data_10078 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonance Assignments for LolA ; _BMRB_accession_number 10078 _BMRB_flat_file_name bmr10078.str _Entry_type original _Submission_date 2007-01-21 _Accession_date 2007-01-21 _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 Nakada Shingo . . 2 Takahashi Hideo . . 3 Sakakura Masayoshi . . 4 Kurono Masuo . . 5 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 162 "13C chemical shifts" 515 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-31 update BMRB 'complete entry citation' 2007-08-22 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignments for the periplasmic chaperone LolA from Escherichia coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636845 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shingo Nakada . . 2 Hideo Takahashi . . 3 Masayoshi Sakakura . . 4 Masuo Kurono . . 5 Ichio Shimada . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 125 _Page_last 127 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LolA monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LolA monomer' $LolA stop_ _System_molecular_weight 21600 _System_physical_state native _System_oligomer_state 'protein monomer' _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Outer-membrane lipoprotein carrier protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LolA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LolA _Molecular_mass 21600 _Mol_thiol_state 'not present' loop_ _Biological_function 'Outer-membrane lipoprotein carrier protein' stop_ _Details ; The signal peptides (21 aa) at the N-terminus of LolA was removed in this recombinant protein. Instead, Met and Ala residues were attached to the N-terminus. ; ############################## # Polymer residue sequence # ############################## _Residue_count 192 _Mol_residue_sequence ; MADAASDLKSRLDKVSSFHA SFTQKVTDGSGAAVQEGQGD LWVKRPNLFNWHMTQPDESI LVSDGKTLWFYNPFVEQATA TWLKDATGNTPFMLIARNQS SDWQQYNIKQNGDDFVLTPK ASNGNLKQFTINVGRDGTIH QFSAVEQDDQRSSYQLKSQQ NGAVDAAKFTFTPPQGVTVD DQRKLEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 0 ALA 3 1 ASP 4 2 ALA 5 3 ALA 6 4 SER 7 5 ASP 8 6 LEU 9 7 LYS 10 8 SER 11 9 ARG 12 10 LEU 13 11 ASP 14 12 LYS 15 13 VAL 16 14 SER 17 15 SER 18 16 PHE 19 17 HIS 20 18 ALA 21 19 SER 22 20 PHE 23 21 THR 24 22 GLN 25 23 LYS 26 24 VAL 27 25 THR 28 26 ASP 29 27 GLY 30 28 SER 31 29 GLY 32 30 ALA 33 31 ALA 34 32 VAL 35 33 GLN 36 34 GLU 37 35 GLY 38 36 GLN 39 37 GLY 40 38 ASP 41 39 LEU 42 40 TRP 43 41 VAL 44 42 LYS 45 43 ARG 46 44 PRO 47 45 ASN 48 46 LEU 49 47 PHE 50 48 ASN 51 49 TRP 52 50 HIS 53 51 MET 54 52 THR 55 53 GLN 56 54 PRO 57 55 ASP 58 56 GLU 59 57 SER 60 58 ILE 61 59 LEU 62 60 VAL 63 61 SER 64 62 ASP 65 63 GLY 66 64 LYS 67 65 THR 68 66 LEU 69 67 TRP 70 68 PHE 71 69 TYR 72 70 ASN 73 71 PRO 74 72 PHE 75 73 VAL 76 74 GLU 77 75 GLN 78 76 ALA 79 77 THR 80 78 ALA 81 79 THR 82 80 TRP 83 81 LEU 84 82 LYS 85 83 ASP 86 84 ALA 87 85 THR 88 86 GLY 89 87 ASN 90 88 THR 91 89 PRO 92 90 PHE 93 91 MET 94 92 LEU 95 93 ILE 96 94 ALA 97 95 ARG 98 96 ASN 99 97 GLN 100 98 SER 101 99 SER 102 100 ASP 103 101 TRP 104 102 GLN 105 103 GLN 106 104 TYR 107 105 ASN 108 106 ILE 109 107 LYS 110 108 GLN 111 109 ASN 112 110 GLY 113 111 ASP 114 112 ASP 115 113 PHE 116 114 VAL 117 115 LEU 118 116 THR 119 117 PRO 120 118 LYS 121 119 ALA 122 120 SER 123 121 ASN 124 122 GLY 125 123 ASN 126 124 LEU 127 125 LYS 128 126 GLN 129 127 PHE 130 128 THR 131 129 ILE 132 130 ASN 133 131 VAL 134 132 GLY 135 133 ARG 136 134 ASP 137 135 GLY 138 136 THR 139 137 ILE 140 138 HIS 141 139 GLN 142 140 PHE 143 141 SER 144 142 ALA 145 143 VAL 146 144 GLU 147 145 GLN 148 146 ASP 149 147 ASP 150 148 GLN 151 149 ARG 152 150 SER 153 151 SER 154 152 TYR 155 153 GLN 156 154 LEU 157 155 LYS 158 156 SER 159 157 GLN 160 158 GLN 161 159 ASN 162 160 GLY 163 161 ALA 164 162 VAL 165 163 ASP 166 164 ALA 167 165 ALA 168 166 LYS 169 167 PHE 170 168 THR 171 169 PHE 172 170 THR 173 171 PRO 174 172 PRO 175 173 GLN 176 174 GLY 177 175 VAL 178 176 THR 179 177 VAL 180 178 ASP 181 179 ASP 182 180 GLN 183 181 ARG 184 182 LYS 185 183 LEU 186 184 GLU 187 185 HIS 188 186 HIS 189 187 HIS 190 188 HIS 191 189 HIS 192 190 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1IWL "Crystal Structure Of The Lipoprotein Localization Factor, Lola" 94.79 182 100.00 100.00 1.48e-129 PDB 1UA8 "Crystal Structure Of The Lipoprotein Localization Factor, Lola" 94.79 182 100.00 100.00 1.48e-129 PDB 2ZPC "Crystal Structure Of The R43l Mutant Of Lola In The Closed Form" 98.96 190 99.47 99.47 1.12e-135 PDB 2ZPD "Crystal Structure Of The R43l Mutant Of Lola In The Open Form" 98.96 190 99.47 99.47 1.12e-135 PDB 3KSN "Crystal Structure Of The Lipoprotein Localization Factor, Lola" 95.31 183 99.45 99.45 1.77e-129 DBJ BAA08390 "lipoprotein carrier protein precursor [Escherichia coli]" 95.31 204 100.00 100.00 9.57e-131 DBJ BAA35616 "chaperone for lipoproteins [Escherichia coli str. K12 substr. W3110]" 95.31 204 100.00 100.00 9.57e-131 DBJ BAB34399 "periplasmic protein effects translocation of lipoproteins from inner membrane to outer [Escherichia coli O157:H7 str. Sakai]" 95.31 204 100.00 100.00 9.57e-131 DBJ BAG76473 "conserved hypothetical protein [Escherichia coli SE11]" 95.31 204 100.00 100.00 9.57e-131 DBJ BAI24333 "chaperone IolA [Escherichia coli O26:H11 str. 11368]" 95.31 204 100.00 100.00 9.57e-131 EMBL CAP75364 "Outer-membrane lipoprotein carrier protein [Escherichia coli LF82]" 95.31 204 100.00 100.00 9.57e-131 EMBL CAQ31419 "periplasmic chaperone, effects translocation of lipoproteins from inner membrane to outer [Escherichia coli BL21(DE3)]" 95.31 204 100.00 100.00 9.57e-131 EMBL CAQ88570 "chaperone for lipoproteins [Escherichia fergusonii ATCC 35469]" 95.31 204 100.00 100.00 9.57e-131 EMBL CAQ97795 "chaperone for lipoproteins [Escherichia coli IAI1]" 95.31 204 100.00 100.00 9.57e-131 EMBL CAR02254 "chaperone for lipoproteins [Escherichia coli S88]" 95.31 204 100.00 100.00 9.57e-131 GB AAC73977 "lipoprotein chaperone [Escherichia coli str. K-12 substr. MG1655]" 95.31 203 100.00 100.00 1.30e-130 GB AAG55378 "periplasmic protein effects translocation of lipoproteins from inner membrane to outer [Escherichia coli O157:H7 str. EDL933]" 95.31 204 100.00 100.00 9.57e-131 GB AAN42483 "periplasmic protein [Shigella flexneri 2a str. 301]" 95.31 204 100.00 100.00 9.57e-131 GB AAN79500 "Outer-membrane lipoproteins carrier protein precursor [Escherichia coli CFT073]" 95.31 204 100.00 100.00 9.57e-131 GB AAP16355 "periplasmic protein [Shigella flexneri 2a str. 2457T]" 95.31 204 100.00 100.00 9.57e-131 PIR F85614 "outer membrane lipoprotein carrier protein precursor [similarity] - Escherichia coli (strain O157:H7, substrain EDL933)" 95.31 204 100.00 100.00 9.57e-131 PIR H90750 "outer membrane lipoprotein carrier protein precursor [similarity] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" 95.31 204 100.00 100.00 9.57e-131 REF NP_309003 "outer-membrane lipoprotein carrier protein [Escherichia coli O157:H7 str. Sakai]" 95.31 204 100.00 100.00 9.57e-131 REF NP_415411 "lipoprotein chaperone [Escherichia coli str. K-12 substr. MG1655]" 95.31 203 100.00 100.00 1.30e-130 REF NP_706776 "lipoprotein chaperone [Shigella flexneri 2a str. 301]" 95.31 204 100.00 100.00 9.57e-131 REF WP_000976047 "MULTISPECIES: outer membrane lipoprotein carrier protein LolA [Enterobacteriaceae]" 95.31 204 100.00 100.00 9.57e-131 REF WP_001245402 "outer membrane lipoprotein carrier protein LolA [Escherichia coli]" 95.31 207 100.00 100.00 1.43e-130 SP A7ZJW0 "RecName: Full=Outer-membrane lipoprotein carrier protein; Flags: Precursor" 95.31 203 100.00 100.00 1.30e-130 SP A7ZYJ5 "RecName: Full=Outer-membrane lipoprotein carrier protein; Flags: Precursor" 95.31 203 100.00 100.00 1.30e-130 SP B1IWN2 "RecName: Full=Outer-membrane lipoprotein carrier protein; Flags: Precursor" 95.31 203 100.00 100.00 1.30e-130 SP B1LJX2 "RecName: Full=Outer-membrane lipoprotein carrier protein; Flags: Precursor" 95.31 203 100.00 100.00 1.30e-130 SP B1X831 "RecName: Full=Outer-membrane lipoprotein carrier protein; Flags: Precursor" 95.31 203 100.00 100.00 1.30e-130 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction $LolA 'Escherichia coli K-12' 83333 Bacteria . Escherichia coli K12 no 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 $LolA 'recombinant technology' 'E. coli' Escherichia coli K12 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $LolA . mM 0.5 1.0 '[U-2H; U-13C; U-15N]' 'sodium phosphate' 66 mM . . . 'sodium chloride' 100 mM . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address 'Bruker Japan' 'Ninomiya 3-21-5, Tsukuba, Ibaraki 305-0051' info@bruker-biospin.jp stop_ loop_ _Task 'data collection' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address 'T. D. Goddard and D. G. Kneller' 'University of California, San Francisco' sparky@cgl.ucsf.edu stop_ loop_ _Task 'peak assignments' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task 'data processing' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance800 _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_TROSY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N TROSY-HSQC' _Sample_label $sample_1 save_ save_TROSY-HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label $sample_1 save_ save_TROSY-HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label $sample_1 save_ save_TROSY-HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label $sample_1 save_ save_TROSY-HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label $sample_1 save_ save_TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label $sample_1 save_ save_TROSY-HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _Sample_label $sample_1 save_ save_1H15N_TROSY-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N TROSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HN(CO)CACB _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCO _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.95 0.20 pH temperature 310 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing_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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H15N TROSY-HSQC' TROSY-HNCACB TROSY-HN(CO)CACB TROSY-HNCA TROSY-HN(CO)CA TROSY-HNCO TROSY-HN(CA)CO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_referencing_1 _Mol_system_component_name 'LolA monomer' _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 2 4 ALA C C 178.940 0.125 1 2 2 4 ALA CA C 55.384 0.293 1 3 2 4 ALA CB C 19.046 0.293 1 4 3 5 ALA H H 8.246 0.004 1 5 3 5 ALA C C 180.495 0.125 1 6 3 5 ALA CA C 55.225 0.293 1 7 3 5 ALA CB C 17.955 0.293 1 8 3 5 ALA N N 118.413 0.172 1 9 4 6 SER H H 7.924 0.004 1 10 4 6 SER C C 176.881 0.125 1 11 4 6 SER CA C 61.182 0.293 1 12 4 6 SER CB C 62.278 0.293 1 13 4 6 SER N N 114.607 0.172 1 14 5 7 ASP H H 8.033 0.004 1 15 5 7 ASP C C 177.661 0.125 1 16 5 7 ASP CA C 57.437 0.293 1 17 5 7 ASP CB C 41.654 0.293 1 18 5 7 ASP N N 125.145 0.172 1 19 6 8 LEU H H 8.045 0.004 1 20 6 8 LEU C C 177.114 0.125 1 21 6 8 LEU CA C 58.095 0.293 1 22 6 8 LEU CB C 39.850 0.293 1 23 6 8 LEU N N 120.663 0.172 1 24 7 9 LYS H H 7.153 0.004 1 25 7 9 LYS C C 180.233 0.125 1 26 7 9 LYS CA C 57.976 0.293 1 27 7 9 LYS CB C 32.423 0.293 1 28 7 9 LYS N N 116.567 0.172 1 29 8 10 SER H H 8.045 0.004 1 30 8 10 SER C C 174.186 0.125 1 31 8 10 SER CA C 61.511 0.293 1 32 8 10 SER CB C 62.617 0.293 1 33 8 10 SER N N 114.489 0.172 1 34 9 11 ARG H H 8.182 0.004 1 35 9 11 ARG C C 178.985 0.125 1 36 9 11 ARG CA C 59.807 0.293 1 37 9 11 ARG CB C 29.846 0.293 1 38 9 11 ARG N N 122.362 0.172 1 39 10 12 LEU H H 7.610 0.004 1 40 10 12 LEU C C 178.660 0.125 1 41 10 12 LEU CA C 57.019 0.293 1 42 10 12 LEU CB C 41.356 0.293 1 43 10 12 LEU N N 117.754 0.172 1 44 11 13 ASP H H 7.833 0.004 1 45 11 13 ASP C C 177.479 0.125 1 46 11 13 ASP CA C 55.366 0.293 1 47 11 13 ASP CB C 41.158 0.293 1 48 11 13 ASP N N 117.585 0.172 1 49 12 14 LYS H H 7.244 0.004 1 50 12 14 LYS C C 176.831 0.125 1 51 12 14 LYS CA C 58.062 0.293 1 52 12 14 LYS CB C 32.071 0.293 1 53 12 14 LYS N N 119.438 0.172 1 54 13 15 VAL H H 7.416 0.004 1 55 13 15 VAL C C 174.923 0.125 1 56 13 15 VAL CA C 60.966 0.293 1 57 13 15 VAL CB C 32.889 0.293 1 58 13 15 VAL N N 117.230 0.172 1 59 14 16 SER C C 174.266 0.125 1 60 14 16 SER CA C 60.075 0.293 1 61 14 16 SER CB C 63.871 0.293 1 62 15 17 SER H H 7.522 0.004 1 63 15 17 SER C C 173.518 0.125 1 64 15 17 SER CA C 57.107 0.293 1 65 15 17 SER CB C 65.012 0.293 1 66 15 17 SER N N 113.717 0.172 1 67 16 18 PHE H H 8.772 0.004 1 68 16 18 PHE C C 172.030 0.125 1 69 16 18 PHE CA C 57.289 0.293 1 70 16 18 PHE CB C 40.490 0.293 1 71 16 18 PHE N N 118.896 0.172 1 72 17 19 HIS H H 8.513 0.004 1 73 17 19 HIS C C 173.625 0.125 1 74 17 19 HIS CA C 52.761 0.293 1 75 17 19 HIS CB C 32.779 0.293 1 76 17 19 HIS N N 117.753 0.172 1 77 18 20 ALA H H 9.682 0.004 1 78 18 20 ALA C C 174.277 0.125 1 79 18 20 ALA CA C 50.520 0.293 1 80 18 20 ALA CB C 23.127 0.293 1 81 18 20 ALA N N 131.881 0.172 1 82 19 21 SER H H 8.214 0.004 1 83 19 21 SER C C 175.908 0.125 1 84 19 21 SER CA C 56.351 0.293 1 85 19 21 SER CB C 64.824 0.293 1 86 19 21 SER N N 116.431 0.172 1 87 20 22 PHE H H 9.297 0.004 1 88 20 22 PHE C C 176.675 0.125 1 89 20 22 PHE CA C 57.348 0.293 1 90 20 22 PHE CB C 44.169 0.293 1 91 20 22 PHE N N 121.388 0.172 1 92 21 23 THR H H 9.240 0.004 1 93 21 23 THR C C 173.387 0.125 1 94 21 23 THR CA C 61.909 0.293 1 95 21 23 THR CB C 69.991 0.293 1 96 21 23 THR N N 115.594 0.172 1 97 22 24 GLN H H 8.558 0.004 1 98 22 24 GLN C C 174.501 0.125 1 99 22 24 GLN CA C 53.722 0.293 1 100 22 24 GLN CB C 32.343 0.293 1 101 22 24 GLN N N 125.983 0.172 1 102 23 25 LYS H H 8.867 0.004 1 103 23 25 LYS C C 175.336 0.125 1 104 23 25 LYS CA C 55.697 0.293 1 105 23 25 LYS CB C 34.813 0.293 1 106 23 25 LYS N N 128.449 0.172 1 107 24 26 VAL H H 8.908 0.004 1 108 24 26 VAL C C 173.808 0.125 1 109 24 26 VAL CA C 60.824 0.293 1 110 24 26 VAL CB C 33.369 0.293 1 111 24 26 VAL N N 127.950 0.172 1 112 25 27 THR H H 9.267 0.004 1 113 25 27 THR C C 173.656 0.125 1 114 25 27 THR CA C 59.502 0.293 1 115 25 27 THR CB C 71.531 0.293 1 116 25 27 THR N N 121.251 0.172 1 117 26 28 ASP H H 8.554 0.004 1 118 26 28 ASP C C 178.628 0.125 1 119 26 28 ASP CA C 52.676 0.293 1 120 26 28 ASP CB C 41.334 0.293 1 121 26 28 ASP N N 121.758 0.172 1 122 27 29 GLY H H 8.776 0.004 1 123 27 29 GLY C C 175.271 0.125 1 124 27 29 GLY CA C 46.975 0.293 1 125 27 29 GLY N N 107.717 0.172 1 126 28 30 SER H H 8.353 0.004 1 127 28 30 SER C C 175.251 0.125 1 128 28 30 SER CA C 58.646 0.293 1 129 28 30 SER CB C 64.212 0.293 1 130 28 30 SER N N 116.456 0.172 1 131 29 31 GLY H H 8.214 0.004 1 132 29 31 GLY C C 173.677 0.125 1 133 29 31 GLY CA C 44.890 0.293 1 134 29 31 GLY N N 111.267 0.172 1 135 30 32 ALA H H 7.987 0.004 1 136 30 32 ALA C C 177.072 0.125 1 137 30 32 ALA CA C 51.902 0.293 1 138 30 32 ALA CB C 18.870 0.293 1 139 30 32 ALA N N 125.171 0.172 1 140 31 33 ALA H H 8.326 0.004 1 141 31 33 ALA C C 177.563 0.125 1 142 31 33 ALA CA C 52.607 0.293 1 143 31 33 ALA CB C 18.269 0.293 1 144 31 33 ALA N N 123.507 0.172 1 145 32 34 VAL H H 8.622 0.004 1 146 32 34 VAL C C 176.069 0.125 1 147 32 34 VAL CA C 62.520 0.293 1 148 32 34 VAL CB C 33.033 0.293 1 149 32 34 VAL N N 122.238 0.172 1 150 33 35 GLN H H 7.825 0.004 1 151 33 35 GLN C C 173.921 0.125 1 152 33 35 GLN CA C 55.440 0.293 1 153 33 35 GLN CB C 31.393 0.293 1 154 33 35 GLN N N 118.565 0.172 1 155 34 36 GLU H H 8.434 0.004 1 156 34 36 GLU C C 175.664 0.125 1 157 34 36 GLU CA C 55.358 0.293 1 158 34 36 GLU CB C 32.065 0.293 1 159 34 36 GLU N N 123.669 0.172 1 160 35 37 GLY H H 8.904 0.004 1 161 35 37 GLY C C 173.537 0.125 1 162 35 37 GLY CA C 45.473 0.293 1 163 35 37 GLY N N 110.442 0.172 1 164 36 38 GLN H H 8.544 0.004 1 165 36 38 GLN C C 173.902 0.125 1 166 36 38 GLN CA C 55.392 0.293 1 167 36 38 GLN CB C 32.059 0.293 1 168 36 38 GLN N N 120.710 0.172 1 169 37 39 GLY H H 8.513 0.004 1 170 37 39 GLY C C 171.000 0.125 1 171 37 39 GLY CA C 46.191 0.293 1 172 37 39 GLY N N 108.246 0.172 1 173 38 40 ASP H H 8.372 0.004 1 174 38 40 ASP C C 172.256 0.125 1 175 38 40 ASP CA C 53.702 0.293 1 176 38 40 ASP CB C 46.632 0.293 1 177 38 40 ASP N N 121.191 0.172 1 178 39 41 LEU H H 9.464 0.004 1 179 39 41 LEU C C 174.696 0.125 1 180 39 41 LEU CA C 53.382 0.293 1 181 39 41 LEU CB C 45.714 0.293 1 182 39 41 LEU N N 122.391 0.172 1 183 40 42 TRP H H 10.058 0.004 1 184 40 42 TRP C C 175.922 0.125 1 185 40 42 TRP CA C 57.229 0.293 1 186 40 42 TRP CB C 31.994 0.293 1 187 40 42 TRP N N 127.943 0.172 1 188 41 43 VAL H H 8.685 0.004 1 189 41 43 VAL C C 174.232 0.125 1 190 41 43 VAL CA C 60.960 0.293 1 191 41 43 VAL CB C 36.029 0.293 1 192 41 43 VAL N N 122.838 0.172 1 193 42 44 LYS H H 8.041 0.004 1 194 42 44 LYS C C 173.940 0.125 1 195 42 44 LYS CA C 56.333 0.293 1 196 42 44 LYS CB C 34.789 0.293 1 197 42 44 LYS N N 127.097 0.172 1 198 43 45 ARG H H 8.672 0.004 1 199 43 45 ARG C C 175.915 0.125 1 200 43 45 ARG CA C 56.379 0.293 1 201 43 45 ARG CB C 27.703 0.293 1 202 43 45 ARG N N 124.766 0.172 1 203 44 46 PRO C C 177.188 0.125 1 204 44 46 PRO CA C 63.262 0.293 1 205 44 46 PRO CB C 34.037 0.293 1 206 45 47 ASN H H 7.823 0.004 1 207 45 47 ASN C C 172.943 0.125 1 208 45 47 ASN CA C 55.447 0.293 1 209 45 47 ASN CB C 37.807 0.293 1 210 45 47 ASN N N 113.291 0.172 1 211 46 48 LEU H H 7.705 0.004 1 212 46 48 LEU C C 176.797 0.125 1 213 46 48 LEU CA C 54.693 0.293 1 214 46 48 LEU CB C 39.193 0.293 1 215 46 48 LEU N N 121.902 0.172 1 216 47 49 PHE H H 7.763 0.004 1 217 47 49 PHE C C 172.901 0.125 1 218 47 49 PHE CA C 57.021 0.293 1 219 47 49 PHE CB C 40.745 0.293 1 220 47 49 PHE N N 115.853 0.172 1 221 48 50 ASN H H 9.640 0.004 1 222 48 50 ASN C C 174.174 0.125 1 223 48 50 ASN CA C 53.037 0.293 1 224 48 50 ASN CB C 41.161 0.293 1 225 48 50 ASN N N 121.337 0.172 1 226 49 51 TRP H H 10.025 0.004 1 227 49 51 TRP C C 173.363 0.125 1 228 49 51 TRP CA C 55.482 0.293 1 229 49 51 TRP CB C 32.164 0.293 1 230 49 51 TRP N N 129.286 0.172 1 231 50 52 HIS H H 9.214 0.004 1 232 50 52 HIS C C 175.185 0.125 1 233 50 52 HIS CA C 52.253 0.293 1 234 50 52 HIS CB C 32.776 0.293 1 235 50 52 HIS N N 129.836 0.172 1 236 51 53 MET H H 8.620 0.004 1 237 51 53 MET C C 175.671 0.125 1 238 51 53 MET CA C 55.404 0.293 1 239 51 53 MET CB C 33.117 0.293 1 240 51 53 MET N N 126.324 0.172 1 241 52 54 THR H H 8.326 0.004 1 242 52 54 THR C C 174.659 0.125 1 243 52 54 THR CA C 61.974 0.293 1 244 52 54 THR CB C 69.659 0.293 1 245 52 54 THR N N 110.630 0.172 1 246 53 55 GLN H H 7.713 0.004 1 247 53 55 GLN C C 174.274 0.125 1 248 53 55 GLN CA C 53.388 0.293 1 249 53 55 GLN CB C 30.775 0.293 1 250 53 55 GLN N N 119.487 0.172 1 251 54 56 PRO C C 175.309 0.125 1 252 54 56 PRO CA C 63.926 0.293 1 253 54 56 PRO CB C 33.381 0.293 1 254 55 57 ASP H H 7.214 0.004 1 255 55 57 ASP C C 177.503 0.125 1 256 55 57 ASP CA C 52.534 0.293 1 257 55 57 ASP CB C 43.245 0.293 1 258 55 57 ASP N N 119.879 0.172 1 259 56 58 GLU H H 8.151 0.004 1 260 56 58 GLU C C 176.395 0.125 1 261 56 58 GLU CA C 55.519 0.293 1 262 56 58 GLU CB C 29.837 0.293 1 263 56 58 GLU N N 122.201 0.172 1 264 57 59 SER H H 8.309 0.004 1 265 57 59 SER C C 172.391 0.125 1 266 57 59 SER CA C 58.373 0.293 1 267 57 59 SER CB C 65.351 0.293 1 268 57 59 SER N N 118.336 0.172 1 269 58 60 ILE H H 8.558 0.004 1 270 58 60 ILE C C 173.267 0.125 1 271 58 60 ILE CA C 61.162 0.293 1 272 58 60 ILE CB C 41.825 0.293 1 273 58 60 ILE N N 122.789 0.172 1 274 59 61 LEU H H 9.127 0.004 1 275 59 61 LEU C C 175.142 0.125 1 276 59 61 LEU CA C 53.743 0.293 1 277 59 61 LEU CB C 45.463 0.293 1 278 59 61 LEU N N 130.631 0.172 1 279 60 62 VAL H H 9.217 0.004 1 280 60 62 VAL C C 174.238 0.125 1 281 60 62 VAL CA C 59.791 0.293 1 282 60 62 VAL CB C 35.248 0.293 1 283 60 62 VAL N N 123.545 0.172 1 284 61 63 SER H H 8.621 0.004 1 285 61 63 SER C C 174.789 0.125 1 286 61 63 SER CA C 54.924 0.293 1 287 61 63 SER CB C 64.891 0.293 1 288 61 63 SER N N 120.583 0.172 1 289 62 64 ASP H H 8.128 0.004 1 290 62 64 ASP C C 177.958 0.125 1 291 62 64 ASP CA C 53.089 0.293 1 292 62 64 ASP CB C 41.718 0.293 1 293 62 64 ASP N N 124.937 0.172 1 294 63 65 GLY H H 8.415 0.004 1 295 63 65 GLY C C 173.397 0.125 1 296 63 65 GLY CA C 45.196 0.293 1 297 63 65 GLY N N 109.492 0.172 1 298 64 66 LYS H H 8.809 0.004 1 299 64 66 LYS C C 176.533 0.125 1 300 64 66 LYS CA C 58.361 0.293 1 301 64 66 LYS CB C 35.184 0.293 1 302 64 66 LYS N N 121.887 0.172 1 303 65 67 THR H H 10.496 0.004 1 304 65 67 THR C C 171.369 0.125 1 305 65 67 THR CA C 63.398 0.293 1 306 65 67 THR CB C 69.883 0.293 1 307 65 67 THR N N 125.678 0.172 1 308 66 68 LEU H H 8.799 0.004 1 309 66 68 LEU C C 174.889 0.125 1 310 66 68 LEU CA C 53.006 0.293 1 311 66 68 LEU CB C 43.721 0.293 1 312 66 68 LEU N N 127.115 0.172 1 313 67 69 TRP H H 9.771 0.004 1 314 67 69 TRP C C 175.165 0.125 1 315 67 69 TRP N N 129.785 0.172 1 316 68 70 PHE H H 8.891 0.004 1 317 68 70 PHE C C 174.763 0.125 1 318 68 70 PHE CA C 55.491 0.293 1 319 68 70 PHE CB C 41.091 0.293 1 320 68 70 PHE N N 121.091 0.172 1 321 69 71 TYR H H 9.242 0.004 1 322 69 71 TYR C C 172.039 0.125 1 323 69 71 TYR CA C 54.328 0.293 1 324 69 71 TYR CB C 40.736 0.293 1 325 69 71 TYR N N 127.971 0.172 1 326 70 72 ASN H H 8.056 0.004 1 327 70 72 ASN CA C 49.045 0.293 1 328 70 72 ASN CB C 40.244 0.293 1 329 70 72 ASN N N 126.522 0.172 1 330 71 73 PRO C C 178.414 0.125 1 331 71 73 PRO CA C 63.459 0.293 1 332 71 73 PRO CB C 31.252 0.293 1 333 72 74 PHE H H 8.232 0.004 1 334 72 74 PHE C C 177.181 0.125 1 335 72 74 PHE CA C 60.443 0.293 1 336 72 74 PHE CB C 38.526 0.293 1 337 72 74 PHE N N 118.686 0.172 1 338 73 75 VAL H H 6.889 0.004 1 339 73 75 VAL C C 175.260 0.125 1 340 73 75 VAL CA C 60.513 0.293 1 341 73 75 VAL CB C 31.213 0.293 1 342 73 75 VAL N N 109.345 0.172 1 343 74 76 GLU H H 7.737 0.004 1 344 74 76 GLU C C 175.121 0.125 1 345 74 76 GLU CA C 57.066 0.293 1 346 74 76 GLU CB C 26.622 0.293 1 347 74 76 GLU N N 117.572 0.172 1 348 75 77 GLN H H 7.409 0.004 1 349 75 77 GLN C C 174.425 0.125 1 350 75 77 GLN CA C 54.731 0.293 1 351 75 77 GLN CB C 32.606 0.293 1 352 75 77 GLN N N 116.869 0.172 1 353 76 78 ALA H H 8.920 0.004 1 354 76 78 ALA C C 176.023 0.125 1 355 76 78 ALA CA C 50.295 0.293 1 356 76 78 ALA CB C 22.646 0.293 1 357 76 78 ALA N N 125.924 0.172 1 358 77 79 THR C C 172.748 0.125 1 359 77 79 THR CA C 61.074 0.293 1 360 77 79 THR CB C 71.810 0.293 1 361 78 80 ALA H H 8.120 0.004 1 362 78 80 ALA C C 175.429 0.125 1 363 78 80 ALA CA C 50.188 0.293 1 364 78 80 ALA CB C 19.981 0.293 1 365 78 80 ALA N N 127.253 0.172 1 366 79 81 THR H H 8.093 0.004 1 367 79 81 THR C C 173.707 0.125 1 368 79 81 THR CA C 59.741 0.293 1 369 79 81 THR CB C 71.873 0.293 1 370 79 81 THR N N 113.829 0.172 1 371 80 82 TRP H H 8.916 0.004 1 372 80 82 TRP C C 178.793 0.125 1 373 80 82 TRP CA C 56.668 0.293 1 374 80 82 TRP CB C 29.573 0.293 1 375 80 82 TRP N N 123.651 0.172 1 376 81 83 LEU H H 8.862 0.004 1 377 81 83 LEU C C 179.027 0.125 1 378 81 83 LEU CA C 58.313 0.293 1 379 81 83 LEU CB C 41.095 0.293 1 380 81 83 LEU N N 126.967 0.172 1 381 82 84 LYS H H 8.296 0.004 1 382 82 84 LYS C C 176.300 0.125 1 383 82 84 LYS CA C 57.868 0.293 1 384 82 84 LYS CB C 30.858 0.293 1 385 82 84 LYS N N 114.878 0.172 1 386 83 85 ASP H H 7.490 0.004 1 387 83 85 ASP C C 175.971 0.125 1 388 83 85 ASP CA C 54.482 0.293 1 389 83 85 ASP CB C 41.910 0.293 1 390 83 85 ASP N N 118.858 0.172 1 391 84 86 ALA H H 7.524 0.004 1 392 84 86 ALA C C 177.598 0.125 1 393 84 86 ALA CA C 52.600 0.293 1 394 84 86 ALA CB C 19.082 0.293 1 395 84 86 ALA N N 124.435 0.172 1 396 85 87 THR H H 8.157 0.004 1 397 85 87 THR C C 175.063 0.125 1 398 85 87 THR CA C 61.431 0.293 1 399 85 87 THR CB C 69.871 0.293 1 400 85 87 THR N N 114.106 0.172 1 401 86 88 GLY H H 8.293 0.004 1 402 86 88 GLY C C 173.760 0.125 1 403 86 88 GLY CA C 45.306 0.293 1 404 86 88 GLY N N 110.415 0.172 1 405 89 91 PRO C C 176.167 0.125 1 406 89 91 PRO CA C 64.862 0.293 1 407 89 91 PRO CB C 30.826 0.293 1 408 90 92 PHE H H 5.870 0.004 1 409 90 92 PHE C C 176.539 0.125 1 410 90 92 PHE CA C 58.921 0.293 1 411 90 92 PHE CB C 37.021 0.293 1 412 90 92 PHE N N 111.643 0.172 1 413 91 93 MET H H 6.761 0.004 1 414 91 93 MET C C 178.186 0.125 1 415 91 93 MET CA C 57.257 0.293 1 416 91 93 MET CB C 31.283 0.293 1 417 91 93 MET N N 116.732 0.172 1 418 92 94 LEU H H 7.292 0.004 1 419 92 94 LEU C C 179.426 0.125 1 420 92 94 LEU CA C 57.697 0.293 1 421 92 94 LEU CB C 39.932 0.293 1 422 92 94 LEU N N 118.346 0.172 1 423 93 95 ILE H H 7.133 0.004 1 424 93 95 ILE C C 177.306 0.125 1 425 93 95 ILE CA C 64.834 0.293 1 426 93 95 ILE CB C 38.031 0.293 1 427 93 95 ILE N N 116.063 0.172 1 428 94 96 ALA H H 7.850 0.004 1 429 94 96 ALA C C 178.424 0.125 1 430 94 96 ALA CA C 54.817 0.293 1 431 94 96 ALA CB C 18.226 0.293 1 432 94 96 ALA N N 121.281 0.172 1 433 95 97 ARG H H 7.821 0.004 1 434 95 97 ARG C C 176.755 0.125 1 435 95 97 ARG CA C 58.357 0.293 1 436 95 97 ARG CB C 30.471 0.293 1 437 95 97 ARG N N 115.602 0.172 1 438 96 98 ASN H H 7.752 0.004 1 439 96 98 ASN C C 173.664 0.125 1 440 96 98 ASN CA C 53.803 0.293 1 441 96 98 ASN CB C 38.168 0.293 1 442 96 98 ASN N N 117.903 0.172 1 443 97 99 GLN H H 8.803 0.004 1 444 97 99 GLN C C 177.156 0.125 1 445 97 99 GLN CA C 53.852 0.293 1 446 97 99 GLN CB C 29.903 0.293 1 447 97 99 GLN N N 117.855 0.172 1 448 99 101 SER C C 176.614 0.125 1 449 99 101 SER CA C 60.792 0.293 1 450 99 101 SER CB C 61.636 0.293 1 451 100 102 ASP H H 7.044 0.004 1 452 100 102 ASP C C 178.931 0.125 1 453 100 102 ASP CA C 56.598 0.293 1 454 100 102 ASP CB C 39.280 0.293 1 455 100 102 ASP N N 122.062 0.172 1 456 101 103 TRP H H 7.297 0.004 1 457 101 103 TRP C C 178.518 0.125 1 458 101 103 TRP CA C 58.700 0.293 1 459 101 103 TRP CB C 29.557 0.293 1 460 101 103 TRP N N 118.892 0.172 1 461 102 104 GLN H H 7.934 0.004 1 462 102 104 GLN C C 176.447 0.125 1 463 102 104 GLN CA C 57.140 0.293 1 464 102 104 GLN CB C 27.975 0.293 1 465 102 104 GLN N N 113.543 0.172 1 466 103 105 GLN H H 7.669 0.004 1 467 103 105 GLN C C 174.690 0.125 1 468 103 105 GLN CA C 55.742 0.293 1 469 103 105 GLN CB C 27.572 0.293 1 470 103 105 GLN N N 116.005 0.172 1 471 104 106 TYR H H 8.017 0.004 1 472 104 106 TYR C C 175.053 0.125 1 473 104 106 TYR CA C 57.383 0.293 1 474 104 106 TYR CB C 40.766 0.293 1 475 104 106 TYR N N 118.603 0.172 1 476 105 107 ASN H H 9.463 0.004 1 477 105 107 ASN C C 175.330 0.125 1 478 105 107 ASN CA C 53.268 0.293 1 479 105 107 ASN CB C 39.250 0.293 1 480 105 107 ASN N N 120.175 0.172 1 481 106 108 ILE H H 8.824 0.004 1 482 106 108 ILE C C 174.792 0.125 1 483 106 108 ILE CA C 61.304 0.293 1 484 106 108 ILE CB C 39.007 0.293 1 485 106 108 ILE N N 124.592 0.172 1 486 107 109 LYS H H 8.933 0.004 1 487 107 109 LYS C C 174.569 0.125 1 488 107 109 LYS CA C 54.373 0.293 1 489 107 109 LYS CB C 34.051 0.293 1 490 107 109 LYS N N 128.882 0.172 1 491 108 110 GLN H H 8.747 0.004 1 492 108 110 GLN C C 174.810 0.125 1 493 108 110 GLN CA C 53.854 0.293 1 494 108 110 GLN CB C 30.520 0.293 1 495 108 110 GLN N N 127.261 0.172 1 496 109 111 ASN H H 8.746 0.004 1 497 109 111 ASN CA C 52.510 0.293 1 498 109 111 ASN CB C 39.358 0.293 1 499 109 111 ASN N N 126.615 0.172 1 500 110 112 GLY C C 173.039 0.125 1 501 110 112 GLY CA C 47.494 0.293 1 502 111 113 ASP H H 8.557 0.004 1 503 111 113 ASP C C 173.536 0.125 1 504 111 113 ASP CA C 53.945 0.293 1 505 111 113 ASP CB C 40.790 0.293 1 506 111 113 ASP N N 127.675 0.172 1 507 112 114 ASP H H 7.584 0.004 1 508 112 114 ASP C C 175.026 0.125 1 509 112 114 ASP CA C 54.627 0.293 1 510 112 114 ASP CB C 43.013 0.293 1 511 112 114 ASP N N 117.355 0.172 1 512 113 115 PHE H H 9.183 0.004 1 513 113 115 PHE C C 175.270 0.125 1 514 113 115 PHE CA C 56.626 0.293 1 515 113 115 PHE CB C 40.412 0.293 1 516 113 115 PHE N N 121.565 0.172 1 517 114 116 VAL H H 8.841 0.004 1 518 114 116 VAL C C 174.872 0.125 1 519 114 116 VAL CA C 62.257 0.293 1 520 114 116 VAL CB C 32.930 0.293 1 521 114 116 VAL N N 122.312 0.172 1 522 115 117 LEU H H 9.700 0.004 1 523 115 117 LEU C C 175.750 0.125 1 524 115 117 LEU CA C 56.535 0.293 1 525 115 117 LEU CB C 41.701 0.293 1 526 115 117 LEU N N 131.640 0.172 1 527 116 118 THR H H 8.933 0.004 1 528 116 118 THR C C 172.545 0.125 1 529 116 118 THR CA C 58.172 0.293 1 530 116 118 THR CB C 70.292 0.293 1 531 116 118 THR N N 115.643 0.172 1 532 117 119 PRO C C 177.263 0.125 1 533 117 119 PRO CA C 63.597 0.293 1 534 117 119 PRO CB C 31.193 0.293 1 535 118 120 LYS H H 8.057 0.004 1 536 118 120 LYS C C 176.914 0.125 1 537 118 120 LYS CA C 58.606 0.293 1 538 118 120 LYS CB C 32.563 0.293 1 539 118 120 LYS N N 122.302 0.172 1 540 119 121 ALA H H 8.091 0.004 1 541 119 121 ALA C C 177.310 0.125 1 542 119 121 ALA CA C 51.041 0.293 1 543 119 121 ALA CB C 19.576 0.293 1 544 119 121 ALA N N 121.779 0.172 1 545 120 122 SER C C 174.076 0.125 1 546 120 122 SER CA C 58.455 0.293 1 547 120 122 SER CB C 63.725 0.293 1 548 121 123 ASN H H 8.076 0.004 1 549 121 123 ASN C C 176.232 0.125 1 550 121 123 ASN CA C 55.249 0.293 1 551 121 123 ASN CB C 40.327 0.293 1 552 121 123 ASN N N 126.244 0.172 1 553 122 124 GLY H H 8.096 0.004 1 554 122 124 GLY C C 174.278 0.125 1 555 122 124 GLY CA C 45.410 0.293 1 556 122 124 GLY N N 113.099 0.172 1 557 123 125 ASN C C 175.013 0.125 1 558 123 125 ASN CA C 54.573 0.293 1 559 123 125 ASN CB C 39.401 0.293 1 560 124 126 LEU H H 7.789 0.004 1 561 124 126 LEU C C 176.269 0.125 1 562 124 126 LEU CA C 54.332 0.293 1 563 124 126 LEU CB C 42.029 0.293 1 564 124 126 LEU N N 118.344 0.172 1 565 125 127 LYS H H 8.832 0.004 1 566 125 127 LYS C C 176.845 0.125 1 567 125 127 LYS CA C 57.525 0.293 1 568 125 127 LYS CB C 33.150 0.293 1 569 125 127 LYS N N 122.744 0.172 1 570 126 128 GLN H H 7.658 0.004 1 571 126 128 GLN C C 173.324 0.125 1 572 126 128 GLN CA C 55.994 0.293 1 573 126 128 GLN CB C 32.886 0.293 1 574 126 128 GLN N N 115.304 0.172 1 575 127 129 PHE H H 9.028 0.004 1 576 127 129 PHE C C 173.032 0.125 1 577 127 129 PHE CA C 55.137 0.293 1 578 127 129 PHE CB C 41.939 0.293 1 579 127 129 PHE N N 127.449 0.172 1 580 128 130 THR H H 9.010 0.004 1 581 128 130 THR C C 171.887 0.125 1 582 128 130 THR CA C 59.315 0.293 1 583 128 130 THR CB C 70.508 0.293 1 584 128 130 THR N N 120.627 0.172 1 585 129 131 ILE H H 8.623 0.004 1 586 129 131 ILE C C 173.310 0.125 1 587 129 131 ILE CA C 59.942 0.293 1 588 129 131 ILE CB C 40.273 0.293 1 589 129 131 ILE N N 118.748 0.172 1 590 130 132 ASN H H 8.868 0.004 1 591 130 132 ASN C C 174.417 0.125 1 592 130 132 ASN CA C 52.271 0.293 1 593 130 132 ASN CB C 40.623 0.293 1 594 130 132 ASN N N 128.939 0.172 1 595 131 133 VAL H H 8.372 0.004 1 596 131 133 VAL C C 175.274 0.125 1 597 131 133 VAL CA C 57.661 0.293 1 598 131 133 VAL CB C 33.170 0.293 1 599 131 133 VAL N N 123.261 0.172 1 600 132 134 GLY H H 8.922 0.004 1 601 132 134 GLY C C 175.972 0.125 1 602 132 134 GLY CA C 44.874 0.293 1 603 132 134 GLY N N 112.787 0.172 1 604 133 135 ARG H H 9.151 0.004 1 605 133 135 ARG C C 176.022 0.125 1 606 133 135 ARG CA C 59.267 0.293 1 607 133 135 ARG CB C 29.046 0.293 1 608 133 135 ARG N N 121.197 0.172 1 609 134 136 ASP H H 8.131 0.004 1 610 134 136 ASP C C 177.312 0.125 1 611 134 136 ASP CA C 52.856 0.293 1 612 134 136 ASP CB C 39.970 0.293 1 613 134 136 ASP N N 114.446 0.172 1 614 135 137 GLY H H 8.054 0.004 1 615 135 137 GLY C C 173.782 0.125 1 616 135 137 GLY CA C 45.449 0.293 1 617 135 137 GLY N N 109.512 0.172 1 618 136 138 THR H H 7.452 0.004 1 619 136 138 THR C C 173.291 0.125 1 620 136 138 THR CA C 63.607 0.293 1 621 136 138 THR CB C 67.795 0.293 1 622 136 138 THR N N 117.858 0.172 1 623 137 139 ILE H H 8.620 0.004 1 624 137 139 ILE C C 173.274 0.125 1 625 137 139 ILE CA C 60.959 0.293 1 626 137 139 ILE CB C 37.279 0.293 1 627 137 139 ILE N N 130.941 0.172 1 628 138 140 HIS H H 8.059 0.004 1 629 138 140 HIS C C 177.159 0.125 1 630 138 140 HIS CA C 59.125 0.293 1 631 138 140 HIS CB C 30.400 0.293 1 632 138 140 HIS N N 123.762 0.172 1 633 139 141 GLN H H 8.042 0.004 1 634 139 141 GLN C C 174.312 0.125 1 635 139 141 GLN CA C 54.815 0.293 1 636 139 141 GLN CB C 31.966 0.293 1 637 139 141 GLN N N 114.094 0.172 1 638 140 142 PHE H H 8.515 0.004 1 639 140 142 PHE C C 173.429 0.125 1 640 140 142 PHE CA C 57.461 0.293 1 641 140 142 PHE CB C 40.082 0.293 1 642 140 142 PHE N N 116.509 0.172 1 643 141 143 SER H H 9.379 0.004 1 644 141 143 SER C C 171.998 0.125 1 645 141 143 SER CA C 57.329 0.293 1 646 141 143 SER CB C 66.832 0.293 1 647 141 143 SER N N 115.714 0.172 1 648 142 144 ALA H H 9.040 0.004 1 649 142 144 ALA C C 175.762 0.125 1 650 142 144 ALA CA C 51.303 0.293 1 651 142 144 ALA CB C 23.238 0.293 1 652 142 144 ALA N N 122.362 0.172 1 653 143 145 VAL H H 8.652 0.004 1 654 143 145 VAL C C 176.405 0.125 1 655 143 145 VAL CA C 61.552 0.293 1 656 143 145 VAL CB C 32.892 0.293 1 657 143 145 VAL N N 122.944 0.172 1 658 144 146 GLU H H 8.606 0.004 1 659 144 146 GLU C C 177.345 0.125 1 660 144 146 GLU CA C 55.780 0.293 1 661 144 146 GLU CB C 31.463 0.293 1 662 144 146 GLU N N 127.257 0.172 1 663 145 147 GLN H H 8.448 0.004 1 664 145 147 GLN C C 175.878 0.125 1 665 145 147 GLN CA C 58.353 0.293 1 666 145 147 GLN CB C 27.614 0.293 1 667 145 147 GLN N N 118.381 0.172 1 668 146 148 ASP H H 8.110 0.004 1 669 146 148 ASP C C 176.278 0.125 1 670 146 148 ASP CA C 53.741 0.293 1 671 146 148 ASP CB C 39.333 0.293 1 672 146 148 ASP N N 118.211 0.172 1 673 147 149 ASP H H 8.220 0.004 1 674 147 149 ASP C C 174.797 0.125 1 675 147 149 ASP CA C 56.653 0.293 1 676 147 149 ASP CB C 39.062 0.293 1 677 147 149 ASP N N 113.303 0.172 1 678 148 150 GLN H H 7.746 0.004 1 679 148 150 GLN C C 175.542 0.125 1 680 148 150 GLN CA C 57.190 0.293 1 681 148 150 GLN CB C 29.372 0.293 1 682 148 150 GLN N N 119.153 0.172 1 683 149 151 ARG H H 8.924 0.004 1 684 149 151 ARG C C 175.275 0.125 1 685 149 151 ARG CA C 54.508 0.293 1 686 149 151 ARG CB C 32.280 0.293 1 687 149 151 ARG N N 128.495 0.172 1 688 150 152 SER H H 8.960 0.004 1 689 150 152 SER C C 172.023 0.125 1 690 150 152 SER CA C 57.092 0.293 1 691 150 152 SER CB C 64.824 0.293 1 692 150 152 SER N N 121.519 0.172 1 693 151 153 SER H H 8.797 0.004 1 694 151 153 SER C C 172.312 0.125 1 695 151 153 SER CA C 56.990 0.293 1 696 151 153 SER CB C 64.792 0.293 1 697 151 153 SER N N 119.291 0.172 1 698 152 154 TYR H H 9.084 0.004 1 699 152 154 TYR C C 174.936 0.125 1 700 152 154 TYR CA C 56.308 0.293 1 701 152 154 TYR CB C 38.861 0.293 1 702 152 154 TYR N N 125.499 0.172 1 703 153 155 GLN H H 8.681 0.004 1 704 153 155 GLN C C 175.555 0.125 1 705 153 155 GLN CA C 54.295 0.293 1 706 153 155 GLN CB C 30.751 0.293 1 707 153 155 GLN N N 122.570 0.172 1 708 154 156 LEU H H 8.463 0.004 1 709 154 156 LEU C C 177.647 0.125 1 710 154 156 LEU CA C 56.955 0.293 1 711 154 156 LEU CB C 41.897 0.293 1 712 154 156 LEU N N 128.946 0.172 1 713 155 157 LYS H H 9.184 0.004 1 714 155 157 LYS C C 176.416 0.125 1 715 155 157 LYS CA C 57.206 0.293 1 716 155 157 LYS CB C 31.882 0.293 1 717 155 157 LYS N N 126.956 0.172 1 718 156 158 SER H H 7.217 0.004 1 719 156 158 SER C C 172.134 0.125 1 720 156 158 SER CA C 57.772 0.293 1 721 156 158 SER CB C 64.181 0.293 1 722 156 158 SER N N 110.884 0.172 1 723 157 159 GLN H H 8.693 0.004 1 724 157 159 GLN C C 174.482 0.125 1 725 157 159 GLN CA C 55.727 0.293 1 726 157 159 GLN CB C 30.316 0.293 1 727 157 159 GLN N N 125.558 0.172 1 728 158 160 GLN H H 9.153 0.004 1 729 158 160 GLN C C 175.227 0.125 1 730 158 160 GLN CA C 54.503 0.293 1 731 158 160 GLN CB C 30.152 0.293 1 732 158 160 GLN N N 126.531 0.172 1 733 159 161 ASN C C 175.938 0.125 1 734 159 161 ASN CA C 53.080 0.293 1 735 159 161 ASN CB C 38.296 0.293 1 736 160 162 GLY H H 8.374 0.004 1 737 160 162 GLY C C 173.202 0.125 1 738 160 162 GLY CA C 44.811 0.293 1 739 160 162 GLY N N 111.324 0.172 1 740 161 163 ALA C C 177.265 0.125 1 741 161 163 ALA CA C 52.883 0.293 1 742 161 163 ALA CB C 18.449 0.293 1 743 162 164 VAL H H 8.093 0.004 1 744 162 164 VAL C C 175.057 0.125 1 745 162 164 VAL CA C 60.614 0.293 1 746 162 164 VAL CB C 34.372 0.293 1 747 162 164 VAL N N 119.874 0.172 1 748 163 165 ASP H H 8.073 0.004 1 749 163 165 ASP C C 176.268 0.125 1 750 163 165 ASP CA C 54.266 0.293 1 751 163 165 ASP CB C 41.643 0.293 1 752 163 165 ASP N N 125.969 0.172 1 753 164 166 ALA H H 8.466 0.004 1 754 164 166 ALA C C 179.760 0.125 1 755 164 166 ALA CA C 54.536 0.293 1 756 164 166 ALA CB C 17.915 0.293 1 757 164 166 ALA N N 127.371 0.172 1 758 165 167 ALA H H 8.282 0.004 1 759 165 167 ALA C C 179.460 0.125 1 760 165 167 ALA CA C 53.715 0.293 1 761 165 167 ALA CB C 17.604 0.293 1 762 165 167 ALA N N 120.146 0.172 1 763 166 168 LYS H H 7.293 0.004 1 764 166 168 LYS C C 176.525 0.125 1 765 166 168 LYS CA C 55.347 0.293 1 766 166 168 LYS CB C 29.477 0.293 1 767 166 168 LYS N N 115.567 0.172 1 768 167 169 PHE H H 7.010 0.004 1 769 167 169 PHE C C 173.984 0.125 1 770 167 169 PHE CA C 55.130 0.293 1 771 167 169 PHE CB C 38.138 0.293 1 772 167 169 PHE N N 116.378 0.172 1 773 168 170 THR H H 6.891 0.004 1 774 168 170 THR C C 172.510 0.125 1 775 168 170 THR CA C 59.830 0.293 1 776 168 170 THR CB C 70.681 0.293 1 777 168 170 THR N N 111.001 0.172 1 778 172 174 PRO C C 175.830 0.125 1 779 172 174 PRO CA C 61.867 0.293 1 780 172 174 PRO CB C 31.485 0.293 1 781 173 175 GLN H H 8.243 0.004 1 782 173 175 GLN C C 177.272 0.125 1 783 173 175 GLN CA C 57.456 0.293 1 784 173 175 GLN CB C 27.865 0.293 1 785 173 175 GLN N N 121.181 0.172 1 786 174 176 GLY H H 8.624 0.004 1 787 174 176 GLY C C 174.170 0.125 1 788 174 176 GLY CA C 45.109 0.293 1 789 174 176 GLY N N 112.554 0.172 1 790 175 177 VAL H H 7.281 0.004 1 791 175 177 VAL C C 176.169 0.125 1 792 175 177 VAL CA C 61.942 0.293 1 793 175 177 VAL CB C 31.802 0.293 1 794 175 177 VAL N N 120.687 0.172 1 795 176 178 THR H H 8.307 0.004 1 796 176 178 THR C C 173.527 0.125 1 797 176 178 THR CA C 61.021 0.293 1 798 176 178 THR CB C 69.476 0.293 1 799 176 178 THR N N 124.216 0.172 1 800 177 179 VAL H H 8.750 0.004 1 801 177 179 VAL C C 175.757 0.125 1 802 177 179 VAL CA C 61.187 0.293 1 803 177 179 VAL CB C 32.977 0.293 1 804 177 179 VAL N N 127.781 0.172 1 805 178 180 ASP H H 9.113 0.004 1 806 178 180 ASP C C 174.481 0.125 1 807 178 180 ASP CA C 52.835 0.293 1 808 178 180 ASP CB C 40.335 0.293 1 809 178 180 ASP N N 130.063 0.172 1 810 179 181 ASP H H 8.439 0.004 1 811 179 181 ASP C C 176.647 0.125 1 812 179 181 ASP CA C 53.054 0.293 1 813 179 181 ASP CB C 39.834 0.293 1 814 179 181 ASP N N 124.882 0.172 1 815 180 182 GLN H H 8.746 0.004 1 816 180 182 GLN C C 177.036 0.125 1 817 180 182 GLN CA C 55.471 0.293 1 818 180 182 GLN CB C 27.003 0.293 1 819 180 182 GLN N N 126.106 0.172 1 820 181 183 ARG H H 7.721 0.004 1 821 181 183 ARG C C 176.638 0.125 1 822 181 183 ARG CA C 56.910 0.293 1 823 181 183 ARG CB C 28.683 0.293 1 824 181 183 ARG N N 120.216 0.172 1 825 182 184 LYS H H 7.662 0.004 1 826 182 184 LYS C C 176.642 0.125 1 827 182 184 LYS CA C 55.921 0.293 1 828 182 184 LYS CB C 31.938 0.293 1 829 182 184 LYS N N 120.563 0.172 1 830 183 185 LEU H H 8.091 0.004 1 831 183 185 LEU C C 177.372 0.125 1 832 183 185 LEU CA C 55.240 0.293 1 833 183 185 LEU CB C 41.704 0.293 1 834 183 185 LEU N N 123.473 0.172 1 835 184 186 GLU H H 8.367 0.004 1 836 184 186 GLU C C 176.207 0.125 1 837 184 186 GLU CA C 56.507 0.293 1 838 184 186 GLU CB C 29.922 0.293 1 839 184 186 GLU N N 121.672 0.172 1 stop_ save_