data_5624 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A Conserved Structural Motif at the N-terminal of Bacterial Translation Initiation Factor IF2 ; _BMRB_accession_number 5624 _BMRB_flat_file_name bmr5624.str _Entry_type original _Submission_date 2002-12-16 _Accession_date 2002-12-16 _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 Laursen Brian S. . 2 Mortensen Kim K. . 3 Sperling-Petersen Hans U. . 4 Hoffman David W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 629 "13C chemical shifts" 374 "15N chemical shifts" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-28 original author . stop_ _Original_release_date 2003-02-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Conserved Structural Motif at the N-terminal of Bacterial Translation Initiation Factor IF2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12600987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Laursen Brian S. . 2 Mortensen Kim K. . 3 Sperling-Petersen Hans U. . 4 Hoffman David W. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 278 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16320 _Page_last 16328 _Year 2003 _Details . loop_ _Keyword IF2 'translation factor' initiation infb stop_ save_ ################################## # Molecular system description # ################################## save_system_IF2 _Saveframe_category molecular_system _Mol_system_name 'translation initiation factor IF2' _Abbreviation_common IF2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'translation factor IF2' $IF2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IF2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Translation factor IF2' _Abbreviation_common IF2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; TDVTIKTLAAERQTSVERLV QQFADAGIRKSADDSVSAQE KQTLIDHLNQKNSGPDKLTL QRKTRSTLNIPGTGGKSKSV QIEVRKKRTFVKRDPQEAER LAAEEQAQREAEEQARREAE ESAKREAQQKAEREAAEQAK REAAEQAKREAAEKDK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 THR 2 3 ASP 3 4 VAL 4 5 THR 5 6 ILE 6 7 LYS 7 8 THR 8 9 LEU 9 10 ALA 10 11 ALA 11 12 GLU 12 13 ARG 13 14 GLN 14 15 THR 15 16 SER 16 17 VAL 17 18 GLU 18 19 ARG 19 20 LEU 20 21 VAL 21 22 GLN 22 23 GLN 23 24 PHE 24 25 ALA 25 26 ASP 26 27 ALA 27 28 GLY 28 29 ILE 29 30 ARG 30 31 LYS 31 32 SER 32 33 ALA 33 34 ASP 34 35 ASP 35 36 SER 36 37 VAL 37 38 SER 38 39 ALA 39 40 GLN 40 41 GLU 41 42 LYS 42 43 GLN 43 44 THR 44 45 LEU 45 46 ILE 46 47 ASP 47 48 HIS 48 49 LEU 49 50 ASN 50 51 GLN 51 52 LYS 52 53 ASN 53 54 SER 54 55 GLY 55 56 PRO 56 57 ASP 57 58 LYS 58 59 LEU 59 60 THR 60 61 LEU 61 62 GLN 62 63 ARG 63 64 LYS 64 65 THR 65 66 ARG 66 67 SER 67 68 THR 68 69 LEU 69 70 ASN 70 71 ILE 71 72 PRO 72 73 GLY 73 74 THR 74 75 GLY 75 76 GLY 76 77 LYS 77 78 SER 78 79 LYS 79 80 SER 80 81 VAL 81 82 GLN 82 83 ILE 83 84 GLU 84 85 VAL 85 86 ARG 86 87 LYS 87 88 LYS 88 89 ARG 89 90 THR 90 91 PHE 91 92 VAL 92 93 LYS 93 94 ARG 94 95 ASP 95 96 PRO 96 97 GLN 97 98 GLU 98 99 ALA 99 100 GLU 100 101 ARG 101 102 LEU 102 103 ALA 103 104 ALA 104 105 GLU 105 106 GLU 106 107 GLN 107 108 ALA 108 109 GLN 109 110 ARG 110 111 GLU 111 112 ALA 112 113 GLU 113 114 GLU 114 115 GLN 115 116 ALA 116 117 ARG 117 118 ARG 118 119 GLU 119 120 ALA 120 121 GLU 121 122 GLU 122 123 SER 123 124 ALA 124 125 LYS 125 126 ARG 126 127 GLU 127 128 ALA 128 129 GLN 129 130 GLN 130 131 LYS 131 132 ALA 132 133 GLU 133 134 ARG 134 135 GLU 135 136 ALA 136 137 ALA 137 138 GLU 138 139 GLN 139 140 ALA 140 141 LYS 141 142 ARG 142 143 GLU 143 144 ALA 144 145 ALA 145 146 GLU 146 147 GLN 147 148 ALA 148 149 LYS 149 150 ARG 150 151 GLU 151 152 ALA 152 153 ALA 153 154 GLU 154 155 LYS 155 156 ASP 156 157 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-16 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 DBJ BAB37472 "protein chain initiation factor IF-2 [Escherichia coli O157:H7 str. Sakai]" 100.00 890 100.00 100.00 4.08e-93 DBJ BAE77214 "fused protein chain initiation factor 2, IF2 [Escherichia coli str. K-12 substr. W3110]" 100.00 890 100.00 100.00 4.08e-93 DBJ BAG78978 "translation initiation factor IF-1 [Escherichia coli SE11]" 100.00 890 100.00 100.00 4.08e-93 DBJ BAI27448 "protein chain initiation factor IF-2 [Escherichia coli O26:H11 str. 11368]" 100.00 890 100.00 100.00 4.08e-93 DBJ BAI32627 "protein chain initiation factor IF-2 [Escherichia coli O103:H2 str. 12009]" 100.00 890 100.00 100.00 4.08e-93 EMBL CAA05529 "initiation factor IF2-alpha [Escherichia coli]" 100.00 890 100.00 100.00 4.08e-93 EMBL CAA05532 "Initiation factor IF2-alpha [Escherichia coli]" 100.00 890 100.00 100.00 4.25e-93 EMBL CAA05535 "Initiation factor IF2-alpha [Escherichia coli]" 100.00 890 100.00 100.00 4.04e-93 EMBL CAA05538 "Initiation factor IF2-alpha [Escherichia coli]" 100.00 890 100.00 100.00 4.25e-93 EMBL CAA05541 "Initiation factor IF2-alpha [Escherichia coli]" 100.00 890 100.00 100.00 4.25e-93 GB AAA57971 "protein chain initiation factor 2 [Escherichia coli str. K-12 substr. MG1655]" 100.00 890 100.00 100.00 4.08e-93 GB AAC76202 "translation initiation factor IF-2 [Escherichia coli str. K-12 substr. MG1655]" 100.00 890 100.00 100.00 4.08e-93 GB AAG58304 "protein chain initiation factor IF-2 [Escherichia coli O157:H7 str. EDL933]" 100.00 890 100.00 100.00 4.30e-93 GB AAN82365 "Translation initiation factor IF-2 [Escherichia coli CFT073]" 100.00 890 100.00 100.00 4.25e-93 GB AAZ89889 "protein chain initiation factor IF-2 [Shigella sonnei Ss046]" 100.00 890 100.00 100.00 4.17e-93 PIR D85980 "protein chain initiation factor IF-2 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 890 100.00 100.00 4.30e-93 REF NP_289744 "translation initiation factor IF-2 [Escherichia coli O157:H7 str. EDL933]" 100.00 890 100.00 100.00 4.30e-93 REF NP_312076 "translation initiation factor IF-2 [Escherichia coli O157:H7 str. Sakai]" 100.00 890 100.00 100.00 4.08e-93 REF NP_417637 "translation initiation factor IF-2 [Escherichia coli str. K-12 substr. MG1655]" 100.00 890 100.00 100.00 4.08e-93 REF NP_755791 "translation initiation factor IF-2 [Escherichia coli CFT073]" 100.00 890 100.00 100.00 4.25e-93 REF WP_000132922 "translation initiation factor IF-2 [Escherichia coli]" 100.00 890 99.36 99.36 4.72e-92 SP A1AG73 "RecName: Full=Translation initiation factor IF-2 [Escherichia coli APEC O1]" 100.00 890 100.00 100.00 4.25e-93 SP A7ZS65 "RecName: Full=Translation initiation factor IF-2 [Escherichia coli E24377A]" 100.00 890 100.00 100.00 4.08e-93 SP A8A4Y4 "RecName: Full=Translation initiation factor IF-2 [Escherichia coli HS]" 100.00 890 100.00 100.00 4.08e-93 SP B1IQV3 "RecName: Full=Translation initiation factor IF-2 [Escherichia coli ATCC 8739]" 100.00 890 100.00 100.00 4.08e-93 SP B1LFS0 "RecName: Full=Translation initiation factor IF-2 [Escherichia coli SMS-3-5]" 100.00 890 100.00 100.00 4.30e-93 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IF2 '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_name $IF2 '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IF2 1.5 mM 1.0 2.0 . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IF2 1.5 mM 1.0 2.0 [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IF2 1.5 mM 1.0 2.0 '[U-15N; U-13C]' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IF2 1.5 mM 1.0 2.0 [U-15N]-Lys stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HACACBCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HACACBCO _Sample_label . save_ save_15N-edited_HSQC_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited HSQC TOCSY' _Sample_label . save_ save_13C-edited_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited HCCH-TOCSY' _Sample_label . save_ save_2QF-COSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _Sample_label . save_ save_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . 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 HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HACACBCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited HSQC TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conds_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HNCO HNCACB HN(CO)CACB HACACBCO '15N-edited HSQC TOCSY' '13C-edited HCCH-TOCSY' 2QF-COSY TOCSY stop_ _Sample_conditions_label $conds_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'translation factor IF2' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ASP HA H 4.81 . 1 2 . 2 ASP HB2 H 2.48 . 2 3 . 2 ASP HB3 H 2.63 . 2 4 . 2 ASP C C 175.1 . 1 5 . 2 ASP CA C 54.6 . 1 6 . 2 ASP CB C 41.5 . 1 7 . 3 VAL H H 8.31 . 1 8 . 3 VAL HA H 4.36 . 1 9 . 3 VAL HB H 2.14 . 1 10 . 3 VAL HG1 H 0.93 . 1 11 . 3 VAL HG2 H 0.98 . 1 12 . 3 VAL C C 174.3 . 1 13 . 3 VAL CA C 61.0 . 1 14 . 3 VAL CB C 33.7 . 1 15 . 3 VAL CG1 C 21.7 . 1 16 . 3 VAL CG2 C 20.6 . 1 17 . 3 VAL N N 121.0 . 1 18 . 4 THR H H 8.22 . 1 19 . 4 THR HA H 4.82 . 1 20 . 4 THR HB H 4.66 . 1 21 . 4 THR HG2 H 1.20 . 1 22 . 4 THR C C 174.6 . 1 23 . 4 THR CA C 60.4 . 1 24 . 4 THR CB C 71.4 . 1 25 . 4 THR CG2 C 22.0 . 1 26 . 4 THR N N 115.0 . 1 27 . 5 ILE H H 8.42 . 1 28 . 5 ILE HA H 3.67 . 1 29 . 5 ILE HB H 2.13 . 1 30 . 5 ILE HG12 H 1.11 . 2 31 . 5 ILE HG13 H 1.57 . 2 32 . 5 ILE HG2 H 0.86 . 1 33 . 5 ILE HD1 H 0.37 . 1 34 . 5 ILE C C 176.6 . 1 35 . 5 ILE CA C 62.7 . 1 36 . 5 ILE CB C 35.6 . 1 37 . 5 ILE CG1 C 27.7 . 1 38 . 5 ILE CG2 C 18.3 . 1 39 . 5 ILE CD1 C 11.5 . 1 40 . 5 ILE N N 122.4 . 1 41 . 6 LYS H H 8.07 . 1 42 . 6 LYS HA H 3.86 . 1 43 . 6 LYS HB2 H 1.79 . 1 44 . 6 LYS HB3 H 1.79 . 1 45 . 6 LYS HG2 H 1.38 . 4 46 . 6 LYS HG3 H 1.38 . 4 47 . 6 LYS HD2 H 1.63 . 4 48 . 6 LYS HD3 H 1.63 . 4 49 . 6 LYS HE2 H 2.92 . 1 50 . 6 LYS HE3 H 2.92 . 1 51 . 6 LYS C C 179.1 . 1 52 . 6 LYS CA C 60.6 . 1 53 . 6 LYS CB C 32.8 . 1 54 . 6 LYS N N 117.9 . 1 55 . 7 THR H H 8.05 . 1 56 . 7 THR HA H 4.00 . 1 57 . 7 THR HB H 4.27 . 1 58 . 7 THR HG2 H 1.21 . 1 59 . 7 THR C C 176.2 . 1 60 . 7 THR CA C 66.1 . 1 61 . 7 THR CB C 68.1 . 1 62 . 7 THR CG2 C 22.3 . 1 63 . 7 THR N N 117.1 . 1 64 . 8 LEU H H 8.67 . 1 65 . 8 LEU HA H 4.13 . 1 66 . 8 LEU HB2 H 1.44 . 2 67 . 8 LEU HB3 H 1.82 . 2 68 . 8 LEU HG H 1.44 . 1 69 . 8 LEU HD1 H 0.96 . 1 70 . 8 LEU HD2 H 0.96 . 1 71 . 8 LEU C C 177.4 . 1 72 . 8 LEU CA C 57.3 . 1 73 . 8 LEU CB C 41.5 . 1 74 . 8 LEU CD1 C 26.9 . 1 75 . 8 LEU CD2 C 26.9 . 1 76 . 8 LEU N N 125.3 . 1 77 . 9 ALA H H 8.59 . 1 78 . 9 ALA HA H 3.70 . 1 79 . 9 ALA HB H 1.38 . 1 80 . 9 ALA C C 178.2 . 1 81 . 9 ALA CA C 55.9 . 1 82 . 9 ALA CB C 17.6 . 1 83 . 9 ALA N N 121.6 . 1 84 . 10 ALA H H 7.16 . 1 85 . 10 ALA HA H 4.18 . 1 86 . 10 ALA HB H 1.52 . 1 87 . 10 ALA C C 181.4 . 1 88 . 10 ALA CA C 55.0 . 1 89 . 10 ALA CB C 17.7 . 1 90 . 10 ALA N N 118.8 . 1 91 . 11 GLU H H 8.24 . 1 92 . 11 GLU HA H 3.98 . 1 93 . 11 GLU HB2 H 2.13 . 1 94 . 11 GLU HB3 H 2.13 . 1 95 . 11 GLU HG2 H 2.38 . 1 96 . 11 GLU HG3 H 2.38 . 1 97 . 11 GLU C C 178.0 . 1 98 . 11 GLU CA C 59.4 . 1 99 . 11 GLU CB C 30.2 . 1 100 . 11 GLU N N 120.6 . 1 101 . 12 ARG H H 7.99 . 1 102 . 12 ARG HA H 4.17 . 1 103 . 12 ARG HB2 H 1.43 . 1 104 . 12 ARG HB3 H 1.43 . 1 105 . 12 ARG HG2 H 2.15 . 1 106 . 12 ARG HG3 H 2.15 . 1 107 . 12 ARG HD2 H 3.20 . 1 108 . 12 ARG HD3 H 3.20 . 1 109 . 12 ARG C C 174.1 . 1 110 . 12 ARG CA C 56.3 . 1 111 . 12 ARG CB C 29.7 . 1 112 . 12 ARG N N 115.8 . 1 113 . 13 GLN H H 7.91 . 1 114 . 13 GLN HA H 3.89 . 1 115 . 13 GLN HB2 H 2.16 . 1 116 . 13 GLN HB3 H 2.16 . 1 117 . 13 GLN HG2 H 2.26 . 1 118 . 13 GLN HG3 H 2.26 . 1 119 . 13 GLN C C 174.0 . 1 120 . 13 GLN CA C 56.6 . 1 121 . 13 GLN CB C 26.4 . 1 122 . 13 GLN N N 117.7 . 1 123 . 14 THR H H 8.30 . 1 124 . 14 THR HA H 4.74 . 1 125 . 14 THR HB H 3.76 . 1 126 . 14 THR HG2 H 1.22 . 1 127 . 14 THR C C 172.0 . 1 128 . 14 THR CA C 59.6 . 1 129 . 14 THR CB C 71.7 . 1 130 . 14 THR CG2 C 19.0 . 1 131 . 14 THR N N 113.6 . 1 132 . 15 SER H H 8.38 . 1 133 . 15 SER HA H 4.58 . 1 134 . 15 SER HB2 H 3.97 . 2 135 . 15 SER HB3 H 4.33 . 2 136 . 15 SER C C 174.8 . 1 137 . 15 SER CA C 56.7 . 1 138 . 15 SER CB C 65.2 . 1 139 . 15 SER N N 118.1 . 1 140 . 16 VAL H H 8.87 . 1 141 . 16 VAL HA H 3.37 . 1 142 . 16 VAL HB H 1.98 . 1 143 . 16 VAL HG1 H 0.88 . 1 144 . 16 VAL HG2 H 1.05 . 1 145 . 16 VAL C C 176.5 . 1 146 . 16 VAL CA C 67.3 . 1 147 . 16 VAL CB C 31.9 . 1 148 . 16 VAL CG1 C 21.5 . 1 149 . 16 VAL CG2 C 24.1 . 1 150 . 16 VAL N N 122.7 . 1 151 . 17 GLU H H 8.80 . 1 152 . 17 GLU HA H 3.87 . 1 153 . 17 GLU HB2 H 1.88 . 2 154 . 17 GLU HB3 H 2.00 . 2 155 . 17 GLU HG2 H 2.21 . 2 156 . 17 GLU HG3 H 2.35 . 2 157 . 17 GLU C C 178.9 . 1 158 . 17 GLU CA C 60.5 . 1 159 . 17 GLU CB C 29.0 . 1 160 . 17 GLU N N 117.2 . 1 161 . 18 ARG H H 7.77 . 1 162 . 18 ARG HA H 4.07 . 1 163 . 18 ARG HB2 H 1.85 . 1 164 . 18 ARG HB3 H 1.85 . 1 165 . 18 ARG HG2 H 1.56 . 1 166 . 18 ARG HG3 H 1.56 . 1 167 . 18 ARG HD2 H 3.17 . 2 168 . 18 ARG HD3 H 3.22 . 2 169 . 18 ARG C C 177.6 . 1 170 . 18 ARG CA C 58.3 . 1 171 . 18 ARG CB C 29.5 . 1 172 . 18 ARG N N 120.0 . 1 173 . 19 LEU H H 8.18 . 1 174 . 19 LEU HA H 4.33 . 1 175 . 19 LEU HB2 H 1.41 . 2 176 . 19 LEU HB3 H 1.92 . 2 177 . 19 LEU HG H 1.72 . 1 178 . 19 LEU HD1 H 0.82 . 1 179 . 19 LEU HD2 H 0.95 . 1 180 . 19 LEU C C 178.8 . 1 181 . 19 LEU CA C 57.7 . 1 182 . 19 LEU CB C 42.4 . 1 183 . 19 LEU CG C 27.3 . 1 184 . 19 LEU CD1 C 24.6 . 1 185 . 19 LEU CD2 C 28.8 . 1 186 . 19 LEU N N 122.0 . 1 187 . 20 VAL H H 8.80 . 1 188 . 20 VAL HA H 3.57 . 1 189 . 20 VAL HB H 2.18 . 1 190 . 20 VAL HG1 H 0.88 . 1 191 . 20 VAL HG2 H 0.95 . 1 192 . 20 VAL C C 178.8 . 1 193 . 20 VAL CA C 68.2 . 1 194 . 20 VAL CB C 32.0 . 1 195 . 20 VAL CG1 C 21.6 . 1 196 . 20 VAL CG2 C 23.1 . 1 197 . 20 VAL N N 118.4 . 1 198 . 21 GLN H H 7.54 . 1 199 . 21 GLN HA H 4.05 . 1 200 . 21 GLN HB2 H 2.24 . 1 201 . 21 GLN HB3 H 2.24 . 1 202 . 21 GLN HG2 H 2.41 . 1 203 . 21 GLN HG3 H 2.41 . 1 204 . 21 GLN HE21 H 6.79 . 1 205 . 21 GLN HE22 H 7.59 . 1 206 . 21 GLN C C 177.0 . 1 207 . 21 GLN CA C 58.7 . 1 208 . 21 GLN CB C 28.4 . 1 209 . 21 GLN CG C 33.4 . 1 210 . 21 GLN CD C 179.7 . 1 211 . 21 GLN N N 121.3 . 1 212 . 21 GLN NE2 N 114.0 . 1 213 . 22 GLN H H 8.42 . 1 214 . 22 GLN HA H 4.04 . 1 215 . 22 GLN HB2 H 1.69 . 2 216 . 22 GLN HB3 H 2.38 . 2 217 . 22 GLN HG2 H 2.27 . 2 218 . 22 GLN HG3 H 2.64 . 2 219 . 22 GLN HE21 H 6.33 . 1 220 . 22 GLN HE22 H 7.16 . 1 221 . 22 GLN C C 178.8 . 1 222 . 22 GLN CA C 59.6 . 1 223 . 22 GLN CB C 28.2 . 1 224 . 22 GLN CG C 34.3 . 1 225 . 22 GLN CD C 178.0 . 1 226 . 22 GLN N N 121.0 . 1 227 . 22 GLN NE2 N 107.9 . 1 228 . 23 PHE H H 8.57 . 1 229 . 23 PHE HA H 3.88 . 1 230 . 23 PHE HB2 H 2.85 . 2 231 . 23 PHE HB3 H 3.27 . 2 232 . 23 PHE HD1 H 7.08 . 1 233 . 23 PHE HD2 H 7.08 . 1 234 . 23 PHE HE1 H 6.99 . 1 235 . 23 PHE HE2 H 6.99 . 1 236 . 23 PHE HZ H 6.78 . 1 237 . 23 PHE C C 177.6 . 1 238 . 23 PHE CA C 64.5 . 1 239 . 23 PHE CB C 37.0 . 1 240 . 23 PHE N N 117.5 . 1 241 . 24 ALA H H 7.96 . 1 242 . 24 ALA HA H 3.93 . 1 243 . 24 ALA HB H 1.55 . 1 244 . 24 ALA C C 182.0 . 1 245 . 24 ALA CA C 55.7 . 1 246 . 24 ALA CB C 17.3 . 1 247 . 24 ALA N N 123.1 . 1 248 . 25 ASP H H 8.50 . 1 249 . 25 ASP HA H 4.24 . 1 250 . 25 ASP HB2 H 2.67 . 2 251 . 25 ASP HB3 H 2.88 . 2 252 . 25 ASP C C 176.0 . 1 253 . 25 ASP CA C 57.1 . 1 254 . 25 ASP CB C 40.5 . 1 255 . 25 ASP N N 122.5 . 1 256 . 26 ALA H H 7.27 . 1 257 . 26 ALA HA H 3.49 . 1 258 . 26 ALA HB H 1.11 . 1 259 . 26 ALA C C 175.6 . 1 260 . 26 ALA CA C 51.5 . 1 261 . 26 ALA CB C 18.4 . 1 262 . 26 ALA N N 120.1 . 1 263 . 27 GLY H H 7.27 . 1 264 . 27 GLY HA2 H 3.65 . 2 265 . 27 GLY HA3 H 4.13 . 2 266 . 27 GLY C C 173.4 . 1 267 . 27 GLY CA C 45.4 . 1 268 . 27 GLY N N 106.4 . 1 269 . 28 ILE H H 8.44 . 1 270 . 28 ILE HA H 4.18 . 1 271 . 28 ILE HB H 1.71 . 1 272 . 28 ILE HG12 H 1.05 . 2 273 . 28 ILE HG13 H 1.44 . 2 274 . 28 ILE HG2 H 0.60 . 1 275 . 28 ILE HD1 H 0.97 . 1 276 . 28 ILE C C 173.6 . 1 277 . 28 ILE CA C 60.3 . 1 278 . 28 ILE CB C 40.5 . 1 279 . 28 ILE CG1 C 27.5 . 1 280 . 28 ILE CG2 C 18.1 . 1 281 . 28 ILE CD1 C 14.0 . 1 282 . 28 ILE N N 123.1 . 1 283 . 29 ARG H H 8.64 . 1 284 . 29 ARG HA H 4.11 . 1 285 . 29 ARG HB2 H 1.69 . 1 286 . 29 ARG HB3 H 1.69 . 1 287 . 29 ARG HG2 H 1.41 . 1 288 . 29 ARG HG3 H 1.41 . 1 289 . 29 ARG HD2 H 3.09 . 1 290 . 29 ARG HD3 H 3.09 . 1 291 . 29 ARG C C 174.4 . 1 292 . 29 ARG CA C 56.0 . 1 293 . 29 ARG CB C 30.1 . 1 294 . 29 ARG N N 129.3 . 1 295 . 30 LYS H H 8.41 . 1 296 . 30 LYS HA H 4.73 . 1 297 . 30 LYS HB2 H 1.33 . 2 298 . 30 LYS HB3 H 1.55 . 2 299 . 30 LYS HG2 H 0.28 . 2 300 . 30 LYS HG3 H 0.73 . 2 301 . 30 LYS HD2 H 1.15 . 2 302 . 30 LYS HD3 H 1.74 . 2 303 . 30 LYS HE2 H 2.21 . 2 304 . 30 LYS HE3 H 2.32 . 2 305 . 30 LYS C C 174.0 . 1 306 . 30 LYS CA C 52.8 . 1 307 . 30 LYS CB C 37.1 . 1 308 . 30 LYS CE C 42.5 . 1 309 . 30 LYS N N 126.3 . 1 310 . 31 SER H H 8.90 . 1 311 . 31 SER HA H 4.65 . 1 312 . 31 SER HB2 H 3.80 . 2 313 . 31 SER HB3 H 3.89 . 2 314 . 31 SER C C 174.1 . 1 315 . 31 SER CA C 56.4 . 1 316 . 31 SER CB C 65.7 . 1 317 . 31 SER N N 116.2 . 1 318 . 32 ALA H H 8.46 . 1 319 . 32 ALA HA H 3.72 . 1 320 . 32 ALA HB H 1.32 . 1 321 . 32 ALA C C 176.4 . 1 322 . 32 ALA CA C 55.1 . 1 323 . 32 ALA CB C 19.5 . 1 324 . 32 ALA N N 120.8 . 1 325 . 33 ASP H H 7.76 . 1 326 . 33 ASP HA H 4.75 . 1 327 . 33 ASP HB2 H 2.38 . 2 328 . 33 ASP HB3 H 2.82 . 2 329 . 33 ASP C C 175.3 . 1 330 . 33 ASP CA C 54.1 . 1 331 . 33 ASP CB C 41.7 . 1 332 . 33 ASP N N 112.9 . 1 333 . 34 ASP H H 7.32 . 1 334 . 34 ASP HA H 4.69 . 1 335 . 34 ASP HB2 H 2.77 . 2 336 . 34 ASP HB3 H 2.86 . 2 337 . 34 ASP C C 175.7 . 1 338 . 34 ASP CA C 55.1 . 1 339 . 34 ASP CB C 44.1 . 1 340 . 34 ASP N N 120.2 . 1 341 . 35 SER H H 8.55 . 1 342 . 35 SER HA H 4.84 . 1 343 . 35 SER HB2 H 3.70 . 1 344 . 35 SER HB3 H 3.70 . 1 345 . 35 SER C C 172.0 . 1 346 . 35 SER CA C 57.9 . 1 347 . 35 SER CB C 65.1 . 1 348 . 35 SER N N 114.4 . 1 349 . 36 VAL H H 8.57 . 1 350 . 36 VAL HA H 4.28 . 1 351 . 36 VAL HB H 1.79 . 1 352 . 36 VAL HG1 H 0.55 . 1 353 . 36 VAL HG2 H 0.90 . 1 354 . 36 VAL C C 174.3 . 1 355 . 36 VAL CA C 60.9 . 1 356 . 36 VAL CB C 35.0 . 1 357 . 36 VAL CG1 C 21.6 . 1 358 . 36 VAL CG2 C 23.2 . 1 359 . 36 VAL N N 120.4 . 1 360 . 37 SER H H 9.43 . 1 361 . 37 SER HA H 4.69 . 1 362 . 37 SER HB2 H 3.89 . 2 363 . 37 SER HB3 H 4.38 . 2 364 . 37 SER C C 174.7 . 1 365 . 37 SER CA C 56.8 . 1 366 . 37 SER CB C 66.2 . 1 367 . 37 SER N N 124.5 . 1 368 . 38 ALA H H 9.02 . 1 369 . 38 ALA HA H 4.05 . 1 370 . 38 ALA HB H 1.46 . 1 371 . 38 ALA C C 180.3 . 1 372 . 38 ALA CA C 55.7 . 1 373 . 38 ALA CB C 18.1 . 1 374 . 38 ALA N N 123.9 . 1 375 . 39 GLN H H 8.44 . 1 376 . 39 GLN HA H 4.09 . 1 377 . 39 GLN HB2 H 2.06 . 1 378 . 39 GLN HB3 H 2.06 . 1 379 . 39 GLN HG2 H 2.37 . 1 380 . 39 GLN HG3 H 2.37 . 1 381 . 39 GLN C C 177.6 . 1 382 . 39 GLN CA C 57.5 . 1 383 . 39 GLN CB C 28.7 . 1 384 . 39 GLN N N 118.0 . 1 385 . 40 GLU H H 7.87 . 1 386 . 40 GLU HA H 3.89 . 1 387 . 40 GLU HB2 H 1.69 . 2 388 . 40 GLU HB3 H 2.51 . 2 389 . 40 GLU HG2 H 2.39 . 1 390 . 40 GLU HG3 H 2.39 . 1 391 . 40 GLU C C 177.8 . 1 392 . 40 GLU CA C 59.5 . 1 393 . 40 GLU CB C 30.4 . 1 394 . 40 GLU N N 121.6 . 1 395 . 41 LYS H H 8.43 . 1 396 . 41 LYS HA H 3.77 . 1 397 . 41 LYS HB2 H 1.76 . 2 398 . 41 LYS HB3 H 1.99 . 2 399 . 41 LYS HG2 H 1.66 . 1 400 . 41 LYS HG3 H 1.66 . 1 401 . 41 LYS HD2 H 1.38 . 1 402 . 41 LYS HD3 H 1.38 . 1 403 . 41 LYS HE2 H 2.86 . 1 404 . 41 LYS HE3 H 2.86 . 1 405 . 41 LYS C C 176.7 . 1 406 . 41 LYS CA C 60.5 . 1 407 . 41 LYS CB C 32.6 . 1 408 . 41 LYS N N 119.3 . 1 409 . 42 GLN H H 7.88 . 1 410 . 42 GLN HA H 3.81 . 1 411 . 42 GLN HB2 H 2.14 . 1 412 . 42 GLN HB3 H 2.14 . 1 413 . 42 GLN HG2 H 2.38 . 1 414 . 42 GLN HG3 H 2.38 . 1 415 . 42 GLN HE21 H 6.75 . 1 416 . 42 GLN HE22 H 7.83 . 1 417 . 42 GLN C C 176.7 . 1 418 . 42 GLN CA C 58.3 . 1 419 . 42 GLN CB C 27.8 . 1 420 . 42 GLN CG C 33.1 . 1 421 . 42 GLN CD C 179.8 . 1 422 . 42 GLN N N 117.7 . 1 423 . 42 GLN NE2 N 115.9 . 1 424 . 43 THR H H 8.21 . 1 425 . 43 THR HA H 3.97 . 1 426 . 43 THR HB H 4.33 . 1 427 . 43 THR HG2 H 1.26 . 1 428 . 43 THR C C 176.1 . 1 429 . 43 THR CA C 67.2 . 1 430 . 43 THR CB C 68.4 . 1 431 . 43 THR CG2 C 21.7 . 1 432 . 43 THR N N 117.3 . 1 433 . 44 LEU H H 7.75 . 1 434 . 44 LEU HA H 3.64 . 1 435 . 44 LEU HB2 H 0.96 . 2 436 . 44 LEU HB3 H 1.85 . 2 437 . 44 LEU HG H 1.04 . 1 438 . 44 LEU HD1 H 0.10 . 1 439 . 44 LEU HD2 H 0.10 . 1 440 . 44 LEU C C 176.6 . 1 441 . 44 LEU CA C 58.8 . 1 442 . 44 LEU CB C 41.0 . 1 443 . 44 LEU CG C 26.4 . 1 444 . 44 LEU CD1 C 23.4 . 1 445 . 44 LEU CD2 C 23.4 . 1 446 . 44 LEU N N 122.8 . 1 447 . 45 ILE H H 8.01 . 1 448 . 45 ILE HA H 3.38 . 1 449 . 45 ILE HB H 1.86 . 1 450 . 45 ILE HG12 H 1.13 . 2 451 . 45 ILE HG13 H 1.54 . 2 452 . 45 ILE HG2 H 0.86 . 1 453 . 45 ILE HD1 H 0.71 . 1 454 . 45 ILE C C 178.0 . 1 455 . 45 ILE CA C 65.3 . 1 456 . 45 ILE CB C 37.7 . 1 457 . 45 ILE CG1 C 29.3 . 1 458 . 45 ILE CG2 C 17.8 . 1 459 . 45 ILE CD1 C 13.8 . 1 460 . 45 ILE N N 119.5 . 1 461 . 46 ASP H H 8.77 . 1 462 . 46 ASP HA H 4.38 . 1 463 . 46 ASP HB2 H 2.62 . 2 464 . 46 ASP HB3 H 2.79 . 2 465 . 46 ASP C C 178.2 . 1 466 . 46 ASP CA C 57.5 . 1 467 . 46 ASP CB C 40.3 . 1 468 . 46 ASP N N 120.4 . 1 469 . 47 HIS H H 8.11 . 1 470 . 47 HIS HA H 4.23 . 1 471 . 47 HIS HB2 H 3.25 . 2 472 . 47 HIS HB3 H 3.36 . 2 473 . 47 HIS HD2 H 6.69 . 1 474 . 47 HIS HE1 H 7.46 . 1 475 . 47 HIS C C 177.5 . 1 476 . 47 HIS CA C 60.4 . 1 477 . 47 HIS CB C 30.4 . 1 478 . 47 HIS N N 121.1 . 1 479 . 48 LEU H H 8.41 . 1 480 . 48 LEU HA H 3.82 . 1 481 . 48 LEU HB2 H 1.34 . 2 482 . 48 LEU HB3 H 1.79 . 2 483 . 48 LEU HG H 1.79 . 1 484 . 48 LEU HD1 H 0.64 . 1 485 . 48 LEU HD2 H 0.76 . 1 486 . 48 LEU C C 178.7 . 1 487 . 48 LEU CA C 57.2 . 1 488 . 48 LEU CB C 41.5 . 1 489 . 48 LEU CG C 26.8 . 1 490 . 48 LEU CD1 C 26.0 . 1 491 . 48 LEU CD2 C 23.2 . 1 492 . 48 LEU N N 119.1 . 1 493 . 49 ASN H H 8.11 . 1 494 . 49 ASN HA H 4.56 . 1 495 . 49 ASN HB2 H 2.84 . 1 496 . 49 ASN HB3 H 2.84 . 1 497 . 49 ASN C C 176.1 . 1 498 . 49 ASN CA C 54.5 . 1 499 . 49 ASN CB C 38.5 . 1 500 . 49 ASN N N 117.5 . 1 501 . 50 GLN H H 7.69 . 1 502 . 50 GLN HA H 4.11 . 1 503 . 50 GLN HB2 H 2.06 . 1 504 . 50 GLN HB3 H 2.06 . 1 505 . 50 GLN HG2 H 2.33 . 2 506 . 50 GLN HG3 H 2.42 . 2 507 . 50 GLN C C 176.2 . 1 508 . 50 GLN CA C 57.3 . 1 509 . 50 GLN CB C 28.8 . 1 510 . 50 GLN N N 119.1 . 1 511 . 51 LYS H H 7.85 . 1 512 . 51 LYS HA H 4.10 . 1 513 . 51 LYS HB2 H 1.68 . 1 514 . 51 LYS HB3 H 1.68 . 1 515 . 51 LYS HG2 H 1.30 . 4 516 . 51 LYS HG3 H 1.30 . 4 517 . 51 LYS HD2 H 1.54 . 4 518 . 51 LYS HD3 H 1.54 . 4 519 . 51 LYS HE2 H 2.92 . 1 520 . 51 LYS HE3 H 2.92 . 1 521 . 51 LYS C C 176.3 . 1 522 . 51 LYS CA C 57.1 . 1 523 . 51 LYS CB C 28.8 . 1 524 . 51 LYS N N 119.9 . 1 525 . 52 ASN H H 8.08 . 1 526 . 52 ASN HA H 4.69 . 1 527 . 52 ASN HB2 H 2.73 . 2 528 . 52 ASN HB3 H 2.85 . 2 529 . 52 ASN HD21 H 6.78 . 1 530 . 52 ASN HD22 H 6.78 . 1 531 . 52 ASN C C 174.6 . 1 532 . 52 ASN CA C 53.4 . 1 533 . 52 ASN CB C 39.1 . 1 534 . 52 ASN N N 117.9 . 1 535 . 53 SER H H 8.01 . 1 536 . 53 SER HA H 4.45 . 1 537 . 53 SER HB2 H 3.85 . 1 538 . 53 SER HB3 H 3.85 . 1 539 . 53 SER C C 173.8 . 1 540 . 53 SER CA C 58.5 . 1 541 . 53 SER CB C 64.1 . 1 542 . 53 SER N N 117.9 . 1 543 . 54 GLY H H 8.16 . 1 544 . 54 GLY HA2 H 4.09 . 1 545 . 54 GLY HA3 H 4.09 . 1 546 . 54 GLY C C 174.6 . 1 547 . 54 GLY CA C 44.9 . 1 548 . 54 GLY N N 110.5 . 1 549 . 55 PRO HA H 4.37 . 1 550 . 55 PRO HB2 H 1.91 . 2 551 . 55 PRO HB3 H 2.35 . 2 552 . 55 PRO HG2 H 2.06 . 1 553 . 55 PRO HG3 H 2.06 . 1 554 . 55 PRO HD2 H 3.64 . 2 555 . 55 PRO HD3 H 3.84 . 2 556 . 55 PRO CA C 63.5 . 1 557 . 55 PRO CB C 32.1 . 1 558 . 55 PRO CG C 27.8 . 1 559 . 55 PRO CD C 51.7 . 1 560 . 56 ASP H H 8.34 . 1 561 . 56 ASP HA H 4.51 . 1 562 . 56 ASP HB2 H 2.64 . 1 563 . 56 ASP HB3 H 2.64 . 1 564 . 56 ASP C C 177.5 . 1 565 . 56 ASP CA C 54.5 . 1 566 . 56 ASP CB C 41.1 . 1 567 . 57 LYS H H 8.21 . 1 568 . 57 LYS HA H 4.14 . 1 569 . 57 LYS HB2 H 1.63 . 1 570 . 57 LYS HB3 H 1.63 . 1 571 . 57 LYS HG2 H 1.43 . 4 572 . 57 LYS HG3 H 1.43 . 4 573 . 57 LYS HD2 H 1.68 . 4 574 . 57 LYS HD3 H 1.68 . 4 575 . 57 LYS HE2 H 2.95 . 1 576 . 57 LYS HE3 H 2.95 . 1 577 . 57 LYS C C 176.0 . 1 578 . 57 LYS CA C 57.2 . 1 579 . 57 LYS CB C 32.6 . 1 580 . 57 LYS N N 121.0 . 1 581 . 58 LEU H H 8.11 . 1 582 . 58 LEU HA H 4.27 . 1 583 . 58 LEU HB2 H 1.57 . 2 584 . 58 LEU HB3 H 1.69 . 2 585 . 58 LEU HG H 1.38 . 1 586 . 58 LEU HD1 H 0.86 . 1 587 . 58 LEU HD2 H 0.86 . 1 588 . 58 LEU C C 177.5 . 1 589 . 58 LEU CA C 56.0 . 1 590 . 58 LEU CB C 42.1 . 1 591 . 58 LEU N N 121.4 . 1 592 . 59 THR H H 7.93 . 1 593 . 59 THR HA H 4.15 . 1 594 . 59 THR HB H 4.16 . 4 595 . 59 THR HG2 H 1.16 . 1 596 . 59 THR C C 174.5 . 1 597 . 59 THR CA C 63.0 . 1 598 . 59 THR CB C 69.3 . 1 599 . 59 THR N N 114.9 . 1 600 . 60 LEU H H 7.99 . 1 601 . 60 LEU HA H 4.22 . 1 602 . 60 LEU HB2 H 1.55 . 1 603 . 60 LEU HB3 H 1.55 . 1 604 . 60 LEU HG H 1.37 . 1 605 . 60 LEU HD1 H 0.83 . 1 606 . 60 LEU HD2 H 0.83 . 1 607 . 60 LEU C C 177.0 . 1 608 . 60 LEU CA C 55.8 . 1 609 . 60 LEU CB C 42.3 . 1 610 . 60 LEU N N 123.4 . 1 611 . 61 GLN H H 8.13 . 1 612 . 61 GLN HA H 4.19 . 1 613 . 61 GLN HB2 H 2.08 . 1 614 . 61 GLN HB3 H 2.08 . 1 615 . 61 GLN HG2 H 2.35 . 1 616 . 61 GLN HG3 H 2.35 . 1 617 . 61 GLN C C 174.4 . 1 618 . 61 GLN CA C 56.1 . 1 619 . 61 GLN CB C 30.1 . 1 620 . 61 GLN N N 120.3 . 1 621 . 67 THR H H 8.15 . 1 622 . 67 THR HA H 4.29 . 1 623 . 67 THR HB H 4.34 . 1 624 . 67 THR HG2 H 1.16 . 1 625 . 67 THR C C 173.6 . 1 626 . 67 THR CA C 61.8 . 1 627 . 67 THR CB C 69.8 . 1 628 . 67 THR N N 116.1 . 1 629 . 68 LEU H H 8.16 . 1 630 . 68 LEU HA H 4.29 . 1 631 . 68 LEU HB2 H 1.55 . 1 632 . 68 LEU HB3 H 1.55 . 1 633 . 68 LEU HD1 H 0.83 . 2 634 . 68 LEU HD2 H 0.86 . 2 635 . 68 LEU C C 175.6 . 1 636 . 68 LEU CA C 55.3 . 1 637 . 68 LEU CB C 42.5 . 1 638 . 68 LEU N N 125.0 . 1 639 . 69 ASN H H 7.81 . 1 640 . 69 ASN HA H 4.11 . 1 641 . 69 ASN HB2 H 2.05 . 1 642 . 69 ASN HB3 H 2.05 . 1 643 . 69 ASN C C 177.2 . 1 644 . 69 ASN CA C 57.3 . 1 645 . 69 ASN CB C 30.7 . 1 646 . 69 ASN N N 125.7 . 1 647 . 70 ILE H H 8.01 . 1 648 . 70 ILE HA H 4.41 . 1 649 . 70 ILE HB H 1.82 . 1 650 . 70 ILE HG12 H 1.11 . 2 651 . 70 ILE HG13 H 1.43 . 2 652 . 70 ILE HG2 H 0.90 . 1 653 . 70 ILE HD1 H 0.82 . 1 654 . 70 ILE C C 174.0 . 1 655 . 70 ILE CA C 59.0 . 1 656 . 70 ILE CB C 38.7 . 1 657 . 70 ILE CG1 C 27.7 . 1 658 . 70 ILE CG2 C 17.3 . 1 659 . 70 ILE CD1 C 13.1 . 1 660 . 70 ILE N N 122.6 . 1 661 . 71 PRO HA H 4.39 . 1 662 . 71 PRO HB2 H 2.25 . 1 663 . 71 PRO HB3 H 2.25 . 1 664 . 71 PRO HG2 H 1.93 . 1 665 . 71 PRO HG3 H 1.93 . 1 666 . 71 PRO HD2 H 3.65 . 1 667 . 71 PRO HD3 H 3.65 . 1 668 . 71 PRO C C 176.8 . 1 669 . 71 PRO CA C 63.6 . 1 670 . 71 PRO CB C 32.3 . 1 671 . 72 GLY H H 8.42 . 1 672 . 72 GLY HA2 H 3.99 . 1 673 . 72 GLY HA3 H 3.99 . 1 674 . 72 GLY C C 174.0 . 1 675 . 72 GLY CA C 45.4 . 1 676 . 72 GLY N N 109.3 . 1 677 . 73 THR H H 8.02 . 1 678 . 73 THR HA H 4.34 . 1 679 . 73 THR HG2 H 1.17 . 1 680 . 73 THR C C 174.8 . 1 681 . 73 THR CA C 62.0 . 1 682 . 73 THR CB C 69.9 . 1 683 . 73 THR N N 112.5 . 1 684 . 74 GLY H H 8.49 . 1 685 . 74 GLY HA2 H 3.94 . 1 686 . 74 GLY HA3 H 3.94 . 1 687 . 74 GLY C C 174.1 . 1 688 . 74 GLY CA C 45.4 . 1 689 . 74 GLY N N 111.2 . 1 690 . 75 GLY H H 8.24 . 1 691 . 75 GLY HA2 H 3.91 . 1 692 . 75 GLY HA3 H 3.91 . 1 693 . 75 GLY C C 176.0 . 1 694 . 75 GLY CA C 45.4 . 1 695 . 75 GLY N N 108.6 . 1 696 . 76 LYS H H 8.11 . 1 697 . 76 LYS HA H 4.32 . 1 698 . 76 LYS HB2 H 1.73 . 2 699 . 76 LYS HB3 H 1.81 . 2 700 . 76 LYS HG2 H 1.39 . 1 701 . 76 LYS HG3 H 1.39 . 1 702 . 76 LYS HD2 H 1.65 . 1 703 . 76 LYS HD3 H 1.65 . 1 704 . 76 LYS HE2 H 2.95 . 1 705 . 76 LYS HE3 H 2.95 . 1 706 . 76 LYS C C 175.8 . 1 707 . 76 LYS CA C 56.3 . 1 708 . 76 LYS CB C 33.1 . 1 709 . 76 LYS N N 121.1 . 1 710 . 77 SER H H 8.25 . 1 711 . 77 SER HA H 4.40 . 1 712 . 77 SER HB2 H 3.82 . 1 713 . 77 SER HB3 H 3.82 . 1 714 . 77 SER C C 173.9 . 1 715 . 77 SER CA C 58.4 . 1 716 . 77 SER CB C 63.8 . 1 717 . 77 SER N N 116.8 . 1 718 . 78 LYS H H 8.31 . 1 719 . 78 LYS HA H 4.27 . 1 720 . 78 LYS HB2 H 1.74 . 1 721 . 78 LYS HB3 H 1.74 . 1 722 . 78 LYS HG2 H 1.41 . 4 723 . 78 LYS HG3 H 1.41 . 4 724 . 78 LYS HD2 H 1.69 . 4 725 . 78 LYS HD3 H 1.69 . 4 726 . 78 LYS HE2 H 2.93 . 1 727 . 78 LYS HE3 H 2.93 . 1 728 . 78 LYS C C 175.8 . 1 729 . 78 LYS CA C 56.3 . 1 730 . 78 LYS CB C 33.0 . 1 731 . 78 LYS N N 123.9 . 1 732 . 79 SER H H 8.25 . 1 733 . 79 SER HA H 4.47 . 1 734 . 79 SER HB2 H 3.84 . 1 735 . 79 SER HB3 H 3.84 . 1 736 . 79 SER C C 173.9 . 1 737 . 79 SER CA C 58.4 . 1 738 . 79 SER CB C 63.8 . 1 739 . 79 SER N N 116.8 . 1 740 . 80 VAL H H 8.09 . 1 741 . 80 VAL HA H 4.09 . 1 742 . 80 VAL HB H 2.02 . 1 743 . 80 VAL HG1 H 0.88 . 4 744 . 80 VAL HG2 H 0.88 . 4 745 . 80 VAL C C 175.2 . 1 746 . 80 VAL CA C 62.3 . 1 747 . 80 VAL CB C 32.8 . 1 748 . 80 VAL CG1 C 20.8 . 4 749 . 80 VAL CG2 C 20.8 . 4 750 . 80 VAL N N 121.8 . 1 751 . 81 GLN H H 8.34 . 1 752 . 81 GLN HA H 4.32 . 1 753 . 81 GLN HB2 H 1.91 . 2 754 . 81 GLN HB3 H 2.01 . 2 755 . 81 GLN HG2 H 2.30 . 1 756 . 81 GLN HG3 H 2.30 . 1 757 . 81 GLN C C 175.1 . 1 758 . 81 GLN CA C 55.7 . 1 759 . 81 GLN CB C 29.6 . 1 760 . 81 GLN N N 124.2 . 1 761 . 82 ILE H H 8.13 . 1 762 . 82 ILE HA H 4.08 . 1 763 . 82 ILE HB H 1.78 . 1 764 . 82 ILE HG12 H 1.41 . 1 765 . 82 ILE HG13 H 1.41 . 1 766 . 82 ILE HG2 H 1.13 . 1 767 . 82 ILE HD1 H 0.83 . 1 768 . 82 ILE C C 175.3 . 1 769 . 82 ILE CA C 61.1 . 1 770 . 82 ILE CB C 38.8 . 1 771 . 82 ILE CD1 C 17.3 . 1 772 . 82 ILE N N 122.7 . 1 773 . 83 GLU H H 8.39 . 1 774 . 83 GLU HA H 4.27 . 1 775 . 83 GLU HB2 H 1.91 . 1 776 . 83 GLU HB3 H 1.91 . 1 777 . 83 GLU HG2 H 2.16 . 1 778 . 83 GLU HG3 H 2.16 . 1 779 . 83 GLU C C 175.6 . 1 780 . 83 GLU CA C 56.6 . 1 781 . 83 GLU CB C 30.6 . 1 782 . 83 GLU N N 125.4 . 1 783 . 84 VAL H H 8.20 . 1 784 . 84 VAL HA H 4.00 . 1 785 . 84 VAL HB H 2.03 . 1 786 . 84 VAL HG1 H 0.88 . 1 787 . 84 VAL HG2 H 0.88 . 1 788 . 84 VAL C C 175.6 . 1 789 . 84 VAL CA C 62.7 . 1 790 . 84 VAL CB C 32.7 . 1 791 . 84 VAL N N 122.5 . 1 792 . 85 ARG H H 8.32 . 1 793 . 85 ARG HA H 4.28 . 1 794 . 85 ARG HB2 H 1.74 . 2 795 . 85 ARG HB3 H 1.93 . 2 796 . 85 ARG HG2 H 1.57 . 1 797 . 85 ARG HG3 H 1.57 . 1 798 . 85 ARG HD2 H 3.14 . 1 799 . 85 ARG HD3 H 3.14 . 1 800 . 85 ARG C C 175.6 . 1 801 . 85 ARG CA C 56.2 . 1 802 . 85 ARG CB C 30.7 . 1 803 . 85 ARG N N 124.4 . 1 804 . 86 LYS H H 8.22 . 1 805 . 86 LYS HA H 4.22 . 1 806 . 86 LYS HB2 H 1.70 . 1 807 . 86 LYS HB3 H 1.70 . 1 808 . 86 LYS HG2 H 1.37 . 1 809 . 86 LYS HG3 H 1.37 . 1 810 . 86 LYS CA C 56.5 . 1 811 . 86 LYS CB C 32.8 . 1 812 . 86 LYS N N 122.5 . 1 813 . 89 THR H H 8.03 . 1 814 . 89 THR HA H 4.27 . 1 815 . 89 THR HB H 4.27 . 4 816 . 89 THR HG2 H 1.15 . 1 817 . 89 THR C C 173.1 . 1 818 . 89 THR CA C 61.8 . 1 819 . 89 THR CB C 69.4 . 1 820 . 89 THR N N 115.2 . 1 821 . 90 PHE H H 8.28 . 1 822 . 90 PHE HA H 4.62 . 1 823 . 90 PHE HB2 H 2.95 . 2 824 . 90 PHE HB3 H 3.06 . 2 825 . 90 PHE HD1 H 7.17 . 1 826 . 90 PHE HD2 H 7.17 . 1 827 . 90 PHE HE1 H 7.26 . 1 828 . 90 PHE HE2 H 7.26 . 1 829 . 90 PHE HZ H 7.22 . 1 830 . 90 PHE C C 174.5 . 1 831 . 90 PHE CA C 57.6 . 1 832 . 90 PHE CB C 40.0 . 1 833 . 90 PHE N N 122.8 . 1 834 . 91 VAL H H 7.99 . 1 835 . 91 VAL HA H 4.00 . 1 836 . 91 VAL HB H 1.92 . 1 837 . 91 VAL HG1 H 0.83 . 4 838 . 91 VAL HG2 H 0.83 . 4 839 . 91 VAL C C 174.7 . 1 840 . 91 VAL CA C 62.1 . 1 841 . 91 VAL CB C 33.2 . 1 842 . 91 VAL N N 122.6 . 1 843 . 92 LYS H H 8.24 . 1 844 . 92 LYS HA H 4.19 . 1 845 . 92 LYS HB2 H 1.67 . 1 846 . 92 LYS HB3 H 1.67 . 1 847 . 92 LYS HG2 H 1.37 . 4 848 . 92 LYS HG3 H 1.37 . 4 849 . 92 LYS HD2 H 1.75 . 4 850 . 92 LYS HD3 H 1.75 . 4 851 . 92 LYS HE2 H 2.95 . 1 852 . 92 LYS HE3 H 2.95 . 1 853 . 92 LYS C C 175.3 . 1 854 . 92 LYS CA C 56.3 . 1 855 . 92 LYS CB C 33.1 . 1 856 . 92 LYS N N 125.4 . 1 857 . 93 ARG H H 8.32 . 1 858 . 93 ARG HA H 4.28 . 1 859 . 93 ARG HB2 H 1.70 . 1 860 . 93 ARG HB3 H 1.70 . 1 861 . 93 ARG HG2 H 1.55 . 1 862 . 93 ARG HG3 H 1.55 . 1 863 . 93 ARG HD2 H 3.08 . 1 864 . 93 ARG HD3 H 3.08 . 1 865 . 93 ARG C C 174.9 . 1 866 . 93 ARG CA C 55.8 . 1 867 . 93 ARG CB C 31.3 . 1 868 . 93 ARG N N 123.1 . 1 869 . 94 ASP H H 8.44 . 1 870 . 94 ASP HA H 4.81 . 1 871 . 94 ASP HB2 H 2.73 . 2 872 . 94 ASP HB3 H 2.85 . 2 873 . 94 ASP C C 174.5 . 1 874 . 94 ASP CA C 52.4 . 1 875 . 94 ASP CB C 41.7 . 1 876 . 94 ASP N N 124.0 . 1 877 . 95 PRO HA H 4.32 . 1 878 . 95 PRO HB2 H 2.32 . 1 879 . 95 PRO HB3 H 2.32 . 1 880 . 95 PRO HG2 H 1.97 . 1 881 . 95 PRO HG3 H 1.97 . 1 882 . 95 PRO HD2 H 3.84 . 1 883 . 95 PRO HD3 H 3.84 . 1 884 . 95 PRO C C 177.5 . 1 885 . 95 PRO CA C 64.6 . 1 886 . 95 PRO CB C 32.2 . 1 887 . 96 GLN H H 8.45 . 1 888 . 96 GLN HA H 4.08 . 1 889 . 96 GLN HB2 H 1.91 . 1 890 . 96 GLN HB3 H 2.11 . 1 891 . 96 GLN HG2 H 2.38 . 1 892 . 96 GLN HG3 H 2.38 . 1 893 . 96 GLN C C 178.4 . 1 894 . 96 GLN CA C 59.4 . 1 895 . 96 GLN CB C 28.2 . 1 896 . 96 GLN N N 117.9 . 1 897 . 97 GLU HA H 4.14 . 1 898 . 97 GLU HB2 H 1.94 . 1 899 . 97 GLU HB3 H 1.94 . 1 900 . 97 GLU C C 178.5 . 1 901 . 97 GLU CA C 58.8 . 1 902 . 97 GLU CB C 30.1 . 1 903 . 98 ALA H H 7.97 . 1 904 . 98 ALA HA H 4.17 . 1 905 . 98 ALA HB H 1.49 . 1 906 . 98 ALA C C 179.8 . 1 907 . 98 ALA CA C 55.0 . 1 908 . 98 ALA CB C 17.7 . 1 909 . 98 ALA N N 121.7 . 1 910 . 99 GLU H H 8.27 . 1 911 . 99 GLU HA H 4.11 . 1 912 . 99 GLU HB2 H 2.15 . 1 913 . 99 GLU HB3 H 2.15 . 1 914 . 99 GLU HG2 H 2.40 . 1 915 . 99 GLU HG3 H 2.40 . 1 916 . 99 GLU C C 178.3 . 1 917 . 99 GLU CA C 59.5 . 1 918 . 99 GLU CB C 30.2 . 1 919 . 99 GLU N N 120.5 . 1 920 . 100 ARG H H 8.18 . 1 921 . 100 ARG HA H 4.08 . 1 922 . 100 ARG HB2 H 2.08 . 1 923 . 100 ARG HB3 H 2.08 . 1 924 . 100 ARG HG2 H 2.38 . 1 925 . 100 ARG HG3 H 2.38 . 1 926 . 100 ARG HD2 H 2.94 . 1 927 . 100 ARG HD3 H 2.94 . 1 928 . 100 ARG C C 178.2 . 1 929 . 100 ARG CA C 59.2 . 1 930 . 100 ARG CB C 29.2 . 1 931 . 100 ARG N N 120.7 . 1 932 . 101 LEU H H 8.01 . 1 933 . 101 LEU HA H 4.41 . 1 934 . 101 LEU HB2 H 1.82 . 1 935 . 101 LEU HB3 H 1.82 . 1 936 . 101 LEU HG H 1.44 . 1 937 . 101 LEU HD1 H 0.81 . 4 938 . 101 LEU HD2 H 0.88 . 4 939 . 101 LEU C C 173.8 . 1 940 . 101 LEU CA C 58.8 . 1 941 . 101 LEU CB C 38.8 . 1 942 . 101 LEU N N 122.8 . 1 943 . 102 ALA H H 8.01 . 1 944 . 102 ALA HA H 4.19 . 1 945 . 102 ALA HB H 1.47 . 1 946 . 102 ALA C C 179.4 . 1 947 . 102 ALA CA C 54.5 . 1 948 . 102 ALA CB C 18.2 . 1 949 . 102 ALA N N 122.3 . 1 950 . 103 ALA H H 7.91 . 1 951 . 103 ALA HA H 4.19 . 1 952 . 103 ALA HB H 1.47 . 1 953 . 103 ALA C C 179.0 . 1 954 . 103 ALA CA C 54.2 . 1 955 . 103 ALA CB C 18.4 . 1 956 . 103 ALA N N 122.0 . 1 957 . 104 GLU H H 7.75 . 1 958 . 104 GLU HA H 4.18 . 1 959 . 104 GLU CA C 58.3 . 1 960 . 104 GLU CB C 32.8 . 1 961 . 104 GLU N N 119.1 . 1 962 . 119 ALA HA H 4.20 . 1 963 . 119 ALA HB H 1.50 . 1 964 . 119 ALA C C 180.2 . 1 965 . 119 ALA CA C 55.1 . 1 966 . 119 ALA CB C 17.9 . 1 967 . 120 GLU H H 8.15 . 1 968 . 120 GLU HA H 4.05 . 1 969 . 120 GLU C C 178.7 . 1 970 . 120 GLU CA C 59.2 . 1 971 . 120 GLU CB C 24.8 . 1 972 . 120 GLU N N 120.4 . 1 973 . 121 GLU H H 8.32 . 1 974 . 121 GLU HA H 4.07 . 1 975 . 121 GLU HB2 H 2.07 . 1 976 . 121 GLU HB3 H 2.07 . 1 977 . 121 GLU HG2 H 2.27 . 1 978 . 121 GLU HG3 H 2.27 . 1 979 . 121 GLU C C 178.8 . 1 980 . 121 GLU CA C 59.3 . 1 981 . 121 GLU CB C 29.4 . 1 982 . 121 GLU N N 120.0 . 1 983 . 122 SER H H 8.36 . 1 984 . 122 SER HA H 4.17 . 1 985 . 122 SER HB2 H 4.00 . 1 986 . 122 SER HB3 H 4.00 . 1 987 . 122 SER C C 176.0 . 1 988 . 122 SER CA C 61.7 . 1 989 . 122 SER CB C 62.7 . 1 990 . 122 SER N N 115.9 . 1 991 . 123 ALA H H 7.94 . 1 992 . 123 ALA HA H 4.20 . 1 993 . 123 ALA HB H 1.50 . 1 994 . 123 ALA C C 180.0 . 1 995 . 123 ALA CA C 55.0 . 1 996 . 123 ALA CB C 18.2 . 1 997 . 123 ALA N N 124.2 . 1 998 . 124 LYS H H 7.77 . 1 999 . 124 LYS HA H 4.11 . 1 1000 . 124 LYS HB2 H 1.87 . 1 1001 . 124 LYS HB3 H 1.87 . 1 1002 . 124 LYS HG2 H 1.38 . 1 1003 . 124 LYS HG3 H 1.38 . 1 1004 . 124 LYS HD2 H 1.59 . 1 1005 . 124 LYS HD3 H 1.59 . 1 1006 . 124 LYS HE2 H 2.95 . 1 1007 . 124 LYS HE3 H 2.95 . 1 1008 . 124 LYS C C 178.5 . 1 1009 . 124 LYS CA C 59.1 . 1 1010 . 124 LYS CB C 32.8 . 1 1011 . 124 LYS N N 119.2 . 1 1012 . 147 ALA H H 7.87 . 1 1013 . 147 ALA HA H 4.21 . 1 1014 . 147 ALA HB H 1.42 . 1 1015 . 147 ALA C C 177.8 . 1 1016 . 147 ALA CA C 53.1 . 1 1017 . 147 ALA CB C 19.1 . 1 1018 . 147 ALA N N 121.8 . 1 1019 . 148 LYS H H 7.99 . 1 1020 . 148 LYS HA H 4.17 . 1 1021 . 148 LYS HB2 H 1.39 . 1 1022 . 148 LYS HB3 H 1.39 . 1 1023 . 148 LYS HG2 H 1.78 . 4 1024 . 148 LYS HG3 H 1.78 . 4 1025 . 148 LYS HD2 H 2.61 . 4 1026 . 148 LYS HD3 H 2.61 . 4 1027 . 148 LYS HE2 H 3.20 . 4 1028 . 148 LYS HE3 H 3.20 . 4 1029 . 148 LYS C C 176.1 . 1 1030 . 148 LYS CA C 56.8 . 1 1031 . 148 LYS CB C 30.2 . 1 1032 . 148 LYS N N 118.6 . 1 1033 . 149 ARG H H 7.93 . 1 1034 . 149 ARG HA H 4.15 . 1 1035 . 149 ARG HB2 H 1.86 . 1 1036 . 149 ARG HB3 H 1.86 . 1 1037 . 149 ARG HG2 H 1.58 . 1 1038 . 149 ARG HG3 H 1.58 . 1 1039 . 149 ARG HD2 H 3.20 . 1 1040 . 149 ARG HD3 H 3.20 . 1 1041 . 149 ARG C C 177.2 . 1 1042 . 149 ARG CA C 58.1 . 1 1043 . 149 ARG CB C 30.4 . 1 1044 . 149 ARG N N 121.0 . 1 1045 . 150 GLU H H 8.21 . 1 1046 . 150 GLU HA H 4.11 . 1 1047 . 150 GLU HB2 H 1.99 . 1 1048 . 150 GLU HB3 H 1.99 . 1 1049 . 150 GLU HG2 H 2.21 . 2 1050 . 150 GLU HG3 H 2.37 . 2 1051 . 150 GLU C C 176.8 . 1 1052 . 150 GLU CA C 57.8 . 1 1053 . 150 GLU CB C 30.0 . 1 1054 . 150 GLU N N 120.1 . 1 1055 . 151 ALA H H 7.90 . 1 1056 . 151 ALA HA H 4.19 . 1 1057 . 151 ALA HB H 1.41 . 1 1058 . 151 ALA C C 177.8 . 1 1059 . 151 ALA CA C 53.5 . 1 1060 . 151 ALA CB C 19.0 . 1 1061 . 151 ALA N N 122.7 . 1 1062 . 152 ALA H H 7.86 . 1 1063 . 152 ALA HA H 4.23 . 1 1064 . 152 ALA HB H 1.41 . 1 1065 . 152 ALA C C 177.8 . 1 1066 . 152 ALA CA C 53.2 . 1 1067 . 152 ALA CB C 19.1 . 1 1068 . 152 ALA N N 121.4 . 1 1069 . 153 GLU H H 8.01 . 1 1070 . 153 GLU HA H 4.19 . 1 1071 . 153 GLU HB2 H 1.96 . 1 1072 . 153 GLU HB3 H 1.96 . 1 1073 . 153 GLU HG2 H 2.28 . 1 1074 . 153 GLU HG3 H 2.28 . 1 1075 . 153 GLU C C 176.2 . 1 1076 . 153 GLU CA C 56.9 . 1 1077 . 153 GLU CB C 30.3 . 1 1078 . 153 GLU N N 118.7 . 1 1079 . 154 LYS H H 7.93 . 1 1080 . 154 LYS HA H 4.26 . 1 1081 . 154 LYS HB2 H 1.80 . 1 1082 . 154 LYS HB3 H 1.80 . 1 1083 . 154 LYS HG2 H 1.38 . 1 1084 . 154 LYS HG3 H 1.38 . 1 1085 . 154 LYS HD2 H 1.65 . 1 1086 . 154 LYS HD3 H 1.65 . 1 1087 . 154 LYS HE2 H 2.96 . 1 1088 . 154 LYS HE3 H 2.96 . 1 1089 . 154 LYS C C 175.7 . 1 1090 . 154 LYS CA C 56.7 . 1 1091 . 154 LYS CB C 33.3 . 1 1092 . 154 LYS N N 120.4 . 1 1093 . 155 ASP H H 8.18 . 1 1094 . 155 ASP HA H 4.56 . 1 1095 . 155 ASP HB2 H 2.38 . 2 1096 . 155 ASP HB3 H 2.72 . 2 1097 . 155 ASP C C 174.4 . 1 1098 . 155 ASP CA C 54.5 . 1 1099 . 155 ASP CB C 41.3 . 1 1100 . 155 ASP N N 121.0 . 1 1101 . 156 LYS H H 7.64 . 1 1102 . 156 LYS HA H 4.09 . 1 1103 . 156 LYS HB2 H 1.68 . 2 1104 . 156 LYS HB3 H 1.78 . 2 1105 . 156 LYS HG2 H 1.34 . 1 1106 . 156 LYS HG3 H 1.34 . 1 1107 . 156 LYS HE2 H 2.94 . 1 1108 . 156 LYS HE3 H 2.94 . 1 1109 . 156 LYS CA C 57.8 . 1 1110 . 156 LYS CB C 33.8 . 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 46 45 '48,47' '516,515' '518,517' '572,571' '574,573' '723,722' '725,724' '744,744,744,743,743,743' '749,748' '838,838,838,837,837,837' '848,847' '850,849' '938,938,938,937,937,937' '1024,1023' '1026,1025' '1028,1027' stop_ save_