data_4329 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Assignment and Secondary Structure Analysis of the NADP(H)-Binding Domain of Escherichia coli Transhydrogenase ; _BMRB_accession_number 4329 _BMRB_flat_file_name bmr4329.str _Entry_type original _Submission_date 1999-04-09 _Accession_date 1999-04-09 _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 Johansson Carina . . 2 Bergkvist Anders . . 3 Fjellstrom Ola . . 4 Rydstrom Jan . . 5 Karlsson Goran . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 344 "13C chemical shifts" 343 "15N chemical shifts" 164 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-26 original author . stop_ _Original_release_date 1999-10-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Johansson, C., Bergkvist, A., Fjellstrom, O., Rydstrom, J., and Karlsson, G., "Sequential Assignment and Secondary Structure Analysis of the NADP(H)-Binding Domain of Escherichia coli Transhydrogenase," J. Biomol. NMR, 14, 295-296 (1999). ; _Citation_title ; Sequential Assignment and Secondary Structure Analysis of the NADP(H)-Binding Domain of Escherichia coli Transhydrogenase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99410898 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johansson Carina . . 2 Bergkvist Anders . . 3 Fjellstrom Ola . . 4 Rydstrom Jan . . 5 Karlsson Goran . . 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 295 _Page_last 296 _Year 1999 _Details . loop_ _Keyword 'backbone assignment' 'seconary structure' 'transhydrogenase NADP(H)-binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_ecIII _Saveframe_category molecular_system _Mol_system_name 'E.coli Transhydrogenase domain III' _Abbreviation_common ecIII _Enzyme_commission_number 1.6.1.1 loop_ _Mol_system_component_name _Mol_label ecIII $ecIII NADP+ $NAP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Reversible reduction of NADP+ by NADH coupled to proton translocation' stop_ _Database_query_date . _Details ; Although a monomer, the protein exhibits unfavourable relaxation properties with a tc of 14 ns. The sequential assignment has thus required deuterium labeling of the protein. ; save_ ######################## # Monomeric polymers # ######################## save_ecIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E.coli transhydrogenase domain III' _Abbreviation_common ecIII _Molecular_mass 20393 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 186 _Mol_residue_sequence ; MHHHHHHSSQEVGEHREITA EETAELLKNSHSVIITPGYG MAVAQAQYPVAEITEKLRAR GINVRFGIHPVAGRLPGHMN VLLAEAKVPYDIVLEMDEIN DDFADTDTVLVIGANDTVNP AAQDDPKSPIAGMPVLEVWK AQNVIVFKRSMNTGYAGVQN PLFFKENTHMLFGDAKASVD AILKAL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 SER 9 SER 10 GLN 11 GLU 12 VAL 13 GLY 14 GLU 15 HIS 16 ARG 17 GLU 18 ILE 19 THR 20 ALA 21 GLU 22 GLU 23 THR 24 ALA 25 GLU 26 LEU 27 LEU 28 LYS 29 ASN 30 SER 31 HIS 32 SER 33 VAL 34 ILE 35 ILE 36 THR 37 PRO 38 GLY 39 TYR 40 GLY 41 MET 42 ALA 43 VAL 44 ALA 45 GLN 46 ALA 47 GLN 48 TYR 49 PRO 50 VAL 51 ALA 52 GLU 53 ILE 54 THR 55 GLU 56 LYS 57 LEU 58 ARG 59 ALA 60 ARG 61 GLY 62 ILE 63 ASN 64 VAL 65 ARG 66 PHE 67 GLY 68 ILE 69 HIS 70 PRO 71 VAL 72 ALA 73 GLY 74 ARG 75 LEU 76 PRO 77 GLY 78 HIS 79 MET 80 ASN 81 VAL 82 LEU 83 LEU 84 ALA 85 GLU 86 ALA 87 LYS 88 VAL 89 PRO 90 TYR 91 ASP 92 ILE 93 VAL 94 LEU 95 GLU 96 MET 97 ASP 98 GLU 99 ILE 100 ASN 101 ASP 102 ASP 103 PHE 104 ALA 105 ASP 106 THR 107 ASP 108 THR 109 VAL 110 LEU 111 VAL 112 ILE 113 GLY 114 ALA 115 ASN 116 ASP 117 THR 118 VAL 119 ASN 120 PRO 121 ALA 122 ALA 123 GLN 124 ASP 125 ASP 126 PRO 127 LYS 128 SER 129 PRO 130 ILE 131 ALA 132 GLY 133 MET 134 PRO 135 VAL 136 LEU 137 GLU 138 VAL 139 TRP 140 LYS 141 ALA 142 GLN 143 ASN 144 VAL 145 ILE 146 VAL 147 PHE 148 LYS 149 ARG 150 SER 151 MET 152 ASN 153 THR 154 GLY 155 TYR 156 ALA 157 GLY 158 VAL 159 GLN 160 ASN 161 PRO 162 LEU 163 PHE 164 PHE 165 LYS 166 GLU 167 ASN 168 THR 169 HIS 170 MET 171 LEU 172 PHE 173 GLY 174 ASP 175 ALA 176 LYS 177 ALA 178 SER 179 VAL 180 ASP 181 ALA 182 ILE 183 LEU 184 LYS 185 ALA 186 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 2BRU "Complex Of The Domain I And Domain Iii Of Escherichia Coli Transhydrogenase" 100.00 186 100.00 100.00 4.09e-133 DBJ BAA15336 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli str. K12 substr. W3110]" 95.16 462 100.00 100.00 2.27e-123 DBJ BAB35731 "pyridine nucleotide transhydrogenase beta subunit [Escherichia coli O157:H7 str. Sakai]" 95.16 462 100.00 100.00 2.27e-123 DBJ BAG77247 "pyridine nucleotide transhydrogenase beta subunit [Escherichia coli SE11]" 95.16 462 100.00 100.00 2.27e-123 DBJ BAI25577 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli O26:H11 str. 11368]" 95.16 462 100.00 100.00 2.27e-123 DBJ BAI30551 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli O103:H2 str. 12009]" 95.16 462 100.00 100.00 2.27e-123 EMBL CAA46885 "pyridine nucleotide transhydrogenase [Escherichia coli K-12]" 95.16 462 100.00 100.00 2.27e-123 EMBL CAB37090 "NAD(P)(+) transhydrogenase subunit beta [Escherichia coli]" 95.16 462 100.00 100.00 2.27e-123 EMBL CAD01834 "pyridine nucleotide transhydrogenase subunit-beta [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 95.16 462 97.18 98.87 5.40e-121 EMBL CAP76101 "Nad(P) transhydrogenase subunit beta [Escherichia coli LF82]" 95.16 462 100.00 100.00 2.27e-123 EMBL CAQ32078 "pyridine nucleotide transhydrogenase, beta subunit, subunit of pyridine nucleotide transhydrogenase [Escherichia coli BL21(DE3)" 95.16 462 100.00 100.00 2.27e-123 GB AAC74674 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli str. K-12 substr. MG1655]" 95.16 462 100.00 100.00 2.27e-123 GB AAG56589 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli O157:H7 str. EDL933]" 95.16 462 100.00 100.00 2.27e-123 GB AAL20399 "pyridine nucleotide transhydrogenase, beta subunit [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 95.16 462 97.18 98.87 5.40e-121 GB AAN43206 "pyridine nucleotide transhydrogenase, beta subunit [Shigella flexneri 2a str. 301]" 95.16 462 100.00 100.00 2.27e-123 GB AAN80454 "NAD(P) transhydrogenase subunit beta [Escherichia coli CFT073]" 95.16 462 100.00 100.00 2.27e-123 PIR AI0682 "NAD(P) transhydrogenase (B-specific) (EC 1.6.1.1) - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 95.16 462 97.18 98.87 5.40e-121 REF NP_310335 "pyridine nucleotide transhydrogenase [Escherichia coli O157:H7 str. Sakai]" 95.16 462 100.00 100.00 2.27e-123 REF NP_416119 "pyridine nucleotide transhydrogenase, beta subunit [Escherichia coli str. K-12 substr. MG1655]" 95.16 462 100.00 100.00 2.27e-123 REF NP_456000 "pyridine nucleotide transhydrogenase subunit beta [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 95.16 462 97.18 98.87 5.40e-121 REF NP_460440 "NAD(P) transhydrogenase subunit beta [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 95.16 462 97.18 98.87 5.40e-121 REF NP_707499 "pyridine nucleotide transhydrogenase [Shigella flexneri 2a str. 301]" 95.16 462 100.00 100.00 2.27e-123 SP P0AB67 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 95.16 462 100.00 100.00 2.27e-123 SP P0AB68 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 95.16 462 100.00 100.00 2.27e-123 SP P0AB69 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 95.16 462 100.00 100.00 2.27e-123 SP P0AB70 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 95.16 462 100.00 100.00 2.27e-123 stop_ save_ ############# # Ligands # ############# save_NAP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' _BMRB_code NAP _PDB_code NAP _Molecular_mass 743.405 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O5B O5B O . 0 . ? C5B C5B C . 0 . ? C4B C4B C . 0 . ? O4B O4B O . 0 . ? C3B C3B C . 0 . ? O3B O3B O . 0 . ? C2B C2B C . 0 . ? O2B O2B O . 0 . ? C1B C1B C . 0 . ? N9A N9A N . 0 . ? C8A C8A C . 0 . ? N7A N7A N . 0 . ? C5A C5A C . 0 . ? C6A C6A C . 0 . ? N6A N6A N . 0 . ? N1A N1A N . 0 . ? C2A C2A C . 0 . ? N3A N3A N . 0 . ? C4A C4A C . 0 . ? O3 O3 O . 0 . ? PN PN P . 0 . ? O1N O1N O . 0 . ? O2N O2N O . -1 . ? O5D O5D O . 0 . ? C5D C5D C . 0 . ? C4D C4D C . 0 . ? O4D O4D O . 0 . ? C3D C3D C . 0 . ? O3D O3D O . 0 . ? C2D C2D C . 0 . ? O2D O2D O . 0 . ? C1D C1D C . 0 . ? N1N N1N N . 1 . ? C2N C2N C . 0 . ? C3N C3N C . 0 . ? C7N C7N C . 0 . ? O7N O7N O . 0 . ? N7N N7N N . 0 . ? C4N C4N C . 0 . ? C5N C5N C . 0 . ? C6N C6N C . 0 . ? P2B P2B P . 0 . ? O1X O1X O . 0 . ? O2X O2X O . 0 . ? O3X O3X O . 0 . ? HOA2 HOA2 H . 0 . ? H51A H51A H . 0 . ? H52A H52A H . 0 . ? H4B H4B H . 0 . ? H3B H3B H . 0 . ? HO3A HO3A H . 0 . ? H2B H2B H . 0 . ? H1B H1B H . 0 . ? H8A H8A H . 0 . ? H61A H61A H . 0 . ? H62A H62A H . 0 . ? H2A H2A H . 0 . ? H51N H51N H . 0 . ? H52N H52N H . 0 . ? H4D H4D H . 0 . ? H3D H3D H . 0 . ? HO3N HO3N H . 0 . ? H2D H2D H . 0 . ? HO2N HO2N H . 0 . ? H1D H1D H . 0 . ? H2N H2N H . 0 . ? H71N H71N H . 0 . ? H72N H72N H . 0 . ? H4N H4N H . 0 . ? H5N H5N H . 0 . ? H6N H6N H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 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 DOUB PA O1A ? ? SING PA O2A ? ? SING PA O5B ? ? SING PA O3 ? ? SING O2A HOA2 ? ? SING O5B C5B ? ? SING C5B C4B ? ? SING C5B H51A ? ? SING C5B H52A ? ? SING C4B O4B ? ? SING C4B C3B ? ? SING C4B H4B ? ? SING O4B C1B ? ? SING C3B O3B ? ? SING C3B C2B ? ? SING C3B H3B ? ? SING O3B HO3A ? ? SING C2B O2B ? ? SING C2B C1B ? ? SING C2B H2B ? ? SING O2B P2B ? ? SING C1B N9A ? ? SING C1B H1B ? ? SING N9A C8A ? ? SING N9A C4A ? ? DOUB C8A N7A ? ? SING C8A H8A ? ? SING N7A C5A ? ? SING C5A C6A ? ? DOUB C5A C4A ? ? SING C6A N6A ? ? DOUB C6A N1A ? ? SING N6A H61A ? ? SING N6A H62A ? ? SING N1A C2A ? ? DOUB C2A N3A ? ? SING C2A H2A ? ? SING N3A C4A ? ? SING O3 PN ? ? DOUB PN O1N ? ? SING PN O2N ? ? SING PN O5D ? ? SING O5D C5D ? ? SING C5D C4D ? ? SING C5D H51N ? ? SING C5D H52N ? ? SING C4D O4D ? ? SING C4D C3D ? ? SING C4D H4D ? ? SING O4D C1D ? ? SING C3D O3D ? ? SING C3D C2D ? ? SING C3D H3D ? ? SING O3D HO3N ? ? SING C2D O2D ? ? SING C2D C1D ? ? SING C2D H2D ? ? SING O2D HO2N ? ? SING C1D N1N ? ? SING C1D H1D ? ? SING N1N C2N ? ? DOUB N1N C6N ? ? DOUB C2N C3N ? ? SING C2N H2N ? ? SING C3N C7N ? ? SING C3N C4N ? ? DOUB C7N O7N ? ? SING C7N N7N ? ? SING N7N H71N ? ? SING N7N H72N ? ? DOUB C4N C5N ? ? SING C4N H4N ? ? SING C5N C6N ? ? SING C5N H5N ? ? SING C6N H6N ? ? DOUB P2B O1X ? ? SING P2B O2X ? ? SING P2B O3X ? ? SING O2X HOP2 ? ? SING O3X HOP3 ? ? 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 $ecIII 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $ecIII 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ecIII . mM 0.9 1.5 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity INOVA' _Field_strength 800 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity INOVA' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_one save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_one save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_one save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_one save_ save_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ecIII _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 . 10 GLN H H 8.38 . 1 2 . 10 GLN C C 175.55 . 1 3 . 10 GLN CA C 55.88 . 1 4 . 10 GLN N N 120.81 . 1 5 . 11 GLU H H 8.29 . 1 6 . 11 GLU C C 176.09 . 1 7 . 11 GLU CA C 56.53 . 1 8 . 11 GLU N N 121.31 . 1 9 . 12 VAL H H 8.08 . 1 10 . 12 VAL HA H 4.02 . 1 11 . 12 VAL C C 175.85 . 1 12 . 12 VAL CA C 62.07 . 1 13 . 12 VAL N N 119.64 . 1 14 . 13 GLY H H 7.78 . 1 15 . 13 GLY HA2 H 3.52 . 2 16 . 13 GLY HA3 H 3.80 . 2 17 . 13 GLY C C 172.63 . 1 18 . 13 GLY CA C 44.81 . 1 19 . 13 GLY N N 111.02 . 1 20 . 14 GLU H H 8.29 . 1 21 . 14 GLU CA C 55.93 . 1 22 . 14 GLU N N 119.85 . 1 23 . 17 GLU C C 175.37 . 1 24 . 17 GLU CA C 55.58 . 1 25 . 18 ILE H H 8.52 . 1 26 . 18 ILE HA H 4.65 . 1 27 . 18 ILE C C 172.32 . 1 28 . 18 ILE CA C 59.63 . 1 29 . 18 ILE N N 123.16 . 1 30 . 19 THR H H 7.75 . 1 31 . 19 THR HA H 4.72 . 1 32 . 19 THR C C 177.90 . 1 33 . 19 THR CA C 59.96 . 1 34 . 19 THR N N 111.99 . 1 35 . 20 ALA H H 9.63 . 1 36 . 20 ALA HA H 3.69 . 1 37 . 20 ALA C C 178.99 . 1 38 . 20 ALA CA C 55.76 . 1 39 . 20 ALA N N 126.35 . 1 40 . 21 GLU H H 9.02 . 1 41 . 21 GLU HA H 3.65 . 1 42 . 21 GLU C C 179.47 . 1 43 . 21 GLU CA C 61.19 . 1 44 . 21 GLU N N 117.51 . 1 45 . 22 GLU H H 7.80 . 1 46 . 22 GLU HA H 3.92 . 1 47 . 22 GLU C C 179.94 . 1 48 . 22 GLU CA C 58.73 . 1 49 . 22 GLU N N 119.38 . 1 50 . 23 THR H H 8.15 . 1 51 . 23 THR HA H 3.49 . 1 52 . 23 THR C C 175.54 . 1 53 . 23 THR CA C 68.86 . 1 54 . 23 THR N N 119.04 . 1 55 . 24 ALA H H 8.36 . 1 56 . 24 ALA HA H 3.72 . 1 57 . 24 ALA C C 178.18 . 1 58 . 24 ALA CA C 55.86 . 1 59 . 24 ALA N N 123.48 . 1 60 . 25 GLU H H 7.35 . 1 61 . 25 GLU HA H 3.84 . 1 62 . 25 GLU C C 178.14 . 1 63 . 25 GLU CA C 59.22 . 1 64 . 25 GLU N N 116.14 . 1 65 . 26 LEU H H 7.64 . 1 66 . 26 LEU HA H 3.96 . 1 67 . 26 LEU C C 181.68 . 1 68 . 26 LEU CA C 57.91 . 1 69 . 26 LEU N N 119.00 . 1 70 . 27 LEU H H 8.47 . 1 71 . 27 LEU HA H 3.74 . 1 72 . 27 LEU C C 177.87 . 1 73 . 27 LEU CA C 58.13 . 1 74 . 27 LEU N N 120.23 . 1 75 . 28 LYS H H 8.00 . 1 76 . 28 LYS HA H 3.62 . 1 77 . 28 LYS C C 176.90 . 1 78 . 28 LYS CA C 59.74 . 1 79 . 28 LYS N N 115.18 . 1 80 . 29 ASN H H 7.16 . 1 81 . 29 ASN HA H 4.75 . 1 82 . 29 ASN C C 174.63 . 1 83 . 29 ASN CA C 51.90 . 1 84 . 29 ASN N N 114.43 . 1 85 . 30 SER H H 7.46 . 1 86 . 30 SER HA H 4.46 . 1 87 . 30 SER C C 171.74 . 1 88 . 30 SER CA C 59.51 . 1 89 . 30 SER N N 116.13 . 1 90 . 31 HIS H H 9.91 . 1 91 . 31 HIS HA H 4.84 . 1 92 . 31 HIS C C 175.43 . 1 93 . 31 HIS CA C 57.14 . 1 94 . 31 HIS N N 119.45 . 1 95 . 32 SER H H 8.27 . 1 96 . 32 SER HA H 5.07 . 1 97 . 32 SER C C 172.74 . 1 98 . 32 SER CA C 56.39 . 1 99 . 32 SER N N 113.92 . 1 100 . 33 VAL H H 8.82 . 1 101 . 33 VAL HA H 5.45 . 1 102 . 33 VAL C C 175.93 . 1 103 . 33 VAL CA C 59.20 . 1 104 . 33 VAL N N 122.80 . 1 105 . 34 ILE H H 8.35 . 1 106 . 34 ILE HA H 5.09 . 1 107 . 34 ILE C C 174.05 . 1 108 . 34 ILE CA C 59.13 . 1 109 . 34 ILE N N 125.44 . 1 110 . 35 ILE H H 8.80 . 1 111 . 35 ILE HA H 4.71 . 1 112 . 35 ILE C C 175.58 . 1 113 . 35 ILE CA C 59.73 . 1 114 . 35 ILE N N 126.89 . 1 115 . 36 THR H H 9.12 . 1 116 . 36 THR HA H 5.51 . 1 117 . 36 THR C C 174.70 . 1 118 . 36 THR CA C 54.12 . 1 119 . 36 THR N N 118.65 . 1 120 . 37 PRO HA H 4.87 . 1 121 . 37 PRO C C 174.12 . 1 122 . 37 PRO CA C 60.83 . 1 123 . 38 GLY H H 7.55 . 1 124 . 38 GLY HA2 H 3.77 . 2 125 . 38 GLY HA3 H 4.74 . 2 126 . 38 GLY C C 174.76 . 1 127 . 38 GLY CA C 44.65 . 1 128 . 38 GLY N N 105.18 . 1 129 . 39 TYR H H 9.35 . 1 130 . 39 TYR HA H 4.85 . 1 131 . 39 TYR C C 176.02 . 1 132 . 39 TYR CA C 60.78 . 1 133 . 39 TYR N N 119.56 . 1 134 . 40 GLY H H 9.75 . 1 135 . 40 GLY HA2 H 2.02 . 2 136 . 40 GLY HA3 H 2.33 . 2 137 . 40 GLY C C 174.04 . 1 138 . 40 GLY CA C 45.49 . 1 139 . 40 GLY N N 103.81 . 1 140 . 41 MET H H 7.89 . 1 141 . 41 MET HA H 3.24 . 1 142 . 41 MET C C 177.11 . 1 143 . 41 MET CA C 59.68 . 1 144 . 41 MET N N 116.66 . 1 145 . 42 ALA H H 6.82 . 1 146 . 42 ALA HA H 3.83 . 1 147 . 42 ALA C C 180.34 . 1 148 . 42 ALA CA C 54.19 . 1 149 . 42 ALA N N 118.05 . 1 150 . 43 VAL H H 7.41 . 1 151 . 43 VAL HA H 3.46 . 1 152 . 43 VAL C C 177.66 . 1 153 . 43 VAL CA C 65.51 . 1 154 . 43 VAL N N 118.30 . 1 155 . 44 ALA H H 7.14 . 1 156 . 44 ALA HA H 4.45 . 1 157 . 44 ALA C C 176.37 . 1 158 . 44 ALA CA C 51.90 . 1 159 . 44 ALA N N 117.46 . 1 160 . 45 GLN H H 7.66 . 1 161 . 45 GLN HA H 4.25 . 1 162 . 45 GLN C C 176.79 . 1 163 . 45 GLN CA C 56.48 . 1 164 . 45 GLN N N 113.26 . 1 165 . 46 ALA H H 7.84 . 1 166 . 46 ALA HA H 4.11 . 1 167 . 46 ALA C C 175.61 . 1 168 . 46 ALA CA C 51.46 . 1 169 . 46 ALA N N 114.83 . 1 170 . 47 GLN H H 10.44 . 1 171 . 47 GLN HA H 3.81 . 1 172 . 47 GLN C C 174.91 . 1 173 . 47 GLN CA C 59.49 . 1 174 . 47 GLN N N 121.35 . 1 175 . 48 TYR H H 6.83 . 1 176 . 48 TYR HA H 4.42 . 1 177 . 48 TYR CA C 63.29 . 1 178 . 48 TYR N N 117.14 . 1 179 . 49 PRO HA H 4.61 . 1 180 . 49 PRO C C 178.54 . 1 181 . 49 PRO CA C 65.39 . 1 182 . 50 VAL H H 7.79 . 1 183 . 50 VAL HA H 3.51 . 1 184 . 50 VAL C C 177.99 . 1 185 . 50 VAL CA C 66.59 . 1 186 . 50 VAL N N 118.33 . 1 187 . 51 ALA H H 8.25 . 1 188 . 51 ALA HA H 3.91 . 1 189 . 51 ALA C C 179.74 . 1 190 . 51 ALA CA C 55.87 . 1 191 . 51 ALA N N 126.87 . 1 192 . 52 GLU H H 7.72 . 1 193 . 52 GLU HA H 4.14 . 1 194 . 52 GLU C C 179.27 . 1 195 . 52 GLU CA C 59.81 . 1 196 . 52 GLU N N 119.23 . 1 197 . 53 ILE H H 8.84 . 1 198 . 53 ILE HA H 3.66 . 1 199 . 53 ILE C C 176.51 . 1 200 . 53 ILE CA C 65.50 . 1 201 . 53 ILE N N 118.56 . 1 202 . 54 THR H H 7.71 . 1 203 . 54 THR HA H 4.10 . 1 204 . 54 THR C C 175.22 . 1 205 . 54 THR CA C 67.82 . 1 206 . 54 THR N N 118.57 . 1 207 . 55 GLU H H 7.74 . 1 208 . 55 GLU HA H 4.04 . 1 209 . 55 GLU C C 179.40 . 1 210 . 55 GLU CA C 59.65 . 1 211 . 55 GLU N N 120.73 . 1 212 . 56 LYS H H 8.14 . 1 213 . 56 LYS HA H 4.01 . 1 214 . 56 LYS C C 179.73 . 1 215 . 56 LYS CA C 59.53 . 1 216 . 56 LYS N N 118.54 . 1 217 . 57 LEU H H 8.40 . 1 218 . 57 LEU HA H 3.98 . 1 219 . 57 LEU C C 179.56 . 1 220 . 57 LEU CA C 57.55 . 1 221 . 57 LEU N N 117.59 . 1 222 . 58 ARG H H 8.66 . 1 223 . 58 ARG HA H 4.56 . 1 224 . 58 ARG C C 181.12 . 1 225 . 58 ARG CA C 59.85 . 1 226 . 58 ARG N N 120.42 . 1 227 . 59 ALA H H 8.05 . 1 228 . 59 ALA HA H 4.23 . 1 229 . 59 ALA C C 178.76 . 1 230 . 59 ALA CA C 54.41 . 1 231 . 59 ALA N N 121.97 . 1 232 . 60 ARG H H 7.33 . 1 233 . 60 ARG HA H 4.44 . 1 234 . 60 ARG C C 176.25 . 1 235 . 60 ARG CA C 55.79 . 1 236 . 60 ARG N N 115.19 . 1 237 . 61 GLY H H 8.04 . 1 238 . 61 GLY HA2 H 3.72 . 2 239 . 61 GLY HA3 H 4.19 . 2 240 . 61 GLY C C 173.63 . 1 241 . 61 GLY CA C 45.32 . 1 242 . 61 GLY N N 107.38 . 1 243 . 62 ILE H H 7.33 . 1 244 . 62 ILE HA H 3.71 . 1 245 . 62 ILE C C 175.17 . 1 246 . 62 ILE CA C 61.62 . 1 247 . 62 ILE N N 122.49 . 1 248 . 63 ASN H H 7.82 . 1 249 . 63 ASN HA H 4.61 . 1 250 . 63 ASN C C 173.69 . 1 251 . 63 ASN CA C 53.24 . 1 252 . 63 ASN N N 125.34 . 1 253 . 64 VAL H H 7.50 . 1 254 . 64 VAL HA H 4.98 . 1 255 . 64 VAL C C 174.29 . 1 256 . 64 VAL CA C 60.79 . 1 257 . 64 VAL N N 127.08 . 1 258 . 65 ARG H H 7.98 . 1 259 . 65 ARG HA H 5.00 . 1 260 . 65 ARG C C 173.60 . 1 261 . 65 ARG CA C 54.02 . 1 262 . 65 ARG N N 122.43 . 1 263 . 66 PHE H H 9.31 . 1 264 . 66 PHE HA H 5.43 . 1 265 . 66 PHE C C 174.27 . 1 266 . 66 PHE CA C 55.98 . 1 267 . 66 PHE N N 117.80 . 1 268 . 67 GLY H H 8.30 . 1 269 . 67 GLY HA2 H 2.80 . 2 270 . 67 GLY HA3 H 4.82 . 2 271 . 67 GLY C C 171.50 . 1 272 . 67 GLY CA C 45.59 . 1 273 . 67 GLY N N 105.93 . 1 274 . 68 ILE H H 8.81 . 1 275 . 68 ILE HA H 4.50 . 1 276 . 68 ILE C C 175.64 . 1 277 . 68 ILE CA C 57.37 . 1 278 . 68 ILE N N 123.08 . 1 279 . 69 HIS H H 9.27 . 1 280 . 69 HIS HA H 4.70 . 1 281 . 69 HIS CA C 54.86 . 1 282 . 69 HIS N N 132.24 . 1 283 . 70 PRO HA H 4.55 . 1 284 . 70 PRO C C 178.72 . 1 285 . 70 PRO CA C 65.11 . 1 286 . 71 VAL H H 10.63 . 1 287 . 71 VAL HA H 4.75 . 1 288 . 71 VAL C C 177.04 . 1 289 . 71 VAL CA C 60.00 . 1 290 . 71 VAL N N 113.18 . 1 291 . 72 ALA H H 8.01 . 1 292 . 72 ALA HA H 4.56 . 1 293 . 72 ALA C C 180.13 . 1 294 . 72 ALA CA C 53.72 . 1 295 . 72 ALA N N 123.70 . 1 296 . 73 GLY H H 9.86 . 1 297 . 73 GLY HA2 H 3.32 . 2 298 . 73 GLY HA3 H 4.69 . 2 299 . 73 GLY CA C 45.12 . 1 300 . 73 GLY N N 107.17 . 1 301 . 74 ARG H H 10.93 . 1 302 . 74 ARG C C 173.71 . 1 303 . 74 ARG CA C 54.10 . 1 304 . 74 ARG N N 122.10 . 1 305 . 75 LEU H H 7.38 . 1 306 . 75 LEU HA H 4.73 . 1 307 . 75 LEU CA C 52.88 . 1 308 . 75 LEU N N 120.16 . 1 309 . 76 PRO HA H 4.59 . 1 310 . 76 PRO C C 178.41 . 1 311 . 76 PRO CA C 63.82 . 1 312 . 77 GLY H H 9.24 . 1 313 . 77 GLY HA2 H 3.40 . 2 314 . 77 GLY HA3 H 3.98 . 2 315 . 77 GLY C C 175.15 . 1 316 . 77 GLY CA C 46.81 . 1 317 . 77 GLY N N 114.39 . 1 318 . 78 HIS H H 7.79 . 1 319 . 78 HIS HA H 4.12 . 1 320 . 78 HIS C C 178.19 . 1 321 . 78 HIS CA C 57.90 . 1 322 . 78 HIS N N 119.78 . 1 323 . 79 MET H H 9.14 . 1 324 . 79 MET HA H 4.07 . 1 325 . 79 MET C C 177.64 . 1 326 . 79 MET CA C 56.62 . 1 327 . 79 MET N N 111.03 . 1 328 . 80 ASN H H 7.72 . 1 329 . 80 ASN HA H 3.89 . 1 330 . 80 ASN C C 178.18 . 1 331 . 80 ASN CA C 57.23 . 1 332 . 80 ASN N N 114.50 . 1 333 . 81 VAL H H 7.78 . 1 334 . 81 VAL HA H 3.68 . 1 335 . 81 VAL C C 178.35 . 1 336 . 81 VAL CA C 65.94 . 1 337 . 81 VAL N N 118.06 . 1 338 . 82 LEU H H 7.50 . 1 339 . 82 LEU HA H 3.95 . 1 340 . 82 LEU C C 178.98 . 1 341 . 82 LEU CA C 57.43 . 1 342 . 82 LEU N N 118.49 . 1 343 . 83 LEU H H 7.82 . 1 344 . 83 LEU HA H 3.56 . 1 345 . 83 LEU C C 177.90 . 1 346 . 83 LEU CA C 57.28 . 1 347 . 83 LEU N N 115.92 . 1 348 . 84 ALA H H 7.66 . 1 349 . 84 ALA HA H 4.05 . 1 350 . 84 ALA C C 182.71 . 1 351 . 84 ALA CA C 54.95 . 1 352 . 84 ALA N N 121.02 . 1 353 . 85 GLU H H 8.09 . 1 354 . 85 GLU HA H 3.96 . 1 355 . 85 GLU C C 177.13 . 1 356 . 85 GLU CA C 59.22 . 1 357 . 85 GLU N N 121.58 . 1 358 . 86 ALA H H 6.96 . 1 359 . 86 ALA HA H 4.16 . 1 360 . 86 ALA C C 174.35 . 1 361 . 86 ALA CA C 51.31 . 1 362 . 86 ALA N N 117.85 . 1 363 . 87 LYS H H 7.61 . 1 364 . 87 LYS HA H 3.66 . 1 365 . 87 LYS C C 176.43 . 1 366 . 87 LYS CA C 56.71 . 1 367 . 87 LYS N N 110.69 . 1 368 . 88 VAL H H 7.73 . 1 369 . 88 VAL HA H 3.92 . 1 370 . 88 VAL C C 177.56 . 1 371 . 88 VAL CA C 61.24 . 1 372 . 88 VAL N N 122.22 . 1 373 . 89 PRO HA H 4.21 . 1 374 . 89 PRO C C 176.96 . 1 375 . 89 PRO CA C 63.29 . 1 376 . 90 TYR H H 8.04 . 1 377 . 90 TYR HA H 4.48 . 1 378 . 90 TYR C C 177.70 . 1 379 . 90 TYR CA C 61.15 . 1 380 . 90 TYR N N 119.99 . 1 381 . 91 ASP H H 8.29 . 1 382 . 91 ASP HA H 4.22 . 1 383 . 91 ASP C C 176.93 . 1 384 . 91 ASP CA C 55.15 . 1 385 . 91 ASP N N 113.37 . 1 386 . 92 ILE H H 7.06 . 1 387 . 92 ILE HA H 4.60 . 1 388 . 92 ILE C C 173.12 . 1 389 . 92 ILE CA C 60.62 . 1 390 . 92 ILE N N 109.13 . 1 391 . 93 VAL H H 7.41 . 1 392 . 93 VAL HA H 4.09 . 1 393 . 93 VAL C C 173.22 . 1 394 . 93 VAL CA C 63.18 . 1 395 . 93 VAL N N 123.44 . 1 396 . 94 LEU H H 8.53 . 1 397 . 94 LEU HA H 4.72 . 1 398 . 94 LEU C C 175.53 . 1 399 . 94 LEU CA C 54.45 . 1 400 . 94 LEU N N 129.25 . 1 401 . 95 GLU H H 8.80 . 1 402 . 95 GLU HA H 4.43 . 1 403 . 95 GLU C C 178.16 . 1 404 . 95 GLU CA C 55.42 . 1 405 . 95 GLU N N 118.81 . 1 406 . 96 MET H H 7.89 . 1 407 . 96 MET HA H 4.18 . 1 408 . 96 MET C C 175.92 . 1 409 . 96 MET CA C 59.76 . 1 410 . 96 MET N N 120.29 . 1 411 . 97 ASP H H 8.87 . 1 412 . 97 ASP HA H 3.90 . 1 413 . 97 ASP C C 177.35 . 1 414 . 97 ASP CA C 57.34 . 1 415 . 97 ASP N N 115.59 . 1 416 . 98 GLU H H 7.64 . 1 417 . 98 GLU HA H 4.25 . 1 418 . 98 GLU C C 176.57 . 1 419 . 98 GLU CA C 56.98 . 1 420 . 98 GLU N N 115.95 . 1 421 . 99 ILE H H 7.44 . 1 422 . 99 ILE HA H 4.16 . 1 423 . 99 ILE C C 175.49 . 1 424 . 99 ILE CA C 60.59 . 1 425 . 99 ILE N N 117.47 . 1 426 . 100 ASN H H 7.81 . 1 427 . 100 ASN HA H 4.76 . 1 428 . 100 ASN C C 178.10 . 1 429 . 100 ASN CA C 54.73 . 1 430 . 100 ASN N N 121.57 . 1 431 . 101 ASP H H 8.35 . 1 432 . 101 ASP HA H 4.43 . 1 433 . 101 ASP C C 177.00 . 1 434 . 101 ASP CA C 56.27 . 1 435 . 101 ASP N N 115.86 . 1 436 . 102 ASP H H 7.94 . 1 437 . 102 ASP HA H 4.49 . 1 438 . 102 ASP C C 179.87 . 1 439 . 102 ASP CA C 54.87 . 1 440 . 102 ASP N N 117.51 . 1 441 . 103 PHE H H 7.22 . 1 442 . 103 PHE HA H 3.77 . 1 443 . 103 PHE C C 176.54 . 1 444 . 103 PHE CA C 64.62 . 1 445 . 103 PHE N N 121.20 . 1 446 . 104 ALA H H 8.02 . 1 447 . 104 ALA HA H 4.07 . 1 448 . 104 ALA C C 177.24 . 1 449 . 104 ALA CA C 53.81 . 1 450 . 104 ALA N N 116.36 . 1 451 . 105 ASP H H 7.18 . 1 452 . 105 ASP HA H 4.91 . 1 453 . 105 ASP C C 175.51 . 1 454 . 105 ASP CA C 53.31 . 1 455 . 105 ASP N N 115.72 . 1 456 . 106 THR H H 7.57 . 1 457 . 106 THR HA H 4.53 . 1 458 . 106 THR C C 173.62 . 1 459 . 106 THR CA C 62.75 . 1 460 . 106 THR N N 117.33 . 1 461 . 107 ASP H H 8.36 . 1 462 . 107 ASP HA H 4.61 . 1 463 . 107 ASP C C 176.01 . 1 464 . 107 ASP CA C 58.15 . 1 465 . 107 ASP N N 126.73 . 1 466 . 108 THR H H 7.47 . 1 467 . 108 THR HA H 5.40 . 1 468 . 108 THR C C 172.38 . 1 469 . 108 THR CA C 61.37 . 1 470 . 108 THR N N 114.00 . 1 471 . 109 VAL H H 9.00 . 1 472 . 109 VAL HA H 5.48 . 1 473 . 109 VAL C C 175.09 . 1 474 . 109 VAL CA C 59.09 . 1 475 . 109 VAL N N 125.80 . 1 476 . 110 LEU H H 8.54 . 1 477 . 110 LEU HA H 5.13 . 1 478 . 110 LEU C C 174.17 . 1 479 . 110 LEU CA C 52.20 . 1 480 . 110 LEU N N 123.55 . 1 481 . 111 VAL H H 9.82 . 1 482 . 111 VAL HA H 4.38 . 1 483 . 111 VAL C C 175.06 . 1 484 . 111 VAL CA C 60.96 . 1 485 . 111 VAL N N 127.35 . 1 486 . 112 ILE H H 7.22 . 1 487 . 112 ILE HA H 4.08 . 1 488 . 112 ILE C C 174.32 . 1 489 . 112 ILE CA C 60.43 . 1 490 . 112 ILE N N 124.26 . 1 491 . 113 GLY H H 8.32 . 1 492 . 113 GLY HA2 H 4.10 . 2 493 . 113 GLY HA3 H 3.43 . 2 494 . 113 GLY C C 170.95 . 1 495 . 113 GLY CA C 46.85 . 1 496 . 113 GLY N N 111.70 . 1 497 . 114 ALA H H 6.39 . 1 498 . 114 ALA HA H 5.20 . 1 499 . 114 ALA C C 175.87 . 1 500 . 114 ALA CA C 49.75 . 1 501 . 114 ALA N N 117.53 . 1 502 . 115 ASN H H 9.69 . 1 503 . 115 ASN HA H 4.39 . 1 504 . 115 ASN C C 174.20 . 1 505 . 115 ASN CA C 55.62 . 1 506 . 115 ASN N N 116.34 . 1 507 . 116 ASP H H 10.40 . 1 508 . 116 ASP C C 176.79 . 1 509 . 116 ASP CA C 58.35 . 1 510 . 116 ASP N N 124.45 . 1 511 . 117 THR H H 7.27 . 1 512 . 117 THR HA H 3.56 . 1 513 . 117 THR C C 173.94 . 1 514 . 117 THR CA C 63.27 . 1 515 . 117 THR N N 99.65 . 1 516 . 118 VAL H H 7.38 . 1 517 . 118 VAL HA H 5.05 . 1 518 . 118 VAL C C 173.20 . 1 519 . 118 VAL CA C 59.32 . 1 520 . 118 VAL N N 111.41 . 1 521 . 119 ASN H H 6.63 . 1 522 . 119 ASN HA H 5.19 . 1 523 . 119 ASN C C 174.53 . 1 524 . 119 ASN CA C 50.45 . 1 525 . 119 ASN N N 117.49 . 1 526 . 120 PRO HA H 4.37 . 1 527 . 120 PRO C C 178.11 . 1 528 . 120 PRO CA C 64.97 . 1 529 . 121 ALA H H 9.29 . 1 530 . 121 ALA HA H 4.02 . 1 531 . 121 ALA C C 176.42 . 1 532 . 121 ALA CA C 54.55 . 1 533 . 121 ALA N N 123.69 . 1 534 . 122 ALA H H 7.51 . 1 535 . 122 ALA HA H 4.24 . 1 536 . 122 ALA C C 177.17 . 1 537 . 122 ALA CA C 52.38 . 1 538 . 122 ALA N N 115.95 . 1 539 . 123 GLN H H 7.61 . 1 540 . 123 GLN HA H 4.35 . 1 541 . 123 GLN C C 177.10 . 1 542 . 123 GLN CA C 56.28 . 1 543 . 123 GLN N N 113.41 . 1 544 . 124 ASP H H 7.95 . 1 545 . 124 ASP HA H 4.53 . 1 546 . 124 ASP C C 175.77 . 1 547 . 124 ASP CA C 55.22 . 1 548 . 124 ASP N N 116.96 . 1 549 . 125 ASP H H 8.03 . 1 550 . 125 ASP HA H 5.16 . 1 551 . 125 ASP C C 175.07 . 1 552 . 125 ASP CA C 50.33 . 1 553 . 125 ASP N N 119.03 . 1 554 . 126 PRO HA H 4.54 . 1 555 . 126 PRO C C 177.12 . 1 556 . 126 PRO CA C 63.14 . 1 557 . 127 LYS H H 7.99 . 1 558 . 127 LYS HA H 4.30 . 1 559 . 127 LYS C C 178.40 . 1 560 . 127 LYS CA C 55.09 . 1 561 . 127 LYS N N 115.15 . 1 562 . 128 SER H H 7.48 . 1 563 . 128 SER HA H 4.46 . 1 564 . 128 SER C C 176.10 . 1 565 . 128 SER CA C 56.50 . 1 566 . 128 SER N N 116.21 . 1 567 . 129 PRO HA H 4.48 . 1 568 . 129 PRO C C 177.55 . 1 569 . 129 PRO CA C 64.67 . 1 570 . 130 ILE H H 7.37 . 1 571 . 130 ILE HA H 4.52 . 1 572 . 130 ILE C C 173.97 . 1 573 . 130 ILE CA C 60.15 . 1 574 . 130 ILE N N 108.38 . 1 575 . 131 ALA H H 7.51 . 1 576 . 131 ALA HA H 4.19 . 1 577 . 131 ALA C C 179.41 . 1 578 . 131 ALA CA C 53.82 . 1 579 . 131 ALA N N 122.72 . 1 580 . 132 GLY H H 8.87 . 1 581 . 132 GLY HA2 H 3.69 . 2 582 . 132 GLY HA3 H 4.18 . 2 583 . 132 GLY C C 174.10 . 1 584 . 132 GLY CA C 45.23 . 1 585 . 132 GLY N N 110.29 . 1 586 . 133 MET H H 8.05 . 1 587 . 133 MET HA H 4.61 . 1 588 . 133 MET CA C 54.05 . 1 589 . 133 MET N N 123.64 . 1 590 . 134 PRO HA H 4.40 . 1 591 . 134 PRO C C 176.80 . 1 592 . 134 PRO CA C 62.94 . 1 593 . 135 VAL H H 8.08 . 1 594 . 135 VAL HA H 4.78 . 1 595 . 135 VAL C C 174.59 . 1 596 . 135 VAL CA C 59.99 . 1 597 . 135 VAL N N 114.37 . 1 598 . 136 LEU H H 8.33 . 1 599 . 136 LEU HA H 4.59 . 1 600 . 136 LEU C C 176.92 . 1 601 . 136 LEU CA C 54.28 . 1 602 . 136 LEU N N 120.67 . 1 603 . 137 GLU H H 8.33 . 1 604 . 137 GLU HA H 2.30 . 1 605 . 137 GLU C C 176.67 . 1 606 . 137 GLU CA C 54.08 . 1 607 . 137 GLU N N 124.98 . 1 608 . 138 VAL H H 7.32 . 1 609 . 138 VAL HA H 2.19 . 1 610 . 138 VAL C C 174.70 . 1 611 . 138 VAL CA C 62.69 . 1 612 . 138 VAL N N 111.48 . 1 613 . 139 TRP H H 6.51 . 1 614 . 139 TRP HA H 4.45 . 1 615 . 139 TRP C C 175.65 . 1 616 . 139 TRP CA C 58.36 . 1 617 . 139 TRP N N 110.91 . 1 618 . 140 LYS H H 6.59 . 1 619 . 140 LYS HA H 4.02 . 1 620 . 140 LYS C C 175.55 . 1 621 . 140 LYS CA C 57.43 . 1 622 . 140 LYS N N 120.23 . 1 623 . 141 ALA H H 7.24 . 1 624 . 141 ALA HA H 4.75 . 1 625 . 141 ALA C C 176.74 . 1 626 . 141 ALA CA C 51.76 . 1 627 . 141 ALA N N 120.90 . 1 628 . 142 GLN H H 7.63 . 1 629 . 142 GLN HA H 4.08 . 1 630 . 142 GLN C C 177.28 . 1 631 . 142 GLN CA C 59.82 . 1 632 . 142 GLN N N 116.49 . 1 633 . 143 ASN H H 8.16 . 1 634 . 143 ASN HA H 5.39 . 1 635 . 143 ASN C C 172.27 . 1 636 . 143 ASN CA C 53.27 . 1 637 . 143 ASN N N 113.24 . 1 638 . 144 VAL H H 8.85 . 1 639 . 144 VAL HA H 4.58 . 1 640 . 144 VAL C C 174.08 . 1 641 . 144 VAL CA C 61.61 . 1 642 . 144 VAL N N 122.09 . 1 643 . 145 ILE H H 9.18 . 1 644 . 145 ILE HA H 5.18 . 1 645 . 145 ILE C C 175.06 . 1 646 . 145 ILE CA C 59.30 . 1 647 . 145 ILE N N 128.09 . 1 648 . 146 VAL H H 9.03 . 1 649 . 146 VAL HA H 4.66 . 1 650 . 146 VAL C C 173.30 . 1 651 . 146 VAL CA C 62.12 . 1 652 . 146 VAL N N 127.54 . 1 653 . 147 PHE H H 9.36 . 1 654 . 147 PHE HA H 5.43 . 1 655 . 147 PHE C C 175.13 . 1 656 . 147 PHE CA C 55.91 . 1 657 . 147 PHE N N 127.08 . 1 658 . 148 LYS H H 7.88 . 1 659 . 148 LYS HA H 5.82 . 1 660 . 148 LYS C C 175.30 . 1 661 . 148 LYS CA C 54.96 . 1 662 . 148 LYS N N 118.50 . 1 663 . 149 ARG H H 10.66 . 1 664 . 149 ARG C C 177.61 . 1 665 . 149 ARG CA C 59.29 . 1 666 . 149 ARG N N 120.84 . 1 667 . 150 SER H H 9.22 . 1 668 . 150 SER HA H 4.32 . 1 669 . 150 SER C C 173.42 . 1 670 . 150 SER CA C 57.88 . 1 671 . 150 SER N N 118.23 . 1 672 . 151 MET H H 8.13 . 1 673 . 151 MET HA H 4.87 . 1 674 . 151 MET C C 176.62 . 1 675 . 151 MET CA C 53.47 . 1 676 . 151 MET N N 115.92 . 1 677 . 152 ASN H H 8.55 . 1 678 . 152 ASN HA H 4.60 . 1 679 . 152 ASN C C 176.99 . 1 680 . 152 ASN CA C 53.56 . 1 681 . 152 ASN N N 118.87 . 1 682 . 153 THR H H 8.18 . 1 683 . 153 THR HA H 4.86 . 1 684 . 153 THR C C 174.84 . 1 685 . 153 THR CA C 61.43 . 1 686 . 153 THR N N 110.04 . 1 687 . 154 GLY H H 8.64 . 1 688 . 154 GLY HA2 H 4.30 . 2 689 . 154 GLY HA3 H 4.59 . 2 690 . 154 GLY C C 174.69 . 1 691 . 154 GLY CA C 43.87 . 1 692 . 154 GLY N N 108.72 . 1 693 . 155 TYR H H 8.54 . 1 694 . 155 TYR HA H 4.70 . 1 695 . 155 TYR C C 178.10 . 1 696 . 155 TYR CA C 62.07 . 1 697 . 155 TYR N N 125.58 . 1 698 . 156 ALA H H 10.96 . 1 699 . 156 ALA HA H 3.71 . 1 700 . 156 ALA C C 178.10 . 1 701 . 156 ALA CA C 53.26 . 1 702 . 156 ALA N N 120.44 . 1 703 . 157 GLY H H 7.88 . 1 704 . 157 GLY HA2 H 3.89 . 1 705 . 157 GLY HA3 H 3.89 . 1 706 . 157 GLY C C 174.47 . 1 707 . 157 GLY CA C 46.35 . 1 708 . 157 GLY N N 105.34 . 1 709 . 158 VAL H H 8.49 . 1 710 . 158 VAL HA H 4.68 . 1 711 . 158 VAL C C 175.46 . 1 712 . 158 VAL CA C 58.85 . 1 713 . 158 VAL N N 112.97 . 1 714 . 159 GLN H H 8.62 . 1 715 . 159 GLN HA H 3.99 . 1 716 . 159 GLN C C 174.29 . 1 717 . 159 GLN CA C 55.73 . 1 718 . 159 GLN N N 121.43 . 1 719 . 160 ASN H H 8.35 . 1 720 . 160 ASN HA H 5.07 . 1 721 . 160 ASN CA C 49.29 . 1 722 . 160 ASN N N 121.12 . 1 723 . 161 PRO HA H 4.26 . 1 724 . 161 PRO C C 178.53 . 1 725 . 161 PRO CA C 63.50 . 1 726 . 162 LEU H H 8.37 . 1 727 . 162 LEU HA H 3.58 . 1 728 . 162 LEU C C 178.44 . 1 729 . 162 LEU CA C 57.68 . 1 730 . 162 LEU N N 118.25 . 1 731 . 163 PHE H H 6.92 . 1 732 . 163 PHE HA H 4.42 . 1 733 . 163 PHE C C 173.80 . 1 734 . 163 PHE CA C 55.02 . 1 735 . 163 PHE N N 112.85 . 1 736 . 164 PHE H H 7.11 . 1 737 . 164 PHE HA H 4.93 . 1 738 . 164 PHE C C 176.44 . 1 739 . 164 PHE CA C 54.92 . 1 740 . 164 PHE N N 113.98 . 1 741 . 165 LYS H H 7.26 . 1 742 . 165 LYS HA H 4.32 . 1 743 . 165 LYS C C 178.65 . 1 744 . 165 LYS CA C 56.70 . 1 745 . 165 LYS N N 120.38 . 1 746 . 166 GLU H H 9.10 . 1 747 . 166 GLU HA H 3.85 . 1 748 . 166 GLU C C 175.24 . 1 749 . 166 GLU CA C 58.98 . 1 750 . 166 GLU N N 120.10 . 1 751 . 167 ASN H H 8.49 . 1 752 . 167 ASN HA H 4.87 . 1 753 . 167 ASN C C 175.68 . 1 754 . 167 ASN CA C 52.10 . 1 755 . 167 ASN N N 112.52 . 1 756 . 168 THR H H 7.61 . 1 757 . 168 THR HA H 5.29 . 1 758 . 168 THR C C 174.27 . 1 759 . 168 THR CA C 61.18 . 1 760 . 168 THR N N 117.99 . 1 761 . 169 HIS H H 9.37 . 1 762 . 169 HIS HA H 5.04 . 1 763 . 169 HIS C C 174.00 . 1 764 . 169 HIS CA C 55.17 . 1 765 . 169 HIS N N 126.11 . 1 766 . 170 MET H H 9.02 . 1 767 . 170 MET HA H 4.50 . 1 768 . 170 MET C C 173.90 . 1 769 . 170 MET CA C 52.55 . 1 770 . 170 MET N N 119.72 . 1 771 . 171 LEU H H 8.83 . 1 772 . 171 LEU HA H 4.52 . 1 773 . 171 LEU C C 175.50 . 1 774 . 171 LEU CA C 52.64 . 1 775 . 171 LEU N N 129.51 . 1 776 . 172 PHE H H 8.63 . 1 777 . 172 PHE HA H 5.59 . 1 778 . 172 PHE C C 177.10 . 1 779 . 172 PHE CA C 57.35 . 1 780 . 172 PHE N N 123.68 . 1 781 . 173 GLY H H 8.72 . 1 782 . 173 GLY HA2 H 3.91 . 2 783 . 173 GLY HA3 H 4.31 . 2 784 . 173 GLY C C 173.79 . 1 785 . 173 GLY CA C 43.82 . 1 786 . 173 GLY N N 110.11 . 1 787 . 174 ASP H H 8.84 . 1 788 . 174 ASP HA H 4.69 . 1 789 . 174 ASP C C 177.92 . 1 790 . 174 ASP CA C 54.79 . 1 791 . 174 ASP N N 122.09 . 1 792 . 175 ALA H H 10.81 . 1 793 . 175 ALA HA H 4.05 . 1 794 . 175 ALA C C 178.65 . 1 795 . 175 ALA CA C 55.90 . 1 796 . 175 ALA N N 126.14 . 1 797 . 176 LYS H H 7.95 . 1 798 . 176 LYS HA H 3.72 . 1 799 . 176 LYS C C 176.69 . 1 800 . 176 LYS CA C 60.26 . 1 801 . 176 LYS N N 116.00 . 1 802 . 177 ALA H H 7.69 . 1 803 . 177 ALA HA H 4.18 . 1 804 . 177 ALA C C 181.83 . 1 805 . 177 ALA CA C 55.19 . 1 806 . 177 ALA N N 121.30 . 1 807 . 178 SER H H 8.91 . 1 808 . 178 SER HA H 4.18 . 1 809 . 178 SER C C 175.55 . 1 810 . 178 SER CA C 61.75 . 1 811 . 178 SER N N 115.22 . 1 812 . 179 VAL H H 8.23 . 1 813 . 179 VAL HA H 3.64 . 1 814 . 179 VAL C C 177.33 . 1 815 . 179 VAL CA C 67.35 . 1 816 . 179 VAL N N 119.39 . 1 817 . 180 ASP H H 8.85 . 1 818 . 180 ASP HA H 4.40 . 1 819 . 180 ASP C C 178.70 . 1 820 . 180 ASP CA C 57.80 . 1 821 . 180 ASP N N 120.95 . 1 822 . 181 ALA H H 7.79 . 1 823 . 181 ALA HA H 4.07 . 1 824 . 181 ALA C C 180.57 . 1 825 . 181 ALA CA C 54.99 . 1 826 . 181 ALA N N 121.12 . 1 827 . 182 ILE H H 8.02 . 1 828 . 182 ILE HA H 3.59 . 1 829 . 182 ILE C C 177.55 . 1 830 . 182 ILE CA C 62.53 . 1 831 . 182 ILE N N 120.00 . 1 832 . 183 LEU H H 8.44 . 1 833 . 183 LEU HA H 3.77 . 1 834 . 183 LEU C C 179.11 . 1 835 . 183 LEU CA C 59.38 . 1 836 . 183 LEU N N 118.75 . 1 837 . 184 LYS H H 7.48 . 1 838 . 184 LYS HA H 4.04 . 1 839 . 184 LYS C C 176.43 . 1 840 . 184 LYS CA C 58.15 . 1 841 . 184 LYS N N 115.96 . 1 842 . 185 ALA H H 7.49 . 1 843 . 185 ALA HA H 4.41 . 1 844 . 185 ALA C C 176.24 . 1 845 . 185 ALA CA C 51.63 . 1 846 . 185 ALA N N 120.55 . 1 847 . 186 LEU H H 7.19 . 1 848 . 186 LEU HA H 3.93 . 1 849 . 186 LEU C C 181.07 . 1 850 . 186 LEU CA C 57.11 . 1 851 . 186 LEU N N 124.86 . 1 stop_ save_