data_50267 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C backbone assignments of GTP-bound Rab4a ; _BMRB_accession_number 50267 _BMRB_flat_file_name bmr50267.str _Entry_type original _Submission_date 2020-05-08 _Accession_date 2020-05-08 _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 Genier Samuel . . 2 Letourneau Danny . . 3 Parent Jean-Luc . . 4 Lavigne Pierre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 145 "13C chemical shifts" 362 "15N chemical shifts" 145 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-10-01 update BMRB 'update entry citation' 2020-05-13 original author 'original release' stop_ _Original_release_date 2020-05-08 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; In-depth NMR characterization of Rab4a structure, nucleotide exchange and hydrolysis kinetics revealed an atypical GTPase profile. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32707235 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Genier Samuel . . 2 Letourneau Danny . . 3 Gauthier Esther . . 4 Picard Samuel . . 5 Boisvert Marilou . . 6 Parent Jean-Luc L. . 7 Lavigne Pierre . . stop_ _Journal_abbreviation 'J. Struct. Biol.' _Journal_name_full 'Journal of structural biology' _Journal_volume 212 _Journal_issue 1 _Journal_ISSN 1095-8657 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 107582 _Page_last 107582 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name Rab4a _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Rab4a $entity_1 GSP $entity_GSP MG $entity_MG 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 178 _Mol_residue_sequence ; MSETYDFLFKFLVIGNAGTG KSCLLHQFIEKKFKDDSNHT IGVEFGSKIINVGGKYVKLQ IWDTAGQERFRSVTRSYYRG AAGALLVYDITSRETYNALT NWLTDARMLASQNIVIILCG NKKDLDADREVTFLEASRFA QENELMFLETSALTGEDVEE AFVQCARKILNKHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLU 4 THR 5 TYR 6 ASP 7 PHE 8 LEU 9 PHE 10 LYS 11 PHE 12 LEU 13 VAL 14 ILE 15 GLY 16 ASN 17 ALA 18 GLY 19 THR 20 GLY 21 LYS 22 SER 23 CYS 24 LEU 25 LEU 26 HIS 27 GLN 28 PHE 29 ILE 30 GLU 31 LYS 32 LYS 33 PHE 34 LYS 35 ASP 36 ASP 37 SER 38 ASN 39 HIS 40 THR 41 ILE 42 GLY 43 VAL 44 GLU 45 PHE 46 GLY 47 SER 48 LYS 49 ILE 50 ILE 51 ASN 52 VAL 53 GLY 54 GLY 55 LYS 56 TYR 57 VAL 58 LYS 59 LEU 60 GLN 61 ILE 62 TRP 63 ASP 64 THR 65 ALA 66 GLY 67 GLN 68 GLU 69 ARG 70 PHE 71 ARG 72 SER 73 VAL 74 THR 75 ARG 76 SER 77 TYR 78 TYR 79 ARG 80 GLY 81 ALA 82 ALA 83 GLY 84 ALA 85 LEU 86 LEU 87 VAL 88 TYR 89 ASP 90 ILE 91 THR 92 SER 93 ARG 94 GLU 95 THR 96 TYR 97 ASN 98 ALA 99 LEU 100 THR 101 ASN 102 TRP 103 LEU 104 THR 105 ASP 106 ALA 107 ARG 108 MET 109 LEU 110 ALA 111 SER 112 GLN 113 ASN 114 ILE 115 VAL 116 ILE 117 ILE 118 LEU 119 CYS 120 GLY 121 ASN 122 LYS 123 LYS 124 ASP 125 LEU 126 ASP 127 ALA 128 ASP 129 ARG 130 GLU 131 VAL 132 THR 133 PHE 134 LEU 135 GLU 136 ALA 137 SER 138 ARG 139 PHE 140 ALA 141 GLN 142 GLU 143 ASN 144 GLU 145 LEU 146 MET 147 PHE 148 LEU 149 GLU 150 THR 151 SER 152 ALA 153 LEU 154 THR 155 GLY 156 GLU 157 ASP 158 VAL 159 GLU 160 GLU 161 ALA 162 PHE 163 VAL 164 GLN 165 CYS 166 ALA 167 ARG 168 LYS 169 ILE 170 LEU 171 ASN 172 LYS 173 HIS 174 HIS 175 HIS 176 HIS 177 HIS 178 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_GSP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_GSP (5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE)" _BMRB_code GSP _PDB_code GSP _Molecular_mass 539.246 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P . 0 . ? O3B O3B O . 0 . ? S1G S1G S . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? HOB2 HOB2 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 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 PG O3B ? ? DOUB PG S1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING O3B PB ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? DOUB C6 O6 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING N1 HN1 ? ? SING C2 N2 ? ? DOUB C2 N3 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_MG (MAGNESIUM ION)" _BMRB_code MG _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli C41 plasmid pet3a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name 'CcpNmr Analysis' _Version 2.4.2 loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name TOPSPIN _Version 3.6.2 loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name DANGLE _Version 1.1 loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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 $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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' 100 . mM pH 7.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251 water H 1 protons ppm 4.7 internal direct . . . 1 DSS N 15 'methyl protons' na 0.00 na indirect . . . 0.101329 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_3 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name Rab4a _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 3 3 GLU CA C 56.022 . 1 2 3 3 GLU CB C 30.959 . 1 3 3 3 GLU CG C 36.286 . 1 4 4 4 THR H H 7.977 0.002 1 5 4 4 THR CA C 61.299 0.0 1 6 4 4 THR CB C 69.952 0.051 1 7 4 4 THR CG2 C 21.242 . 1 8 4 4 THR N N 115.831 0.01 1 9 5 5 TYR H H 7.217 0.002 1 10 5 5 TYR CA C 56.034 0.023 1 11 5 5 TYR CB C 38.816 0.023 1 12 5 5 TYR N N 116.203 0.018 1 13 6 6 ASP H H 9.289 0.002 1 14 6 6 ASP CA C 56.309 0.006 1 15 6 6 ASP CB C 44.445 0.001 1 16 6 6 ASP N N 119.432 0.011 1 17 7 7 PHE H H 7.693 0.001 1 18 7 7 PHE CA C 56.409 0.128 1 19 7 7 PHE CB C 45.032 0.003 1 20 7 7 PHE N N 114.654 0.002 1 21 8 8 LEU H H 8.485 0.001 1 22 8 8 LEU CA C 53.768 0.02 1 23 8 8 LEU CB C 45.057 0.03 1 24 8 8 LEU N N 125.313 0.0 1 25 9 9 PHE H H 8.614 0.001 1 26 9 9 PHE CA C 53.155 0.004 1 27 9 9 PHE CB C 42.858 0.004 1 28 9 9 PHE N N 122.686 0.005 1 29 10 10 LYS H H 9.038 0.003 1 30 10 10 LYS CA C 56.180 . 1 31 10 10 LYS CB C 35.382 . 1 32 10 10 LYS N N 123.807 0.002 1 33 12 12 LEU CA C 62.542 . 1 34 12 12 LEU CB C 42.751 . 1 35 13 13 VAL CA C 62.563 . 1 36 13 13 VAL CB C 32.180 . 1 37 13 13 VAL CG2 C 22.172 . 1 38 14 14 ILE H H 8.079 0.001 1 39 14 14 ILE CA C 59.169 0.257 1 40 14 14 ILE CB C 39.917 0.114 1 41 14 14 ILE N N 126.427 0.001 1 42 15 15 GLY H H 8.062 0.002 1 43 15 15 GLY CA C 45.595 0.039 1 44 15 15 GLY N N 114.746 0.006 1 45 16 16 ASN H H 8.447 0.001 1 46 16 16 ASN CA C 51.962 0.0 1 47 16 16 ASN CB C 41.251 0.037 1 48 16 16 ASN N N 123.220 0.123 1 49 17 17 ALA H H 7.075 0.001 1 50 17 17 ALA CA C 53.232 0.02 1 51 17 17 ALA CB C 21.617 0.009 1 52 17 17 ALA N N 110.433 0.0 1 53 18 18 GLY H H 9.682 0.002 1 54 18 18 GLY CA C 46.146 0.505 1 55 18 18 GLY N N 112.410 0.014 1 56 19 19 THR H H 7.717 0.003 1 57 19 19 THR CA C 62.324 0.584 1 58 19 19 THR CB C 69.587 0.299 1 59 19 19 THR CG2 C 21.387 . 1 60 19 19 THR N N 110.949 0.011 1 61 20 20 GLY H H 8.400 0.002 1 62 20 20 GLY CA C 45.376 0.043 1 63 20 20 GLY N N 111.729 0.001 1 64 21 21 LYS H H 7.701 0.002 1 65 21 21 LYS CA C 57.369 . 1 66 21 21 LYS CB C 33.734 . 1 67 21 21 LYS N N 125.719 0.005 1 68 22 22 SER CA C 59.843 . 1 69 22 22 SER CB C 61.329 . 1 70 23 23 CYS H H 8.849 0.003 1 71 23 23 CYS CA C 64.538 0.019 1 72 23 23 CYS CB C 26.469 0.006 1 73 23 23 CYS N N 123.547 0.006 1 74 24 24 LEU H H 9.293 0.004 1 75 24 24 LEU CA C 59.407 . 1 76 24 24 LEU CB C 42.109 . 1 77 24 24 LEU N N 126.767 0.002 1 78 25 25 LEU CA C 58.442 . 1 79 25 25 LEU CB C 41.874 . 1 80 26 26 HIS H H 8.133 0.001 1 81 26 26 HIS CA C 60.263 0.018 1 82 26 26 HIS CB C 30.077 0.04 1 83 26 26 HIS N N 117.491 0.103 1 84 27 27 GLN H H 8.217 0.001 1 85 27 27 GLN CA C 58.508 0.015 1 86 27 27 GLN CB C 29.965 0.009 1 87 27 27 GLN N N 118.410 0.048 1 88 28 28 PHE H H 8.115 0.001 1 89 28 28 PHE CA C 58.826 . 1 90 28 28 PHE CB C 39.721 . 1 91 28 28 PHE N N 119.040 0.007 1 92 29 29 ILE CA C 63.546 . 1 93 29 29 ILE CB C 37.788 . 1 94 30 30 GLU H H 8.400 0.001 1 95 30 30 GLU CA C 55.681 . 1 96 30 30 GLU CB C 30.574 . 1 97 30 30 GLU N N 116.298 0.005 1 98 34 34 LYS CA C 55.397 . 1 99 34 34 LYS CB C 32.203 0.016 1 100 35 35 ASP H H 7.658 0.003 1 101 35 35 ASP CA C 55.100 0.051 1 102 35 35 ASP CB C 40.960 0.014 1 103 35 35 ASP N N 124.346 0.039 1 104 36 36 ASP H H 7.878 0.001 1 105 36 36 ASP CA C 52.568 0.007 1 106 36 36 ASP CB C 39.781 0.04 1 107 36 36 ASP N N 118.485 0.004 1 108 37 37 SER H H 7.401 0.002 1 109 37 37 SER CA C 58.468 0.031 1 110 37 37 SER CB C 63.477 0.004 1 111 37 37 SER N N 113.740 0.007 1 112 38 38 ASN H H 8.226 0.001 1 113 38 38 ASN CA C 51.609 . 1 114 38 38 ASN CB C 40.995 . 1 115 38 38 ASN N N 124.120 0.002 1 116 40 40 THR H H 7.714 . 1 117 40 40 THR CA C 61.935 . 1 118 40 40 THR CB C 69.752 . 1 119 40 40 THR CG2 C 21.529 . 1 120 40 40 THR N N 120.177 . 1 121 41 41 ILE H H 8.055 0.002 1 122 41 41 ILE CA C 61.319 0.002 1 123 41 41 ILE CB C 38.711 0.0 1 124 41 41 ILE CG1 C 27.213 . 1 125 41 41 ILE CG2 C 17.161 . 1 126 41 41 ILE CD1 C 12.843 . 1 127 41 41 ILE N N 123.150 0.018 1 128 42 42 GLY H H 8.378 0.003 1 129 42 42 GLY CA C 45.304 0.007 1 130 42 42 GLY N N 112.734 0.002 1 131 43 43 VAL H H 7.819 0.001 1 132 43 43 VAL CA C 62.228 0.019 1 133 43 43 VAL CB C 32.857 0.037 1 134 43 43 VAL CG1 C 20.380 . 1 135 43 43 VAL N N 118.934 0.003 1 136 44 44 GLU H H 8.462 0.001 1 137 44 44 GLU CA C 56.362 0.064 1 138 44 44 GLU CB C 30.165 0.103 1 139 44 44 GLU CG C 35.958 . 1 140 44 44 GLU N N 123.717 0.052 1 141 45 45 PHE H H 8.196 . 1 142 45 45 PHE CA C 58.136 0.025 1 143 45 45 PHE CB C 39.402 0.005 1 144 45 45 PHE N N 121.506 0.014 1 145 46 46 GLY H H 8.220 0.0 1 146 46 46 GLY CA C 45.268 0.144 1 147 46 46 GLY N N 110.574 0.014 1 148 47 47 SER H H 7.979 0.0 1 149 47 47 SER CA C 56.135 0.155 1 150 47 47 SER CB C 66.335 0.012 1 151 47 47 SER N N 112.135 0.0 1 152 48 48 LYS H H 7.794 0.001 1 153 48 48 LYS CA C 56.002 0.007 1 154 48 48 LYS CB C 37.421 0.009 1 155 48 48 LYS N N 121.635 0.003 1 156 49 49 ILE H H 8.343 0.001 1 157 49 49 ILE CA C 60.313 0.006 1 158 49 49 ILE CB C 38.497 0.006 1 159 49 49 ILE N N 125.216 0.002 1 160 50 50 ILE H H 8.917 0.001 1 161 50 50 ILE CA C 59.090 0.035 1 162 50 50 ILE CB C 41.339 0.016 1 163 50 50 ILE CG2 C 18.467 . 1 164 50 50 ILE N N 121.087 0.003 1 165 51 51 ASN H H 8.551 0.003 1 166 51 51 ASN CA C 51.638 0.003 1 167 51 51 ASN CB C 39.477 0.048 1 168 51 51 ASN N N 121.442 0.0 1 169 52 52 VAL H H 8.977 0.002 1 170 52 52 VAL CA C 60.677 . 1 171 52 52 VAL CB C 32.541 . 1 172 52 52 VAL N N 126.187 0.001 1 173 53 53 GLY CA C 46.921 0.008 1 174 54 54 GLY H H 8.114 0.004 1 175 54 54 GLY CA C 44.756 0.026 1 176 54 54 GLY N N 106.213 0.025 1 177 55 55 LYS H H 7.345 0.0 1 178 55 55 LYS CA C 52.837 0.015 1 179 55 55 LYS CB C 33.488 0.035 1 180 55 55 LYS N N 118.720 0.011 1 181 56 56 TYR H H 9.742 0.001 1 182 56 56 TYR CA C 58.202 0.001 1 183 56 56 TYR CB C 39.103 0.008 1 184 56 56 TYR N N 122.238 0.008 1 185 57 57 VAL H H 9.502 0.002 1 186 57 57 VAL CA C 60.356 0.021 1 187 57 57 VAL CB C 34.069 0.025 1 188 57 57 VAL CG2 C 22.649 . 1 189 57 57 VAL N N 127.171 0.006 1 190 58 58 LYS H H 9.040 0.005 1 191 58 58 LYS CA C 55.339 0.018 1 192 58 58 LYS CB C 33.277 0.142 1 193 58 58 LYS N N 128.298 0.001 1 194 59 59 LEU H H 8.658 0.0 1 195 59 59 LEU CA C 52.761 0.021 1 196 59 59 LEU CB C 42.839 0.008 1 197 59 59 LEU N N 126.508 0.004 1 198 60 60 GLN H H 8.592 0.003 1 199 60 60 GLN CA C 55.086 . 1 200 60 60 GLN CB C 30.119 . 1 201 60 60 GLN N N 124.489 0.002 1 202 62 62 TRP H H 10.677 . 1 203 62 62 TRP NE1 N 128.833 . 1 204 63 63 ASP CA C 53.099 . 1 205 63 63 ASP CB C 41.601 . 1 206 64 64 THR H H 7.382 0.003 1 207 64 64 THR CA C 60.448 0.052 1 208 64 64 THR CB C 71.516 0.004 1 209 64 64 THR N N 112.369 0.008 1 210 65 65 ALA H H 7.728 0.003 1 211 65 65 ALA CA C 53.012 0.085 1 212 65 65 ALA CB C 19.061 0.004 1 213 65 65 ALA N N 121.980 0.0 1 214 66 66 GLY H H 8.285 0.002 1 215 66 66 GLY CA C 45.388 0.002 1 216 66 66 GLY N N 107.590 0.037 1 217 67 67 GLN H H 7.730 0.002 1 218 67 67 GLN CA C 57.246 . 1 219 67 67 GLN CB C 30.352 . 1 220 67 67 GLN N N 124.477 0.005 1 221 71 71 ARG CA C 55.991 . 1 222 71 71 ARG CB C 31.014 . 1 223 71 71 ARG CG C 26.930 . 1 224 71 71 ARG CD C 43.175 . 1 225 72 72 SER H H 7.846 0.001 1 226 72 72 SER CA C 60.043 . 1 227 72 72 SER CB C 64.782 . 1 228 72 72 SER N N 122.883 0.005 1 229 74 74 THR CA C 61.583 . 1 230 74 74 THR CB C 70.043 . 1 231 74 74 THR CG2 C 21.275 . 1 232 75 75 ARG H H 7.959 0.002 1 233 75 75 ARG CA C 58.163 . 1 234 75 75 ARG CB C 31.054 . 1 235 75 75 ARG N N 127.943 0.016 1 236 76 76 SER CA C 59.786 . 1 237 76 76 SER CB C 63.186 . 1 238 77 77 TYR H H 7.649 0.002 1 239 77 77 TYR CA C 59.402 0.004 1 240 77 77 TYR CB C 37.512 0.015 1 241 77 77 TYR N N 118.991 0.002 1 242 78 78 TYR H H 7.388 0.001 1 243 78 78 TYR CA C 60.406 0.018 1 244 78 78 TYR CB C 38.772 0.008 1 245 78 78 TYR N N 118.061 0.016 1 246 79 79 ARG H H 7.314 0.001 1 247 79 79 ARG CA C 58.158 . 1 248 79 79 ARG CB C 29.412 . 1 249 79 79 ARG N N 116.466 0.005 1 250 80 80 GLY CA C 45.318 . 1 251 81 81 ALA H H 7.952 0.001 1 252 81 81 ALA CA C 53.168 0.012 1 253 81 81 ALA CB C 19.060 0.021 1 254 81 81 ALA N N 122.687 0.006 1 255 82 82 ALA H H 8.984 0.001 1 256 82 82 ALA CA C 52.469 0.034 1 257 82 82 ALA CB C 21.178 0.004 1 258 82 82 ALA N N 124.135 0.105 1 259 83 83 GLY H H 7.636 0.002 1 260 83 83 GLY CA C 43.745 0.016 1 261 83 83 GLY N N 103.845 0.017 1 262 84 84 ALA H H 8.377 0.02 1 263 84 84 ALA CA C 50.571 0.049 1 264 84 84 ALA CB C 21.606 0.017 1 265 84 84 ALA N N 120.138 1.653 1 266 85 85 LEU H H 8.422 0.002 1 267 85 85 LEU CA C 53.937 1.077 1 268 85 85 LEU CB C 42.969 0.4 1 269 85 85 LEU N N 123.835 0.002 1 270 86 86 LEU H H 8.760 0.002 1 271 86 86 LEU CA C 55.009 . 1 272 86 86 LEU CB C 41.643 . 1 273 86 86 LEU N N 128.108 0.006 1 274 87 87 VAL CA C 61.410 . 1 275 87 87 VAL CB C 31.930 . 1 276 88 88 TYR H H 8.517 0.001 1 277 88 88 TYR CA C 55.443 0.022 1 278 88 88 TYR CB C 39.085 0.011 1 279 88 88 TYR N N 120.737 0.005 1 280 89 89 ASP H H 8.575 0.001 1 281 89 89 ASP CA C 50.976 0.007 1 282 89 89 ASP CB C 43.765 0.008 1 283 89 89 ASP N N 120.672 0.001 1 284 90 90 ILE H H 8.536 0.002 1 285 90 90 ILE CA C 65.107 0.013 1 286 90 90 ILE CB C 38.467 0.004 1 287 90 90 ILE CG1 C 29.180 . 1 288 90 90 ILE CG2 C 18.379 . 1 289 90 90 ILE N N 119.791 0.003 1 290 91 91 THR H H 9.157 0.004 1 291 91 91 THR CA C 61.893 0.019 1 292 91 91 THR CB C 69.739 0.004 1 293 91 91 THR CG2 C 19.664 . 1 294 91 91 THR N N 112.781 0.016 1 295 92 92 SER H H 7.921 0.002 1 296 92 92 SER CA C 54.778 0.022 1 297 92 92 SER CB C 62.870 0.022 1 298 92 92 SER N N 114.475 0.007 1 299 93 93 ARG H H 10.178 0.001 1 300 93 93 ARG CA C 60.077 0.011 1 301 93 93 ARG CB C 29.307 0.035 1 302 93 93 ARG N N 132.992 0.006 1 303 94 94 GLU H H 9.009 0.001 1 304 94 94 GLU CA C 60.099 0.043 1 305 94 94 GLU CB C 29.320 0.046 1 306 94 94 GLU CG C 36.155 . 1 307 94 94 GLU N N 119.018 0.001 1 308 95 95 THR H H 7.718 0.005 1 309 95 95 THR CA C 64.900 0.043 1 310 95 95 THR CB C 69.085 0.028 1 311 95 95 THR CG2 C 22.538 . 1 312 95 95 THR N N 109.059 0.002 1 313 96 96 TYR H H 7.091 0.001 1 314 96 96 TYR CA C 58.688 0.103 1 315 96 96 TYR CB C 40.359 0.016 1 316 96 96 TYR N N 124.819 0.002 1 317 97 97 ASN H H 8.725 0.002 1 318 97 97 ASN CA C 54.766 0.015 1 319 97 97 ASN CB C 37.512 0.036 1 320 97 97 ASN N N 120.864 0.001 1 321 98 98 ALA H H 6.898 0.001 1 322 98 98 ALA CA C 52.891 0.002 1 323 98 98 ALA CB C 20.013 0.002 1 324 98 98 ALA N N 118.412 0.002 1 325 99 99 LEU H H 7.279 0.002 1 326 99 99 LEU CA C 58.811 0.036 1 327 99 99 LEU CB C 42.879 0.051 1 328 99 99 LEU N N 116.532 0.0 1 329 100 100 THR H H 7.965 0.002 1 330 100 100 THR CA C 61.294 0.02 1 331 100 100 THR CB C 67.821 0.033 1 332 100 100 THR CG2 C 21.569 . 1 333 100 100 THR N N 112.178 0.1 1 334 101 101 ASN H H 7.763 0.001 1 335 101 101 ASN CA C 56.300 0.003 1 336 101 101 ASN CB C 37.681 0.098 1 337 101 101 ASN N N 121.510 0.019 1 338 102 102 TRP H H 7.228 0.001 1 339 102 102 TRP HE1 H 10.416 . 1 340 102 102 TRP CA C 60.349 0.007 1 341 102 102 TRP CB C 31.601 0.001 1 342 102 102 TRP N N 119.109 0.002 1 343 102 102 TRP NE1 N 127.837 . 1 344 103 103 LEU H H 8.543 0.001 1 345 103 103 LEU CA C 58.080 0.073 1 346 103 103 LEU CB C 42.508 0.051 1 347 103 103 LEU CG C 23.891 . 1 348 103 103 LEU CD1 C 23.891 . 1 349 103 103 LEU CD2 C 23.891 . 1 350 103 103 LEU N N 118.096 0.054 1 351 104 104 THR H H 7.965 0.001 1 352 104 104 THR CA C 66.480 0.132 1 353 104 104 THR CB C 68.617 0.078 1 354 104 104 THR CG2 C 21.513 . 1 355 104 104 THR N N 114.848 0.004 1 356 105 105 ASP H H 7.560 0.001 1 357 105 105 ASP CA C 57.574 0.022 1 358 105 105 ASP CB C 40.045 0.026 1 359 105 105 ASP N N 121.724 0.002 1 360 106 106 ALA H H 8.514 0.001 1 361 106 106 ALA CA C 55.666 0.003 1 362 106 106 ALA CB C 17.388 0.011 1 363 106 106 ALA N N 120.648 0.001 1 364 107 107 ARG H H 7.848 0.005 1 365 107 107 ARG CA C 58.240 0.01 1 366 107 107 ARG CB C 30.081 0.048 1 367 107 107 ARG N N 113.661 0.015 1 368 108 108 MET H H 7.722 0.002 1 369 108 108 MET CA C 57.530 0.008 1 370 108 108 MET CB C 33.446 0.004 1 371 108 108 MET CG C 31.574 . 1 372 108 108 MET N N 116.223 0.003 1 373 109 109 LEU H H 8.166 0.001 1 374 109 109 LEU CA C 56.014 0.006 1 375 109 109 LEU CB C 42.981 0.178 1 376 109 109 LEU N N 116.784 0.052 1 377 110 110 ALA H H 7.821 0.001 1 378 110 110 ALA CA C 51.973 0.049 1 379 110 110 ALA CB C 19.671 0.034 1 380 110 110 ALA N N 120.583 0.002 1 381 111 111 SER H H 7.457 0.001 1 382 111 111 SER CA C 58.830 . 1 383 111 111 SER CB C 64.455 . 1 384 111 111 SER N N 111.451 0.014 1 385 113 113 ASN CA C 52.590 . 1 386 113 113 ASN CB C 38.773 . 1 387 114 114 ILE H H 7.244 0.001 1 388 114 114 ILE CA C 62.492 0.056 1 389 114 114 ILE CB C 38.539 0.066 1 390 114 114 ILE N N 121.601 0.002 1 391 115 115 VAL H H 7.481 0.005 1 392 115 115 VAL CA C 62.529 . 1 393 115 115 VAL CB C 32.001 . 1 394 115 115 VAL N N 129.613 0.004 1 395 116 116 ILE H H 7.796 . 1 396 116 116 ILE CA C 59.388 . 1 397 116 116 ILE CB C 39.861 . 1 398 116 116 ILE N N 130.282 . 1 399 117 117 ILE H H 8.601 0.0 1 400 117 117 ILE CA C 57.917 0.02 1 401 117 117 ILE CB C 41.555 0.014 1 402 117 117 ILE N N 126.297 0.002 1 403 118 118 LEU H H 9.032 0.001 1 404 118 118 LEU CA C 53.803 0.018 1 405 118 118 LEU CB C 44.067 0.045 1 406 118 118 LEU N N 131.616 0.001 1 407 119 119 CYS H H 9.222 0.0 1 408 119 119 CYS CA C 56.624 0.004 1 409 119 119 CYS CB C 29.281 0.129 1 410 119 119 CYS N N 124.043 0.003 1 411 120 120 GLY H H 8.649 0.002 1 412 120 120 GLY CA C 45.505 . 1 413 120 120 GLY N N 111.411 0.011 1 414 122 122 LYS CA C 56.939 . 1 415 122 122 LYS CB C 28.963 . 1 416 123 123 LYS H H 8.633 0.001 1 417 123 123 LYS CA C 58.228 0.018 1 418 123 123 LYS CB C 30.965 0.004 1 419 123 123 LYS N N 117.147 0.004 1 420 124 124 ASP H H 8.446 0.001 1 421 124 124 ASP CA C 55.045 0.009 1 422 124 124 ASP CB C 40.386 0.009 1 423 124 124 ASP N N 114.854 0.004 1 424 125 125 LEU H H 8.053 0.001 1 425 125 125 LEU CA C 53.502 0.003 1 426 125 125 LEU CB C 39.407 0.009 1 427 125 125 LEU CG C 26.142 . 1 428 125 125 LEU CD1 C 26.142 . 1 429 125 125 LEU CD2 C 26.142 . 1 430 125 125 LEU N N 123.219 0.001 1 431 126 126 ASP H H 6.903 0.001 1 432 126 126 ASP CA C 57.874 0.01 1 433 126 126 ASP CB C 42.573 0.004 1 434 126 126 ASP N N 118.390 0.004 1 435 127 127 ALA H H 8.558 0.001 1 436 127 127 ALA CA C 54.738 0.03 1 437 127 127 ALA CB C 18.437 0.009 1 438 127 127 ALA N N 120.575 0.0 1 439 128 128 ASP H H 7.864 0.001 1 440 128 128 ASP CA C 53.193 0.006 1 441 128 128 ASP CB C 41.917 0.011 1 442 128 128 ASP N N 116.074 0.003 1 443 129 129 ARG H H 7.151 0.001 1 444 129 129 ARG CA C 58.139 0.032 1 445 129 129 ARG CB C 32.430 0.151 1 446 129 129 ARG N N 119.191 0.003 1 447 130 130 GLU H H 9.446 0.0 1 448 130 130 GLU CA C 56.323 0.03 1 449 130 130 GLU CB C 33.452 0.001 1 450 130 130 GLU CG C 36.836 . 1 451 130 130 GLU N N 122.767 0.008 1 452 131 131 VAL H H 7.345 0.001 1 453 131 131 VAL CA C 60.724 0.032 1 454 131 131 VAL CB C 34.106 0.016 1 455 131 131 VAL CG1 C 19.554 . 1 456 131 131 VAL CG2 C 19.554 . 1 457 131 131 VAL N N 121.110 0.002 1 458 132 132 THR H H 9.867 0.003 1 459 132 132 THR CA C 61.948 0.02 1 460 132 132 THR CB C 70.344 0.016 1 461 132 132 THR CG2 C 21.915 . 1 462 132 132 THR N N 120.526 0.003 1 463 133 133 PHE H H 8.941 0.001 1 464 133 133 PHE CA C 61.613 0.01 1 465 133 133 PHE CB C 39.432 0.022 1 466 133 133 PHE N N 124.555 0.098 1 467 134 134 LEU H H 8.456 0.001 1 468 134 134 LEU CA C 58.199 0.009 1 469 134 134 LEU CB C 42.233 0.006 1 470 134 134 LEU CG C 24.084 . 1 471 134 134 LEU CD2 C 24.084 . 1 472 134 134 LEU N N 118.092 0.001 1 473 135 135 GLU H H 8.091 0.002 1 474 135 135 GLU CA C 58.793 0.027 1 475 135 135 GLU CB C 28.120 0.012 1 476 135 135 GLU CG C 35.681 . 1 477 135 135 GLU N N 119.318 0.003 1 478 136 136 ALA H H 7.067 0.001 1 479 136 136 ALA CA C 54.435 0.023 1 480 136 136 ALA CB C 20.652 0.0 1 481 136 136 ALA N N 126.866 0.001 1 482 137 137 SER H H 7.966 0.001 1 483 137 137 SER CA C 61.313 0.007 1 484 137 137 SER CB C 62.570 0.005 1 485 137 137 SER N N 113.313 0.003 1 486 138 138 ARG H H 7.572 0.001 1 487 138 138 ARG CA C 59.107 0.009 1 488 138 138 ARG CB C 29.436 0.005 1 489 138 138 ARG CG C 27.087 . 1 490 138 138 ARG CD C 43.441 . 1 491 138 138 ARG N N 122.742 0.001 1 492 139 139 PHE H H 7.825 0.002 1 493 139 139 PHE CA C 61.624 0.001 1 494 139 139 PHE CB C 39.392 0.018 1 495 139 139 PHE N N 122.152 0.001 1 496 140 140 ALA H H 8.718 0.001 1 497 140 140 ALA CA C 55.670 0.005 1 498 140 140 ALA CB C 18.144 0.032 1 499 140 140 ALA N N 122.355 0.003 1 500 141 141 GLN H H 8.029 0.001 1 501 141 141 GLN CA C 59.139 0.003 1 502 141 141 GLN CB C 28.466 0.017 1 503 141 141 GLN CG C 33.759 . 1 504 141 141 GLN N N 118.422 0.001 1 505 142 142 GLU H H 8.274 0.001 1 506 142 142 GLU CA C 58.497 0.0 1 507 142 142 GLU CB C 29.425 0.012 1 508 142 142 GLU CG C 36.579 . 1 509 142 142 GLU N N 118.700 0.005 1 510 143 143 ASN H H 7.092 0.0 1 511 143 143 ASN CA C 53.505 0.019 1 512 143 143 ASN CB C 39.719 0.01 1 513 143 143 ASN N N 113.970 0.003 1 514 144 144 GLU H H 7.568 0.003 1 515 144 144 GLU CA C 57.545 0.004 1 516 144 144 GLU CB C 26.922 0.037 1 517 144 144 GLU CG C 36.906 . 1 518 144 144 GLU N N 116.172 0.007 1 519 145 145 LEU H H 8.498 0.002 1 520 145 145 LEU CA C 52.810 0.052 1 521 145 145 LEU CB C 43.442 0.049 1 522 145 145 LEU N N 117.142 0.0 1 523 146 146 MET H H 7.364 0.001 1 524 146 146 MET CA C 56.303 0.007 1 525 146 146 MET CB C 35.298 0.007 1 526 146 146 MET CG C 33.635 . 1 527 146 146 MET N N 120.591 0.001 1 528 147 147 PHE H H 8.373 0.001 1 529 147 147 PHE CA C 56.303 0.001 1 530 147 147 PHE CB C 42.813 0.03 1 531 147 147 PHE N N 122.194 0.001 1 532 148 148 LEU H H 8.438 0.001 1 533 148 148 LEU CA C 54.107 0.016 1 534 148 148 LEU CB C 46.652 0.004 1 535 148 148 LEU CG C 25.930 . 1 536 148 148 LEU CD2 C 25.930 . 1 537 148 148 LEU N N 129.563 0.004 1 538 149 149 GLU H H 8.059 0.001 1 539 149 149 GLU CA C 55.387 0.003 1 540 149 149 GLU CB C 31.274 0.024 1 541 149 149 GLU N N 117.133 0.0 1 542 150 150 THR H H 8.725 0.002 1 543 150 150 THR CA C 59.531 0.002 1 544 150 150 THR CB C 73.259 0.02 1 545 150 150 THR N N 111.658 0.105 1 546 151 151 SER H H 8.117 0.001 1 547 151 151 SER CA C 57.514 0.012 1 548 151 151 SER CB C 65.071 0.001 1 549 151 151 SER N N 111.445 0.0 1 550 152 152 ALA H H 9.157 0.002 1 551 152 152 ALA CA C 54.731 0.009 1 552 152 152 ALA CB C 18.757 0.004 1 553 152 152 ALA N N 133.033 0.005 1 554 153 153 LEU H H 7.116 0.001 1 555 153 153 LEU CA C 57.613 0.029 1 556 153 153 LEU CB C 43.152 0.014 1 557 153 153 LEU N N 117.544 0.003 1 558 154 154 THR H H 7.936 0.002 1 559 154 154 THR CA C 61.852 0.086 1 560 154 154 THR CB C 69.873 0.051 1 561 154 154 THR CG2 C 21.312 . 1 562 154 154 THR N N 106.504 0.006 1 563 155 155 GLY H H 7.963 0.002 1 564 155 155 GLY CA C 45.047 0.006 1 565 155 155 GLY N N 110.339 0.001 1 566 156 156 GLU H H 7.928 0.0 1 567 156 156 GLU CA C 59.111 0.036 1 568 156 156 GLU CB C 29.460 0.016 1 569 156 156 GLU CG C 35.369 . 1 570 156 156 GLU N N 124.920 0.003 1 571 157 157 ASP H H 8.975 0.003 1 572 157 157 ASP CA C 54.744 0.015 1 573 157 157 ASP CB C 37.546 0.001 1 574 157 157 ASP N N 119.580 0.003 1 575 158 158 VAL H H 7.593 0.001 1 576 158 158 VAL CA C 68.497 0.019 1 577 158 158 VAL CB C 30.661 0.017 1 578 158 158 VAL N N 120.538 0.001 1 579 159 159 GLU H H 8.619 0.001 1 580 159 159 GLU CA C 60.382 0.007 1 581 159 159 GLU CB C 29.417 0.015 1 582 159 159 GLU CG C 36.620 . 1 583 159 159 GLU N N 118.936 0.009 1 584 160 160 GLU H H 8.482 0.001 1 585 160 160 GLU CA C 59.456 0.015 1 586 160 160 GLU CB C 28.725 0.016 1 587 160 160 GLU CG C 36.307 . 1 588 160 160 GLU N N 116.425 0.008 1 589 161 161 ALA H H 7.628 0.003 1 590 161 161 ALA CA C 55.599 0.028 1 591 161 161 ALA CB C 17.799 0.029 1 592 161 161 ALA N N 121.161 0.005 1 593 162 162 PHE H H 6.794 0.0 1 594 162 162 PHE CA C 62.623 0.032 1 595 162 162 PHE CB C 40.364 0.003 1 596 162 162 PHE N N 112.791 0.001 1 597 163 163 VAL H H 8.609 0.001 1 598 163 163 VAL CA C 67.231 0.036 1 599 163 163 VAL CB C 31.870 0.033 1 600 163 163 VAL N N 118.862 0.001 1 601 164 164 GLN H H 9.226 0.0 1 602 164 164 GLN CA C 59.416 0.011 1 603 164 164 GLN CB C 27.325 0.14 1 604 164 164 GLN CG C 34.373 . 1 605 164 164 GLN N N 118.158 0.002 1 606 165 165 CYS H H 7.232 0.002 1 607 165 165 CYS CA C 63.211 0.008 1 608 165 165 CYS CB C 26.558 0.02 1 609 165 165 CYS N N 118.117 0.036 1 610 166 166 ALA H H 8.055 0.002 1 611 166 166 ALA CA C 55.662 0.009 1 612 166 166 ALA CB C 18.637 0.033 1 613 166 166 ALA N N 118.336 0.001 1 614 167 167 ARG H H 9.123 0.001 1 615 167 167 ARG CA C 60.029 0.006 1 616 167 167 ARG CB C 30.470 0.013 1 617 167 167 ARG N N 117.294 0.0 1 618 168 168 LYS H H 7.630 0.002 1 619 168 168 LYS CA C 58.453 0.016 1 620 168 168 LYS CB C 31.522 0.007 1 621 168 168 LYS CG C 23.755 . 1 622 168 168 LYS CD C 28.464 . 1 623 168 168 LYS CE C 41.543 . 1 624 168 168 LYS N N 118.966 0.01 1 625 169 169 ILE H H 7.710 0.004 1 626 169 169 ILE CA C 65.730 0.005 1 627 169 169 ILE CB C 38.505 0.087 1 628 169 169 ILE N N 119.768 0.002 1 629 170 170 LEU H H 7.996 0.002 1 630 170 170 LEU CA C 57.936 0.1 1 631 170 170 LEU CB C 41.602 0.002 1 632 170 170 LEU CG C 26.211 . 1 633 170 170 LEU CD1 C 25.054 . 1 634 170 170 LEU N N 119.000 0.003 1 635 171 171 ASN H H 7.998 0.001 1 636 171 171 ASN CA C 55.350 0.013 1 637 171 171 ASN CB C 39.074 0.006 1 638 171 171 ASN N N 116.598 0.003 1 639 172 172 LYS H H 7.944 0.002 1 640 172 172 LYS CA C 57.821 0.018 1 641 172 172 LYS CB C 32.766 0.058 1 642 172 172 LYS CG C 24.695 . 1 643 172 172 LYS CD C 29.142 . 1 644 172 172 LYS N N 118.420 0.009 1 645 173 173 HIS H H 7.890 0.002 1 646 173 173 HIS CA C 56.989 . 1 647 173 173 HIS CB C 31.284 . 1 648 173 173 HIS N N 116.510 0.004 1 649 174 174 HIS H H 7.768 0.001 1 650 174 174 HIS CA C 57.537 . 1 651 174 174 HIS CB C 30.973 . 1 652 174 174 HIS N N 125.631 0.0 1 stop_ save_