data_4236 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific Resonance Assignments for the NADP(H)-binding Component (domain III) of Proton-translocating Transhydrogenase from Rhodospirillum rubrum. ; _BMRB_accession_number 4236 _BMRB_flat_file_name bmr4236.str _Entry_type original _Submission_date 1998-10-02 _Accession_date 1998-10-14 _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 Jeeves Mark . . 2 Smith John K. . 3 Quirk Philip G. . 4 Cotton Nick P.J. . 5 Jackson Baz J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 387 "13C chemical shifts" 549 "15N chemical shifts" 182 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11004437 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jeeves Mark . . 2 Smith John K. . 3 Quirk Philip G. . 4 Cotton Nick P.J. . 5 Jackson Baz J. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_volume 1459 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 248 _Page_last 257 _Year 2000 _Details . loop_ _Keyword NADP(H) 'NMR assignment' nucleotide-binding 'proton translocation' 'Rhodospirillum rubrum' transhydrogenase stop_ save_ ################################## # Molecular system description # ################################## save_system_THIII-NADP _Saveframe_category molecular_system _Mol_system_name THIII-NADP _Abbreviation_common THIII-NADP _Enzyme_commission_number 1.6.1.1 loop_ _Mol_system_component_name _Mol_label THIII $THIII NADP $entity_NAP stop_ _System_molecular_weight 22209 _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; THIII, NADP(H)-binding component (domain III) of proton-translocating transhydrogenase ; stop_ _Database_query_date . _Details ; This is the 1:1 complex of THIII and NADP. Complex of proton-translocating nicotinamide nucleotide transhydrogenase domain III with nicotinamide-adenine-dinucleotide phosphate. ; save_ ######################## # Monomeric polymers # ######################## save_THIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Proton-translocating nicotinamide nucleotide transhydrogenase domain III' _Abbreviation_common dIII _Molecular_mass 21466 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 203 _Mol_residue_sequence ; MNRSIFNVILGGFGSEGGVA AAGGAAGDRSVKAGSAEDAA FIMKNASKVIIVPGYGMAVA QAQHALREMADVLKKEGVEV SYAIHPVAGRMPGHMNVLLA EANVPYDEVFELEEINSSFQ TADVAFVIGANDVTNPAAKT DPSSPIYGMPILDVEKAGTV LFIKRSMASGYAGVENELFF RNNTMMLFGDAKKMTEQIVQ AMN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASN 3 3 ARG 4 4 SER 5 5 ILE 6 6 PHE 7 7 ASN 8 8 VAL 9 9 ILE 10 10 LEU 11 11 GLY 12 12 GLY 13 13 PHE 14 14 GLY 15 15 SER 16 16 GLU 17 17 GLY 18 18 GLY 19 19 VAL 20 20 ALA 21 21 ALA 22 22 ALA 23 23 GLY 24 24 GLY 25 25 ALA 26 26 ALA 27 27 GLY 28 28 ASP 29 29 ARG 30 30 SER 31 31 VAL 32 32 LYS 33 33 ALA 34 34 GLY 35 35 SER 36 36 ALA 37 37 GLU 38 38 ASP 39 39 ALA 40 40 ALA 41 41 PHE 42 42 ILE 43 43 MET 44 44 LYS 45 45 ASN 46 46 ALA 47 47 SER 48 48 LYS 49 49 VAL 50 50 ILE 51 51 ILE 52 52 VAL 53 53 PRO 54 54 GLY 55 55 TYR 56 56 GLY 57 57 MET 58 58 ALA 59 59 VAL 60 60 ALA 61 61 GLN 62 62 ALA 63 63 GLN 64 64 HIS 65 65 ALA 66 66 LEU 67 67 ARG 68 68 GLU 69 69 MET 70 70 ALA 71 71 ASP 72 72 VAL 73 73 LEU 74 74 LYS 75 75 LYS 76 76 GLU 77 77 GLY 78 78 VAL 79 79 GLU 80 80 VAL 81 81 SER 82 82 TYR 83 83 ALA 84 84 ILE 85 85 HIS 86 86 PRO 87 87 VAL 88 88 ALA 89 89 GLY 90 90 ARG 91 91 MET 92 92 PRO 93 93 GLY 94 94 HIS 95 95 MET 96 96 ASN 97 97 VAL 98 98 LEU 99 99 LEU 100 100 ALA 101 101 GLU 102 102 ALA 103 103 ASN 104 104 VAL 105 105 PRO 106 106 TYR 107 107 ASP 108 108 GLU 109 109 VAL 110 110 PHE 111 111 GLU 112 112 LEU 113 113 GLU 114 114 GLU 115 115 ILE 116 116 ASN 117 117 SER 118 118 SER 119 119 PHE 120 120 GLN 121 121 THR 122 122 ALA 123 123 ASP 124 124 VAL 125 125 ALA 126 126 PHE 127 127 VAL 128 128 ILE 129 129 GLY 130 130 ALA 131 131 ASN 132 132 ASP 133 133 VAL 134 134 THR 135 135 ASN 136 136 PRO 137 137 ALA 138 138 ALA 139 139 LYS 140 140 THR 141 141 ASP 142 142 PRO 143 143 SER 144 144 SER 145 145 PRO 146 146 ILE 147 147 TYR 148 148 GLY 149 149 MET 150 150 PRO 151 151 ILE 152 152 LEU 153 153 ASP 154 154 VAL 155 155 GLU 156 156 LYS 157 157 ALA 158 158 GLY 159 159 THR 160 160 VAL 161 161 LEU 162 162 PHE 163 163 ILE 164 164 LYS 165 165 ARG 166 166 SER 167 167 MET 168 168 ALA 169 169 SER 170 170 GLY 171 171 TYR 172 172 ALA 173 173 GLY 174 174 VAL 175 175 GLU 176 176 ASN 177 177 GLU 178 178 LEU 179 179 PHE 180 180 PHE 181 181 ARG 182 182 ASN 183 183 ASN 184 184 THR 185 185 MET 186 186 MET 187 187 LEU 188 188 PHE 189 189 GLY 190 190 ASP 191 191 ALA 192 192 LYS 193 193 LYS 194 194 MET 195 195 THR 196 196 GLU 197 197 GLN 198 198 ILE 199 199 VAL 200 200 GLN 201 201 ALA 202 202 MET 203 203 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-15 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 1E3T "Solution Structure Of The Nadp(H) Binding Component (Diii) Of Proton-Translocating Transhydrogenase From Rhodospirillum Rubrum" 100.00 203 100.00 100.00 6.77e-143 PDB 1HZZ "The Asymmetric Complex Of The Two Nucleotide-Binding Components (Di, Diii) Of Proton-Translocating Transhydrogenase" 100.00 203 100.00 100.00 6.77e-143 PDB 1NM5 "R. Rubrum Transhydrogenase (Di.Q132n)2(Diii)1 Asymmetric Complex" 100.00 203 100.00 100.00 6.77e-143 PDB 1PNO "Crystal Structure Of R. Rubrum Transhydrogenase Domain Iii Bound To Nadp" 84.24 180 100.00 100.00 4.47e-119 PDB 1PNQ "Crystal Structure Of R. Rubrum Transhydrogenase Domain Iii Bound To Nadph" 84.24 180 100.00 100.00 4.47e-119 PDB 1PTJ "Crystal Structure Analysis Of The Di And Diii Complex Of Transhydrogenase With A Thio-Nicotinamide Nucleotide Analogue" 85.71 174 100.00 100.00 1.56e-121 PDB 1U28 "R. Rubrum Transhydrogenase Asymmetric Complex (Di.Nad+)2(Diii.Nadp+)1" 100.00 203 100.00 100.00 6.77e-143 PDB 1U2D "Structre Of Transhydrogenaes (Di.Nadh)2(Diii.Nadph)1 Asymmetric Complex" 100.00 203 100.00 100.00 6.77e-143 PDB 1U2G "Transhydrogenase (Di.Adpr)2(Diii.Nadph)1 Asymmetric Complex" 100.00 203 100.00 100.00 6.77e-143 PDB 1XLT "Crystal Structure Of Transhydrogenase [(Domain I)2:domain Iii] Heterotrimer Complex" 84.24 174 100.00 100.00 2.67e-119 PDB 2FR8 "Structure Of Transhydrogenase (Di.R127a.Nad+)2(Diii.Nadp+)1 Asymmetric Complex" 100.00 203 100.00 100.00 6.77e-143 PDB 2FRD "Structure Of Transhydrogenase (di.s138a.nadh)2(diii.nadph)1 Asymmetric Complex" 100.00 203 100.00 100.00 6.77e-143 PDB 2FSV "Structure Of Transhydrogenase (Di.D135n.Nad+)2(Diii.E155w.Nadp+)1 Asymmetric Complex" 100.00 203 99.51 99.51 6.03e-142 PDB 2OO5 "Structure Of Transhydrogenase (Di.H2nadh)2(Diii.Nadp+)1 Asymmetric Complex" 85.71 174 100.00 100.00 1.56e-121 PDB 2OOR "Structure Of Transhydrogenase (Di.Nad+)2(Diii.H2nadph)1 Asymmetric Complex" 85.71 174 100.00 100.00 1.56e-121 GB AAA62495 "proton-translocating nicotinamide nucleotide transhydrogenase subunit PntB [Rhodospirillum rubrum ATCC 11170]" 100.00 464 100.00 100.00 2.77e-141 GB AAC43257 "nicotinamide nucleotide transhydrogenase, subunit beta [Rhodospirillum rubrum]" 100.00 464 100.00 100.00 2.77e-141 GB ABC22981 "NAD(P) transhydrogenase, beta subunit [Rhodospirillum rubrum ATCC 11170]" 100.00 464 100.00 100.00 2.77e-141 GB AEO48711 "NAD(P) transhydrogenase, subunit beta [Rhodospirillum rubrum F11]" 100.00 464 100.00 100.00 2.77e-141 PRF 2102322C "energy-transducing nicotinamide nucleotide transhydrogenase:" 100.00 464 100.00 100.00 2.77e-141 REF WP_011390030 "NAD(P) transhydrogenase subunit beta [Rhodospirillum rubrum]" 100.00 464 100.00 100.00 2.77e-141 REF YP_427268 "NAD(P) transhydrogenase subunit beta [Rhodospirillum rubrum ATCC 11170]" 100.00 464 100.00 100.00 2.77e-141 SP P0C188 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 100.00 464 100.00 100.00 2.77e-141 SP Q2RSB4 "RecName: Full=NAD(P) transhydrogenase subunit beta; AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; AltNam" 100.00 464 100.00 100.00 2.77e-141 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 no _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 'not present' _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $THIII R.rubrum 1085 Eubacteria . Rhodospirillum rubrum S1 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 _Vendor_name _Details $THIII 'recombinant technology' 'E. coli' . . BL21(DE3) plasmid pET21c . 'natural source' $entity_NAP 'chemical synthesis' . . . . . . Sigma . 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 _Isotopic_labeling $THIII 0.8 mM '[U-13C; U-15N]' $entity_NAP 0.8 mM . H2O 90 % . D2O 10 % . HEPES 20 mM . 'sodium azide' 0.01 '% (w/v)' . 'AEBSF protease inhibitor' 20 uM . NADP+ 2 uM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model UNITY-PLUS _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 external 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_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name THIII _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 . 13 PHE CA C 57.36 . 1 2 . 13 PHE H H 8.24 . 1 3 . 13 PHE N N 119.82 . 1 4 . 13 PHE C C 176.46 . 1 5 . 13 PHE HA H 4.66 . 1 6 . 13 PHE CB C 39.71 . 1 7 . 14 GLY N N 110.74 . 1 8 . 14 GLY H H 8.51 . 1 9 . 14 GLY CA C 45.25 . 1 10 . 14 GLY HA2 H 4.60 . 1 11 . 14 GLY HA3 H 4.60 . 1 12 . 14 GLY C C 174.33 . 1 13 . 15 SER N N 115.54 . 1 14 . 15 SER H H 8.23 . 1 15 . 15 SER CA C 58.49 . 1 16 . 15 SER HA H 4.51 . 1 17 . 15 SER C C 174.92 . 1 18 . 15 SER CB C 63.52 . 1 19 . 16 GLU C C 177.13 . 1 20 . 16 GLU CB C 29.51 . 1 21 . 16 GLU N N 122.62 . 1 22 . 16 GLU H H 8.67 . 1 23 . 16 GLU HA H 4.36 . 1 24 . 16 GLU CA C 56.49 . 1 25 . 17 GLY HA2 H 4.02 . 1 26 . 17 GLY HA3 H 4.02 . 1 27 . 17 GLY CA C 45.31 . 1 28 . 17 GLY C C 174.74 . 1 29 . 17 GLY N N 108.41 . 1 30 . 17 GLY H H 8.44 . 1 31 . 18 GLY H H 8.23 . 1 32 . 18 GLY HA2 H 4.01 . 1 33 . 18 GLY HA3 H 4.01 . 1 34 . 18 GLY CA C 45.19 . 1 35 . 18 GLY C C 174.23 . 1 36 . 18 GLY N N 108.45 . 1 37 . 19 VAL H H 8.01 . 1 38 . 19 VAL HA H 4.15 . 1 39 . 19 VAL CA C 62.19 . 1 40 . 19 VAL C C 176.12 . 1 41 . 19 VAL CB C 20.24 . 1 42 . 19 VAL N N 119.10 . 1 43 . 20 ALA H H 8.39 . 1 44 . 20 ALA HA H 4.32 . 1 45 . 20 ALA CA C 52.46 . 1 46 . 20 ALA C C 177.56 . 1 47 . 20 ALA CB C 18.38 . 1 48 . 20 ALA N N 127.36 . 1 49 . 21 ALA H H 8.20 . 1 50 . 21 ALA HA H 4.31 . 1 51 . 21 ALA CA C 52.35 . 1 52 . 21 ALA C C 177.56 . 1 53 . 21 ALA CB C 18.71 . 1 54 . 21 ALA N N 123.29 . 1 55 . 22 ALA N N 123.21 . 1 56 . 22 ALA H H 8.26 . 1 57 . 22 ALA HA H 4.32 . 1 58 . 22 ALA CA C 52.46 . 1 59 . 22 ALA C C 178.31 . 1 60 . 22 ALA CB C 18.45 . 1 61 . 23 GLY N N 107.78 . 1 62 . 23 GLY H H 8.36 . 1 63 . 23 GLY HA2 H 3.99 . 1 64 . 23 GLY HA3 H 3.99 . 1 65 . 23 GLY CA C 45.31 . 1 66 . 23 GLY C C 174.42 . 1 67 . 24 GLY N N 107.95 . 1 68 . 24 GLY H H 8.20 . 1 69 . 24 GLY HA2 H 4.01 . 1 70 . 24 GLY HA3 H 4.01 . 1 71 . 24 GLY CA C 45.09 . 1 72 . 24 GLY C C 174.04 . 1 73 . 25 ALA N N 123.89 . 1 74 . 25 ALA H H 8.28 . 1 75 . 25 ALA HA H 4.37 . 1 76 . 25 ALA CA C 52.18 . 1 77 . 25 ALA C C 177.69 . 1 78 . 25 ALA CB C 18.76 . 1 79 . 26 ALA N N 122.99 . 1 80 . 26 ALA H H 8.35 . 1 81 . 26 ALA HA H 4.32 . 1 82 . 26 ALA CA C 52.63 . 1 83 . 26 ALA C C 178.37 . 1 84 . 26 ALA CB C 18.40 . 1 85 . 27 GLY N N 107.52 . 1 86 . 27 GLY H H 8.26 . 1 87 . 27 GLY HA2 H 3.98 . 1 88 . 27 GLY HA3 H 3.98 . 1 89 . 27 GLY CA C 45.25 . 1 90 . 27 GLY C C 173.99 . 1 91 . 28 ASP N N 120.26 . 1 92 . 28 ASP H H 8.22 . 1 93 . 28 ASP HA H 4.64 . 1 94 . 28 ASP CA C 54.36 . 1 95 . 28 ASP C C 176.18 . 1 96 . 28 ASP CB C 40.83 . 1 97 . 29 ARG N N 120.90 . 1 98 . 29 ARG H H 8.17 . 1 99 . 29 ARG HA H 4.42 . 1 100 . 29 ARG CA C 55.70 . 1 101 . 29 ARG C C 175.55 . 1 102 . 29 ARG CB C 30.80 . 1 103 . 30 SER N N 117.05 . 1 104 . 30 SER H H 8.51 . 1 105 . 30 SER HA H 4.85 . 1 106 . 30 SER CA C 57.94 . 1 107 . 30 SER C C 173.67 . 1 108 . 30 SER CB C 64.55 . 1 109 . 31 VAL N N 118.26 . 1 110 . 31 VAL H H 8.30 . 1 111 . 31 VAL HA H 4.53 . 1 112 . 31 VAL CA C 60.39 . 1 113 . 31 VAL C C 175.55 . 1 114 . 31 VAL CB C 33.57 . 1 115 . 32 LYS N N 127.73 . 1 116 . 32 LYS H H 9.31 . 1 117 . 32 LYS HA H 4.57 . 1 118 . 32 LYS CA C 55.59 . 1 119 . 32 LYS C C 173.98 . 1 120 . 32 LYS CB C 31.24 . 1 121 . 33 ALA N N 129.10 . 1 122 . 33 ALA H H 8.50 . 1 123 . 33 ALA HA H 5.26 . 1 124 . 33 ALA CA C 50.56 . 1 125 . 33 ALA C C 177.93 . 1 126 . 33 ALA CB C 20.04 . 1 127 . 34 GLY N N 109.90 . 1 128 . 34 GLY H H 8.67 . 1 129 . 34 GLY HA2 H 4.81 . 1 130 . 34 GLY HA3 H 4.81 . 1 131 . 34 GLY C C 172.17 . 1 132 . 35 SER N N 114.27 . 1 133 . 35 SER H H 8.95 . 1 134 . 35 SER HA H 4.98 . 1 135 . 35 SER CA C 55.59 . 1 136 . 35 SER C C 175.12 . 1 137 . 35 SER CB C 67.40 . 1 138 . 36 ALA N N 122.70 . 1 139 . 36 ALA H H 9.13 . 1 140 . 36 ALA HA H 3.94 . 1 141 . 36 ALA CA C 55.37 . 1 142 . 36 ALA C C 179.20 . 1 143 . 36 ALA CB C 18.27 . 1 144 . 37 GLU N N 115.47 . 1 145 . 37 GLU H H 8.65 . 1 146 . 37 GLU HA H 3.84 . 1 147 . 37 GLU CA C 60.56 . 1 148 . 37 GLU C C 179.37 . 1 149 . 37 GLU CB C 28.17 . 1 150 . 38 ASP N N 121.05 . 1 151 . 38 ASP H H 7.83 . 1 152 . 38 ASP HA H 4.51 . 1 153 . 38 ASP CA C 57.39 . 1 154 . 38 ASP C C 178.56 . 1 155 . 38 ASP CB C 40.53 . 1 156 . 39 ALA N N 120.44 . 1 157 . 39 ALA H H 7.92 . 1 158 . 39 ALA HA H 3.96 . 1 159 . 39 ALA CA C 54.92 . 1 160 . 39 ALA C C 178.44 . 1 161 . 39 ALA CB C 18.78 . 1 162 . 40 ALA N N 118.96 . 1 163 . 40 ALA H H 8.48 . 1 164 . 40 ALA HA H 3.84 . 1 165 . 40 ALA CA C 55.20 . 1 166 . 40 ALA C C 178.25 . 1 167 . 40 ALA CB C 18.63 . 1 168 . 41 PHE N N 116.78 . 1 169 . 41 PHE H H 7.73 . 1 170 . 41 PHE HA H 3.95 . 1 171 . 41 PHE CA C 61.62 . 1 172 . 41 PHE C C 178.01 . 1 173 . 41 PHE CB C 38.47 . 1 174 . 42 ILE N N 117.97 . 1 175 . 42 ILE H H 7.99 . 1 176 . 42 ILE HA H 3.62 . 1 177 . 42 ILE CA C 64.42 . 1 178 . 42 ILE C C 178.76 . 1 179 . 42 ILE CB C 38.42 . 1 180 . 43 MET N N 116.08 . 1 181 . 43 MET H H 8.08 . 1 182 . 43 MET HA H 3.89 . 1 183 . 43 MET CA C 60.11 . 1 184 . 43 MET C C 176.87 . 1 185 . 43 MET CB C 33.52 . 1 186 . 44 LYS N N 115.41 . 1 187 . 44 LYS H H 8.19 . 1 188 . 44 LYS HA H 3.82 . 1 189 . 44 LYS CA C 59.17 . 1 190 . 44 LYS C C 176.56 . 1 191 . 44 LYS CB C 31.44 . 1 192 . 45 ASN N N 113.12 . 1 193 . 45 ASN H H 6.78 . 1 194 . 45 ASN HA H 4.66 . 1 195 . 45 ASN CA C 52.96 . 1 196 . 45 ASN C C 173.67 . 1 197 . 45 ASN CB C 39.29 . 1 198 . 46 ALA N N 123.30 . 1 199 . 46 ALA H H 7.12 . 1 200 . 46 ALA HA H 4.34 . 1 201 . 46 ALA CA C 51.45 . 1 202 . 46 ALA C C 175.87 . 1 203 . 46 ALA CB C 20.27 . 1 204 . 47 SER N N 113.09 . 1 205 . 47 SER H H 8.76 . 1 206 . 47 SER HA H 4.85 . 1 207 . 47 SER CA C 60.16 . 1 208 . 47 SER C C 175.87 . 1 209 . 47 SER CB C 63.61 . 1 210 . 48 LYS C C 174.49 . 1 211 . 48 LYS CB C 35.48 . 1 212 . 48 LYS N N 124.21 . 1 213 . 48 LYS H H 8.45 . 1 214 . 48 LYS HA H 5.22 . 1 215 . 48 LYS CA C 56.32 . 1 216 . 49 VAL CA C 60.39 . 1 217 . 49 VAL C C 174.24 . 1 218 . 49 VAL CB C 35.10 . 1 219 . 49 VAL N N 126.72 . 1 220 . 49 VAL H H 8.88 . 1 221 . 49 VAL HA H 4.83 . 1 222 . 50 ILE CA C 59.73 . 1 223 . 50 ILE C C 174.93 . 1 224 . 50 ILE CB C 39.13 . 1 225 . 50 ILE N N 124.33 . 1 226 . 50 ILE H H 8.37 . 1 227 . 50 ILE HA H 4.63 . 1 228 . 51 ILE CA C 60.90 . 1 229 . 51 ILE C C 174.99 . 1 230 . 51 ILE CB C 38.20 . 1 231 . 51 ILE N N 129.92 . 1 232 . 51 ILE H H 9.45 . 1 233 . 51 ILE HA H 4.74 . 1 234 . 52 VAL CA C 59.16 . 1 235 . 52 VAL CB C 33.09 . 1 236 . 52 VAL N N 128.62 . 1 237 . 52 VAL H H 9.65 . 1 238 . 52 VAL HA H 5.08 . 1 239 . 53 PRO CA C 60.95 . 1 240 . 53 PRO C C 175.36 . 1 241 . 53 PRO CB C 33.01 . 1 242 . 53 PRO HA H 5.33 . 1 243 . 54 GLY CA C 44.86 . 1 244 . 54 GLY C C 175.24 . 1 245 . 54 GLY N N 105.33 . 1 246 . 54 GLY H H 7.35 . 1 247 . 54 GLY HA2 H 4.88 . 1 248 . 54 GLY HA3 H 4.88 . 1 249 . 55 TYR CA C 61.06 . 1 250 . 55 TYR C C 176.31 . 1 251 . 55 TYR CB C 39.77 . 1 252 . 55 TYR N N 119.74 . 1 253 . 55 TYR H H 9.52 . 1 254 . 55 TYR HA H 4.09 . 1 255 . 56 GLY CA C 45.31 . 1 256 . 56 GLY C C 174.49 . 1 257 . 56 GLY N N 105.09 . 1 258 . 56 GLY H H 10.12 . 1 259 . 56 GLY HA2 H 2.10 . 1 260 . 56 GLY HA3 H 2.32 . 1 261 . 57 MET CA C 59.50 . 1 262 . 57 MET C C 177.69 . 1 263 . 57 MET CB C 32.43 . 1 264 . 57 MET N N 117.31 . 1 265 . 57 MET H H 7.88 . 1 266 . 57 MET HA H 3.43 . 1 267 . 58 ALA CA C 54.14 . 1 268 . 58 ALA C C 180.51 . 1 269 . 58 ALA CB C 18.15 . 1 270 . 58 ALA N N 119.03 . 1 271 . 58 ALA H H 6.95 . 1 272 . 58 ALA HA H 3.94 . 1 273 . 59 VAL CA C 65.65 . 1 274 . 59 VAL C C 178.00 . 1 275 . 59 VAL CB C 31.07 . 1 276 . 59 VAL N N 118.90 . 1 277 . 59 VAL H H 7.65 . 1 278 . 59 VAL HA H 3.57 . 1 279 . 60 ALA CA C 51.79 . 1 280 . 60 ALA C C 176.61 . 1 281 . 60 ALA CB C 21.18 . 1 282 . 60 ALA N N 117.64 . 1 283 . 60 ALA H H 7.18 . 1 284 . 60 ALA HA H 4.57 . 1 285 . 61 GLN CA C 56.15 . 1 286 . 61 GLN C C 177.56 . 1 287 . 61 GLN CB C 25.36 . 1 288 . 61 GLN N N 114.52 . 1 289 . 61 GLN H H 7.74 . 1 290 . 61 GLN HA H 4.35 . 1 291 . 62 ALA CA C 52.24 . 1 292 . 62 ALA C C 176.12 . 1 293 . 62 ALA CB C 18.62 . 1 294 . 62 ALA N N 117.31 . 1 295 . 62 ALA H H 7.88 . 1 296 . 62 ALA HA H 4.32 . 1 297 . 63 GLN H H 10.14 . 1 298 . 63 GLN HA H 3.99 . 1 299 . 63 GLN CA C 59.61 . 1 300 . 63 GLN C C 174.93 . 1 301 . 63 GLN CB C 25.12 . 1 302 . 63 GLN N N 119.37 . 1 303 . 64 HIS H H 7.23 . 1 304 . 64 HIS HA H 4.44 . 1 305 . 64 HIS CA C 59.50 . 1 306 . 64 HIS C C 178.25 . 1 307 . 64 HIS CB C 29.25 . 1 308 . 64 HIS N N 121.06 . 1 309 . 65 ALA H H 8.38 . 1 310 . 65 ALA HA H 4.26 . 1 311 . 65 ALA CA C 54.58 . 1 312 . 65 ALA C C 179.06 . 1 313 . 65 ALA CB C 17.03 . 1 314 . 65 ALA N N 124.63 . 1 315 . 66 LEU H H 8.36 . 1 316 . 66 LEU HA H 3.99 . 1 317 . 66 LEU CA C 57.27 . 1 318 . 66 LEU C C 177.18 . 1 319 . 66 LEU CB C 42.66 . 1 320 . 66 LEU N N 117.54 . 1 321 . 67 ARG H H 7.64 . 1 322 . 67 ARG HA H 4.06 . 1 323 . 67 ARG CA C 59.72 . 1 324 . 67 ARG C C 178.88 . 1 325 . 67 ARG CB C 27.11 . 1 326 . 67 ARG N N 119.37 . 1 327 . 68 GLU H H 7.97 . 1 328 . 68 GLU HA H 4.05 . 1 329 . 68 GLU CA C 59.95 . 1 330 . 68 GLU C C 179.01 . 1 331 . 68 GLU CB C 28.49 . 1 332 . 68 GLU N N 119.04 . 1 333 . 69 MET H H 8.24 . 1 334 . 69 MET HA H 3.66 . 1 335 . 69 MET CA C 59.56 . 1 336 . 69 MET C C 177.87 . 1 337 . 69 MET CB C 32.86 . 1 338 . 69 MET N N 120.11 . 1 339 . 70 ALA H H 8.55 . 1 340 . 70 ALA HA H 3.76 . 1 341 . 70 ALA CA C 55.70 . 1 342 . 70 ALA C C 179.38 . 1 343 . 70 ALA CB C 18.40 . 1 344 . 70 ALA N N 122.09 . 1 345 . 71 ASP H H 8.66 . 1 346 . 71 ASP HA H 4.49 . 1 347 . 71 ASP CA C 57.82 . 1 348 . 71 ASP C C 180.07 . 1 349 . 71 ASP CB C 39.47 . 1 350 . 71 ASP N N 118.04 . 1 351 . 72 VAL H H 7.95 . 1 352 . 72 VAL HA H 3.72 . 1 353 . 72 VAL CA C 66.76 . 1 354 . 72 VAL C C 178.44 . 1 355 . 72 VAL CB C 31.50 . 1 356 . 72 VAL N N 122.29 . 1 357 . 73 LEU H H 7.96 . 1 358 . 73 LEU HA H 3.87 . 1 359 . 73 LEU CA C 57.77 . 1 360 . 73 LEU C C 179.51 . 1 361 . 73 LEU CB C 40.45 . 1 362 . 73 LEU N N 119.32 . 1 363 . 74 LYS H H 8.95 . 1 364 . 74 LYS HA H 4.42 . 1 365 . 74 LYS CA C 60.17 . 1 366 . 74 LYS C C 181.83 . 1 367 . 74 LYS CB C 31.61 . 1 368 . 74 LYS N N 119.34 . 1 369 . 75 LYS H H 7.94 . 1 370 . 75 LYS HA H 4.15 . 1 371 . 75 LYS CA C 59.17 . 1 372 . 75 LYS C C 178.37 . 1 373 . 75 LYS CB C 31.28 . 1 374 . 75 LYS N N 121.96 . 1 375 . 76 GLU H H 7.61 . 1 376 . 76 GLU HA H 4.42 . 1 377 . 76 GLU CA C 55.59 . 1 378 . 76 GLU C C 176.50 . 1 379 . 76 GLU CB C 28.80 . 1 380 . 76 GLU N N 117.10 . 1 381 . 77 GLY H H 7.89 . 1 382 . 77 GLY HA2 H 4.33 . 1 383 . 77 GLY HA3 H 3.75 . 1 384 . 77 GLY CA C 45.04 . 1 385 . 77 GLY C C 173.98 . 1 386 . 77 GLY N N 106.41 . 1 387 . 78 VAL H H 7.88 . 1 388 . 78 VAL HA H 3.64 . 1 389 . 78 VAL CA C 62.85 . 1 390 . 78 VAL C C 175.87 . 1 391 . 78 VAL CB C 32.09 . 1 392 . 78 VAL N N 124.12 . 1 393 . 79 GLU H H 8.03 . 1 394 . 79 GLU HA H 4.41 . 1 395 . 79 GLU CA C 56.49 . 1 396 . 79 GLU C C 175.05 . 1 397 . 79 GLU CB C 29.69 . 1 398 . 79 GLU N N 127.30 . 1 399 . 80 VAL H H 8.14 . 1 400 . 80 VAL HA H 5.06 . 1 401 . 80 VAL CA C 60.95 . 1 402 . 80 VAL C C 174.87 . 1 403 . 80 VAL CB C 34.42 . 1 404 . 80 VAL N N 125.74 . 1 405 . 81 SER H H 7.70 . 1 406 . 81 SER HA H 5.14 . 1 407 . 81 SER CA C 56.71 . 1 408 . 81 SER C C 171.35 . 1 409 . 81 SER CB C 66.01 . 1 410 . 81 SER N N 116.87 . 1 411 . 82 TYR H H 9.46 . 1 412 . 82 TYR HA H 5.52 . 1 413 . 82 TYR CA C 56.54 . 1 414 . 82 TYR C C 174.11 . 1 415 . 82 TYR CB C 40.30 . 1 416 . 82 TYR N N 129.68 . 1 417 . 83 ALA H H 9.23 . 1 418 . 83 ALA HA H 5.01 . 1 419 . 83 ALA CA C 50.00 . 1 420 . 83 ALA C C 175.11 . 1 421 . 83 ALA CB C 23.03 . 1 422 . 83 ALA N N 124.58 . 1 423 . 84 ILE H H 9.01 . 1 424 . 84 ILE HA H 4.53 . 1 425 . 84 ILE CA C 57.94 . 1 426 . 84 ILE C C 175.86 . 1 427 . 84 ILE CB C 36.19 . 1 428 . 84 ILE N N 122.12 . 1 429 . 85 HIS H H 8.82 . 1 430 . 85 HIS HA H 4.81 . 1 431 . 85 HIS CA C 54.25 . 1 432 . 85 HIS CB C 32.02 . 1 433 . 85 HIS N N 130.44 . 1 434 . 86 PRO CA C 65.20 . 1 435 . 86 PRO C C 178.82 . 1 436 . 86 PRO CB C 32.01 . 1 437 . 87 VAL H H 10.62 . 1 438 . 87 VAL HA H 4.83 . 1 439 . 87 VAL CA C 60.06 . 1 440 . 87 VAL C C 177.50 . 1 441 . 87 VAL CB C 30.69 . 1 442 . 87 VAL N N 113.35 . 1 443 . 88 ALA H H 8.12 . 1 444 . 88 ALA HA H 4.65 . 1 445 . 88 ALA CA C 53.58 . 1 446 . 88 ALA C C 180.20 . 1 447 . 88 ALA CB C 18.87 . 1 448 . 88 ALA N N 124.65 . 1 449 . 89 GLY H H 10.21 . 1 450 . 89 GLY CA C 45.25 . 1 451 . 89 GLY C C 175.05 . 1 452 . 89 GLY N N 108.33 . 1 453 . 90 ARG H H 11.18 . 1 454 . 90 ARG HA H 3.63 . 1 455 . 90 ARG CA C 53.97 . 1 456 . 90 ARG C C 174.29 . 1 457 . 90 ARG CB C 31.71 . 1 458 . 90 ARG N N 122.90 . 1 459 . 91 MET H H 7.61 . 1 460 . 91 MET HA H 4.98 . 1 461 . 91 MET C C 174.00 . 1 462 . 91 MET CA C 54.03 . 1 463 . 91 MET CB C 33.11 . 1 464 . 91 MET N N 118.19 . 1 465 . 92 PRO HA H 4.77 . 1 466 . 92 PRO CA C 64.08 . 1 467 . 92 PRO C C 178.62 . 1 468 . 92 PRO CB C 30.99 . 1 469 . 93 GLY H H 9.42 . 1 470 . 93 GLY HA2 H 4.10 . 1 471 . 93 GLY HA3 H 4.10 . 1 472 . 93 GLY CA C 46.65 . 1 473 . 93 GLY C C 175.12 . 1 474 . 93 GLY N N 114.12 . 1 475 . 94 HIS H H 7.83 . 1 476 . 94 HIS HA H 4.38 . 1 477 . 94 HIS CA C 57.77 . 1 478 . 94 HIS C C 178.31 . 1 479 . 94 HIS CB C 34.01 . 1 480 . 94 HIS N N 120.51 . 1 481 . 95 MET H H 9.11 . 1 482 . 95 MET HA H 4.25 . 1 483 . 95 MET CA C 56.71 . 1 484 . 95 MET C C 177.94 . 1 485 . 95 MET CB C 34.55 . 1 486 . 95 MET N N 111.13 . 1 487 . 96 ASN H H 7.85 . 1 488 . 96 ASN HA H 4.02 . 1 489 . 96 ASN CA C 57.38 . 1 490 . 96 ASN C C 178.44 . 1 491 . 96 ASN CB C 37.43 . 1 492 . 96 ASN N N 114.61 . 1 493 . 97 VAL H H 7.81 . 1 494 . 97 VAL HA H 3.83 . 1 495 . 97 VAL CA C 65.87 . 1 496 . 97 VAL C C 178.63 . 1 497 . 97 VAL CB C 31.54 . 1 498 . 97 VAL N N 117.56 . 1 499 . 98 LEU H H 7.39 . 1 500 . 98 LEU HA H 4.09 . 1 501 . 98 LEU CA C 57.55 . 1 502 . 98 LEU C C 179.07 . 1 503 . 98 LEU CB C 41.46 . 1 504 . 98 LEU N N 119.26 . 1 505 . 99 LEU H H 8.05 . 1 506 . 99 LEU HA H 3.79 . 1 507 . 99 LEU CA C 57.79 . 1 508 . 99 LEU C C 178.82 . 1 509 . 99 LEU CB C 38.44 . 1 510 . 99 LEU N N 116.54 . 1 511 . 100 ALA H H 7.69 . 1 512 . 100 ALA HA H 4.16 . 1 513 . 100 ALA CA C 55.25 . 1 514 . 100 ALA C C 182.65 . 1 515 . 100 ALA CB C 16.99 . 1 516 . 100 ALA N N 121.14 . 1 517 . 101 GLU H H 7.95 . 1 518 . 101 GLU HA H 4.07 . 1 519 . 101 GLU CA C 59.05 . 1 520 . 101 GLU C C 177.43 . 1 521 . 101 GLU CB C 28.97 . 1 522 . 101 GLU N N 120.81 . 1 523 . 102 ALA H H 7.07 . 1 524 . 102 ALA HA H 4.56 . 1 525 . 102 ALA CA C 51.17 . 1 526 . 102 ALA C C 175.68 . 1 527 . 102 ALA CB C 18.43 . 1 528 . 102 ALA N N 18.28 . 1 529 . 103 ASN H H 8.01 . 1 530 . 103 ASN HA H 4.29 . 1 531 . 103 ASN CA C 54.19 . 1 532 . 103 ASN C C 175.17 . 1 533 . 103 ASN CB C 36.43 . 1 534 . 103 ASN N N 112.58 . 1 535 . 104 VAL H H 7.60 . 1 536 . 104 VAL HA H 3.78 . 1 537 . 104 VAL CA C 61.40 . 1 538 . 104 VAL CB C 31.81 . 1 539 . 104 VAL N N 121.22 . 1 540 . 105 PRO HA H 4.28 . 1 541 . 105 PRO CA C 62.85 . 1 542 . 105 PRO C C 177.81 . 1 543 . 105 PRO CB C 32.10 . 1 544 . 106 TYR H H 8.20 . 1 545 . 106 TYR HA H 3.98 . 1 546 . 106 TYR CA C 61.23 . 1 547 . 106 TYR C C 177.56 . 1 548 . 106 TYR CB C 37.46 . 1 549 . 106 TYR N N 122.41 . 1 550 . 107 ASP H H 8.10 . 1 551 . 107 ASP HA H 4.28 . 1 552 . 107 ASP CA C 54.42 . 1 553 . 107 ASP C C 176.43 . 1 554 . 107 ASP CB C 38.89 . 1 555 . 107 ASP N N 114.19 . 1 556 . 108 GLU H H 7.41 . 1 557 . 108 GLU HA H 4.68 . 1 558 . 108 GLU CA C 55.87 . 1 559 . 108 GLU C C 174.05 . 1 560 . 108 GLU CB C 30.10 . 1 561 . 108 GLU N N 116.61 . 1 562 . 109 VAL H H 7.05 . 1 563 . 109 VAL HA H 4.28 . 1 564 . 109 VAL CA C 62.63 . 1 565 . 109 VAL C C 174.61 . 1 566 . 109 VAL CB C 31.86 . 1 567 . 109 VAL N N 120.80 . 1 568 . 110 PHE H H 8.93 . 1 569 . 110 PHE HA H 4.85 . 1 570 . 110 PHE CA C 56.59 . 1 571 . 110 PHE C C 174.49 . 1 572 . 110 PHE CB C 43.75 . 1 573 . 110 PHE N N 125.06 . 1 574 . 111 GLU H H 9.05 . 1 575 . 111 GLU HA H 4.78 . 1 576 . 111 GLU CA C 55.36 . 1 577 . 111 GLU C C 174.36 . 1 578 . 111 GLU CB C 30.63 . 1 579 . 111 GLU N N 120.43 . 1 580 . 112 LEU H H 7.63 . 1 581 . 112 LEU HA H 3.76 . 1 582 . 112 LEU CA C 60.29 . 1 583 . 112 LEU C C 176.93 . 1 584 . 112 LEU CB C 43.80 . 1 585 . 112 LEU N N 121.71 . 1 586 . 113 GLU H H 9.30 . 1 587 . 113 GLU HA H 4.05 . 1 588 . 113 GLU CA C 59.89 . 1 589 . 113 GLU C C 178.56 . 1 590 . 113 GLU CB C 28.59 . 1 591 . 113 GLU N N 116.83 . 1 592 . 114 GLU H H 7.89 . 1 593 . 114 GLU HA H 4.42 . 1 594 . 114 GLU CA C 57.49 . 1 595 . 114 GLU C C 177.56 . 1 596 . 114 GLU CB C 30.45 . 1 597 . 114 GLU N N 116.00 . 1 598 . 115 ILE H H 7.77 . 1 599 . 115 ILE HA H 4.38 . 1 600 . 115 ILE CA C 58.49 . 1 601 . 115 ILE C C 176.75 . 1 602 . 115 ILE CB C 40.80 . 1 603 . 115 ILE N N 116.75 . 1 604 . 116 ASN N N 123.20 . 1 605 . 116 ASN H H 8.08 . 1 606 . 116 ASN HA H 5.22 . 1 607 . 116 ASN CA C 55.13 . 1 608 . 116 ASN C C 179.19 . 1 609 . 116 ASN CB C 36.97 . 1 610 . 117 SER N N 112.04 . 1 611 . 117 SER H H 8.55 . 1 612 . 117 SER HA H 4.42 . 1 613 . 117 SER CA C 60.28 . 1 614 . 117 SER C C 175.69 . 1 615 . 117 SER CB C 62.30 . 1 616 . 118 SER N N 114.69 . 1 617 . 118 SER H H 8.24 . 1 618 . 118 SER HA H 4.35 . 1 619 . 118 SER CA C 59.78 . 1 620 . 118 SER C C 176.62 . 1 621 . 118 SER CB C 63.01 . 1 622 . 119 PHE N N 119.30 . 1 623 . 119 PHE H H 7.26 . 1 624 . 119 PHE HA H 3.90 . 1 625 . 119 PHE CA C 63.63 . 1 626 . 119 PHE C C 177.06 . 1 627 . 119 PHE CB C 39.27 . 1 628 . 120 GLN N N 112.01 . 1 629 . 120 GLN H H 8.05 . 1 630 . 120 GLN HA H 4.16 . 1 631 . 120 GLN CA C 57.43 . 1 632 . 120 GLN C C 176.31 . 1 633 . 120 GLN CB C 28.10 . 1 634 . 121 THR N N 106.71 . 1 635 . 121 THR H H 7.28 . 1 636 . 121 THR HA H 4.53 . 1 637 . 121 THR CA C 60.28 . 1 638 . 121 THR C C 173.54 . 1 639 . 121 THR CB C 68.85 . 1 640 . 122 ALA N N 124.68 . 1 641 . 122 ALA H H 7.66 . 1 642 . 122 ALA HA H 4.25 . 1 643 . 122 ALA CA C 51.45 . 1 644 . 122 ALA C C 176.87 . 1 645 . 122 ALA CB C 18.31 . 1 646 . 123 ASP N N 121.86 . 1 647 . 123 ASP H H 8.54 . 1 648 . 123 ASP HA H 4.76 . 1 649 . 123 ASP CA C 56.59 . 1 650 . 123 ASP C C 177.25 . 1 651 . 123 ASP CB C 42.24 . 1 652 . 124 VAL N N 114.46 . 1 653 . 124 VAL H H 7.51 . 1 654 . 124 VAL HA H 5.30 . 1 655 . 124 VAL CA C 59.72 . 1 656 . 124 VAL C C 174.42 . 1 657 . 124 VAL CB C 37.11 . 1 658 . 125 ALA N N 128.41 . 1 659 . 125 ALA H H 8.67 . 1 660 . 125 ALA HA H 5.51 . 1 661 . 125 ALA CA C 49.78 . 1 662 . 125 ALA C C 173.74 . 1 663 . 125 ALA CB C 19.54 . 1 664 . 126 PHE N N 127.99 . 1 665 . 126 PHE H H 9.42 . 1 666 . 126 PHE HA H 4.64 . 1 667 . 126 PHE CA C 56.76 . 1 668 . 126 PHE C C 172.11 . 1 669 . 126 PHE CB C 39.50 . 1 670 . 127 VAL N N 130.13 . 1 671 . 127 VAL H H 9.34 . 1 672 . 127 VAL HA H 4.56 . 1 673 . 127 VAL CA C 61.68 . 1 674 . 127 VAL C C 173.73 . 1 675 . 127 VAL CB C 29.60 . 1 676 . 128 ILE N N 123.89 . 1 677 . 128 ILE H H 8.54 . 1 678 . 128 ILE HA H 4.64 . 1 679 . 128 ILE CA C 56.82 . 1 680 . 128 ILE C C 174.61 . 1 681 . 128 ILE CB C 38.82 . 1 682 . 129 GLY N N 112.69 . 1 683 . 129 GLY H H 8.83 . 1 684 . 129 GLY HA2 H 3.94 . 1 685 . 129 GLY HA3 H 3.43 . 1 686 . 129 GLY CA C 46.15 . 1 687 . 129 GLY C C 171.04 . 1 688 . 130 ALA N N 117.93 . 1 689 . 130 ALA H H 6.95 . 1 690 . 130 ALA HA H 5.44 . 1 691 . 130 ALA CA C 49.22 . 1 692 . 130 ALA C C 176.25 . 1 693 . 130 ALA CB C 20.65 . 1 694 . 131 ASN N N 114.90 . 1 695 . 131 ASN H H 10.66 . 1 696 . 131 ASN HA H 4.67 . 1 697 . 131 ASN CA C 56.08 . 1 698 . 131 ASN C C 176.25 . 1 699 . 131 ASN CB C 38.92 . 1 700 . 132 ASP N N 127.81 . 1 701 . 132 ASP H H 10.81 . 1 702 . 132 ASP HA H 4.52 . 1 703 . 132 ASP CA C 58.94 . 1 704 . 132 ASP C C 177.75 . 1 705 . 132 ASP CB C 39.70 . 1 706 . 133 VAL N N 102.54 . 1 707 . 133 VAL H H 7.11 . 1 708 . 133 VAL HA H 3.86 . 1 709 . 133 VAL CA C 63.85 . 1 710 . 133 VAL C C 174.17 . 1 711 . 133 VAL CB C 30.47 . 1 712 . 134 THR N N 108.18 . 1 713 . 134 THR H H 8.07 . 1 714 . 134 THR HA H 4.90 . 1 715 . 134 THR CA C 61.28 . 1 716 . 134 THR C C 174.11 . 1 717 . 134 THR CB C 70.88 . 1 718 . 135 ASN N N 120.44 . 1 719 . 135 ASN H H 7.13 . 1 720 . 135 ASN HA H 4.62 . 1 721 . 135 ASN CA C 52.12 . 1 722 . 135 ASN CB C 38.91 . 1 723 . 136 PRO HA H 4.37 . 1 724 . 136 PRO CA C 64.53 . 1 725 . 136 PRO C C 178.43 . 1 726 . 136 PRO CB C 31.51 . 1 727 . 137 ALA N N 126.07 . 1 728 . 137 ALA H H 8.79 . 1 729 . 137 ALA HA H 4.45 . 1 730 . 137 ALA CA C 54.58 . 1 731 . 137 ALA C C 179.06 . 1 732 . 137 ALA CB C 17.83 . 1 733 . 138 ALA N N 116.34 . 1 734 . 138 ALA H H 7.86 . 1 735 . 138 ALA HA H 4.06 . 1 736 . 138 ALA CA C 54.70 . 1 737 . 138 ALA C C 178.57 . 1 738 . 138 ALA CB C 20.08 . 1 739 . 139 LYS N N 112.14 . 1 740 . 139 LYS H H 7.85 . 1 741 . 139 LYS HA H 4.50 . 1 742 . 139 LYS CA C 56.70 . 1 743 . 139 LYS C C 178.75 . 1 744 . 139 LYS CB C 33.88 . 1 745 . 140 THR N N 106.86 . 1 746 . 140 THR H H 7.83 . 1 747 . 140 THR HA H 4.66 . 1 748 . 140 THR CA C 62.80 . 1 749 . 140 THR C C 174.93 . 1 750 . 140 THR CB C 70.69 . 1 751 . 141 ASP N N 121.33 . 1 752 . 141 ASP H H 8.32 . 1 753 . 141 ASP HA H 5.32 . 1 754 . 141 ASP CA C 50.67 . 1 755 . 141 ASP CB C 41.76 . 1 756 . 141 ASP C C 173.50 . 1 757 . 142 PRO CA C 62.58 . 1 758 . 142 PRO C C 176.88 . 1 759 . 142 PRO CB C 31.34 . 1 760 . 143 SER N N 112.24 . 1 761 . 143 SER H H 7.99 . 1 762 . 143 SER HA H 4.45 . 1 763 . 143 SER CA C 58.44 . 1 764 . 143 SER C C 174.55 . 1 765 . 143 SER CB C 63.88 . 1 766 . 144 SER N N 119.27 . 1 767 . 144 SER H H 8.11 . 1 768 . 144 SER HA H 4.71 . 1 769 . 144 SER CA C 56.15 . 1 770 . 144 SER C C 176.30 . 1 771 . 144 SER CB C 63.97 . 1 772 . 145 PRO HA H 4.66 . 1 773 . 145 PRO CA C 64.43 . 1 774 . 145 PRO C C 177.69 . 1 775 . 145 PRO CB C 32.05 . 1 776 . 146 ILE N N 107.70 . 1 777 . 146 ILE H H 7.16 . 1 778 . 146 ILE HA H 4.64 . 1 779 . 146 ILE CA C 60.29 . 1 780 . 146 ILE CB C 37.45 . 1 781 . 147 TYR CA C 60.39 . 1 782 . 147 TYR HA H 4.52 . 1 783 . 147 TYR C C 178.00 . 1 784 . 147 TYR CB C 37.16 . 1 785 . 148 GLY N N 115.99 . 1 786 . 148 GLY H H 8.70 . 1 787 . 148 GLY HA2 H 4.03 . 1 788 . 148 GLY HA3 H 3.25 . 1 789 . 148 GLY CA C 44.42 . 1 790 . 148 GLY C C 174.24 . 1 791 . 149 MET N N 124.30 . 1 792 . 149 MET H H 8.04 . 1 793 . 149 MET HA H 4.63 . 1 794 . 149 MET CA C 53.91 . 1 795 . 149 MET CB C 33.50 . 1 796 . 149 MET C C 173.70 . 1 797 . 150 PRO HA H 4.48 . 1 798 . 150 PRO CA C 62.85 . 1 799 . 150 PRO C C 176.93 . 1 800 . 150 PRO CB C 31.73 . 1 801 . 151 ILE N N 115.06 . 1 802 . 151 ILE H H 8.26 . 1 803 . 151 ILE HA H 4.82 . 1 804 . 151 ILE CA C 59.61 . 1 805 . 151 ILE C C 176.06 . 1 806 . 151 ILE CB C 43.38 . 1 807 . 152 LEU N N 119.12 . 1 808 . 152 LEU H H 8.48 . 1 809 . 152 LEU HA H 5.06 . 1 810 . 152 LEU CA C 53.19 . 1 811 . 152 LEU C C 177.76 . 1 812 . 152 LEU CB C 42.85 . 1 813 . 153 ASP N N 128.77 . 1 814 . 153 ASP H H 9.07 . 1 815 . 153 ASP HA H 4.65 . 1 816 . 153 ASP CA C 53.91 . 1 817 . 153 ASP C C 176.06 . 1 818 . 153 ASP CB C 38.35 . 1 819 . 154 VAL N N 114.90 . 1 820 . 154 VAL H H 7.56 . 1 821 . 154 VAL HA H 2.71 . 1 822 . 154 VAL CA C 63.63 . 1 823 . 154 VAL C C 175.61 . 1 824 . 154 VAL CB C 30.18 . 1 825 . 155 GLU N N 113.35 . 1 826 . 155 GLU H H 7.70 . 1 827 . 155 GLU HA H 4.05 . 1 828 . 155 GLU CA C 57.26 . 1 829 . 155 GLU C C 175.81 . 1 830 . 155 GLU CB C 29.20 . 1 831 . 156 LYS N N 115.96 . 1 832 . 156 LYS H H 7.17 . 1 833 . 156 LYS HA H 4.15 . 1 834 . 156 LYS CA C 55.93 . 1 835 . 156 LYS C C 176.37 . 1 836 . 156 LYS CB C 32.08 . 1 837 . 157 ALA N N 121.13 . 1 838 . 157 ALA H H 7.62 . 1 839 . 157 ALA HA H 4.80 . 1 840 . 157 ALA CA C 51.68 . 1 841 . 157 ALA C C 177.69 . 1 842 . 157 ALA CB C 20.34 . 1 843 . 158 GLY N N 106.22 . 1 844 . 158 GLY H H 8.01 . 1 845 . 158 GLY HA2 H 4.07 . 1 846 . 158 GLY HA3 H 3.96 . 1 847 . 158 GLY CA C 48.61 . 1 848 . 158 GLY C C 175.56 . 1 849 . 159 THR N N 116.06 . 1 850 . 159 THR H H 7.92 . 1 851 . 159 THR HA H 4.94 . 1 852 . 159 THR CA C 62.30 . 1 853 . 159 THR C C 171.92 . 1 854 . 159 THR CB C 71.83 . 1 855 . 160 VAL N N 127.84 . 1 856 . 160 VAL H H 9.08 . 1 857 . 160 VAL HA H 4.56 . 1 858 . 160 VAL CA C 61.23 . 1 859 . 160 VAL C C 173.74 . 1 860 . 160 VAL CB C 32.46 . 1 861 . 161 LEU N N 127.05 . 1 862 . 161 LEU H H 8.76 . 1 863 . 161 LEU HA H 5.52 . 1 864 . 161 LEU CA C 52.23 . 1 865 . 161 LEU C C 175.18 . 1 866 . 161 LEU CB C 43.77 . 1 867 . 162 PHE N N 119.89 . 1 868 . 162 PHE H H 8.23 . 1 869 . 162 PHE HA H 5.21 . 1 870 . 162 PHE CA C 57.54 . 1 871 . 162 PHE C C 175.11 . 1 872 . 162 PHE CB C 41.65 . 1 873 . 163 ILE N N 121.04 . 1 874 . 163 ILE H H 8.80 . 1 875 . 163 ILE HA H 5.13 . 1 876 . 163 ILE CA C 61.01 . 1 877 . 163 ILE C C 175.49 . 1 878 . 163 ILE CB C 38.92 . 1 879 . 164 LYS N N 123.34 . 1 880 . 164 LYS H H 8.23 . 1 881 . 164 LYS HA H 5.73 . 1 882 . 164 LYS CA C 54.35 . 1 883 . 164 LYS C C 175.05 . 1 884 . 164 LYS CB C 31.21 . 1 885 . 165 ARG N N 119.76 . 1 886 . 165 ARG H H 10.45 . 1 887 . 165 ARG HA H 3.80 . 1 888 . 165 ARG CA C 59.39 . 1 889 . 165 ARG C C 178.69 . 1 890 . 165 ARG CB C 28.66 . 1 891 . 166 SER N N 118.61 . 1 892 . 166 SER H H 9.53 . 1 893 . 166 SER HA H 4.46 . 1 894 . 166 SER CA C 58.04 . 1 895 . 166 SER C C 173.60 . 1 896 . 166 SER CB C 66.92 . 1 897 . 167 MET N N 116.70 . 1 898 . 167 MET H H 8.03 . 1 899 . 167 MET HA H 4.83 . 1 900 . 167 MET CA C 53.35 . 1 901 . 167 MET C C 176.50 . 1 902 . 167 MET CB C 29.13 . 1 903 . 168 ALA N N 122.68 . 1 904 . 168 ALA H H 8.55 . 1 905 . 168 ALA HA H 4.25 . 1 906 . 168 ALA CA C 53.24 . 1 907 . 168 ALA C C 178.63 . 1 908 . 168 ALA CB C 19.89 . 1 909 . 169 SER N N 113.99 . 1 910 . 169 SER H H 8.26 . 1 911 . 169 SER HA H 4.95 . 1 912 . 169 SER CA C 57.94 . 1 913 . 169 SER C C 174.81 . 1 914 . 169 SER CB C 63.60 . 1 915 . 170 GLY N N 110.10 . 1 916 . 170 GLY H H 8.91 . 1 917 . 170 GLY HA2 H 4.74 . 1 918 . 170 GLY HA3 H 4.59 . 1 919 . 170 GLY CA C 43.74 . 1 920 . 170 GLY C C 174.99 . 1 921 . 171 TYR N N 126.86 . 1 922 . 171 TYR H H 9.16 . 1 923 . 171 TYR HA H 3.96 . 1 924 . 171 TYR CA C 61.95 . 1 925 . 171 TYR C C 178.13 . 1 926 . 171 TYR CB C 38.53 . 1 927 . 172 ALA N N 119.77 . 1 928 . 172 ALA H H 10.97 . 1 929 . 172 ALA HA H 4.15 . 1 930 . 172 ALA CA C 53.36 . 1 931 . 172 ALA C C 178.37 . 1 932 . 172 ALA CB C 18.67 . 1 933 . 173 GLY N N 105.46 . 1 934 . 173 GLY H H 8.04 . 1 935 . 173 GLY HA2 H 3.99 . 1 936 . 173 GLY HA3 H 3.99 . 1 937 . 173 GLY CA C 46.37 . 1 938 . 173 GLY C C 174.67 . 1 939 . 174 VAL N N 113.14 . 1 940 . 174 VAL H H 8.45 . 1 941 . 174 VAL HA H 4.78 . 1 942 . 174 VAL CA C 58.89 . 1 943 . 174 VAL C C 175.74 . 1 944 . 174 VAL CB C 34.31 . 1 945 . 175 GLU N N 123.07 . 1 946 . 175 GLU H H 8.63 . 1 947 . 175 GLU HA H 4.06 . 1 948 . 175 GLU CA C 56.82 . 1 949 . 175 GLU C C 175.00 . 1 950 . 175 GLU CB C 30.19 . 1 951 . 176 ASN N N 122.67 . 1 952 . 176 ASN H H 7.88 . 1 953 . 176 ASN HA H 4.60 . 1 954 . 176 ASN CA C 51.57 . 1 955 . 176 ASN C C 175.37 . 1 956 . 176 ASN CB C 38.02 . 1 957 . 177 GLU N N 124.10 . 1 958 . 177 GLU H H 9.42 . 1 959 . 177 GLU HA H 4.26 . 1 960 . 177 GLU CA C 57.94 . 1 961 . 177 GLU C C 178.51 . 1 962 . 177 GLU CB C 29.15 . 1 963 . 178 LEU N N 117.58 . 1 964 . 178 LEU H H 8.52 . 1 965 . 178 LEU HA H 4.07 . 1 966 . 178 LEU CA C 57.15 . 1 967 . 178 LEU C C 179.76 . 1 968 . 178 LEU CB C 40.91 . 1 969 . 179 PHE N N 115.94 . 1 970 . 179 PHE H H 7.06 . 1 971 . 179 PHE HA H 4.49 . 1 972 . 179 PHE CA C 56.14 . 1 973 . 179 PHE C C 174.61 . 1 974 . 179 PHE CB C 35.55 . 1 975 . 180 PHE N N 112.23 . 1 976 . 180 PHE H H 7.10 . 1 977 . 180 PHE HA H 4.90 . 1 978 . 180 PHE CA C 56.04 . 1 979 . 180 PHE C C 176.62 . 1 980 . 180 PHE CB C 39.37 . 1 981 . 181 ARG N N 119.31 . 1 982 . 181 ARG H H 7.25 . 1 983 . 181 ARG HA H 4.52 . 1 984 . 181 ARG CA C 55.47 . 1 985 . 181 ARG C C 177.62 . 1 986 . 181 ARG CB C 31.07 . 1 987 . 182 ASN N N 121.75 . 1 988 . 182 ASN H H 7.63 . 1 989 . 182 ASN HA H 4.56 . 1 990 . 182 ASN CA C 55.81 . 1 991 . 182 ASN C C 175.68 . 1 992 . 182 ASN CB C 37.71 . 1 993 . 183 ASN N N 114.58 . 1 994 . 183 ASN H H 8.33 . 1 995 . 183 ASN HA H 5.05 . 1 996 . 183 ASN CA C 52.46 . 1 997 . 183 ASN C C 173.24 . 1 998 . 183 ASN CB C 36.49 . 1 999 . 184 THR N N 117.72 . 1 1000 . 184 THR H H 7.55 . 1 1001 . 184 THR HA H 5.57 . 1 1002 . 184 THR CA C 60.90 . 1 1003 . 184 THR C C 174.37 . 1 1004 . 184 THR CB C 70.00 . 1 1005 . 185 MET N N 128.41 . 1 1006 . 185 MET H H 9.46 . 1 1007 . 185 MET HA H 4.84 . 1 1008 . 185 MET CA C 54.53 . 1 1009 . 185 MET C C 173.73 . 1 1010 . 185 MET CB C 36.34 . 1 1011 . 186 MET N N 122.82 . 1 1012 . 186 MET H H 8.74 . 1 1013 . 186 MET HA H 4.74 . 1 1014 . 186 MET CA C 52.46 . 1 1015 . 186 MET C C 174.99 . 1 1016 . 186 MET CB C 29.73 . 1 1017 . 187 LEU N N 127.38 . 1 1018 . 187 LEU H H 8.96 . 1 1019 . 187 LEU HA H 4.50 . 1 1020 . 187 LEU CA C 52.46 . 1 1021 . 187 LEU C C 174.49 . 1 1022 . 187 LEU CB C 41.30 . 1 1023 . 188 PHE N N 117.95 . 1 1024 . 188 PHE H H 7.91 . 1 1025 . 188 PHE HA H 5.78 . 1 1026 . 188 PHE CA C 56.54 . 1 1027 . 188 PHE C C 177.12 . 1 1028 . 188 PHE CB C 38.07 . 1 1029 . 189 GLY N N 113.88 . 1 1030 . 189 GLY HA2 H 8.62 . 1 1031 . 189 GLY HA3 H 4.05 . 2 1032 . 189 GLY H H 4.05 . 2 1033 . 189 GLY CA C 44.75 . 1 1034 . 189 GLY C C 169.85 . 1 1035 . 190 ASP N N 115.90 . 1 1036 . 190 ASP H H 8.23 . 1 1037 . 190 ASP HA H 4.77 . 1 1038 . 190 ASP CA C 53.63 . 1 1039 . 190 ASP C C 178.25 . 1 1040 . 190 ASP CB C 44.72 . 1 1041 . 191 ALA N N 125.23 . 1 1042 . 191 ALA H H 10.80 . 1 1043 . 191 ALA HA H 4.03 . 1 1044 . 191 ALA CA C 55.37 . 1 1045 . 191 ALA C C 178.82 . 1 1046 . 191 ALA CB C 16.77 . 1 1047 . 192 LYS N N 118.69 . 1 1048 . 192 LYS H H 8.23 . 1 1049 . 192 LYS HA H 4.03 . 1 1050 . 192 LYS CA C 60.17 . 1 1051 . 192 LYS C C 176.81 . 1 1052 . 192 LYS CB C 32.51 . 1 1053 . 193 LYS N N 119.07 . 1 1054 . 193 LYS H H 8.32 . 1 1055 . 193 LYS HA H 4.25 . 1 1056 . 193 LYS CA C 59.05 . 1 1057 . 193 LYS C C 179.57 . 1 1058 . 193 LYS CB C 32.00 . 1 1059 . 194 MET N N 115.30 . 1 1060 . 194 MET H H 9.18 . 1 1061 . 194 MET HA H 4.67 . 1 1062 . 194 MET CA C 56.71 . 1 1063 . 194 MET C C 178.19 . 1 1064 . 194 MET CB C 30.19 . 1 1065 . 195 THR N N 116.50 . 1 1066 . 195 THR H H 7.19 . 1 1067 . 195 THR HA H 3.83 . 1 1068 . 195 THR CA C 68.89 . 1 1069 . 195 THR C C 176.56 . 1 1070 . 195 THR CB C 66.96 . 1 1071 . 196 GLU N N 120.24 . 1 1072 . 196 GLU H H 8.54 . 1 1073 . 196 GLU HA H 3.95 . 1 1074 . 196 GLU CA C 60.06 . 1 1075 . 196 GLU C C 180.13 . 1 1076 . 196 GLU CB C 29.04 . 1 1077 . 197 GLN N N 118.96 . 1 1078 . 197 GLN H H 8.26 . 1 1079 . 197 GLN HA H 4.08 . 1 1080 . 197 GLN CA C 59.17 . 1 1081 . 197 GLN C C 179.45 . 1 1082 . 197 GLN CB C 28.19 . 1 1083 . 198 ILE N N 123.40 . 1 1084 . 198 ILE H H 8.48 . 1 1085 . 198 ILE HA H 3.58 . 1 1086 . 198 ILE CA C 66.32 . 1 1087 . 198 ILE C C 177.31 . 1 1088 . 198 ILE CB C 37.48 . 1 1089 . 199 VAL N N 119.11 . 1 1090 . 199 VAL H H 8.27 . 1 1091 . 199 VAL HA H 3.41 . 1 1092 . 199 VAL CA C 67.78 . 1 1093 . 199 VAL C C 179.32 . 1 1094 . 199 VAL CB C 31.02 . 1 1095 . 200 GLN N N 117.65 . 1 1096 . 200 GLN H H 7.92 . 1 1097 . 200 GLN HA H 4.08 . 1 1098 . 200 GLN CA C 58.61 . 1 1099 . 200 GLN C C 178.19 . 1 1100 . 200 GLN CB C 27.67 . 1 1101 . 201 ALA N N 120.13 . 1 1102 . 201 ALA H H 7.83 . 1 1103 . 201 ALA HA H 4.35 . 1 1104 . 201 ALA CA C 53.18 . 1 1105 . 201 ALA C C 178.25 . 1 1106 . 201 ALA CB C 17.86 . 1 1107 . 202 MET N N 117.15 . 1 1108 . 202 MET H H 7.76 . 1 1109 . 202 MET HA H 4.23 . 1 1110 . 202 MET CA C 57.38 . 1 1111 . 202 MET C C 175.17 . 1 1112 . 202 MET CB C 33.47 . 1 1113 . 203 ASN N N 123.08 . 1 1114 . 203 ASN H H 7.41 . 1 1115 . 203 ASN HA H 4.47 . 1 1116 . 203 ASN CA C 55.25 . 1 1117 . 203 ASN CB C 40.34 . 1 1118 . 203 ASN C C 179.50 . 1 stop_ save_