33 MET N N 118.386 . . 155 34 34 ASP H H 8.8 . . 156 34 34 ASP C C 173.79 . . 157 34 34 ASP CA C 52.771 . . 158 34 34 ASP CB C 40.193 . . 159 34 34 ASP N N 123.79 . . 160 35 35 ILE H H 7.095 . . 161 35 35 ILE C C 176.61 . . 162 35 35 ILE CA C 58.188 . . 163 35 35 ILE CB C 37.477 . . 164 35 35 ILE N N 123.68 . . 165 36 36 GLY H H 8.81 . . 166 36 36 GLY C C 172.91 . . 167 36 36 GLY CA C 45.248 . . 168 36 36 GLY N N 113.13 . . 169 37 37 PRO C C 178.46 . . 170 37 37 PRO CA C 64.521 . . 171 37 37 PRO CB C 31.58 . . 172 38 38 LYS H H 8.255 . . 173 38 38 LYS C C 176.33 . . 174 38 38 LYS CA C 54.445 . . 175 38 38 LYS CB C 31.987 . . 176 38 38 LYS N N 116.94 . . 177 39 39 GLN H H 7.66 . . 178 39 39 GLN C C 176.111 . . 179 39 39 GLN CA C 55.181 . . 180 39 39 GLN CB C 28.881 . . 181 39 39 GLN N N 122.01 . . 182 40 40 THR H H 8.682 . . 183 40 40 THR C C 172.488 . . 184 40 40 THR CA C 63.187 . . 185 40 40 THR CB C 69.29 . . 186 40 40 THR N N 125.44 . . 187 41 41 GLN H H 8.915 . . 188 41 41 GLN C C 174.159 . . 189 41 41 GLN CA C 54.604 . . 190 41 41 GLN CB C 33.261 . . 191 41 41 GLN N N 123.062 . . 192 42 42 VAL H H 8.07 . . 193 42 42 VAL C C 173.401 . . 194 42 42 VAL CA C 59.462 . . 195 42 42 VAL CB C 36.128 . . 196 42 42 VAL N N 118.8 . . 197 43 43 GLY H H 8.65 . . 198 43 43 GLY C C 172.18 . . 199 43 43 GLY CA C 42.818 . . 200 43 43 GLY N N 110.81 . . 201 44 44 ILE H H 7.16 . . 202 44 44 ILE C C 174.187 . . 203 44 44 ILE CA C 60.418 . . 204 44 44 ILE CB C 40.827 . . 205 44 44 ILE N N 115.54 . . 206 45 45 VAL H H 9.19 . . 207 45 45 VAL C C 173.387 . . 208 45 45 VAL CA C 59.462 . . 209 45 45 VAL CB C 34.854 . . 210 45 45 VAL N N 127.43 . . 211 46 46 GLN H H 9.22 . . 212 46 46 GLN C C 174.426 . . 213 46 46 GLN CA C 52.772 . . 214 46 46 GLN CB C 31.907 . . 215 46 46 GLN N N 125.59 . . 216 47 47 TYR H H 9.42 . . 217 47 47 TYR C C 172.573 . . 218 47 47 TYR CA C 54.684 . . 219 47 47 TYR CB C 43.295 . . 220 47 47 TYR N N 125.5 . . 221 48 48 GLY H H 7.75 . . 222 48 48 GLY C C 173.738 . . 223 48 48 GLY CA C 47.357 . . 224 48 48 GLY N N 109.93 . . 225 49 49 GLU H H 8.87 . . 226 49 49 GLU C C 175.269 . . 227 49 49 GLU CA C 57.79 . . 228 49 49 GLU CB C 29.774 . . 229 49 49 GLU N N 126.73 . . 230 50 50 ASN H H 7.734 . . 231 50 50 ASN C C 174.173 . . 232 50 50 ASN CA C 50.628 . . 233 50 50 ASN CB C 40.982 . . 234 50 50 ASN N N 113.71 . . 235 51 51 VAL H H 8.642 . . 236 51 51 VAL C C 174.861 . . 237 51 51 VAL CA C 61.771 . . 238 51 51 VAL CB C 33.181 . . 239 51 51 VAL N N 118.7 . . 240 52 52 THR H H 9.08 . . 241 52 52 THR C C 173.485 . . 242 52 52 THR CA C 61.533 . . 243 52 52 THR CB C 71.487 . . 244 52 52 THR N N 122.66 . . 245 53 53 HIS H H 8.98 . . 246 53 53 HIS C C 175.69 . . 247 53 53 HIS CA C 56.117 . . 248 53 53 HIS CB C 30.235 . . 249 53 53 HIS N N 126.5 . . 250 54 54 GLU H H 8.85 . . 251 54 54 GLU C C 178.947 . . 252 54 54 GLU CA C 57.664 . . 253 54 54 GLU CB C 27.718 . . 254 54 54 GLU N N 128.06 . . 255 55 55 PHE H H 7.18 . . 256 55 55 PHE C C 174.286 . . 257 55 55 PHE CA C 56.511 . . 258 55 55 PHE CB C 40.298 . . 259 55 55 PHE N N 106.241 . . 260 56 56 ASN H H 8.26 . . 261 56 56 ASN C C 176.364 . . 262 56 56 ASN CA C 51.402 . . 263 56 56 ASN CB C 38.977 . . 264 56 56 ASN N N 119.46 . . 265 57 57 LEU H H 9.13 . . 266 57 57 LEU C C 176.041 . . 267 57 57 LEU CA C 58.267 . . 268 57 57 LEU CB C 43.136 . . 269 57 57 LEU N N 122.97 . . 270 58 58 ASN H H 7.35 . . 271 58 58 ASN C C 177.066 . . 272 58 58 ASN CA C 50.498 . . 273 58 58 ASN CB C 38.317 . . 274 58 58 ASN N N 108.48 . . 275 59 59 LYS H H 7.79 . . 276 59 59 LYS C C 176.42 . . 277 59 59 LYS CA C 58.688 . . 278 59 59 LYS CB C 32.437 . . 279 59 59 LYS N N 121.89 . . 280 60 60 TYR H H 8.75 . . 281 60 60 TYR C C 176.546 . . 282 60 60 TYR CA C 56.448 . . 283 60 60 TYR CB C 40.418 . . 284 60 60 TYR N N 115.64 . . 285 61 61 SER H H 8.89 . . 286 61 61 SER C C 172.02 . . 287 61 61 SER CA C 57.261 . . 288 61 61 SER CB C 64.218 . . 289 61 61 SER N N 114.08 . . 290 62 62 SER H H 7.24 . . 291 62 62 SER C C 174.412 . . 292 62 62 SER CA C 56.728 . . 293 62 62 SER CB C 66.668 . . 294 62 62 SER N N 111.27 . . 295 63 63 THR H H 9.23 . . 296 63 63 THR C C 175.577 . . 297 63 63 THR CA C 66.878 . . 298 63 63 THR CB C 68.768 . . 299 63 63 THR N N 120.54 . . 300 64 64 GLU H H 8.88 . . 301 64 64 GLU C C 178.849 . . 302 64 64 GLU CA C 60.088 . . 303 64 64 GLU CB C 28.867 . . 304 64 64 GLU N N 119.18 . . 305 65 65 GLU H H 7.271 . . 306 65 65 GLU C C 179.228 . . 307 65 65 GLU CA C 58.618 . . 308 65 65 GLU CB C 30.547 . . 309 65 65 GLU N N 114.76 . . 310 66 66 VAL H H 7.3 . . 311 66 66 VAL C C 176.729 . . 312 66 66 VAL CA C 65.408 . . 313 66 66 VAL CB C 30.897 . . 314 66 66 VAL N N 118.88 . . 315 67 67 LEU H H 8.03 . . 316 67 67 LEU C C 180.127 . . 317 67 67 LEU CA C 57.568 . . 318 67 67 LEU CB C 40.418 . . 319 67 67 LEU N N 118.91 . . 320 68 68 VAL H H 7.03 . . 321 68 68 VAL C C 178.231 . . 322 68 68 VAL CA C 65.758 . . 323 68 68 VAL CB C 31.667 . . 324 68 68 VAL N N 117.63 . . 325 69 69 ALA H H 6.87 . . 326 69 69 ALA C C 181.629 . . 327 69 69 ALA CA C 54.488 . . 328 69 69 ALA CB C 19.627 . . 329 69 69 ALA N N 119.82 . . 330 70 70 ALA H H 8.86 . . 331 70 70 ALA C C 178.245 . . 332 70 70 ALA CA C 54.628 . . 333 70 70 ALA CB C 17.207 . . 334 70 70 ALA N N 120.54 . . 335 71 71 LYS H H 7.01 . . 336 71 71 LYS C C 177.627 . . 337 71 71 LYS CA C 57.778 . . 338 71 71 LYS CB C 32.227 . . 339 71 71 LYS N N 111.63 . . 340 72 72 LYS H H 7.19 . . 341 72 72 LYS C C 176.813 . . 342 72 72 LYS CA C 55.608 . . 343 72 72 LYS CB C 33.067 . . 344 72 72 LYS N N 115.13 . . 345 73 73 ILE H H 7.06 . . 346 73 73 ILE C C 176.911 . . 347 73 73 ILE CA C 62.818 . . 348 73 73 ILE CB C 37.407 . . 349 73 73 ILE N N 120.42 . . 350 74 74 VAL H H 8.441 . . 351 74 74 VAL C C 173.808 . . 352 74 74 VAL CA C 59.808 . . 353 74 74 VAL CB C 33.137 . . 354 74 74 VAL N N 128.21 . . 355 75 75 GLN H H 7.57 . . 356 75 75 GLN C C 177.361 . . 357 75 75 GLN CA C 55.118 . . 358 75 75 GLN CB C 27.257 . . 359 75 75 GLN N N 123.61 . . 360 76 76 ARG H H 9.51 . . 361 76 76 ARG C C 177.964 . . 362 76 76 ARG CA C 57.498 . . 363 76 76 ARG CB C 29.567 . . 364 76 76 ARG N N 129.279 . . 365 77 77 GLY H H 7.49 . . 366 77 77 GLY C C 173.878 . . 367 77 77 GLY CA C 45.458 . . 368 77 77 GLY N N 107.22 . . 369 78 78 GLY H H 7.733 . . 370 78 78 GLY C C 181.039 . . 371 78 78 GLY CA C 44.968 . . 372 78 78 GLY N N 105.94 . . 373 81 81 THR C C 175.49 . . 374 81 81 THR CA C 62.379 . . 375 81 81 THR CB C 69.359 . . 376 82 82 MET H H 8.39 . . 377 82 82 MET C C 174.92 . . 378 82 82 MET CA C 52.066 . . 379 82 82 MET CB C 28.637 . . 380 82 82 MET N N 128.91 . . 381 83 83 THR H H 7.281 . . 382 83 83 THR C C 175.86 . . 383 83 83 THR CA C 65.346 . . 384 83 83 THR CB C 68.381 . . 385 83 83 THR N N 118.06 . . 386 84 84 ALA H H 9.86 . . 387 84 84 ALA C C 179.291 . . 388 84 84 ALA CA C 56.145 . . 389 84 84 ALA CB C 16.591 . . 390 84 84 ALA N N 124.99 . . 391 85 85 LEU H H 8.648 . . 392 85 85 LEU C C 181.23 . . 393 85 85 LEU CA C 57.471 . . 394 85 85 LEU CB C 40.906 . . 395 85 85 LEU N N 120.76 . . 396 86 86 GLY H H 8.47 . . 397 86 86 GLY C C 174.047 . . 398 86 86 GLY CA C 46.799 . . 399 86 86 GLY N N 109.75 . . 400 87 87 ILE H H 8.22 . . 401 87 87 ILE C C 177.726 . . 402 87 87 ILE CA C 65.548 . . 403 87 87 ILE CB C 38.457 . . 404 87 87 ILE N N 120.43 . . 405 88 88 ASP H H 8.79 . . 406 88 88 ASP C C 178.821 . . 407 88 88 ASP CA C 57.232 . . 408 88 88 ASP CB C 42.499 . . 409 88 88 ASP N N 118.73 . . 410 89 89 THR H H 8.36 . . 411 89 89 THR C C 176.785 . . 412 89 89 THR CA C 66.812 . . 413 89 89 THR CB C 67.948 . . 414 89 89 THR N N 112.56 . . 415 90 90 ALA H H 8.14 . . 416 90 90 ALA C C 178.38 . . 417 90 90 ALA CA C 55.382 . . 418 90 90 ALA CB C 18.322 . . 419 90 90 ALA N N 125.26 . . 420 91 91 ARG H H 8.53 . . 421 91 91 ARG C C 177.403 . . 422 91 91 ARG CA C 60.47 . . 423 91 91 ARG CB C 29.317 . . 424 91 91 ARG N N 116.8 . . 425 92 92 LYS H H 8.394 . . 426 92 92 LYS C C 177.178 . . 427 92 92 LYS CA C 58.222 . . 428 92 92 LYS CB C 33.659 . . 429 92 92 LYS N N 113.37 . . 430 93 93 GLU H H 8.4 . . 431 93 93 GLU C C 177.684 . . 432 93 93 GLU CA C 56.675 . . 433 93 93 GLU CB C 32.066 . . 434 93 93 GLU N N 112.63 . . 435 94 94 ALA H H 8.09 . . 436 94 94 ALA C C 178.259 . . 437 94 94 ALA CA C 55.241 . . 438 94 94 ALA CB C 19.085 . . 439 94 94 ALA N N 120.96 . . 440 95 95 PHE H H 7.07 . . 441 95 95 PHE C C 175.325 . . 442 95 95 PHE CA C 57.187 . . 443 95 95 PHE CB C 36.969 . . 444 95 95 PHE N N 112.41 . . 445 96 96 THR H H 7.02 . . 446 96 96 THR C C 176.518 . . 447 96 96 THR CA C 59.216 . . 448 96 96 THR CB C 72.208 . . 449 96 96 THR N N 106.26 . . 450 97 97 GLU C C 180.75 . . 451 97 97 GLU CA C 58.718 . . 452 97 97 GLU CB C 29.252 . . 453 98 98 ALA H H 8.543 . . 454 98 98 ALA C C 179.256 . . 455 98 98 ALA CA C 54.46 . . 456 98 98 ALA CB C 18.175 . . 457 98 98 ALA N N 120.902 . . 458 99 99 ARG H H 7.049 . . 459 99 99 ARG C C 173.963 . . 460 99 99 ARG CA C 56.428 . . 461 99 99 ARG CB C 29.386 . . 462 99 99 ARG N N 114.58 . . 463 100 100 GLY H H 7.49 . . 464 100 100 GLY C C 174.075 . . 465 100 100 GLY CA C 45.303 . . 466 100 100 GLY N N 102.13 . . 467 101 101 ALA H H 7.8 . . 468 101 101 ALA C C 178.077 . . 469 101 101 ALA CA C 52.577 . . 470 101 101 ALA CB C 17.833 . . 471 101 101 ALA N N 123.52 . . 472 102 102 ARG H H 9.41 . . 473 102 102 ARG C C 176.574 . . 474 102 102 ARG CA C 54.545 . . 475 102 102 ARG CB C 31.867 . . 476 102 102 ARG N N 125.03 . . 477 103 103 ARG H H 8.57 . . 478 103 103 ARG C C 178.203 . . 479 103 103 ARG CA C 57.113 . . 480 103 103 ARG CB C 29.471 . . 481 103 103 ARG N N 123.9 . . 482 104 104 GLY C C 174.23 . . 483 104 104 GLY CA C 45.551 . . 484 105 105 VAL H H 7.2 . . 485 105 105 VAL C C 175.858 . . 486 105 105 VAL CA C 61 . . 487 105 105 VAL CB C 31.571 . . 488 105 105 VAL N N 117.74 . . 489 106 106 LYS H H 8.21 . . 490 106 106 LYS C C 174.089 . . 491 106 106 LYS CA C 57.39 . . 492 106 106 LYS CB C 32.984 . . 493 106 106 LYS N N 127.51 . . 494 107 107 LYS H H 8.36 . . 495 107 107 LYS C C 176.265 . . 496 107 107 LYS CA C 55.036 . . 497 107 107 LYS CB C 34.788 . . 498 107 107 LYS N N 123.97 . . 499 108 108 VAL H H 8.958 . . 500 108 108 VAL C C 173.892 . . 501 108 108 VAL CA C 60.215 . . 502 108 108 VAL CB C 36.28 . . 503 108 108 VAL N N 123.06 . . 504 109 109 MET H H 9.69 . . 505 109 109 MET C C 175.1 . . 506 109 109 MET CA C 53.388 . . 507 109 109 MET CB C 38.791 . . 508 109 109 MET N N 126.01 . . 509 110 110 VAL H H 8.44 . . 510 110 110 VAL C C 174.033 . . 511 110 110 VAL CA C 60.608 . . 512 110 110 VAL CB C 33.768 . . 513 110 110 VAL N N 124.41 . . 514 111 111 ILE H H 9.17 . . 515 111 111 ILE C C 174.047 . . 516 111 111 ILE CA C 61 . . 517 111 111 ILE CB C 41.381 . . 518 111 111 ILE N N 128.48 . . 519 112 112 VAL H H 8.56 . . 520 112 112 VAL C C 173.907 . . 521 112 112 VAL CA C 60.765 . . 522 112 112 VAL CB C 33.768 . . 523 112 112 VAL N N 127.26 . . 524 113 113 THR H H 8.4 . . 525 113 113 THR C C 171.365 . . 526 113 113 THR CA C 61.392 . . 527 113 113 THR CB C 68.612 . . 528 113 113 THR N N 118.13 . . 529 114 114 ASP C C 176.31 . . 530 114 114 ASP CA C 52.39 . . 531 115 115 GLY H H 7.61 . . 532 115 115 GLY C C 171.37 . . 533 115 115 GLY CA C 45.704 . . 534 115 115 GLY N N 107.28 . . 535 116 116 GLU H H 6.97 . . 536 116 116 GLU C C 176.95 . . 537 116 116 GLU CA C 56.129 . . 538 116 116 GLU CB C 29.5 . . 539 116 116 GLU N N 116.43 . . 540 117 117 SER H H 10.49 . . 541 117 117 SER CA C 59.018 . . 542 117 117 SER CB C 64.428 . . 543 117 117 SER N N 120.43 . . 544 118 118 HIS CB C 30.941 . . 545 119 119 ASP H H 8.56 . . 546 119 119 ASP CA C 51.529 . . 547 119 119 ASP CB C 38.886 . . 548 119 119 ASP N N 119.106 . . 549 120 120 ASN H H 7.326 . . 550 120 120 ASN CA C 56.4 . . 551 120 120 ASN CB C 37.984 . . 552 120 120 ASN N N 115.556 . . 553 121 121 HIS C C 176.6 . . 554 121 121 HIS CA C 58.188 . . 555 121 121 HIS CB C 29.12 . . 556 122 122 ARG H H 7.31 . . 557 122 122 ARG C C 176.701 . . 558 122 122 ARG CA C 55.639 . . 559 122 122 ARG CB C 30.951 . . 560 122 122 ARG N N 117.88 . . 561 123 123 LEU H H 7.24 . . 562 123 123 LEU C C 177.08 . . 563 123 123 LEU CA C 58.224 . . 564 123 123 LEU CB C 41.937 . . 565 123 123 LEU N N 119.06 . . 566 124 124 LYS H H 8.36 . . 567 124 124 LYS C C 179.369 . . 568 124 124 LYS CA C 59.94 . . 569 124 124 LYS CB C 31.332 . . 570 124 124 LYS N N 116.88 . . 571 125 125 LYS H H 7.75 . . 572 125 125 LYS C C 177.41 . . 573 125 125 LYS CA C 58.244 . . 574 125 125 LYS CB C 31.861 . . 575 125 125 LYS N N 119.76 . . 576 126 126 VAL H H 7.72 . . 577 126 126 VAL C C 179.748 . . 578 126 126 VAL CA C 65.577 . . 579 126 126 VAL CB C 31.786 . . 580 126 126 VAL N N 117.87 . . 581 127 127 ILE H H 8.68 . . 582 127 127 ILE C C 177.894 . . 583 127 127 ILE CA C 63.536 . . 584 127 127 ILE CB C 35.263 . . 585 127 127 ILE N N 120.16 . . 586 128 128 GLN H H 7.87 . . 587 128 128 GLN C C 178.301 . . 588 128 128 GLN CA C 58.395 . . 589 128 128 GLN CB C 27.703 . . 590 128 128 GLN N N 121.09 . . 591 129 129 ASP H H 8.52 . . 592 129 129 ASP C C 179.551 . . 593 129 129 ASP CA C 57.564 . . 594 129 129 ASP CB C 39.194 . . 595 129 129 ASP N N 119.25 . . 596 130 130 CYS H H 7.643 . . 597 130 130 CYS C C 176.855 . . 598 130 130 CYS CA C 64.065 . . 599 130 130 CYS CB C 27.325 . . 600 130 130 CYS N N 115.65 . . 601 131 131 GLU H H 8.524 . . 602 131 131 GLU C C 180.941 . . 603 131 131 GLU CA C 58.547 . . 604 131 131 GLU CB C 28.762 . . 605 131 131 GLU N N 123.02 . . 606 132 132 ASP H H 8.823 . . 607 132 132 ASP C C 177.684 . . 608 132 132 ASP CA C 56.808 . . 609 132 132 ASP CB C 39.874 . . 610 132 132 ASP N N 121.52 . . 611 133 133 GLU H H 7.04 . . 612 133 133 GLU CA C 55.75 . . 613 133 133 GLU CB C 29.442 . . 614 133 133 GLU N N 116.55 . . 615 134 134 ASN H H 8 . . 616 134 134 ASN C C 174.833 . . 617 134 134 ASN CA C 54.011 . . 618 134 134 ASN CB C 36.624 . . 619 134 134 ASN N N 113.99 . . 620 135 135 ILE H H 7.65 . . 621 135 135 ILE C C 175.212 . . 622 135 135 ILE CA C 61.084 . . 623 135 135 ILE CB C 38.715 . . 624 135 135 ILE N N 118.49 . . 625 136 136 GLN H H 8.18 . . 626 136 136 GLN C C 175.114 . . 627 136 136 GLN CA C 55.58 . . 628 136 136 GLN CB C 29.118 . . 629 136 136 GLN N N 131.68 . . 630 137 137 ARG H H 9.15 . . 631 137 137 ARG C C 175.605 . . 632 137 137 ARG CA C 54.522 . . 633 137 137 ARG CB C 30.741 . . 634 137 137 ARG N N 124.12 . . 635 138 138 PHE H H 9.18 . . 636 138 138 PHE C C 175.437 . . 637 138 138 PHE CA C 56.427 . . 638 138 138 PHE CB C 41.608 . . 639 138 138 PHE N N 122.1 . . 640 139 139 SER H H 9.571 . . 641 139 139 SER C C 171.61 . . 642 139 139 SER CA C 55.51 . . 643 139 139 SER CB C 66.73 . . 644 139 139 SER N N 117.12 . . 645 140 140 ILE H H 8.94 . . 646 140 140 ILE C C 173.86 . . 647 140 140 ILE CA C 59.603 . . 648 140 140 ILE CB C 40.479 . . 649 140 140 ILE N N 122.27 . . 650 141 141 ALA H H 8.373 . . 651 141 141 ALA C C 175.4 . . 652 141 141 ALA CA C 49.159 . . 653 141 141 ALA CB C 19.309 . . 654 141 141 ALA N N 126.96 . . 655 142 142 ILE H H 8.89 . . 656 142 142 ILE C C 176.94 . . 657 142 142 ILE CA C 60.097 . . 658 142 142 ILE CB C 37.939 . . 659 142 142 ILE N N 121.7 . . 660 143 143 LEU H H 8.743 . . 661 143 143 LEU CA C 56.431 . . 662 143 143 LEU CB C 39.776 . . 663 143 143 LEU N N 126.394 . . 664 144 144 GLY H H 6.67 . . 665 144 144 GLY CA C 48.798 . . 666 144 144 GLY N N 104.319 . . 667 146 146 TYR C C 178.82 . . 668 146 146 TYR CA C 61.72 . . 669 146 146 TYR CB C 36.52 . . 670 147 147 ASN H H 8.71 . . 671 147 147 ASN C C 180.716 . . 672 147 147 ASN CA C 55.705 . . 673 147 147 ASN CB C 37.186 . . 674 147 147 ASN N N 117.9 . . 675 148 148 ARG H H 9.166 . . 676 148 148 ARG C C 178.329 . . 677 148 148 ARG CA C 59.871 . . 678 148 148 ARG CB C 30.889 . . 679 148 148 ARG N N 121.36 . . 680 149 149 GLY H H 7.75 . . 681 149 149 GLY C C 173.345 . . 682 149 149 GLY CA C 44.492 . . 683 149 149 GLY N N 104.38 . . 684 150 150 ASN H H 7.85 . . 685 150 150 ASN C C 174.286 . . 686 150 150 ASN CA C 54.231 . . 687 150 150 ASN CB C 37.251 . . 688 150 150 ASN N N 116.45 . . 689 151 151 LEU H H 8.508 . . 690 151 151 LEU C C 177.543 . . 691 151 151 LEU CA C 53.482 . . 692 151 151 LEU CB C 43.077 . . 693 151 151 LEU N N 118.13 . . 694 152 152 SER H H 8.42 . . 695 152 152 SER C C 178.133 . . 696 152 152 SER CA C 58.566 . . 697 152 152 SER CB C 62.721 . . 698 152 152 SER N N 115.24 . . 699 153 153 THR H H 8.866 . . 700 153 153 THR C C 175.254 . . 701 153 153 THR CA C 61.802 . . 702 153 153 THR CB C 69.779 . . 703 153 153 THR N N 115.24 . . 704 154 154 GLU H H 8 . . 705 154 154 GLU C C 178.568 . . 706 154 154 GLU CA C 61.075 . . 707 154 154 GLU CB C 29.315 . . 708 154 154 GLU N N 122.67 . . 709 155 155 LYS H H 8.39 . . 710 155 155 LYS C C 179.158 . . 711 155 155 LYS CA C 58.945 . . 712 155 155 LYS CB C 31.537 . . 713 155 155 LYS N N 119.47 . . 714 156 156 PHE H H 8.31 . . 715 156 156 PHE C C 176.013 . . 716 156 156 PHE CA C 57.927 . . 717 156 156 PHE CB C 38.667 . . 718 156 156 PHE N N 121.91 . . 719 157 157 VAL H H 8.38 . . 720 157 157 VAL C C 177.375 . . 721 157 157 VAL CA C 67.372 . . 722 157 157 VAL CB C 30.797 . . 723 157 157 VAL N N 117.67 . . 724 158 158 GLU H H 7.39 . . 725 158 158 GLU C C 179.158 . . 726 158 158 GLU CA C 59.131 . . 727 158 158 GLU CB C 28.852 . . 728 158 158 GLU N N 116.52 . . 729 159 159 GLU H H 8.15 . . 730 159 159 GLU C C 179.579 . . 731 159 159 GLU CA C 59.497 . . 732 159 159 GLU CB C 29.5 . . 733 159 159 GLU N N 120.99 . . 734 160 160 ILE H H 8.28 . . 735 160 160 ILE C C 180.576 . . 736 160 160 ILE CA C 61.639 . . 737 160 160 ILE CB C 33.256 . . 738 160 160 ILE N N 118.84 . . 739 161 161 LYS H H 8.4 . . 740 161 161 LYS C C 178.442 . . 741 161 161 LYS CA C 60.307 . . 742 161 161 LYS CB C 31.757 . . 743 161 161 LYS N N 125.26 . . 744 162 162 SER H H 7.33 . . 745 162 162 SER C C 174.974 . . 746 162 162 SER CA C 60.807 . . 747 162 162 SER CB C 62.555 . . 748 162 162 SER N N 112.68 . . 749 163 163 ILE H H 7.093 . . 750 163 163 ILE C C 175.395 . . 751 163 163 ILE CA C 62.388 . . 752 163 163 ILE CB C 39.165 . . 753 163 163 ILE N N 120.56 . . 754 164 164 ALA H H 6.79 . . 755 164 164 ALA C C 178.498 . . 756 164 164 ALA CA C 51.9 . . 757 164 164 ALA CB C 19.189 . . 758 164 164 ALA N N 121.7 . . 759 165 165 SER H H 8.58 . . 760 165 165 SER C C 171.44 . . 761 165 165 SER CA C 61.371 . . 762 165 165 SER CB C 61.563 . . 763 165 165 SER N N 120.74 . . 764 166 166 GLU H H 8.089 . . 765 166 166 GLU C C 176.602 . . 766 166 166 GLU CA C 53.756 . . 767 166 166 GLU CB C 29.291 . . 768 166 166 GLU N N 117.43 . . 769 168 168 THR C C 176.34 . . 770 168 168 THR CA C 66.868 . . 771 168 168 THR CB C 68.62 . . 772 169 169 GLU H H 9.27 . . 773 169 169 GLU C C 177.501 . . 774 169 169 GLU CA C 58.801 . . 775 169 169 GLU CB C 28.448 . . 776 169 169 GLU N N 118.39 . . 777 170 170 LYS H H 7.1 . . 778 170 170 LYS C C 176.16 . . 779 170 170 LYS CA C 55.481 . . 780 170 170 LYS CB C 33.475 . . 781 170 170 LYS N N 114.62 . . 782 171 171 HIS H H 7 . . 783 171 171 HIS C C 172.488 . . 784 171 171 HIS CA C 57.852 . . 785 171 171 HIS CB C 31.483 . . 786 171 171 HIS N N 114.1 . . 787 172 172 PHE H H 7.79 . . 788 172 172 PHE C C 174.061 . . 789 172 172 PHE CA C 55.386 . . 790 172 172 PHE CB C 41.158 . . 791 172 172 PHE N N 118.94 . . 792 173 173 PHE H H 8.42 . . 793 173 173 PHE C C 184.929 . . 794 173 173 PHE CA C 55.576 . . 795 173 173 PHE CB C 42.391 . . 796 173 173 PHE N N 126.2 . . 797 174 174 ASN H H 8.13 . . 798 174 174 ASN C C 174.37 . . 799 174 174 ASN CA C 51.307 . . 800 174 174 ASN CB C 40.399 . . 801 174 174 ASN N N 117.67 . . 802 175 175 VAL H H 8.544 . . 803 175 175 VAL C C 175.872 . . 804 175 175 VAL CA C 59.465 . . 805 175 175 VAL CB C 33.854 . . 806 175 175 VAL N N 118.816 . . 807 176 176 SER H H 8.78 . . 808 176 176 SER C C 173.32 . . 809 176 176 SER CA C 61.725 . . 810 176 176 SER CB C 62.785 . . 811 176 176 SER N N 119.29 . . 812 177 177 ASP H H 7.107 . . 813 177 177 ASP C C 174.328 . . 814 177 177 ASP CA C 53.11 . . 815 177 177 ASP CB C 43.34 . . 816 177 177 ASP N N 111.37 . . 817 178 178 GLU H H 12 . . 818 178 178 GLU C C 178.821 . . 819 178 178 GLU CA C 62.121 . . 820 178 178 GLU CB C 29.112 . . 821 178 178 GLU N N 123 . . 822 179 179 LEU H H 7.945 . . 823 179 179 LEU C C 178.203 . . 824 179 179 LEU CA C 56.833 . . 825 179 179 LEU CB C 40.036 . . 826 179 179 LEU N N 116.49 . . 827 180 180 ALA H H 7.64 . . 828 180 180 ALA C C 179.79 . . 829 180 180 ALA CA C 51.203 . . 830 180 180 ALA CB C 18.923 . . 831 180 180 ALA N N 117.52 . . 832 181 181 LEU H H 7.677 . . 833 181 181 LEU C C 177.67 . . 834 181 181 LEU CA C 58.897 . . 835 181 181 LEU CB C 40.881 . . 836 181 181 LEU N N 124.258 . . 837 182 182 VAL H H 7.49 . . 838 182 182 VAL C C 177.838 . . 839 182 182 VAL CA C 64.246 . . 840 182 182 VAL CB C 31.122 . . 841 182 182 VAL N N 108.449 . . 842 183 183 THR H H 7.681 . . 843 183 183 THR C C 176.813 . . 844 183 183 THR CA C 63.871 . . 845 183 183 THR CB C 69.595 . . 846 183 183 THR N N 110.24 . . 847 184 184 ILE H H 7.14 . . 848 184 184 ILE C C 176.111 . . 849 184 184 ILE CA C 61.056 . . 850 184 184 ILE CB C 38.066 . . 851 184 184 ILE N N 112.08 . . 852 185 185 VAL H H 6.99 . . 853 185 185 VAL C C 177.122 . . 854 185 185 VAL CA C 67.061 . . 855 185 185 VAL CB C 31.122 . . 856 185 185 VAL N N 120.21 . . 857 186 186 LYS H H 8.36 . . 858 186 186 LYS C C 178.428 . . 859 186 186 LYS CA C 59.37 . . 860 186 186 LYS CB C 31.483 . . 861 186 186 LYS N N 119.92 . . 862 187 187 THR H H 7.61 . . 863 187 187 THR C C 177.627 . . 864 187 187 THR CA C 65.441 . . 865 187 187 THR CB C 68.381 . . 866 187 187 THR N N 114.61 . . 867 188 188 LEU H H 8.13 . . 868 188 188 LEU C C 178.315 . . 869 188 188 LEU CA C 58.327 . . 870 188 188 LEU CB C 40.968 . . 871 188 188 LEU N N 120.56 . . 872 189 189 GLY H H 8.29 . . 873 189 189 GLY C C 175.971 . . 874 189 189 GLY CA C 46.47 . . 875 189 189 GLY N N 102.641 . . 876 190 190 GLU H H 7.45 . . 877 190 190 GLU C C 177.712 . . 878 190 190 GLU CA C 57.188 . . 879 190 190 GLU CB C 29.396 . . 880 190 190 GLU N N 116.92 . . 881 191 191 ARG H H 7.568 . . 882 191 191 ARG C C 175.437 . . 883 191 191 ARG CA C 56.619 . . 884 191 191 ARG CB C 32.052 . . 885 191 191 ARG N N 118.02 . . 886 192 192 ILE H H 6.84 . . 887 192 192 ILE C C 180.057 . . 888 192 192 ILE CA C 64.966 . . 889 192 192 ILE CB C 38.502 . . 890 192 192 ILE N N 124.05 . . stop_ save_