data_4341 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme ; _BMRB_accession_number 4341 _BMRB_flat_file_name bmr4341.str _Entry_type original _Submission_date 1999-05-04 _Accession_date 1999-05-04 _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 Vathyam Surekha . . 2 Byrd R. Andrew . 3 Miller Anne-Frances . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 117 "13C chemical shifts" 381 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-11-30 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4315 'Oxidized Fe-superoxide Dismutase' stop_ _Original_release_date 1999-11-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Vathyam, S., Byrd, R. A., and Miller, A-F., "Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme," J. Biomol. NMR 14, 293-294 (1999). ; _Citation_title ; Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99410897 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vathyam Surekha . . 2 Byrd R. Andrew . 3 Miller Anne-Frances . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 293 _Page_last 294 _Year 1999 _Details . loop_ _Keyword metalloenzyme paramagnetic reduced 'superoxide dismutase' stop_ save_ ################################## # Molecular system description # ################################## save_Fe-SOD _Saveframe_category molecular_system _Mol_system_name 'Iron-containing superoxide dismutase' _Abbreviation_common Fe-SOD _Enzyme_commission_number 1.15.1.1 loop_ _Mol_system_component_name _Mol_label 'Fe(II)SOD monomer 1' $Fe-SOD_peptide 'Fe(II)SOD monomer 2' $Fe-SOD_peptide 'Fe(II) monomer 1' $FE 'Fe(II) monomer 2' $FE 'H2O monomer 1' $HOH 'H2O monomer 2' $HOH stop_ _System_molecular_weight 42000 _System_physical_state native _System_oligomer_state dimer _System_paramagnetic yes _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Fe(II)SOD monomer 1' 1 'Fe(II)SOD monomer 2' 3 'H2O monomer 1' 3 'H2O monomer 2' stop_ loop_ _Biological_function ; Disproportionation of superoxide radicals. ; stop_ _Database_query_date . _Details ; This is the first substantial backbone assignment of a mono-nuclear non-heme iron-containing redox-active enzyme. ; save_ ######################## # Monomeric polymers # ######################## save_Fe-SOD_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Fe-superoxide dismutase' _Abbreviation_common FeSOD _Molecular_mass 21000 _Mol_thiol_state . _Details ; Relatively large by solution NMR standards, one paramagnetic Fe(II) per monomer. ; ############################## # Polymer residue sequence # ############################## _Residue_count 192 _Mol_residue_sequence ; SFELPALPYAKDALAPHISA ETIEYHYGKHHQTYVTNLNN LIKGTAFEGKSLEEIIRSSE GGVFNNAAQVWNHWFYWNCL APNAGGEPTGKVAEAIAASF GSFADFKAQFTDAAIKNFGS GWTWLVKNSDGKLAIVSTSN AGTPLTTDATPLLTVDVWEH AYYIDYRNARPGYLEHFWAL VNWEFVAKNLAA ; loop_ _Residue_seq_code _Residue_label 1 SER 2 PHE 3 GLU 4 LEU 5 PRO 6 ALA 7 LEU 8 PRO 9 TYR 10 ALA 11 LYS 12 ASP 13 ALA 14 LEU 15 ALA 16 PRO 17 HIS 18 ILE 19 SER 20 ALA 21 GLU 22 THR 23 ILE 24 GLU 25 TYR 26 HIS 27 TYR 28 GLY 29 LYS 30 HIS 31 HIS 32 GLN 33 THR 34 TYR 35 VAL 36 THR 37 ASN 38 LEU 39 ASN 40 ASN 41 LEU 42 ILE 43 LYS 44 GLY 45 THR 46 ALA 47 PHE 48 GLU 49 GLY 50 LYS 51 SER 52 LEU 53 GLU 54 GLU 55 ILE 56 ILE 57 ARG 58 SER 59 SER 60 GLU 61 GLY 62 GLY 63 VAL 64 PHE 65 ASN 66 ASN 67 ALA 68 ALA 69 GLN 70 VAL 71 TRP 72 ASN 73 HIS 74 TRP 75 PHE 76 TYR 77 TRP 78 ASN 79 CYS 80 LEU 81 ALA 82 PRO 83 ASN 84 ALA 85 GLY 86 GLY 87 GLU 88 PRO 89 THR 90 GLY 91 LYS 92 VAL 93 ALA 94 GLU 95 ALA 96 ILE 97 ALA 98 ALA 99 SER 100 PHE 101 GLY 102 SER 103 PHE 104 ALA 105 ASP 106 PHE 107 LYS 108 ALA 109 GLN 110 PHE 111 THR 112 ASP 113 ALA 114 ALA 115 ILE 116 LYS 117 ASN 118 PHE 119 GLY 120 SER 121 GLY 122 TRP 123 THR 124 TRP 125 LEU 126 VAL 127 LYS 128 ASN 129 SER 130 ASP 131 GLY 132 LYS 133 LEU 134 ALA 135 ILE 136 VAL 137 SER 138 THR 139 SER 140 ASN 141 ALA 142 GLY 143 THR 144 PRO 145 LEU 146 THR 147 THR 148 ASP 149 ALA 150 THR 151 PRO 152 LEU 153 LEU 154 THR 155 VAL 156 ASP 157 VAL 158 TRP 159 GLU 160 HIS 161 ALA 162 TYR 163 TYR 164 ILE 165 ASP 166 TYR 167 ARG 168 ASN 169 ALA 170 ARG 171 PRO 172 GLY 173 TYR 174 LEU 175 GLU 176 HIS 177 PHE 178 TRP 179 ALA 180 LEU 181 VAL 182 ASN 183 TRP 184 GLU 185 PHE 186 VAL 187 ALA 188 LYS 189 ASN 190 LEU 191 ALA 192 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 4315 "Fe-superoxide dismutase" 100.00 192 100.00 100.00 8.40e-137 PDB 1ISA "Structure-Function In E. Coli Iron Superoxide Dismutase: Comparisons With The Manganese Enzyme From T. Thermophilus" 100.00 192 99.48 99.48 2.21e-135 PDB 1ISB "Structure-Function In E. Coli Iron Superoxide Dismutase: Comparisons With The Manganese Enzyme From T. Thermophilus" 100.00 192 99.48 99.48 2.21e-135 PDB 1ISC "Structure-Function In E. Coli Iron Superoxide Dismutase: Comparisons With The Manganese Enzyme From T. Thermophilus" 100.00 192 99.48 99.48 2.21e-135 PDB 1ZA5 Q69h-Fesod 100.00 192 98.96 98.96 2.32e-134 PDB 2BKB Q69e-Fesod 100.00 192 98.96 99.48 8.86e-135 PDB 2NYB "Crystal Structure Of E.Coli Iron Superoxide Dismutase Q69e At 1.1 Angstrom Resolution" 100.00 192 98.96 99.48 8.86e-135 DBJ BAA15422 "superoxide dismutase, Fe [Escherichia coli str. K12 substr. W3110]" 100.00 193 99.48 99.48 2.19e-135 DBJ BAA84485 "iron-containing superoxide dismutase [Escherichia coli]" 78.65 151 99.34 99.34 1.06e-102 DBJ BAA84490 "iron-containing superoxide disumutase [Escherichia coli]" 78.65 151 99.34 99.34 1.06e-102 DBJ BAB35788 "superoxide dismutase [Escherichia coli O157:H7 str. Sakai]" 100.00 193 99.48 99.48 2.19e-135 DBJ BAG77304 "superoxide dismutase [Escherichia coli SE11]" 100.00 193 99.48 99.48 2.19e-135 EMBL CAP76155 "Superoxide dismutase [Fe] [Escherichia coli LF82]" 100.00 193 99.48 99.48 2.19e-135 EMBL CAQ32133 "superoxide dismutase (Fe) [Escherichia coli BL21(DE3)]" 100.00 193 99.48 99.48 2.19e-135 EMBL CAQ88908 "superoxide dismutase, Fe [Escherichia fergusonii ATCC 35469]" 99.48 193 97.38 97.91 2.76e-132 EMBL CAQ98565 "superoxide dismutase, Fe [Escherichia coli IAI1]" 100.00 193 99.48 99.48 2.19e-135 EMBL CAR03017 "superoxide dismutase, Fe [Escherichia coli S88]" 100.00 193 99.48 99.48 2.19e-135 GB AAA24637 "superoxide dismutase (sodB) [Escherichia coli]" 100.00 193 99.48 99.48 2.19e-135 GB AAC74728 "superoxide dismutase, Fe [Escherichia coli str. K-12 substr. MG1655]" 100.00 193 99.48 99.48 2.19e-135 GB AAG56645 "superoxide dismutase, iron [Escherichia coli O157:H7 str. EDL933]" 100.00 193 99.48 99.48 2.19e-135 GB AAN43263 "superoxide dismutase [Shigella flexneri 2a str. 301]" 100.00 193 99.48 99.48 2.19e-135 GB AAN80510 "Superoxide dismutase (Fe) [Escherichia coli CFT073]" 100.00 193 99.48 99.48 2.19e-135 REF NP_310392 "superoxide dismutase [Escherichia coli O157:H7 str. Sakai]" 100.00 193 99.48 99.48 2.19e-135 REF NP_416173 "superoxide dismutase, Fe [Escherichia coli str. K-12 substr. MG1655]" 100.00 193 99.48 99.48 2.19e-135 REF NP_707556 "superoxide dismutase [Shigella flexneri 2a str. 301]" 100.00 193 99.48 99.48 2.19e-135 REF WP_000007270 "superoxide dismutase [Fe] [Escherichia coli]" 100.00 193 98.96 98.96 1.26e-134 REF WP_000007272 "superoxide dismutase [Shigella dysenteriae]" 100.00 193 98.44 98.44 7.41e-134 SP P0AGD3 "RecName: Full=Superoxide dismutase [Fe]" 100.00 193 99.48 99.48 2.19e-135 SP P0AGD4 "RecName: Full=Superoxide dismutase [Fe]" 100.00 193 99.48 99.48 2.19e-135 SP P0AGD5 "RecName: Full=Superoxide dismutase [Fe]" 100.00 193 99.48 99.48 2.19e-135 SP P0AGD6 "RecName: Full=Superoxide dismutase [Fe]" 100.00 193 99.48 99.48 2.19e-135 stop_ save_ ############# # Ligands # ############# save_FE _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FE (III) ION' _BMRB_code FE _PDB_code FE _Molecular_mass 55.845 _Mol_charge 3 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 3 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $Fe-SOD_peptide 'E. coli' 562 Eubacteria . Escherichia coli sodB 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 $Fe-SOD_peptide 'recombinant technology' . . . . . 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 $Fe-SOD_peptide 1.57 mM '[U-99% 2H, U-99% 13C, U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 1.6 loop_ _Task 'processed NMR data' stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'made peak assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity-Plus _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample_1 save_ save_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample_1 save_ save_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.46 0.06 na temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Fe(II)SOD monomer 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 SER C C 170.64 . 1 2 . 1 SER CA C 56.815 . 1 3 . 1 SER CB C 62.535 . 1 4 . 2 PHE N N 120.3 . 1 5 . 2 PHE H H 9.282 . 1 6 . 2 PHE C C 175.06 . 1 7 . 2 PHE CA C 58.505 . 1 8 . 2 PHE CB C 39.485 . 1 9 . 3 GLU N N 120.08 . 1 10 . 3 GLU H H 8.473 . 1 11 . 3 GLU C C 175.05 . 1 12 . 3 GLU CA C 53.485 . 1 13 . 3 GLU CB C 31.855 . 1 14 . 4 LEU N N 124.75 . 1 15 . 4 LEU H H 8.569 . 1 16 . 4 LEU CA C 51.895 . 1 17 . 4 LEU CB C 41.735 . 1 18 . 5 PRO C C 177.12 . 1 19 . 5 PRO CA C 62.035 . 1 20 . 5 PRO CB C 30.885 . 1 21 . 6 ALA N N 125.94 . 1 22 . 6 ALA H H 8.642 . 1 23 . 6 ALA C C 177.75 . 1 24 . 6 ALA CA C 52.015 . 1 25 . 6 ALA CB C 17.995 . 1 26 . 7 LEU N N 125.98 . 1 27 . 7 LEU H H 8.447 . 1 28 . 7 LEU CA C 52.705 . 1 29 . 7 LEU CB C 42.055 . 1 30 . 8 PRO C C 173.93 . 1 31 . 8 PRO CA C 62.825 . 1 32 . 8 PRO CB C 30.645 . 1 33 . 9 TYR N N 114.24 . 1 34 . 9 TYR H H 6.484 . 1 35 . 9 TYR C C 174.77 . 1 36 . 9 TYR CA C 53.105 . 1 37 . 9 TYR CB C 39.225 . 1 38 . 10 ALA N N 119.98 . 1 39 . 10 ALA H H 8.826 . 1 40 . 10 ALA C C 179.2 . 1 41 . 10 ALA CA C 52.155 . 1 42 . 10 ALA CB C 19.725 . 1 43 . 11 LYS N N 116.88 . 1 44 . 11 LYS H H 8.97 . 1 45 . 11 LYS C C 175.56 . 1 46 . 11 LYS CA C 59.625 . 1 47 . 11 LYS CB C 32.335 . 1 48 . 12 ASP N N 111.62 . 1 49 . 12 ASP H H 8.386 . 1 50 . 12 ASP C C 178.94 . 1 51 . 12 ASP CA C 52.385 . 1 52 . 12 ASP CB C 40.315 . 1 53 . 13 ALA N N 120.5 . 1 54 . 13 ALA H H 8.368 . 1 55 . 13 ALA C C 178.45 . 1 56 . 13 ALA CA C 54.325 . 1 57 . 13 ALA CB C 20.585 . 1 58 . 14 LEU N N 114.62 . 1 59 . 14 LEU H H 8.994 . 1 60 . 14 LEU C C 177 . 1 61 . 14 LEU CA C 52.995 . 1 62 . 14 LEU CB C 39.395 . 1 63 . 15 ALA N N 125.93 . 1 64 . 15 ALA H H 7.456 . 1 65 . 15 ALA CA C 51.785 . 1 66 . 15 ALA CB C 16.955 . 1 67 . 16 PRO C C 174.83 . 1 68 . 16 PRO CA C 62.935 . 1 69 . 16 PRO CB C 33.315 . 1 70 . 17 HIS N N 126.46 . 1 71 . 17 HIS H H 7.933 . 1 72 . 17 HIS CA C 58.505 . 1 73 . 17 HIS CB C 31.075 . 1 74 . 18 ILE C C 176.38 . 1 75 . 18 ILE CA C 62.435 . 1 76 . 18 ILE CB C 41.935 . 1 77 . 19 SER N N 124.38 . 1 78 . 19 SER H H 9.43 . 1 79 . 19 SER C C 175.46 . 1 80 . 19 SER CA C 59.045 . 1 81 . 19 SER CB C 65.375 . 1 82 . 20 ALA N N 121.73 . 1 83 . 20 ALA H H 9.437 . 1 84 . 20 ALA C C 180.81 . 1 85 . 20 ALA CA C 54.685 . 1 86 . 20 ALA CB C 18.075 . 1 87 . 21 GLU N N 119.5 . 1 88 . 21 GLU H H 8.592 . 1 89 . 21 GLU CA C 59.865 . 1 90 . 21 GLU CB C 28.865 . 1 91 . 23 ILE CA C 67.785 . 1 92 . 23 ILE CB C 36.545 . 1 93 . 24 GLU N N 123.08 . 1 94 . 24 GLU H H 10.271 . 1 95 . 24 GLU CA C 61.025 . 1 96 . 24 GLU CB C 29.185 . 1 97 . 34 TYR C C 176.42 . 1 98 . 34 TYR CA C 59.955 . 1 99 . 34 TYR CB C 35.605 . 1 100 . 35 VAL N N 117.43 . 1 101 . 35 VAL H H 6.535 . 1 102 . 35 VAL C C 176.2 . 1 103 . 35 VAL CA C 65.995 . 1 104 . 35 VAL CB C 30.425 . 1 105 . 36 THR N N 116.58 . 1 106 . 36 THR H H 8.101 . 1 107 . 36 THR C C 176.34 . 1 108 . 36 THR CA C 65.845 . 1 109 . 36 THR CB C 68.605 . 1 110 . 37 ASN N N 119.07 . 1 111 . 37 ASN H H 8.569 . 1 112 . 37 ASN CA C 54.705 . 1 113 . 37 ASN CB C 35.905 . 1 114 . 38 LEU N N 119.76 . 1 115 . 38 LEU H H 7.823 . 1 116 . 38 LEU C C 177.26 . 1 117 . 38 LEU CA C 57.925 . 1 118 . 38 LEU CB C 40.765 . 1 119 . 39 ASN N N 115.39 . 1 120 . 39 ASN H H 8.187 . 1 121 . 39 ASN C C 178.34 . 1 122 . 39 ASN CA C 55.205 . 1 123 . 39 ASN CB C 37.235 . 1 124 . 40 ASN N N 116.87 . 1 125 . 40 ASN H H 7.98 . 1 126 . 40 ASN C C 177.48 . 1 127 . 40 ASN CA C 55.305 . 1 128 . 40 ASN CB C 37.945 . 1 129 . 41 LEU N N 118.96 . 1 130 . 41 LEU H H 8.133 . 1 131 . 41 LEU C C 179.38 . 1 132 . 41 LEU CA C 56.785 . 1 133 . 41 LEU CB C 43.115 . 1 134 . 42 ILE N N 106.89 . 1 135 . 42 ILE H H 7.829 . 1 136 . 42 ILE C C 177.93 . 1 137 . 42 ILE CA C 60.845 . 1 138 . 42 ILE CB C 38.465 . 1 139 . 43 LYS N N 126.18 . 1 140 . 43 LYS H H 7.211 . 1 141 . 43 LYS C C 177.74 . 1 142 . 43 LYS CA C 57.705 . 1 143 . 43 LYS CB C 31.145 . 1 144 . 44 GLY N N 114.68 . 1 145 . 44 GLY H H 9.398 . 1 146 . 44 GLY C C 174.41 . 1 147 . 44 GLY CA C 45.735 . 1 148 . 45 THR N N 109.46 . 1 149 . 45 THR H H 7.968 . 1 150 . 45 THR C C 176.31 . 1 151 . 45 THR CA C 60.235 . 1 152 . 45 THR CB C 73.456 . 1 153 . 46 ALA N N 121.7 . 1 154 . 46 ALA H H 8.835 . 1 155 . 46 ALA C C 178.05 . 1 156 . 46 ALA CA C 52.915 . 1 157 . 46 ALA CB C 17.455 . 1 158 . 47 PHE N N 113.72 . 1 159 . 47 PHE H H 8.015 . 1 160 . 47 PHE C C 176.54 . 1 161 . 47 PHE CA C 58.935 . 1 162 . 47 PHE CB C 38.885 . 1 163 . 48 GLU N N 118.26 . 1 164 . 48 GLU H H 7.372 . 1 165 . 48 GLU C C 176.98 . 1 166 . 48 GLU CA C 58.725 . 1 167 . 48 GLU CB C 28.685 . 1 168 . 49 GLY N N 111.42 . 1 169 . 49 GLY H H 8.354 . 1 170 . 49 GLY C C 174.34 . 1 171 . 49 GLY CA C 44.755 . 1 172 . 50 LYS N N 119.72 . 1 173 . 50 LYS H H 7.462 . 1 174 . 50 LYS C C 176.28 . 1 175 . 50 LYS CA C 54.395 . 1 176 . 50 LYS CB C 33.545 . 1 177 . 51 SER N N 116.06 . 1 178 . 51 SER H H 8.826 . 1 179 . 51 SER C C 174.61 . 1 180 . 51 SER CA C 57.075 . 1 181 . 51 SER CB C 64.725 . 1 182 . 52 LEU N N 121.18 . 1 183 . 52 LEU H H 8.945 . 1 184 . 52 LEU C C 178.34 . 1 185 . 52 LEU CA C 57.655 . 1 186 . 52 LEU CB C 40.985 . 1 187 . 53 GLU N N 115.67 . 1 188 . 53 GLU H H 9.149 . 1 189 . 53 GLU C C 177.91 . 1 190 . 53 GLU CA C 60.955 . 1 191 . 53 GLU CB C 27.375 . 1 192 . 54 GLU N N 117.32 . 1 193 . 54 GLU H H 7.543 . 1 194 . 54 GLU CA C 58.595 . 1 195 . 54 GLU CB C 29.465 . 1 196 . 56 ILE C C 175.9 . 1 197 . 56 ILE CA C 65.635 . 1 198 . 56 ILE CB C 37.195 . 1 199 . 57 ARG N N 112.9 . 1 200 . 57 ARG H H 7.384 . 1 201 . 57 ARG C C 176.37 . 1 202 . 57 ARG CA C 57.805 . 1 203 . 57 ARG CB C 30.145 . 1 204 . 58 SER N N 111.01 . 1 205 . 58 SER H H 7.737 . 1 206 . 58 SER C C 173 . 1 207 . 58 SER CA C 57.695 . 1 208 . 58 SER CB C 65.055 . 1 209 . 59 SER N N 114.83 . 1 210 . 59 SER H H 7.512 . 1 211 . 59 SER C C 173.06 . 1 212 . 59 SER CA C 57.355 . 1 213 . 59 SER CB C 67.995 . 1 214 . 60 GLU N N 115.49 . 1 215 . 60 GLU H H 8.736 . 1 216 . 60 GLU C C 177.08 . 1 217 . 60 GLU CA C 54.345 . 1 218 . 60 GLU CB C 33.255 . 1 219 . 61 GLY N N 109.21 . 1 220 . 61 GLY H H 9.112 . 1 221 . 61 GLY C C 174.94 . 1 222 . 61 GLY CA C 46.525 . 1 223 . 62 GLY N N 111.78 . 1 224 . 62 GLY H H 9.069 . 1 225 . 62 GLY C C 177.15 . 1 226 . 62 GLY CA C 47.475 . 1 227 . 63 VAL N N 122.78 . 1 228 . 63 VAL H H 8.449 . 1 229 . 63 VAL C C 175.76 . 1 230 . 63 VAL CA C 67.435 . 1 231 . 63 VAL CB C 31.155 . 1 232 . 64 PHE N N 119.32 . 1 233 . 64 PHE H H 6.538 . 1 234 . 64 PHE C C 176.49 . 1 235 . 64 PHE CA C 62.215 . 1 236 . 64 PHE CB C 37.465 . 1 237 . 65 ASN N N 115.54 . 1 238 . 65 ASN H H 9.006 . 1 239 . 65 ASN C C 178.02 . 1 240 . 65 ASN CA C 55.225 . 1 241 . 65 ASN CB C 37.495 . 1 242 . 66 ASN N N 112.71 . 1 243 . 66 ASN H H 7.618 . 1 244 . 66 ASN C C 175.28 . 1 245 . 66 ASN CA C 57.225 . 1 246 . 66 ASN CB C 39.255 . 1 247 . 67 ALA N N 120.83 . 1 248 . 67 ALA H H 8.331 . 1 249 . 67 ALA CA C 53.355 . 1 250 . 67 ALA CB C 18.025 . 1 251 . 82 PRO C C 175.72 . 1 252 . 82 PRO CA C 61.155 . 1 253 . 82 PRO CB C 31.575 . 1 254 . 83 ASN N N 115.55 . 1 255 . 83 ASN H H 8.9 . 1 256 . 83 ASN C C 174.26 . 1 257 . 83 ASN CA C 53.875 . 1 258 . 83 ASN CB C 37.435 . 1 259 . 84 ALA N N 124.45 . 1 260 . 84 ALA H H 8.949 . 1 261 . 84 ALA C C 177.1 . 1 262 . 84 ALA CA C 50.675 . 1 263 . 84 ALA CB C 18.925 . 1 264 . 85 GLY N N 111.72 . 1 265 . 85 GLY H H 8.638 . 1 266 . 85 GLY C C 174.74 . 1 267 . 85 GLY CA C 45.765 . 1 268 . 86 GLY N N 107.54 . 1 269 . 86 GLY H H 8.111 . 1 270 . 86 GLY C C 177.15 . 1 271 . 86 GLY CA C 44.775 . 1 272 . 87 GLU N N 122.25 . 1 273 . 87 GLU H H 8.478 . 1 274 . 87 GLU CA C 53.145 . 1 275 . 87 GLU CB C 28.525 . 1 276 . 88 PRO C C 174.76 . 1 277 . 88 PRO CA C 61.255 . 1 278 . 88 PRO CB C 30.645 . 1 279 . 89 THR N N 109.51 . 1 280 . 89 THR H H 8.199 . 1 281 . 89 THR C C 175.88 . 1 282 . 89 THR CA C 59.355 . 1 283 . 89 THR CB C 71.935 . 1 284 . 90 GLY N N 108.27 . 1 285 . 90 GLY H H 8.684 . 1 286 . 90 GLY C C 175.46 . 1 287 . 90 GLY CA C 45.965 . 1 288 . 91 LYS N N 124.25 . 1 289 . 91 LYS H H 8.79 . 1 290 . 91 LYS C C 179.81 . 1 291 . 91 LYS CA C 58.425 . 1 292 . 91 LYS CB C 31.465 . 1 293 . 92 VAL N N 118.28 . 1 294 . 92 VAL H H 8.495 . 1 295 . 92 VAL C C 176.79 . 1 296 . 92 VAL CA C 65.755 . 1 297 . 92 VAL CB C 30.835 . 1 298 . 93 ALA N N 120.57 . 1 299 . 93 ALA H H 6.493 . 1 300 . 93 ALA C C 180.13 . 1 301 . 93 ALA CA C 54.465 . 1 302 . 93 ALA CB C 16.615 . 1 303 . 94 GLU N N 117.88 . 1 304 . 94 GLU H H 7.989 . 1 305 . 94 GLU C C 178.9 . 1 306 . 94 GLU CA C 58.635 . 1 307 . 94 GLU CB C 29.275 . 1 308 . 95 ALA N N 122.61 . 1 309 . 95 ALA H H 8.116 . 1 310 . 95 ALA CA C 54.445 . 1 311 . 95 ALA CB C 17.855 . 1 312 . 96 ILE C C 177.82 . 1 313 . 96 ILE CA C 65.065 . 1 314 . 96 ILE CB C 36.955 . 1 315 . 97 ALA N N 122.89 . 1 316 . 97 ALA H H 8.289 . 1 317 . 97 ALA C C 179.91 . 1 318 . 97 ALA CA C 55.055 . 1 319 . 97 ALA CB C 17.055 . 1 320 . 98 ALA N N 118.55 . 1 321 . 98 ALA H H 8.1 . 1 322 . 98 ALA C C 179.85 . 1 323 . 98 ALA CA C 54.375 . 1 324 . 98 ALA CB C 17.865 . 1 325 . 99 SER N N 110.54 . 1 326 . 99 SER H H 7.529 . 1 327 . 99 SER C C 174.37 . 1 328 . 99 SER CA C 61.405 . 1 329 . 99 SER CB C 64.615 . 1 330 . 100 PHE N N 115.36 . 1 331 . 100 PHE H H 8.535 . 1 332 . 100 PHE C C 175.42 . 1 333 . 100 PHE CA C 57.845 . 1 334 . 100 PHE CB C 40.375 . 1 335 . 101 GLY N N 113.39 . 1 336 . 101 GLY H H 8.032 . 1 337 . 101 GLY C C 174.8 . 1 338 . 101 GLY CA C 46.455 . 1 339 . 102 SER N N 109.48 . 1 340 . 102 SER H H 7.553 . 1 341 . 102 SER C C 173.65 . 1 342 . 102 SER CA C 57.135 . 1 343 . 102 SER CB C 65.895 . 1 344 . 103 PHE N N 122.37 . 1 345 . 103 PHE H H 9.396 . 1 346 . 103 PHE C C 176.01 . 1 347 . 103 PHE CA C 61.335 . 1 348 . 103 PHE CB C 37.525 . 1 349 . 104 ALA N N 120.79 . 1 350 . 104 ALA H H 8.68 . 1 351 . 104 ALA C C 180.63 . 1 352 . 104 ALA CA C 54.915 . 1 353 . 104 ALA CB C 17.365 . 1 354 . 105 ASP N N 118.33 . 1 355 . 105 ASP H H 7.897 . 1 356 . 105 ASP C C 180.37 . 1 357 . 105 ASP CA C 57.515 . 1 358 . 105 ASP CB C 40.995 . 1 359 . 106 PHE N N 120.3 . 1 360 . 106 PHE H H 7.583 . 1 361 . 106 PHE CA C 59.715 . 1 362 . 106 PHE CB C 38.075 . 1 363 . 107 LYS N N 116.3 . 1 364 . 107 LYS H H 7.675 . 1 365 . 107 LYS C C 179.85 . 1 366 . 107 LYS CA C 57.285 . 1 367 . 107 LYS CB C 31.265 . 1 368 . 108 ALA N N 122.78 . 1 369 . 108 ALA H H 7.658 . 1 370 . 108 ALA CA C 54.765 . 1 371 . 108 ALA CB C 17.375 . 1 372 . 109 GLN N N 119.85 . 1 373 . 109 GLN H H 7.676 . 1 374 . 109 GLN CA C 58.165 . 1 375 . 109 GLN CB C 27.575 . 1 376 . 111 THR C C 175 . 1 377 . 111 THR CA C 67.435 . 1 378 . 111 THR CB C 68.845 . 1 379 . 112 ASP N N 119.18 . 1 380 . 112 ASP H H 7.984 . 1 381 . 112 ASP CA C 57.485 . 1 382 . 112 ASP CB C 41.695 . 1 383 . 115 ILE C C 177.9 . 1 384 . 115 ILE CA C 64.265 . 1 385 . 115 ILE CB C 36.725 . 1 386 . 116 LYS N N 117.31 . 1 387 . 116 LYS H H 8.01 . 1 388 . 116 LYS C C 176.91 . 1 389 . 116 LYS CA C 57.255 . 1 390 . 116 LYS CB C 32.555 . 1 391 . 117 ASN N N 118.78 . 1 392 . 117 ASN H H 7.185 . 1 393 . 117 ASN C C 174.97 . 1 394 . 117 ASN CA C 53.945 . 1 395 . 117 ASN CB C 37.245 . 1 396 . 118 PHE N N 132.19 . 1 397 . 118 PHE H H 9.465 . 1 398 . 118 PHE C C 177.13 . 1 399 . 118 PHE CA C 60.585 . 1 400 . 118 PHE CB C 41.075 . 1 401 . 119 GLY N N 117.11 . 1 402 . 119 GLY H H 10.124 . 1 403 . 119 GLY CA C 45.955 . 1 404 . 120 SER N N 119.71 . 1 405 . 120 SER H H 11.137 . 1 406 . 120 SER CA C 61.385 . 1 407 . 120 SER CB C 65.355 . 1 408 . 127 LYS C C 176.14 . 1 409 . 127 LYS CA C 54.315 . 1 410 . 127 LYS CB C 34.195 . 1 411 . 128 ASN N N 126.77 . 1 412 . 128 ASN H H 9.098 . 1 413 . 128 ASN C C 177.8 . 1 414 . 128 ASN CA C 52.485 . 1 415 . 128 ASN CB C 39.355 . 1 416 . 129 SER N N 116.32 . 1 417 . 129 SER H H 9.255 . 1 418 . 129 SER C C 174.93 . 1 419 . 129 SER CA C 60.695 . 1 420 . 129 SER CB C 62.325 . 1 421 . 130 ASP N N 118.91 . 1 422 . 130 ASP H H 7.806 . 1 423 . 130 ASP C C 177.01 . 1 424 . 130 ASP CA C 53.175 . 1 425 . 130 ASP CB C 39.785 . 1 426 . 131 GLY N N 108.57 . 1 427 . 131 GLY H H 8.266 . 1 428 . 131 GLY C C 173.7 . 1 429 . 131 GLY CA C 44.805 . 1 430 . 132 LYS N N 121.1 . 1 431 . 132 LYS H H 7.823 . 1 432 . 132 LYS C C 175.43 . 1 433 . 132 LYS CA C 55.535 . 1 434 . 132 LYS CB C 32.255 . 1 435 . 133 LEU N N 119.44 . 1 436 . 133 LEU H H 8.052 . 1 437 . 133 LEU CA C 53.165 . 1 438 . 133 LEU CB C 42.435 . 1 439 . 134 ALA C C 175.09 . 1 440 . 134 ALA CA C 51.035 . 1 441 . 134 ALA CB C 22.705 . 1 442 . 135 ILE N N 121.74 . 1 443 . 135 ILE H H 9.095 . 1 444 . 135 ILE CA C 59.675 . 1 445 . 135 ILE CB C 39.205 . 1 446 . 136 VAL C C 174.69 . 1 447 . 136 VAL CA C 59.465 . 1 448 . 136 VAL CB C 36.115 . 1 449 . 137 SER N N 121.16 . 1 450 . 137 SER H H 9.423 . 1 451 . 137 SER C C 174.3 . 1 452 . 137 SER CA C 58.235 . 1 453 . 137 SER CB C 65.405 . 1 454 . 138 THR N N 113.44 . 1 455 . 138 THR H H 10.875 . 1 456 . 138 THR C C 175.34 . 1 457 . 138 THR CA C 59.705 . 1 458 . 138 THR CB C 72.975 . 1 459 . 139 SER N N 117.51 . 1 460 . 139 SER H H 10.211 . 1 461 . 139 SER C C 178.05 . 1 462 . 139 SER CA C 58.325 . 1 463 . 139 SER CB C 65.655 . 1 464 . 140 ASN N N 129.5 . 1 465 . 140 ASN H H 12.155 . 1 466 . 140 ASN C C 178.07 . 1 467 . 140 ASN CA C 59.765 . 1 468 . 140 ASN CB C 38.245 . 1 469 . 141 ALA N N 132.85 . 1 470 . 141 ALA H H 11.542 . 1 471 . 141 ALA C C 176.5 . 1 472 . 141 ALA CA C 53.765 . 1 473 . 141 ALA CB C 24.135 . 1 474 . 142 GLY N N 103.67 . 1 475 . 142 GLY H H 10.501 . 1 476 . 142 GLY C C 174.25 . 1 477 . 142 GLY CA C 47.965 . 1 478 . 143 THR N N 118.48 . 1 479 . 143 THR H H 9.502 . 1 480 . 143 THR CA C 54.795 . 1 481 . 143 THR CB C 69.585 . 1 482 . 144 PRO C C 176.3 . 1 483 . 144 PRO CA C 62.215 . 1 484 . 144 PRO CB C 30.785 . 1 485 . 145 LEU N N 117.54 . 1 486 . 145 LEU H H 6.892 . 1 487 . 145 LEU C C 177.39 . 1 488 . 145 LEU CA C 56.265 . 1 489 . 145 LEU CB C 41.925 . 1 490 . 146 THR N N 105.01 . 1 491 . 146 THR H H 7.326 . 1 492 . 146 THR C C 173.79 . 1 493 . 146 THR CA C 62.705 . 1 494 . 146 THR CB C 67.215 . 1 495 . 147 THR N N 113.89 . 1 496 . 147 THR H H 7.815 . 1 497 . 147 THR C C 172.8 . 1 498 . 147 THR CA C 60.025 . 1 499 . 147 THR CB C 71.615 . 1 500 . 148 ASP N N 116.65 . 1 501 . 148 ASP H H 8.301 . 1 502 . 148 ASP C C 175.33 . 1 503 . 148 ASP CA C 53.365 . 1 504 . 148 ASP CB C 39.795 . 1 505 . 149 ALA N N 123.31 . 1 506 . 149 ALA H H 8.022 . 1 507 . 149 ALA C C 176.19 . 1 508 . 149 ALA CA C 50.825 . 1 509 . 149 ALA CB C 20.245 . 1 510 . 150 THR N N 117.12 . 1 511 . 150 THR H H 8.648 . 1 512 . 150 THR CA C 59.455 . 1 513 . 150 THR CB C 70.705 . 1 514 . 163 TYR C C 178.12 . 1 515 . 163 TYR CA C 60.165 . 1 516 . 163 TYR CB C 34.985 . 1 517 . 164 ILE N N 114.17 . 1 518 . 164 ILE H H 7.229 . 1 519 . 164 ILE CA C 64.335 . 1 520 . 164 ILE CB C 35.615 . 1 521 . 165 ASP N N 114.09 . 1 522 . 165 ASP H H 5.706 . 1 523 . 165 ASP CA C 54.985 . 1 524 . 165 ASP CB C 42.635 . 1 525 . 166 TYR C C 174.86 . 1 526 . 166 TYR CA C 57.025 . 1 527 . 166 TYR CB C 38.255 . 1 528 . 167 ARG N N 118.63 . 1 529 . 167 ARG H H 6.406 . 1 530 . 167 ARG C C 170.75 . 1 531 . 167 ARG CA C 53.115 . 1 532 . 167 ARG CB C 26.695 . 1 533 . 168 ASN N N 109.82 . 1 534 . 168 ASN H H 6.96 . 1 535 . 168 ASN C C 174.58 . 1 536 . 168 ASN CA C 53.045 . 1 537 . 168 ASN CB C 37.265 . 1 538 . 169 ALA N N 125.82 . 1 539 . 169 ALA H H 7.31 . 1 540 . 169 ALA C C 174.83 . 1 541 . 169 ALA CA C 49.785 . 1 542 . 169 ALA CB C 15.495 . 1 543 . 170 ARG N N 125.36 . 1 544 . 170 ARG H H 7.28 . 1 545 . 170 ARG CA C 59.325 . 1 546 . 170 ARG CB C 28.285 . 1 547 . 171 PRO C C 178.35 . 1 548 . 171 PRO CA C 65.845 . 1 549 . 171 PRO CB C 29.865 . 1 550 . 172 GLY N N 106.15 . 1 551 . 172 GLY H H 6.688 . 1 552 . 172 GLY CA C 46.345 . 1 553 . 174 LEU C C 177.09 . 1 554 . 174 LEU CA C 53.785 . 1 555 . 174 LEU CB C 39.435 . 1 556 . 175 GLU N N 116 . 1 557 . 175 GLU H H 7.365 . 1 558 . 175 GLU C C 179.49 . 1 559 . 175 GLU CA C 59.255 . 1 560 . 175 GLU CB C 28.775 . 1 561 . 176 HIS N N 116.83 . 1 562 . 176 HIS H H 7.475 . 1 563 . 176 HIS CA C 58.735 . 1 564 . 176 HIS CB C 29.095 . 1 565 . 178 TRP C C 177.97 . 1 566 . 178 TRP CA C 58.375 . 1 567 . 178 TRP CB C 28.615 . 1 568 . 179 ALA N N 118.29 . 1 569 . 179 ALA H H 7.18 . 1 570 . 179 ALA CA C 52.575 . 1 571 . 179 ALA CB C 16.695 . 1 572 . 182 ASN C C 175.94 . 1 573 . 182 ASN CA C 49.375 . 1 574 . 182 ASN CB C 36.215 . 1 575 . 183 TRP N N 124.05 . 1 576 . 183 TRP H H 7.945 . 1 577 . 183 TRP C C 178.41 . 1 578 . 183 TRP CA C 58.945 . 1 579 . 183 TRP CB C 28.575 . 1 580 . 184 GLU N N 119.63 . 1 581 . 184 GLU H H 8.08 . 1 582 . 184 GLU C C 179.01 . 1 583 . 184 GLU CA C 58.935 . 1 584 . 184 GLU CB C 28.575 . 1 585 . 185 PHE N N 121.65 . 1 586 . 185 PHE H H 7.082 . 1 587 . 185 PHE CA C 59.585 . 1 588 . 185 PHE CB C 39.425 . 1 589 . 187 ALA C C 180.37 . 1 590 . 187 ALA CA C 54.695 . 1 591 . 187 ALA CB C 17.585 . 1 592 . 188 LYS N N 120.26 . 1 593 . 188 LYS H H 7.619 . 1 594 . 188 LYS C C 179.16 . 1 595 . 188 LYS CA C 58.815 . 1 596 . 188 LYS CB C 31.175 . 1 597 . 189 ASN N N 117.53 . 1 598 . 189 ASN H H 7.707 . 1 599 . 189 ASN C C 176.82 . 1 600 . 189 ASN CA C 54.675 . 1 601 . 189 ASN CB C 38.235 . 1 602 . 190 LEU N N 120.7 . 1 603 . 190 LEU H H 8.155 . 1 604 . 190 LEU C C 176.32 . 1 605 . 190 LEU CA C 56.375 . 1 606 . 190 LEU CB C 41.895 . 1 607 . 191 ALA N N 119.84 . 1 608 . 191 ALA H H 7.484 . 1 609 . 191 ALA C C 176.51 . 1 610 . 191 ALA CA C 52.045 . 1 611 . 191 ALA CB C 18.255 . 1 612 . 192 ALA N N 126.7 . 1 613 . 192 ALA H H 7.275 . 1 614 . 192 ALA CA C 53.915 . 1 615 . 192 ALA CB C 19.295 . 1 stop_ save_