data_17064 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C, and 15N Chemical Shift Assignments for Anabaena sensory rhodopsin 1-229 ; _BMRB_accession_number 17064 _BMRB_flat_file_name bmr17064.str _Entry_type original _Submission_date 2010-07-16 _Accession_date 2010-07-16 _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 Shi Lichi . . 2 Kawamura Izuru . . 3 Jung Kwang-Hwang . . 4 Brown Leonid . . 5 Ladizhansky Vladimir . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 668 "15N chemical shifts" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-01-19 original author . stop_ _Original_release_date 2011-01-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Conformation of a Seven-Helical Transmembrane Photosensor in the Lipid Environment.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21191921 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shi Lichi . . 2 Kawamura Izuru . . 3 Jung Kwang-Hwan . . 4 Brown Leonid S. . 5 Ladizhansky Vladimir . . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed. Engl.' _Journal_name_full 'Angewandte Chemie (International ed. in English)' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2010 _Details . loop_ _Keyword 'membrane proteins' 'protein structure' receptor rhodopsin 'Solid state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ASR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label opsin $opsin retinal $RET stop_ _System_molecular_weight 27487 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'photoreptor for chromatic adaptation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_opsin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common opsin _Molecular_mass 27220 _Mol_thiol_state 'all free' loop_ _Biological_function 'photoreceptor for chromatic adaptation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 235 _Mol_residue_sequence ; MNLESLLHWIYVAGMTIGAL HFWSLSRNPRGVPQYEYLVA MFIPIWSGLAYMAMAIDQGK VEAAGQIAHYARYIDWMVTT PLLLLSLSWTAMQFIKKDWT LIGFLMSTQIVVITSGLIAD LSERDWVRYLWYICGVCAFL IILWGIWNPLRAKTRTQSSE LANLYDKLVTYFTVLWIGYP IVWIIGPSGFGWINQTIDTF LFCLLPFFSKVGFSFLDLHG LRNLNDSRQHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 LEU 4 GLU 5 SER 6 LEU 7 LEU 8 HIS 9 TRP 10 ILE 11 TYR 12 VAL 13 ALA 14 GLY 15 MET 16 THR 17 ILE 18 GLY 19 ALA 20 LEU 21 HIS 22 PHE 23 TRP 24 SER 25 LEU 26 SER 27 ARG 28 ASN 29 PRO 30 ARG 31 GLY 32 VAL 33 PRO 34 GLN 35 TYR 36 GLU 37 TYR 38 LEU 39 VAL 40 ALA 41 MET 42 PHE 43 ILE 44 PRO 45 ILE 46 TRP 47 SER 48 GLY 49 LEU 50 ALA 51 TYR 52 MET 53 ALA 54 MET 55 ALA 56 ILE 57 ASP 58 GLN 59 GLY 60 LYS 61 VAL 62 GLU 63 ALA 64 ALA 65 GLY 66 GLN 67 ILE 68 ALA 69 HIS 70 TYR 71 ALA 72 ARG 73 TYR 74 ILE 75 ASP 76 TRP 77 MET 78 VAL 79 THR 80 THR 81 PRO 82 LEU 83 LEU 84 LEU 85 LEU 86 SER 87 LEU 88 SER 89 TRP 90 THR 91 ALA 92 MET 93 GLN 94 PHE 95 ILE 96 LYS 97 LYS 98 ASP 99 TRP 100 THR 101 LEU 102 ILE 103 GLY 104 PHE 105 LEU 106 MET 107 SER 108 THR 109 GLN 110 ILE 111 VAL 112 VAL 113 ILE 114 THR 115 SER 116 GLY 117 LEU 118 ILE 119 ALA 120 ASP 121 LEU 122 SER 123 GLU 124 ARG 125 ASP 126 TRP 127 VAL 128 ARG 129 TYR 130 LEU 131 TRP 132 TYR 133 ILE 134 CYS 135 GLY 136 VAL 137 CYS 138 ALA 139 PHE 140 LEU 141 ILE 142 ILE 143 LEU 144 TRP 145 GLY 146 ILE 147 TRP 148 ASN 149 PRO 150 LEU 151 ARG 152 ALA 153 LYS 154 THR 155 ARG 156 THR 157 GLN 158 SER 159 SER 160 GLU 161 LEU 162 ALA 163 ASN 164 LEU 165 TYR 166 ASP 167 LYS 168 LEU 169 VAL 170 THR 171 TYR 172 PHE 173 THR 174 VAL 175 LEU 176 TRP 177 ILE 178 GLY 179 TYR 180 PRO 181 ILE 182 VAL 183 TRP 184 ILE 185 ILE 186 GLY 187 PRO 188 SER 189 GLY 190 PHE 191 GLY 192 TRP 193 ILE 194 ASN 195 GLN 196 THR 197 ILE 198 ASP 199 THR 200 PHE 201 LEU 202 PHE 203 CYS 204 LEU 205 LEU 206 PRO 207 PHE 208 PHE 209 SER 210 LYS 211 VAL 212 GLY 213 PHE 214 SER 215 PHE 216 LEU 217 ASP 218 LEU 219 HIS 220 GLY 221 LEU 222 ARG 223 ASN 224 LEU 225 ASN 226 ASP 227 SER 228 ARG 229 GLN 230 HIS 231 HIS 232 HIS 233 HIS 234 HIS 235 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-07 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 18595 ASR 100.00 235 100.00 100.00 2.38e-170 BMRB 25290 Anabaena_sensory_rhodopsin 100.00 235 100.00 100.00 2.38e-170 PDB 1XIO "Anabaena Sensory Rhodopsin" 97.45 261 100.00 100.00 4.07e-165 PDB 2M3G "Structure Of Anabaena Sensory Rhodopsin Determined By Solid State Nmr Spectroscopy" 100.00 235 99.57 99.57 2.29e-169 PDB 4TL3 "Mechanistic Insights From The Crystal Structure Of An Inward Proton- Transporting Anabaena Sensory Rhodopsin Mutant" 96.17 226 99.56 100.00 1.48e-161 DBJ BAB74864 "bacteriorhodopsin [Nostoc sp. PCC 7120]" 97.45 261 100.00 100.00 4.07e-165 REF WP_010997316 "lactococcin [Nostoc sp. PCC 7120]" 97.45 261 100.00 100.00 4.07e-165 stop_ save_ ############# # Ligands # ############# save_RET _Saveframe_category ligand _Mol_type non-polymer _Name_common "RET (RETINAL)" _BMRB_code . _PDB_code RET _Molecular_mass 284.436 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 16:01:03 2009 The retinal is covalently bound to the Lys210 of ASR via a Schiff Base ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C18 C18 C . 0 . ? C19 C19 C . 0 . ? C2 C2 C . 0 . ? C20 C20 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H14 H14 H . 0 . ? H15 H15 H . 0 . ? H161 H161 H . 0 . ? H162 H162 H . 0 . ? H163 H163 H . 0 . ? H171 H171 H . 0 . ? H172 H172 H . 0 . ? H173 H173 H . 0 . ? H181 H181 H . 0 . ? H182 H182 H . 0 . ? H183 H183 H . 0 . ? H191 H191 H . 0 . ? H192 H192 H . 0 . ? H193 H193 H . 0 . ? H201 H201 H . 0 . ? H202 H202 H . 0 . ? H203 H203 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? O1 O1 O . 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 C1 C2 ? ? SING C1 C6 ? ? SING C1 C16 ? ? SING C1 C17 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? DOUB C5 C6 ? ? SING C5 C18 ? ? SING C6 C7 ? ? DOUB C7 C8 ? ? SING C7 H7 ? ? SING C8 C9 ? ? SING C8 H8 ? ? DOUB C9 C10 ? ? SING C9 C19 ? ? SING C10 C11 ? ? SING C10 H10 ? ? DOUB C11 C12 ? ? SING C11 H11 ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 C20 ? ? SING C14 C15 ? ? SING C14 H14 ? ? DOUB C15 O1 ? ? SING C15 H15 ? ? SING C16 H161 ? ? SING C16 H162 ? ? SING C16 H163 ? ? SING C17 H171 ? ? SING C17 H172 ? ? SING C17 H173 ? ? SING C18 H181 ? ? SING C18 H182 ? ? SING C18 H183 ? ? SING C19 H191 ? ? SING C19 H192 ? ? SING C19 H193 ? ? SING C20 H201 ? ? SING C20 H202 ? ? SING C20 H203 ? ? stop_ _Mol_thiol_state 'not present' _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 _Gene_mnemonic $opsin 'Anabaena PCC7120' 103690 Bacteria . Nostoc . aso 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 $opsin 'recombinant technology' . Escherichia coli BL21 na stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $opsin 11 mg '[U-99% 13C; U-99% 15N]' $RET 110 ug 'natural abundance' H2O 100 % 'natural abundance' NaCl 10 mM 'natural abundance' CHES 25 mM '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 collection 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_3D_CONCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONCA' _Sample_label $sample_1 save_ save_3D_NCACX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '10 mM NaCl, 25 mM CHES' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 90 1 mM pH 9 0.1 pH pressure 1 . atm temperature 273 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details '10mM NaCl, 25mM CHES' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 90 5 mM pD 9 0.1 pH 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $entry_citation $entry_citation 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 '3D CONCA' '3D NCACX' '3D NCOCX' 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 opsin _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 6 6 LEU C C 176.8 0.2 1 2 6 6 LEU CA C 57.4 0.2 1 3 6 6 LEU CB C 43.0 0.2 1 4 6 6 LEU CD1 C 25.2 0.2 2 5 6 6 LEU CD2 C 24.4 0.2 2 6 6 6 LEU CG C 26.6 0.2 1 7 6 6 LEU N N 117.1 0.2 1 8 7 7 LEU C C 178.3 0.2 1 9 7 7 LEU CA C 58.6 0.2 1 10 7 7 LEU CB C 41.2 0.2 1 11 7 7 LEU CG C 26.8 0.2 1 12 7 7 LEU N N 117.4 0.2 1 13 8 8 HIS C C 177.9 0.2 1 14 8 8 HIS CA C 63.4 0.2 1 15 8 8 HIS CB C 28.6 0.2 1 16 8 8 HIS CD2 C 127.1 0.2 1 17 8 8 HIS CG C 129.2 0.2 1 18 8 8 HIS N N 115.8 0.2 1 19 9 9 TRP C C 179.6 0.2 1 20 9 9 TRP CA C 61.0 0.2 1 21 9 9 TRP CB C 30.5 0.2 1 22 9 9 TRP CG C 111.9 0.2 1 23 9 9 TRP N N 119.8 0.2 1 24 10 10 ILE C C 177.6 0.2 1 25 10 10 ILE CA C 66.0 0.2 1 26 10 10 ILE CB C 37.4 0.2 1 27 10 10 ILE CG1 C 29.8 0.2 1 28 10 10 ILE CG2 C 18.1 0.2 1 29 10 10 ILE N N 119.9 0.2 1 30 11 11 TYR C C 177.3 0.2 1 31 11 11 TYR CA C 63.6 0.2 1 32 11 11 TYR CB C 38.5 0.2 1 33 11 11 TYR N N 121.2 0.2 1 34 12 12 VAL C C 179.8 0.2 1 35 12 12 VAL CA C 68.1 0.2 1 36 12 12 VAL CB C 31.9 0.2 1 37 12 12 VAL CG1 C 22.6 0.2 2 38 12 12 VAL CG2 C 21.7 0.2 2 39 12 12 VAL N N 121.5 0.2 1 40 13 13 ALA C C 179.2 0.2 1 41 13 13 ALA CA C 55.9 0.2 1 42 13 13 ALA CB C 18.0 0.2 1 43 13 13 ALA N N 124.2 0.2 1 44 14 14 GLY C C 175.6 0.2 1 45 14 14 GLY CA C 48.2 0.2 1 46 14 14 GLY N N 106.6 0.2 1 47 15 15 MET C C 178.1 0.2 1 48 15 15 MET CA C 56.9 0.2 1 49 15 15 MET CB C 35.3 0.2 1 50 15 15 MET CG C 33.6 0.2 1 51 15 15 MET N N 121.0 0.2 1 52 16 16 THR C C 176.1 0.2 1 53 16 16 THR CA C 68.1 0.2 1 54 16 16 THR CG2 C 21.1 0.2 1 55 16 16 THR N N 116.7 0.2 1 56 17 17 ILE C C 177.8 0.2 1 57 17 17 ILE CA C 65.6 0.2 1 58 17 17 ILE CB C 38.0 0.2 1 59 17 17 ILE CG2 C 17.6 0.2 1 60 17 17 ILE N N 119.5 0.2 1 61 18 18 GLY C C 172.7 0.2 1 62 18 18 GLY CA C 48.0 0.2 1 63 18 18 GLY N N 105.1 0.2 1 64 19 19 ALA C C 179.8 0.2 1 65 19 19 ALA CA C 56.7 0.2 1 66 19 19 ALA CB C 18.2 0.2 1 67 19 19 ALA N N 122.2 0.2 1 68 20 20 LEU C C 179.4 0.2 1 69 20 20 LEU CA C 58.1 0.2 1 70 20 20 LEU CB C 42.7 0.2 1 71 20 20 LEU CG C 27.1 0.2 1 72 20 20 LEU N N 115.9 0.2 1 73 39 39 VAL C C 176.5 0.2 1 74 39 39 VAL CA C 68.6 0.2 1 75 39 39 VAL CB C 32.9 0.2 1 76 39 39 VAL CG1 C 26.4 0.2 2 77 39 39 VAL CG2 C 23.8 0.2 2 78 39 39 VAL N N 118.2 0.2 1 79 40 40 ALA C C 178.0 0.2 1 80 40 40 ALA CA C 55.3 0.2 1 81 40 40 ALA CB C 19.1 0.2 1 82 40 40 ALA N N 118.6 0.2 1 83 41 41 MET C C 176.6 0.2 1 84 41 41 MET CA C 59.2 0.2 1 85 41 41 MET CB C 34.3 0.2 1 86 41 41 MET N N 110.7 0.2 1 87 42 42 PHE C C 177.4 0.2 1 88 42 42 PHE CA C 63.2 0.2 1 89 42 42 PHE CB C 40.4 0.2 1 90 42 42 PHE N N 119.5 0.2 1 91 43 43 ILE C C 174.7 0.2 1 92 43 43 ILE CA C 67.9 0.2 1 93 43 43 ILE CB C 36.8 0.2 1 94 43 43 ILE CD1 C 14.8 0.2 1 95 43 43 ILE CG2 C 17.6 0.2 1 96 43 43 ILE N N 115.1 0.2 1 97 44 44 PRO C C 178.5 0.2 1 98 44 44 PRO CA C 65.5 0.2 1 99 44 44 PRO CB C 32.6 0.2 1 100 44 44 PRO CD C 51.4 0.2 1 101 44 44 PRO CG C 27.8 0.2 1 102 44 44 PRO N N 132.2 0.2 1 103 45 45 ILE C C 176.0 0.2 1 104 45 45 ILE CA C 64.6 0.2 1 105 45 45 ILE CB C 37.1 0.2 1 106 45 45 ILE CG1 C 29.0 0.2 1 107 45 45 ILE CG2 C 16.8 0.2 1 108 45 45 ILE N N 119.6 0.2 1 109 46 46 TRP C C 177.1 0.2 1 110 46 46 TRP CA C 60.9 0.2 1 111 46 46 TRP CB C 29.4 0.2 1 112 46 46 TRP CD1 C 125.8 0.2 2 113 46 46 TRP CE2 C 139.7 0.2 1 114 46 46 TRP CG C 112.0 0.2 1 115 46 46 TRP N N 120.1 0.2 1 116 46 46 TRP NE1 N 126.6 0.2 1 117 47 47 SER C C 177.7 0.2 1 118 47 47 SER CA C 60.2 0.2 1 119 47 47 SER CB C 65.7 0.2 1 120 47 47 SER N N 106.4 0.2 1 121 48 48 GLY C C 174.9 0.2 1 122 48 48 GLY CA C 47.5 0.2 1 123 48 48 GLY N N 106.4 0.2 1 124 49 49 LEU C C 178.4 0.2 1 125 49 49 LEU CA C 58.3 0.2 1 126 49 49 LEU CB C 41.4 0.2 1 127 49 49 LEU CD1 C 26.7 0.2 2 128 49 49 LEU CD2 C 22.9 0.2 2 129 49 49 LEU CG C 27.2 0.2 1 130 49 49 LEU N N 121.5 0.2 1 131 50 50 ALA C C 178.7 0.2 1 132 50 50 ALA CA C 55.3 0.2 1 133 50 50 ALA CB C 18.2 0.2 1 134 50 50 ALA N N 121.1 0.2 1 135 51 51 TYR C C 178.3 0.2 1 136 51 51 TYR CA C 60.7 0.2 1 137 51 51 TYR CB C 38.5 0.2 1 138 51 51 TYR CZ C 157.4 0.2 1 139 51 51 TYR N N 119.1 0.2 1 140 52 52 MET C C 177.5 0.2 1 141 52 52 MET CA C 59.2 0.2 1 142 52 52 MET CB C 33.2 0.2 1 143 52 52 MET CE C 17.6 0.2 1 144 52 52 MET CG C 31.6 0.2 1 145 52 52 MET N N 126.2 0.2 1 146 53 53 ALA C C 179.2 0.2 1 147 53 53 ALA CA C 54.8 0.2 1 148 53 53 ALA CB C 17.5 0.2 1 149 53 53 ALA N N 118.4 0.2 1 150 54 54 MET C C 180.7 0.2 1 151 54 54 MET CA C 58.8 0.2 1 152 54 54 MET CB C 33.2 0.2 1 153 54 54 MET CE C 16.5 0.2 1 154 54 54 MET CG C 31.2 0.2 1 155 54 54 MET N N 114.0 0.2 1 156 55 55 ALA C C 179.4 0.2 1 157 55 55 ALA CA C 55.6 0.2 1 158 55 55 ALA CB C 15.7 0.2 1 159 55 55 ALA N N 127.1 0.2 1 160 56 56 ILE C C 174.4 0.2 1 161 56 56 ILE CA C 60.5 0.2 1 162 56 56 ILE CB C 36.2 0.2 1 163 56 56 ILE CD1 C 15.4 0.2 1 164 56 56 ILE CG1 C 23.6 0.2 1 165 56 56 ILE CG2 C 18.7 0.2 1 166 56 56 ILE N N 111.2 0.2 1 167 57 57 ASP C C 175.0 0.2 1 168 57 57 ASP CA C 56.6 0.2 1 169 57 57 ASP CB C 38.7 0.2 1 170 57 57 ASP CG C 182.0 0.2 1 171 57 57 ASP N N 115.3 0.2 1 172 58 58 GLN C C 175.2 0.2 1 173 58 58 GLN CA C 54.8 0.2 1 174 58 58 GLN CB C 32.0 0.2 1 175 58 58 GLN CG C 35.6 0.2 1 176 58 58 GLN N N 117.4 0.2 1 177 59 59 GLY C C 172.3 0.2 1 178 59 59 GLY CA C 46.0 0.2 1 179 59 59 GLY N N 101.7 0.2 1 180 60 60 LYS C C 175.4 0.2 1 181 60 60 LYS CA C 54.0 0.2 1 182 60 60 LYS CB C 36.6 0.2 1 183 60 60 LYS CD C 30.0 0.2 1 184 60 60 LYS CE C 41.9 0.2 1 185 60 60 LYS CG C 24.2 0.2 1 186 60 60 LYS N N 114.1 0.2 1 187 60 60 LYS NZ N 33.4 0.2 1 188 61 61 VAL C C 171.6 0.2 1 189 61 61 VAL CA C 60.1 0.2 1 190 61 61 VAL CB C 35.9 0.2 1 191 61 61 VAL CG1 C 21.4 0.2 2 192 61 61 VAL CG2 C 20.7 0.2 2 193 61 61 VAL N N 120.5 0.2 1 194 62 62 GLU C C 175.9 0.2 1 195 62 62 GLU CA C 56.7 0.2 1 196 62 62 GLU CB C 29.9 0.2 1 197 62 62 GLU CD C 183.6 0.2 1 198 62 62 GLU CG C 36.3 0.2 1 199 62 62 GLU N N 128.1 0.2 1 200 63 63 ALA C C 176.6 0.2 1 201 63 63 ALA CA C 52.3 0.2 1 202 63 63 ALA CB C 21.7 0.2 1 203 63 63 ALA N N 128.8 0.2 1 204 64 64 ALA C C 177.7 0.2 1 205 64 64 ALA CA C 53.0 0.2 1 206 64 64 ALA CB C 18.1 0.2 1 207 64 64 ALA N N 127.2 0.2 1 208 65 65 GLY C C 173.2 0.2 1 209 65 65 GLY CA C 46.1 0.2 1 210 65 65 GLY N N 103.8 0.2 1 211 66 66 GLN C C 172.4 0.2 1 212 66 66 GLN CA C 53.0 0.2 1 213 66 66 GLN CB C 29.9 0.2 1 214 66 66 GLN CD C 179.3 0.2 1 215 66 66 GLN N N 117.9 0.2 1 216 67 67 ILE C C 176.5 0.2 1 217 67 67 ILE CA C 59.2 0.2 1 218 67 67 ILE CB C 36.2 0.2 1 219 67 67 ILE CD1 C 10.1 0.2 1 220 67 67 ILE CG1 C 26.2 0.2 1 221 67 67 ILE CG2 C 18.3 0.2 1 222 67 67 ILE N N 119.1 0.2 1 223 68 68 ALA C C 177.3 0.2 1 224 68 68 ALA CA C 51.0 0.2 1 225 68 68 ALA CB C 17.7 0.2 1 226 68 68 ALA N N 134.2 0.2 1 227 69 69 HIS C C 176.2 0.2 1 228 69 69 HIS CA C 55.3 0.2 1 229 69 69 HIS CB C 25.3 0.2 1 230 69 69 HIS CG C 128.8 0.2 1 231 69 69 HIS N N 129.4 0.2 1 232 70 70 TYR C C 177.4 0.2 1 233 70 70 TYR CA C 60.0 0.2 1 234 70 70 TYR CB C 37.0 0.2 1 235 70 70 TYR N N 121.5 0.2 1 236 71 71 ALA C C 178.8 0.2 1 237 71 71 ALA CA C 55.3 0.2 1 238 71 71 ALA CB C 17.3 0.2 1 239 71 71 ALA N N 124.8 0.2 1 240 72 72 ARG C C 176.0 0.2 1 241 72 72 ARG CA C 59.5 0.2 1 242 72 72 ARG CB C 28.8 0.2 1 243 72 72 ARG CD C 43.9 0.2 1 244 72 72 ARG CG C 27.7 0.2 1 245 72 72 ARG CZ C 159.5 0.2 1 246 72 72 ARG N N 113.9 0.2 1 247 72 72 ARG NE N 83.3 0.2 1 248 72 72 ARG NH1 N 77.3 0.2 2 249 72 72 ARG NH2 N 69.7 0.2 2 250 73 73 TYR C C 177.3 0.2 1 251 73 73 TYR CA C 59.8 0.2 1 252 73 73 TYR CB C 37.9 0.2 1 253 73 73 TYR CG C 128.6 0.2 1 254 73 73 TYR CZ C 158.1 0.2 1 255 73 73 TYR N N 112.6 0.2 1 256 74 74 ILE C C 177.1 0.2 1 257 74 74 ILE CA C 66.0 0.2 1 258 74 74 ILE CB C 37.7 0.2 1 259 74 74 ILE CD1 C 14.6 0.2 1 260 74 74 ILE CG1 C 29.4 0.2 1 261 74 74 ILE CG2 C 17.6 0.2 1 262 74 74 ILE N N 119.8 0.2 1 263 75 75 ASP C C 178.3 0.2 1 264 75 75 ASP CA C 56.1 0.2 1 265 75 75 ASP CB C 40.9 0.2 1 266 75 75 ASP CG C 178.7 0.2 1 267 75 75 ASP N N 116.1 0.2 1 268 76 76 TRP C C 179.6 0.2 1 269 76 76 TRP CA C 56.6 0.2 1 270 76 76 TRP CB C 30.1 0.2 1 271 76 76 TRP CD1 C 124.5 0.2 2 272 76 76 TRP CE2 C 139.2 0.2 1 273 76 76 TRP CG C 113.7 0.2 1 274 76 76 TRP N N 114.7 0.2 1 275 76 76 TRP NE1 N 128.1 0.2 1 276 77 77 MET C C 172.8 0.2 1 277 77 77 MET CA C 58.1 0.2 1 278 77 77 MET CB C 32.4 0.2 1 279 77 77 MET CG C 31.6 0.2 1 280 77 77 MET N N 125.4 0.2 1 281 78 78 VAL C C 178.7 0.2 1 282 78 78 VAL CA C 63.4 0.2 1 283 78 78 VAL CB C 34.5 0.2 1 284 78 78 VAL CG1 C 22.4 0.2 2 285 78 78 VAL CG2 C 21.2 0.2 2 286 78 78 VAL N N 109.6 0.2 1 287 79 79 THR C C 177.6 0.2 1 288 79 79 THR CA C 66.1 0.2 1 289 79 79 THR CB C 70.5 0.2 1 290 79 79 THR CG2 C 24.5 0.2 1 291 79 79 THR N N 107.3 0.2 1 292 80 80 THR C C 176.6 0.2 1 293 80 80 THR CA C 67.0 0.2 1 294 80 80 THR CB C 68.1 0.2 1 295 80 80 THR CG2 C 23.7 0.2 1 296 80 80 THR N N 112.7 0.2 1 297 81 81 PRO C C 178.9 0.2 1 298 81 81 PRO CA C 66.9 0.2 1 299 81 81 PRO CB C 31.9 0.2 1 300 81 81 PRO CD C 51.0 0.2 1 301 81 81 PRO CG C 29.0 0.2 1 302 81 81 PRO N N 137.6 0.2 1 303 82 82 LEU C C 177.7 0.2 1 304 82 82 LEU CA C 57.8 0.2 1 305 82 82 LEU CB C 41.1 0.2 1 306 82 82 LEU CD1 C 26.4 0.2 2 307 82 82 LEU CD2 C 22.3 0.2 2 308 82 82 LEU CG C 27.2 0.2 1 309 82 82 LEU N N 113.6 0.2 1 310 83 83 LEU C C 179.4 0.2 1 311 83 83 LEU CA C 58.2 0.2 1 312 83 83 LEU CB C 43.2 0.2 1 313 83 83 LEU CD1 C 27.6 0.2 2 314 83 83 LEU CD2 C 24.4 0.2 2 315 83 83 LEU CG C 27.9 0.2 1 316 83 83 LEU N N 120.8 0.2 1 317 84 84 LEU C C 179.4 0.2 1 318 84 84 LEU CA C 57.9 0.2 1 319 84 84 LEU CB C 41.9 0.2 1 320 84 84 LEU CD2 C 24.0 0.2 2 321 84 84 LEU CG C 27.8 0.2 1 322 84 84 LEU N N 118.4 0.2 1 323 85 85 LEU C C 176.9 0.2 1 324 85 85 LEU CA C 58.2 0.2 1 325 85 85 LEU CB C 40.5 0.2 1 326 85 85 LEU CD2 C 24.9 0.2 2 327 85 85 LEU CG C 27.5 0.2 1 328 85 85 LEU N N 126.9 0.2 1 329 86 86 SER C C 178.5 0.2 1 330 86 86 SER CA C 64.4 0.2 1 331 86 86 SER CB C 63.6 0.2 1 332 86 86 SER N N 116.1 0.2 1 333 87 87 LEU C C 178.4 0.2 1 334 87 87 LEU CA C 58.1 0.2 1 335 87 87 LEU CB C 42.0 0.2 1 336 87 87 LEU CD1 C 24.7 0.2 2 337 87 87 LEU CD2 C 22.5 0.2 2 338 87 87 LEU CG C 26.4 0.2 1 339 87 87 LEU N N 122.0 0.2 1 340 88 88 SER C C 176.5 0.2 1 341 88 88 SER CA C 62.9 0.2 1 342 88 88 SER N N 117.0 0.2 1 343 89 89 TRP C C 180.0 0.2 1 344 89 89 TRP CA C 58.6 0.2 1 345 89 89 TRP CB C 28.3 0.2 1 346 89 89 TRP CG C 115.6 0.2 1 347 89 89 TRP N N 122.8 0.2 1 348 90 90 THR C C 175.3 0.2 1 349 90 90 THR CA C 69.2 0.2 1 350 90 90 THR CB C 66.7 0.2 1 351 90 90 THR CG2 C 21.7 0.2 1 352 90 90 THR N N 118.8 0.2 1 353 91 91 ALA C C 177.3 0.2 1 354 91 91 ALA CA C 54.2 0.2 1 355 91 91 ALA CB C 18.9 0.2 1 356 91 91 ALA N N 120.2 0.2 1 357 92 92 MET C C 176.8 0.2 1 358 92 92 MET CA C 53.4 0.2 1 359 92 92 MET CB C 34.2 0.2 1 360 92 92 MET CG C 33.2 0.2 1 361 92 92 MET N N 108.9 0.2 1 362 102 102 ILE C C 177.8 0.2 1 363 102 102 ILE CA C 66.5 0.2 1 364 102 102 ILE CB C 38.3 0.2 1 365 102 102 ILE CG1 C 29.6 0.2 1 366 102 102 ILE CG2 C 19.2 0.2 1 367 102 102 ILE N N 117.1 0.2 1 368 103 103 GLY C C 176.3 0.2 1 369 103 103 GLY CA C 47.6 0.2 1 370 103 103 GLY N N 107.5 0.2 1 371 104 104 PHE CA C 59.7 0.2 1 372 104 104 PHE N N 125.3 0.2 1 373 106 106 MET C C 177.3 0.2 1 374 106 106 MET CA C 61.3 0.2 1 375 106 106 MET CB C 35.2 0.2 1 376 106 106 MET CG C 31.6 0.2 1 377 106 106 MET N N 113.9 0.2 1 378 107 107 SER C C 176.7 0.2 1 379 107 107 SER CA C 62.4 0.2 1 380 107 107 SER N N 111.8 0.2 1 381 108 108 THR C C 177.0 0.2 1 382 108 108 THR CA C 68.4 0.2 1 383 108 108 THR CB C 67.6 0.2 1 384 108 108 THR CG2 C 23.1 0.2 1 385 108 108 THR N N 121.1 0.2 1 386 109 109 GLN C C 178.4 0.2 1 387 109 109 GLN CA C 57.3 0.2 1 388 109 109 GLN CB C 26.7 0.2 1 389 109 109 GLN CD C 175.0 0.2 1 390 109 109 GLN CG C 31.3 0.2 1 391 109 109 GLN N N 122.0 0.2 1 392 109 109 GLN NE2 N 98.3 0.2 1 393 110 110 ILE C C 180.4 0.2 1 394 110 110 ILE CA C 64.1 0.2 1 395 110 110 ILE CB C 36.6 0.2 1 396 110 110 ILE CG1 C 28.9 0.2 1 397 110 110 ILE CG2 C 17.5 0.2 1 398 110 110 ILE N N 120.2 0.2 1 399 111 111 VAL C C 178.5 0.2 1 400 111 111 VAL CA C 67.8 0.2 1 401 111 111 VAL CB C 30.9 0.2 1 402 111 111 VAL CG1 C 22.7 0.2 2 403 111 111 VAL CG2 C 21.4 0.2 2 404 111 111 VAL N N 123.4 0.2 1 405 112 112 VAL C C 177.1 0.2 1 406 112 112 VAL CA C 67.5 0.2 1 407 112 112 VAL CB C 31.8 0.2 1 408 112 112 VAL CG1 C 22.1 0.2 2 409 112 112 VAL CG2 C 21.8 0.2 2 410 112 112 VAL N N 121.5 0.2 1 411 113 113 ILE C C 178.3 0.2 1 412 113 113 ILE CA C 61.6 0.2 1 413 113 113 ILE CB C 34.7 0.2 1 414 113 113 ILE CD1 C 8.9 0.2 1 415 113 113 ILE CG1 C 25.6 0.2 1 416 113 113 ILE CG2 C 20.7 0.2 1 417 113 113 ILE N N 113.3 0.2 1 418 114 114 THR C C 175.9 0.2 1 419 114 114 THR CA C 68.8 0.2 1 420 114 114 THR CB C 68.0 0.2 1 421 114 114 THR CG2 C 22.2 0.2 1 422 114 114 THR N N 118.1 0.2 1 423 115 115 SER C C 175.7 0.2 1 424 115 115 SER CA C 63.9 0.2 1 425 115 115 SER CB C 62.4 0.2 1 426 115 115 SER N N 116.4 0.2 1 427 116 116 GLY C C 173.1 0.2 1 428 116 116 GLY CA C 47.8 0.2 1 429 116 116 GLY N N 106.7 0.2 1 430 117 117 LEU C C 176.7 0.2 1 431 117 117 LEU CA C 57.4 0.2 1 432 117 117 LEU CB C 41.0 0.2 1 433 117 117 LEU CD1 C 26.4 0.2 2 434 117 117 LEU CD2 C 23.2 0.2 2 435 117 117 LEU CG C 27.5 0.2 1 436 117 117 LEU N N 123.2 0.2 1 437 118 118 ILE C C 180.1 0.2 1 438 118 118 ILE CA C 65.3 0.2 1 439 118 118 ILE CB C 36.9 0.2 1 440 118 118 ILE CD1 C 15.0 0.2 1 441 118 118 ILE CG1 C 27.6 0.2 1 442 118 118 ILE CG2 C 19.5 0.2 1 443 118 118 ILE N N 116.5 0.2 1 444 119 119 ALA C C 179.4 0.2 1 445 119 119 ALA CA C 56.1 0.2 1 446 119 119 ALA CB C 19.6 0.2 1 447 119 119 ALA N N 122.8 0.2 1 448 120 120 ASP C C 179.0 0.2 1 449 120 120 ASP CA C 54.1 0.2 1 450 120 120 ASP CB C 40.7 0.2 1 451 120 120 ASP CG C 181.1 0.2 1 452 120 120 ASP N N 112.9 0.2 1 453 121 121 LEU C C 176.6 0.2 1 454 121 121 LEU CA C 54.4 0.2 1 455 121 121 LEU CB C 43.1 0.2 1 456 121 121 LEU CD1 C 25.5 0.2 2 457 121 121 LEU CD2 C 21.8 0.2 2 458 121 121 LEU CG C 25.8 0.2 1 459 121 121 LEU N N 115.2 0.2 1 460 122 122 SER C C 174.3 0.2 1 461 122 122 SER CA C 61.7 0.2 1 462 122 122 SER CB C 63.8 0.2 1 463 122 122 SER N N 115.2 0.2 1 464 123 123 GLU CA C 55.4 0.2 1 465 123 123 GLU N N 122.3 0.2 1 466 126 126 TRP C C 176.3 0.2 1 467 126 126 TRP CA C 60.0 0.2 1 468 126 126 TRP CB C 27.4 0.2 1 469 126 126 TRP CG C 111.6 0.2 1 470 126 126 TRP N N 115.8 0.2 1 471 127 127 VAL C C 176.9 0.2 1 472 127 127 VAL CA C 65.8 0.2 1 473 127 127 VAL CB C 31.7 0.2 1 474 127 127 VAL CG1 C 22.6 0.2 2 475 127 127 VAL CG2 C 20.4 0.2 2 476 127 127 VAL N N 122.2 0.2 1 477 128 128 ARG C C 178.8 0.2 1 478 128 128 ARG CA C 60.4 0.2 1 479 128 128 ARG CB C 30.7 0.2 1 480 128 128 ARG N N 119.7 0.2 1 481 130 130 LEU C C 178.5 0.2 1 482 130 130 LEU CA C 59.4 0.2 1 483 130 130 LEU CB C 42.3 0.2 1 484 130 130 LEU CD1 C 27.5 0.2 2 485 130 130 LEU CD2 C 25.9 0.2 2 486 130 130 LEU CG C 27.7 0.2 1 487 130 130 LEU N N 123.1 0.2 1 488 131 131 TRP C C 178.9 0.2 1 489 131 131 TRP CA C 61.4 0.2 1 490 131 131 TRP CB C 29.5 0.2 1 491 131 131 TRP CD1 C 129.0 0.2 2 492 131 131 TRP CG C 111.6 0.2 1 493 131 131 TRP N N 119.5 0.2 1 494 132 132 TYR C C 176.7 0.2 1 495 132 132 TYR CA C 62.4 0.2 1 496 132 132 TYR CB C 38.4 0.2 1 497 132 132 TYR CG C 129.1 0.2 1 498 132 132 TYR CZ C 158.3 0.2 1 499 132 132 TYR N N 119.6 0.2 1 500 133 133 ILE C C 178.5 0.2 1 501 133 133 ILE CA C 65.5 0.2 1 502 133 133 ILE CB C 37.3 0.2 1 503 133 133 ILE N N 119.8 0.2 1 504 134 134 CYS C C 176.9 0.2 1 505 134 134 CYS CA C 65.8 0.2 1 506 134 134 CYS CB C 25.9 0.2 1 507 134 134 CYS N N 121.5 0.2 1 508 135 135 GLY C C 176.1 0.2 1 509 135 135 GLY CA C 48.3 0.2 1 510 135 135 GLY N N 105.7 0.2 1 511 136 136 VAL C C 177.6 0.2 1 512 136 136 VAL CA C 67.6 0.2 1 513 136 136 VAL CB C 31.3 0.2 1 514 136 136 VAL CG1 C 24.4 0.2 2 515 136 136 VAL CG2 C 22.1 0.2 2 516 136 136 VAL N N 123.6 0.2 1 517 137 137 CYS C C 176.2 0.2 1 518 137 137 CYS CA C 65.8 0.2 1 519 137 137 CYS CB C 26.8 0.2 1 520 137 137 CYS N N 118.6 0.2 1 521 138 138 ALA C C 177.9 0.2 1 522 138 138 ALA CA C 55.3 0.2 1 523 138 138 ALA CB C 18.1 0.2 1 524 138 138 ALA N N 119.1 0.2 1 525 139 139 PHE C C 176.7 0.2 1 526 139 139 PHE CA C 59.5 0.2 1 527 139 139 PHE CB C 40.1 0.2 1 528 139 139 PHE N N 119.8 0.2 1 529 145 145 GLY C C 175.6 0.2 1 530 145 145 GLY CA C 47.0 0.2 1 531 145 145 GLY N N 108.4 0.2 1 532 146 146 ILE C C 178.4 0.2 1 533 146 146 ILE CA C 64.4 0.2 1 534 146 146 ILE CB C 35.6 0.2 1 535 146 146 ILE CD1 C 13.3 0.2 1 536 146 146 ILE CG1 C 24.2 0.2 1 537 146 146 ILE CG2 C 16.9 0.2 1 538 146 146 ILE N N 114.7 0.2 1 539 147 147 TRP C C 175.5 0.2 1 540 147 147 TRP CA C 60.0 0.2 1 541 147 147 TRP CB C 30.0 0.2 1 542 147 147 TRP CD1 C 127.1 0.2 2 543 147 147 TRP CG C 114.2 0.2 1 544 147 147 TRP N N 120.8 0.2 1 545 148 148 ASN C C 172.0 0.2 1 546 148 148 ASN CA C 55.1 0.2 1 547 148 148 ASN CB C 39.1 0.2 1 548 148 148 ASN CG C 176.7 0.2 1 549 148 148 ASN N N 116.9 0.2 1 550 156 156 THR C C 174.9 0.2 1 551 156 156 THR CA C 61.8 0.2 1 552 156 156 THR CB C 69.3 0.2 1 553 156 156 THR N N 104.7 0.2 1 554 157 157 GLN C C 173.3 0.2 1 555 157 157 GLN CA C 55.0 0.2 1 556 157 157 GLN N N 120.5 0.2 1 557 158 158 SER C C 174.8 0.2 1 558 158 158 SER CA C 57.8 0.2 1 559 158 158 SER CB C 65.3 0.2 1 560 158 158 SER N N 113.0 0.2 1 561 159 159 SER C C 176.7 0.2 1 562 159 159 SER CA C 61.8 0.2 1 563 159 159 SER CB C 62.7 0.2 1 564 159 159 SER N N 118.2 0.2 1 565 160 160 GLU C C 179.6 0.2 1 566 160 160 GLU CA C 60.3 0.2 1 567 160 160 GLU CB C 29.4 0.2 1 568 160 160 GLU N N 119.5 0.2 1 569 161 161 LEU C C 178.9 0.2 1 570 161 161 LEU CA C 56.8 0.2 1 571 161 161 LEU CB C 41.0 0.2 1 572 161 161 LEU CD1 C 22.8 0.2 2 573 161 161 LEU CG C 28.1 0.2 1 574 161 161 LEU N N 124.9 0.2 1 575 162 162 ALA C C 179.9 0.2 1 576 162 162 ALA CA C 56.2 0.2 1 577 162 162 ALA CB C 18.0 0.2 1 578 162 162 ALA N N 123.1 0.2 1 579 163 163 ASN C C 178.1 0.2 1 580 163 163 ASN CA C 55.9 0.2 1 581 163 163 ASN CB C 38.3 0.2 1 582 163 163 ASN CG C 176.2 0.2 1 583 163 163 ASN N N 115.7 0.2 1 584 164 164 LEU C C 178.0 0.2 1 585 164 164 LEU CA C 58.3 0.2 1 586 164 164 LEU CB C 41.0 0.2 1 587 164 164 LEU CD1 C 26.1 0.2 2 588 164 164 LEU CD2 C 22.8 0.2 2 589 164 164 LEU CG C 27.5 0.2 1 590 164 164 LEU N N 123.5 0.2 1 591 165 165 TYR C C 176.1 0.2 1 592 165 165 TYR CA C 63.7 0.2 1 593 165 165 TYR CB C 38.7 0.2 1 594 165 165 TYR N N 118.9 0.2 1 595 166 166 ASP C C 179.4 0.2 1 596 166 166 ASP CA C 56.9 0.2 1 597 166 166 ASP CB C 39.8 0.2 1 598 166 166 ASP CG C 180.1 0.2 1 599 166 166 ASP N N 118.9 0.2 1 600 167 167 LYS C C 178.4 0.2 1 601 167 167 LYS CA C 60.0 0.2 1 602 167 167 LYS CB C 32.4 0.2 1 603 167 167 LYS N N 123.2 0.2 1 604 169 169 VAL C C 178.8 0.2 1 605 169 169 VAL CA C 64.7 0.2 1 606 169 169 VAL CB C 30.1 0.2 1 607 169 169 VAL CG1 C 22.9 0.2 2 608 169 169 VAL CG2 C 19.1 0.2 2 609 169 169 VAL N N 119.8 0.2 1 610 170 170 THR C C 174.4 0.2 1 611 170 170 THR CA C 69.5 0.2 1 612 170 170 THR CB C 68.0 0.2 1 613 170 170 THR CG2 C 21.7 0.2 1 614 170 170 THR N N 125.1 0.2 1 615 171 171 TYR C C 175.4 0.2 1 616 171 171 TYR CA C 62.8 0.2 1 617 171 171 TYR N N 123.1 0.2 1 618 172 172 PHE C C 176.8 0.2 1 619 172 172 PHE CA C 60.7 0.2 1 620 172 172 PHE CB C 41.9 0.2 1 621 172 172 PHE N N 118.1 0.2 1 622 173 173 THR C C 174.9 0.2 1 623 173 173 THR CA C 69.1 0.2 1 624 173 173 THR CG2 C 21.5 0.2 1 625 173 173 THR N N 113.1 0.2 1 626 174 174 VAL C C 175.8 0.2 1 627 174 174 VAL CA C 67.4 0.2 1 628 174 174 VAL CB C 31.8 0.2 1 629 174 174 VAL CG1 C 23.3 0.2 2 630 174 174 VAL CG2 C 22.0 0.2 2 631 174 174 VAL N N 117.8 0.2 1 632 175 175 LEU C C 179.9 0.2 1 633 175 175 LEU CA C 57.5 0.2 1 634 175 175 LEU CB C 41.8 0.2 1 635 175 175 LEU CD1 C 26.7 0.2 2 636 175 175 LEU CD2 C 23.5 0.2 2 637 175 175 LEU CG C 27.8 0.2 1 638 175 175 LEU N N 112.8 0.2 1 639 176 176 TRP C C 179.6 0.2 1 640 176 176 TRP CA C 62.6 0.2 1 641 176 176 TRP CB C 27.1 0.2 1 642 176 176 TRP N N 117.7 0.2 1 643 177 177 ILE C C 175.7 0.2 1 644 177 177 ILE CA C 65.5 0.2 1 645 177 177 ILE CB C 38.2 0.2 1 646 177 177 ILE CG2 C 18.0 0.2 1 647 177 177 ILE N N 118.2 0.2 1 648 178 178 GLY C C 174.8 0.2 1 649 178 178 GLY CA C 47.6 0.2 1 650 178 178 GLY N N 102.1 0.2 1 651 179 179 TYR C C 175.2 0.2 1 652 179 179 TYR CA C 63.5 0.2 1 653 179 179 TYR CB C 35.4 0.2 1 654 179 179 TYR N N 115.7 0.2 1 655 180 180 PRO C C 180.0 0.2 1 656 180 180 PRO CA C 65.1 0.2 1 657 180 180 PRO CB C 29.0 0.2 1 658 180 180 PRO CD C 49.7 0.2 1 659 180 180 PRO CG C 27.7 0.2 1 660 180 180 PRO N N 132.2 0.2 1 661 181 181 ILE C C 175.4 0.2 1 662 181 181 ILE CA C 65.5 0.2 1 663 181 181 ILE CB C 37.6 0.2 1 664 181 181 ILE CD1 C 13.8 0.2 1 665 181 181 ILE CG1 C 28.7 0.2 1 666 181 181 ILE CG2 C 17.0 0.2 1 667 181 181 ILE N N 121.4 0.2 1 668 182 182 VAL C C 177.3 0.2 1 669 182 182 VAL CA C 67.1 0.2 1 670 182 182 VAL CB C 30.7 0.2 1 671 182 182 VAL CG1 C 24.2 0.2 2 672 182 182 VAL CG2 C 23.2 0.2 2 673 182 182 VAL N N 118.8 0.2 1 674 183 183 TRP C C 179.0 0.2 1 675 183 183 TRP CA C 62.8 0.2 1 676 183 183 TRP CB C 32.5 0.2 1 677 183 183 TRP CD1 C 127.6 0.2 2 678 183 183 TRP CD2 C 129.1 0.2 2 679 183 183 TRP CG C 112.2 0.2 1 680 183 183 TRP N N 116.5 0.2 1 681 184 184 ILE C C 175.0 0.2 1 682 184 184 ILE CA C 60.7 0.2 1 683 184 184 ILE CB C 39.6 0.2 1 684 184 184 ILE N N 113.1 0.2 1 685 185 185 ILE C C 176.5 0.2 1 686 185 185 ILE CA C 63.0 0.2 1 687 185 185 ILE CB C 38.7 0.2 1 688 185 185 ILE CD1 C 14.7 0.2 1 689 185 185 ILE CG2 C 18.0 0.2 1 690 185 185 ILE N N 112.8 0.2 1 691 186 186 GLY C C 173.8 0.2 1 692 186 186 GLY CA C 45.2 0.2 1 693 186 186 GLY N N 109.8 0.2 1 694 187 187 PRO C C 176.9 0.2 1 695 187 187 PRO CA C 64.9 0.2 1 696 187 187 PRO CB C 33.1 0.2 1 697 187 187 PRO CD C 49.8 0.2 1 698 187 187 PRO CG C 27.3 0.2 1 699 187 187 PRO N N 133.4 0.2 1 700 188 188 SER C C 172.6 0.2 1 701 188 188 SER CA C 61.8 0.2 1 702 188 188 SER CB C 60.7 0.2 1 703 188 188 SER N N 109.1 0.2 1 704 189 189 GLY C C 173.9 0.2 1 705 189 189 GLY CA C 44.2 0.2 1 706 189 189 GLY N N 109.0 0.2 1 707 190 190 PHE C C 177.2 0.2 1 708 190 190 PHE CA C 56.5 0.2 1 709 190 190 PHE N N 125.3 0.2 1 710 191 191 GLY C C 174.7 0.2 1 711 191 191 GLY CA C 46.7 0.2 1 712 191 191 GLY N N 105.6 0.2 1 713 192 192 TRP C C 177.1 0.2 1 714 192 192 TRP CA C 57.5 0.2 1 715 192 192 TRP CB C 29.0 0.2 1 716 192 192 TRP N N 121.0 0.2 1 717 193 193 ILE C C 175.1 0.2 1 718 193 193 ILE CA C 58.6 0.2 1 719 193 193 ILE CB C 40.2 0.2 1 720 193 193 ILE CD1 C 13.2 0.2 1 721 193 193 ILE CG1 C 27.2 0.2 1 722 193 193 ILE CG2 C 18.5 0.2 1 723 193 193 ILE N N 106.5 0.2 1 724 194 194 ASN C C 175.7 0.2 1 725 194 194 ASN CA C 51.4 0.2 1 726 194 194 ASN CB C 39.3 0.2 1 727 194 194 ASN N N 118.5 0.2 1 728 195 195 GLN C C 176.8 0.2 1 729 195 195 GLN CA C 57.7 0.2 1 730 195 195 GLN CB C 29.3 0.2 1 731 195 195 GLN CD C 180.7 0.2 1 732 195 195 GLN CG C 34.4 0.2 1 733 195 195 GLN N N 116.2 0.2 1 734 196 196 THR C C 175.9 0.2 1 735 196 196 THR CA C 67.8 0.2 1 736 196 196 THR CG2 C 23.3 0.2 1 737 196 196 THR N N 117.7 0.2 1 738 197 197 ILE C C 177.5 0.2 1 739 197 197 ILE CA C 63.6 0.2 1 740 197 197 ILE CB C 37.2 0.2 1 741 197 197 ILE CG1 C 27.4 0.2 1 742 197 197 ILE CG2 C 18.8 0.2 1 743 197 197 ILE N N 119.6 0.2 1 744 198 198 ASP C C 177.0 0.2 1 745 198 198 ASP CA C 59.0 0.2 1 746 198 198 ASP CB C 44.0 0.2 1 747 198 198 ASP CG C 177.8 0.2 1 748 198 198 ASP N N 123.5 0.2 1 749 199 199 THR C C 175.8 0.2 1 750 199 199 THR CA C 68.1 0.2 1 751 199 199 THR CG2 C 23.6 0.2 1 752 199 199 THR N N 116.6 0.2 1 753 200 200 PHE C C 178.4 0.2 1 754 200 200 PHE CA C 62.1 0.2 1 755 200 200 PHE CB C 39.1 0.2 1 756 200 200 PHE N N 120.3 0.2 1 757 201 201 LEU C C 178.5 0.2 1 758 201 201 LEU CA C 58.4 0.2 1 759 201 201 LEU CB C 41.9 0.2 1 760 201 201 LEU CD1 C 26.9 0.2 2 761 201 201 LEU CD2 C 22.6 0.2 2 762 201 201 LEU CG C 27.4 0.2 1 763 201 201 LEU N N 120.4 0.2 1 764 202 202 PHE C C 174.6 0.2 1 765 202 202 PHE CA C 60.9 0.2 1 766 202 202 PHE CB C 35.8 0.2 1 767 202 202 PHE CE1 C 131.1 0.2 3 768 202 202 PHE CG C 140.4 0.2 1 769 202 202 PHE N N 115.3 0.2 1 770 203 203 CYS C C 175.3 0.2 1 771 203 203 CYS CA C 62.7 0.2 1 772 203 203 CYS CB C 28.7 0.2 1 773 203 203 CYS N N 117.7 0.2 1 774 204 204 LEU C C 178.4 0.2 1 775 204 204 LEU CA C 59.1 0.2 1 776 204 204 LEU CB C 43.9 0.2 1 777 204 204 LEU CD1 C 25.9 0.2 2 778 204 204 LEU CD2 C 25.1 0.2 2 779 204 204 LEU CG C 27.0 0.2 1 780 204 204 LEU N N 121.6 0.2 1 781 205 205 LEU C C 180.0 0.2 1 782 205 205 LEU CA C 60.0 0.2 1 783 205 205 LEU CB C 38.2 0.2 1 784 205 205 LEU CD1 C 24.0 0.2 2 785 205 205 LEU CD2 C 22.5 0.2 2 786 205 205 LEU CG C 27.6 0.2 1 787 205 205 LEU N N 115.0 0.2 1 788 206 206 PRO C C 177.4 0.2 1 789 206 206 PRO CA C 66.6 0.2 1 790 206 206 PRO CB C 29.5 0.2 1 791 206 206 PRO CD C 51.2 0.2 1 792 206 206 PRO CG C 28.6 0.2 1 793 206 206 PRO N N 139.3 0.2 1 794 207 207 PHE N N 121.6 0.2 1 795 209 209 SER C C 171.3 0.2 1 796 209 209 SER CA C 60.7 0.2 1 797 209 209 SER CB C 63.5 0.2 1 798 209 209 SER N N 115.5 0.2 1 799 210 210 LYS C C 173.0 0.2 1 800 210 210 LYS CA C 57.3 0.2 1 801 210 210 LYS CB C 33.3 0.2 1 802 210 210 LYS CD C 30.3 0.2 1 803 210 210 LYS CE C 55.7 0.2 1 804 210 210 LYS CG C 29.4 0.2 1 805 210 210 LYS N N 117.5 0.2 1 806 210 210 LYS NZ N 177.2 0.2 1 807 211 211 VAL C C 177.8 0.2 1 808 211 211 VAL CA C 65.6 0.2 1 809 211 211 VAL CB C 31.7 0.2 1 810 211 211 VAL CG1 C 23.6 0.2 2 811 211 211 VAL CG2 C 22.1 0.2 2 812 211 211 VAL N N 116.9 0.2 1 813 212 212 GLY C C 173.3 0.2 1 814 212 212 GLY CA C 48.3 0.2 1 815 212 212 GLY N N 101.7 0.2 1 816 213 213 PHE C C 175.6 0.2 1 817 213 213 PHE CA C 62.1 0.2 1 818 213 213 PHE CB C 40.5 0.2 1 819 213 213 PHE N N 119.9 0.2 1 820 214 214 SER C C 175.2 0.2 1 821 214 214 SER CA C 62.9 0.2 1 822 214 214 SER N N 116.4 0.2 1 823 216 216 LEU C C 179.9 0.2 1 824 216 216 LEU CA C 57.8 0.2 1 825 216 216 LEU CB C 42.5 0.2 1 826 216 216 LEU CD2 C 22.9 0.2 2 827 216 216 LEU CG C 26.1 0.2 1 828 216 216 LEU N N 119.1 0.2 1 829 217 217 ASP C C 177.1 0.2 1 830 217 217 ASP CA C 57.9 0.2 1 831 217 217 ASP CB C 42.2 0.2 1 832 217 217 ASP CG C 176.1 0.2 1 833 217 217 ASP N N 121.0 0.2 1 834 218 218 LEU C C 180.8 0.2 1 835 218 218 LEU CA C 58.0 0.2 1 836 218 218 LEU CB C 42.0 0.2 1 837 218 218 LEU CD2 C 21.6 0.2 2 838 218 218 LEU CG C 26.1 0.2 1 839 218 218 LEU N N 114.8 0.2 1 840 219 219 HIS C C 178.4 0.2 1 841 219 219 HIS CA C 61.4 0.2 1 842 219 219 HIS N N 114.1 0.2 1 843 220 220 GLY C C 176.6 0.2 1 844 220 220 GLY CA C 47.5 0.2 1 845 220 220 GLY N N 109.5 0.2 1 stop_ save_