data_4116 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Chemical Shift Assignments of the Colicin E9 Immunity Protein from Escherichia coli ; _BMRB_accession_number 4116 _BMRB_flat_file_name bmr4116.str _Entry_type original _Submission_date 1997-03-04 _Accession_date 1997-03-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represents the immunity protein Im9 (residues 3-86) of colicin E9 DNase. This study reports 1H, 13C and 15N chemical shifts for backbone and sidechains obtained from triple-resonance data. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boetzel R. . . 2 Czisch M. . . 3 MacDonald C. J. . 4 Kaptein R. . . 5 Hemmings A. M. . 6 James Richard . . 7 Kleanthous Colin . . 8 Moore Geoffrey R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 438 "13C chemical shifts" 239 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-24 original author 'original release' 2006-10-27 update BMRB 'add the relationship loop' stop_ loop_ _Related_BMRB_accession_number _Relationship 4115 'homologous Immunity protein Im9 bound to DNase domain of colicin E9' 4293 'DNase domain of non cognate binding partner E9' 4352 'Im9 bound DNase domain of non cognate binding partner E9' 7323 'Colicin immunity protein IM2' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Boetzel, R., Czisch, M., MacDonald, C. J., Kaptein, R., Hemmings, A.M., James, R., Kleanthous, C., Moore, G. R., "Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9," J. Biomol. NMR 12, 567-568 (1998). ; _Citation_title ; Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99109973 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boetzel R. . . 2 Czisch M. . . 3 MacDonald C. J. . 4 Kaptein R. . . 5 Hemmings A. M. . 6 James Richard . . 7 Kleanthous Colin . . 8 Moore Geoffrey R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 567 _Page_last 568 _Year 1998 _Details . loop_ _Keyword colicin 'immunity protein' NMR 'nuclear magnetic resonance' protein 'protein-protein interaction' 'resonance assignments' 'secondary structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_IM9 _Saveframe_category molecular_system _Mol_system_name 'Im9 immunity protein' _Abbreviation_common IM9 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IM9 $IM9 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IM9 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Im9 immunity protein' _Abbreviation_common IM9 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; MELKHSISDYTEAEFLQLVT TICNADTSSEEELVKLVTHF EEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGK SGFKQG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LEU 4 LYS 5 HIS 6 SER 7 ILE 8 SER 9 ASP 10 TYR 11 THR 12 GLU 13 ALA 14 GLU 15 PHE 16 LEU 17 GLN 18 LEU 19 VAL 20 THR 21 THR 22 ILE 23 CYS 24 ASN 25 ALA 26 ASP 27 THR 28 SER 29 SER 30 GLU 31 GLU 32 GLU 33 LEU 34 VAL 35 LYS 36 LEU 37 VAL 38 THR 39 HIS 40 PHE 41 GLU 42 GLU 43 MET 44 THR 45 GLU 46 HIS 47 PRO 48 SER 49 GLY 50 SER 51 ASP 52 LEU 53 ILE 54 TYR 55 TYR 56 PRO 57 LYS 58 GLU 59 GLY 60 ASP 61 ASP 62 ASP 63 SER 64 PRO 65 SER 66 GLY 67 ILE 68 VAL 69 ASN 70 THR 71 VAL 72 LYS 73 GLN 74 TRP 75 ARG 76 ALA 77 ALA 78 ASN 79 GLY 80 LYS 81 SER 82 GLY 83 PHE 84 LYS 85 GLN 86 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4115 IM9 100.00 86 100.00 100.00 3.29e-56 PDB 1BXI "Crystal Structure Of The Escherichia Coli Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" 100.00 86 97.67 98.84 1.78e-54 PDB 1E0H "Inhibitor Protein Im9 Bound To Its Partner E9 Dnase" 100.00 86 100.00 100.00 3.29e-56 PDB 1EMV "Crystal Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9 (1.7 Angstroms)" 100.00 86 100.00 100.00 3.29e-56 PDB 1FR2 "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9(E41a)" 100.00 86 98.84 98.84 1.76e-55 PDB 1IMP "Colicin E9 Immunity Protein Im9, Nmr, 21 Structures" 98.84 86 100.00 100.00 3.87e-55 PDB 1IMQ "Colicin E9 Immunity Protein Im9, Nmr, Minimized Average Structure" 100.00 86 100.00 100.00 3.29e-56 PDB 2GYK "Crystal Structure Of The Complex Of The Colicin E9 Dnase Domain With A Mutant Immunity Protein, Imme9 (D51a)" 100.00 86 98.84 98.84 3.36e-55 PDB 2GZE "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55a)" 100.00 86 98.84 98.84 4.56e-55 PDB 2GZF "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y54f)" 100.00 86 98.84 100.00 1.22e-55 PDB 2GZG "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55f)" 100.00 86 98.84 100.00 1.22e-55 PDB 2GZI "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (V34a)" 100.00 86 98.84 98.84 1.22e-55 PDB 2GZJ "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (D51a)" 100.00 86 98.84 98.84 3.36e-55 PDB 2K5X "Chemical Shift Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" 100.00 86 100.00 100.00 3.29e-56 PDB 2VLN "N75a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 86 100.00 100.00 3.29e-56 PDB 2VLO "K97a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 93 100.00 100.00 4.87e-56 PDB 2VLP "R54a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 86 100.00 100.00 3.29e-56 PDB 2VLQ "F86a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 86 100.00 100.00 3.29e-56 EMBL CAA33863 "E9 immunity protein (86 AA) [Plasmid ColE9-J]" 100.00 86 100.00 100.00 3.29e-56 GB AAA23076 "E9imm peptide [Plasmid ColE9]" 100.00 86 98.84 100.00 1.37e-55 GB ACM07431 "colicin E9 immunity protein [Escherichia coli]" 100.00 86 100.00 100.00 3.29e-56 REF WP_012644887 "colicin E9 immunity protein [Escherichia coli]" 100.00 86 100.00 100.00 3.29e-56 REF YP_002533538 "colicin E9 immunity protein [Escherichia coli]" 100.00 86 100.00 100.00 3.29e-56 SP P13479 "RecName: Full=Colicin-E9 immunity protein; AltName: Full=ImmE9; AltName: Full=Microcin-E9 immunity protein" 100.00 86 100.00 100.00 3.29e-56 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IM9 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 $IM9 'recombinant technology' 'E. coli' Escherichia coli JM1 . 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 $IM9 4.0 mM '[U-100%15N; U-100%13C]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _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 6.2 . pH temperature 298 . 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 . C 13 . ppm . . . . . . . $entry_citation $entry_citation dioxane H 1 'methylene protons' ppm 3.77 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . 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_chemical_shift_assignment_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 IM9 _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 . 3 LEU H H 8.51 . 1 2 . 3 LEU N N 125.40 . 1 3 . 3 LEU HA H 4.45 . 1 4 . 3 LEU CA C 52.42 . 1 5 . 3 LEU HB2 H 1.57 . 1 6 . 3 LEU HB3 H 0.91 . 1 7 . 3 LEU CB C 39.18 . 1 8 . 3 LEU HG H 1.59 . 1 9 . 3 LEU HD1 H 0.65 . 1 10 . 3 LEU HD2 H 0.56 . 1 11 . 3 LEU CD1 C 22.65 . 1 12 . 3 LEU CD2 C 20.11 . 1 13 . 4 LYS H H 7.91 . 1 14 . 4 LYS N N 122.80 . 1 15 . 4 LYS HA H 4.35 . 1 16 . 4 LYS CA C 53.33 . 1 17 . 4 LYS HB2 H 1.34 . 1 18 . 4 LYS CB C 31.31 . 1 19 . 4 LYS HG2 H 1.16 . 1 20 . 4 LYS HG3 H 1.03 . 1 21 . 4 LYS CG C 23.56 . 1 22 . 4 LYS HD2 H 1.34 . 1 23 . 4 LYS HD3 H 1.21 . 1 24 . 4 LYS CD C 26.86 . 1 25 . 4 LYS HE2 H 2.75 . 1 26 . 4 LYS HE3 H 2.75 . 1 27 . 4 LYS CE C 40.31 . 1 28 . 5 HIS H H 8.86 . 1 29 . 5 HIS N N 116.20 . 1 30 . 5 HIS HA H 4.76 . 1 31 . 5 HIS CA C 55.15 . 1 32 . 5 HIS HB2 H 3.44 . 1 33 . 5 HIS HB3 H 3.28 . 1 34 . 5 HIS CB C 27.84 . 1 35 . 5 HIS HD2 H 7.35 . 1 36 . 5 HIS HE1 H 8.53 . 1 37 . 6 SER H H 8.02 . 1 38 . 6 SER N N 114.30 . 1 39 . 6 SER HA H 4.78 . 1 40 . 6 SER CA C 55.46 . 1 41 . 6 SER HB2 H 3.93 . 1 42 . 6 SER HB3 H 3.70 . 1 43 . 6 SER CB C 63.55 . 1 44 . 7 ILE H H 9.38 . 1 45 . 7 ILE N N 127.70 . 1 46 . 7 ILE HA H 4.12 . 1 47 . 7 ILE CA C 63.38 . 1 48 . 7 ILE HB H 1.66 . 1 49 . 7 ILE CB C 34.87 . 1 50 . 7 ILE HG12 H 0.92 . 1 51 . 7 ILE HG13 H 0.92 . 1 52 . 7 ILE CG1 C 28.48 . 1 53 . 7 ILE HG2 H 0.51 . 1 54 . 7 ILE CG2 C 13.22 . 1 55 . 7 ILE HD1 H -0.14 . 1 56 . 7 ILE CD1 C 10.95 . 1 57 . 8 SER H H 7.58 . 1 58 . 8 SER N N 113.40 . 1 59 . 8 SER HA H 4.80 . 1 60 . 8 SER CA C 57.08 . 1 61 . 8 SER HB2 H 3.98 . 1 62 . 8 SER HB3 H 3.91 . 1 63 . 8 SER CB C 61.21 . 1 64 . 9 ASP H H 7.95 . 1 65 . 9 ASP N N 119.00 . 1 66 . 9 ASP HA H 4.83 . 1 67 . 9 ASP CA C 52.80 . 1 68 . 9 ASP HB2 H 2.85 . 1 69 . 9 ASP CB C 40.74 . 1 70 . 10 TYR H H 8.31 . 1 71 . 10 TYR N N 121.10 . 1 72 . 10 TYR HA H 4.95 . 1 73 . 10 TYR CA C 56.43 . 1 74 . 10 TYR HB2 H 3.57 . 1 75 . 10 TYR HB3 H 3.57 . 1 76 . 10 TYR CB C 38.30 . 1 77 . 10 TYR HD1 H 7.46 . 1 78 . 10 TYR HD2 H 7.46 . 1 79 . 10 TYR HE1 H 7.01 . 1 80 . 10 TYR HE2 H 7.01 . 1 81 . 11 THR H H 8.97 . 1 82 . 11 THR N N 112.60 . 1 83 . 11 THR HA H 5.03 . 1 84 . 11 THR CA C 58.78 . 1 85 . 11 THR HB H 4.73 . 1 86 . 11 THR CB C 68.77 . 1 87 . 11 THR HG2 H 1.28 . 1 88 . 11 THR CG2 C 19.93 . 1 89 . 12 GLU H H 9.35 . 1 90 . 12 GLU N N 124.80 . 1 91 . 12 GLU HA H 2.44 . 1 92 . 12 GLU CA C 58.28 . 1 93 . 12 GLU HB2 H 1.86 . 1 94 . 12 GLU HB3 H 1.83 . 1 95 . 12 GLU CB C 27.13 . 1 96 . 12 GLU HG2 H 2.02 . 1 97 . 12 GLU HG3 H 1.81 . 1 98 . 12 GLU CG C 33.92 . 1 99 . 13 ALA H H 8.45 . 1 100 . 13 ALA N N 119.70 . 1 101 . 13 ALA HA H 4.12 . 1 102 . 13 ALA CA C 53.10 . 1 103 . 13 ALA HB H 1.43 . 1 104 . 13 ALA CB C 16.27 . 1 105 . 14 GLU H H 8.04 . 1 106 . 14 GLU N N 120.11 . 1 107 . 14 GLU HA H 4.17 . 1 108 . 14 GLU CA C 56.66 . 1 109 . 14 GLU HB2 H 2.76 . 1 110 . 14 GLU HB3 H 2.35 . 1 111 . 14 GLU CB C 29.41 . 1 112 . 14 GLU HG2 H 2.56 . 1 113 . 14 GLU HG3 H 2.45 . 1 114 . 14 GLU CG C 35.13 . 1 115 . 15 PHE H H 8.79 . 1 116 . 15 PHE N N 124.40 . 1 117 . 15 PHE HA H 3.93 . 1 118 . 15 PHE CA C 60.30 . 1 119 . 15 PHE HB2 H 2.89 . 1 120 . 15 PHE HB3 H 2.71 . 1 121 . 15 PHE CB C 38.55 . 1 122 . 16 LEU H H 9.09 . 1 123 . 16 LEU N N 120.50 . 1 124 . 16 LEU HA H 3.97 . 1 125 . 16 LEU CA C 56.21 . 1 126 . 16 LEU HB2 H 2.08 . 1 127 . 16 LEU HB3 H 1.63 . 1 128 . 16 LEU CB C 39.09 . 1 129 . 16 LEU HG H 1.48 . 1 130 . 16 LEU CG C 25.25 . 1 131 . 16 LEU HD1 H 0.95 . 1 132 . 16 LEU HD2 H 0.84 . 1 133 . 16 LEU CD1 C 23.38 . 1 134 . 16 LEU CD2 C 21.57 . 1 135 . 17 GLN H H 7.95 . 1 136 . 17 GLN N N 123.10 . 1 137 . 17 GLN HA H 4.10 . 1 138 . 17 GLN CA C 57.03 . 1 139 . 17 GLN HB2 H 2.28 . 1 140 . 17 GLN HB3 H 2.28 . 1 141 . 17 GLN CB C 25.64 . 1 142 . 17 GLN HG2 H 2.48 . 1 143 . 17 GLN CG C 31.62 . 1 144 . 17 GLN HE21 H 7.49 . 1 145 . 17 GLN HE22 H 6.96 . 1 146 . 17 GLN NE2 N 112.85 . 1 147 . 18 LEU H H 7.54 . 1 148 . 18 LEU N N 124.20 . 1 149 . 18 LEU HB2 H 1.82 . 1 150 . 18 LEU HB3 H 1.58 . 1 151 . 18 LEU CB C 38.76 . 1 152 . 18 LEU HG H 1.44 . 1 153 . 18 LEU CG C 25.71 . 1 154 . 18 LEU HD1 H 1.06 . 1 155 . 18 LEU HD2 H 0.72 . 1 156 . 18 LEU CD1 C 22.95 . 1 157 . 18 LEU CD2 C 23.78 . 1 158 . 19 VAL H H 8.25 . 1 159 . 19 VAL N N 118.60 . 1 160 . 19 VAL HA H 3.16 . 1 161 . 19 VAL CA C 65.17 . 1 162 . 19 VAL HB H 1.94 . 1 163 . 19 VAL CB C 29.97 . 1 164 . 19 VAL HG1 H 0.90 . 1 165 . 19 VAL CG1 C 21.16 . 1 166 . 19 VAL HG2 H 0.78 . 1 167 . 19 VAL CG2 C 22.61 . 1 168 . 20 THR H H 8.75 . 1 169 . 20 THR N N 119.00 . 1 170 . 20 THR HA H 3.57 . 1 171 . 20 THR CA C 66.24 . 1 172 . 20 THR HB H 4.36 . 1 173 . 20 THR CB C 66.89 . 1 174 . 20 THR HG2 H 1.24 . 1 175 . 20 THR CG2 C 18.83 . 1 176 . 21 THR H H 8.18 . 1 177 . 21 THR N N 120.10 . 1 178 . 21 THR HA H 3.90 . 1 179 . 21 THR CA C 65.69 . 1 180 . 21 THR HB H 4.50 . 1 181 . 21 THR CB C 66.74 . 1 182 . 21 THR HG2 H 1.14 . 1 183 . 21 THR CG2 C 19.59 . 1 184 . 22 ILE H H 7.76 . 1 185 . 22 ILE N N 120.50 . 1 186 . 22 ILE HA H 3.46 . 1 187 . 22 ILE CA C 63.77 . 1 188 . 22 ILE HB H 1.77 . 1 189 . 22 ILE CB C 36.29 . 1 190 . 22 ILE HG12 H 1.85 . 1 191 . 22 ILE HG13 H 1.85 . 1 192 . 22 ILE CG1 C 27.10 . 1 193 . 22 ILE HG2 H 0.73 . 1 194 . 22 ILE CG2 C 16.33 . 1 195 . 22 ILE HD1 H 0.60 . 1 196 . 22 ILE CD1 C 12.13 . 1 197 . 23 CYS H H 8.87 . 1 198 . 23 CYS N N 120.20 . 1 199 . 23 CYS HA H 3.81 . 1 200 . 23 CYS CA C 62.35 . 1 201 . 23 CYS HB2 H 3.00 . 1 202 . 23 CYS HB3 H 2.68 . 1 203 . 23 CYS CB C 24.76 . 1 204 . 24 ASN H H 8.16 . 1 205 . 24 ASN N N 116.10 . 1 206 . 24 ASN HA H 4.68 . 1 207 . 24 ASN CA C 50.92 . 1 208 . 24 ASN HB2 H 2.98 . 1 209 . 24 ASN HB3 H 2.73 . 1 210 . 24 ASN CB C 36.24 . 1 211 . 24 ASN HD21 H 7.93 . 1 212 . 24 ASN HD22 H 7.00 . 1 213 . 24 ASN ND2 N 112.30 . 1 214 . 25 ALA H H 8.16 . 1 215 . 25 ALA N N 125.30 . 1 216 . 25 ALA HA H 3.91 . 1 217 . 25 ALA CA C 50.81 . 1 218 . 25 ALA HB H 1.50 . 1 219 . 25 ALA CB C 14.89 . 1 220 . 26 ASP H H 8.42 . 1 221 . 26 ASP N N 120.30 . 1 222 . 26 ASP HA H 4.91 . 1 223 . 26 ASP CA C 51.30 . 1 224 . 26 ASP HB2 H 2.91 . 1 225 . 26 ASP HB3 H 2.43 . 1 226 . 26 ASP CB C 38.41 . 1 227 . 27 THR H H 7.80 . 1 228 . 27 THR N N 109.10 . 1 229 . 27 THR HA H 4.62 . 1 230 . 27 THR CA C 57.89 . 1 231 . 27 THR HB H 4.49 . 1 232 . 27 THR CB C 69.04 . 1 233 . 27 THR HG2 H 0.97 . 1 234 . 27 THR CG2 C 20.40 . 1 235 . 28 SER H H 8.97 . 1 236 . 28 SER N N 116.40 . 1 237 . 28 SER HA H 4.48 . 1 238 . 28 SER CA C 57.69 . 1 239 . 28 SER HB2 H 4.04 . 1 240 . 28 SER HB3 H 4.00 . 1 241 . 28 SER CB C 61.81 . 1 242 . 29 SER H H 7.66 . 1 243 . 29 SER N N 113.50 . 1 244 . 29 SER HA H 4.82 . 1 245 . 29 SER CA C 54.97 . 1 246 . 29 SER HB2 H 4.30 . 1 247 . 29 SER HB3 H 4.07 . 1 248 . 29 SER CB C 64.20 . 1 249 . 30 GLU H H 9.33 . 1 250 . 30 GLU N N 125.80 . 1 251 . 30 GLU HA H 4.14 . 1 252 . 30 GLU CA C 56.87 . 1 253 . 30 GLU HB2 H 2.11 . 1 254 . 30 GLU CB C 27.39 . 1 255 . 30 GLU HG2 H 2.38 . 1 256 . 30 GLU CG C 34.21 . 1 257 . 31 GLU H H 8.84 . 1 258 . 31 GLU N N 120.10 . 1 259 . 31 GLU HA H 4.06 . 1 260 . 31 GLU CA C 57.92 . 1 261 . 31 GLU HB2 H 2.15 . 1 262 . 31 GLU HB3 H 2.00 . 1 263 . 31 GLU CB C 27.02 . 1 264 . 31 GLU HG2 H 2.39 . 1 265 . 31 GLU CG C 34.53 . 1 266 . 32 GLU H H 7.94 . 1 267 . 32 GLU N N 120.40 . 1 268 . 32 GLU HA H 4.08 . 1 269 . 32 GLU CA C 56.95 . 1 270 . 32 GLU HB2 H 2.14 . 1 271 . 32 GLU CB C 28.21 . 1 272 . 33 LEU H H 7.48 . 1 273 . 33 LEU N N 121.30 . 1 274 . 33 LEU HA H 4.10 . 1 275 . 33 LEU CA C 56.36 . 1 276 . 33 LEU HB2 H 1.75 . 1 277 . 33 LEU HB3 H 1.04 . 1 278 . 33 LEU CB C 38.70 . 1 279 . 33 LEU HG H 1.76 . 1 280 . 33 LEU CG C 24.96 . 1 281 . 33 LEU HD1 H 1.05 . 1 282 . 33 LEU HD2 H 1.06 . 1 283 . 33 LEU CD1 C 24.11 . 1 284 . 33 LEU CD2 C 22.02 . 1 285 . 34 VAL H H 7.78 . 1 286 . 34 VAL N N 120.91 . 1 287 . 34 VAL HA H 3.70 . 1 288 . 34 VAL CA C 64.76 . 1 289 . 34 VAL HB H 2.02 . 1 290 . 34 VAL CB C 29.69 . 1 291 . 34 VAL HG1 H 1.15 . 1 292 . 34 VAL CG1 C 20.78 . 1 293 . 34 VAL HG2 H 1.03 . 1 294 . 34 VAL CG2 C 19.02 . 1 295 . 35 LYS H H 7.78 . 1 296 . 35 LYS N N 120.90 . 1 297 . 35 LYS HA H 4.16 . 1 298 . 35 LYS CA C 57.65 . 1 299 . 35 LYS HB2 H 2.03 . 1 300 . 35 LYS HB3 H 2.03 . 1 301 . 35 LYS CB C 30.39 . 1 302 . 35 LYS HG2 H 1.67 . 1 303 . 35 LYS HG3 H 1.44 . 1 304 . 35 LYS CG C 23.17 . 1 305 . 35 LYS HE2 H 2.97 . 1 306 . 35 LYS HE3 H 2.97 . 1 307 . 35 LYS CE C 40.09 . 1 308 . 36 LEU H H 8.21 . 1 309 . 36 LEU N N 121.40 . 1 310 . 36 LEU HA H 4.22 . 1 311 . 36 LEU CA C 56.24 . 1 312 . 36 LEU HB2 H 2.17 . 1 313 . 36 LEU HB3 H 1.45 . 1 314 . 36 LEU CB C 39.89 . 1 315 . 36 LEU HG H 2.05 . 1 316 . 36 LEU CG C 24.32 . 1 317 . 36 LEU HD1 H 0.88 . 1 318 . 36 LEU HD2 H 0.88 . 1 319 . 36 LEU CD1 C 20.82 . 1 320 . 36 LEU CD2 C 23.81 . 1 321 . 37 VAL H H 8.21 . 1 322 . 37 VAL N N 122.50 . 1 323 . 37 VAL HA H 3.58 . 1 324 . 37 VAL CA C 66.03 . 1 325 . 37 VAL HB H 2.39 . 1 326 . 37 VAL CB C 29.36 . 1 327 . 37 VAL HG1 H 1.25 . 1 328 . 37 VAL CG1 C 22.57 . 1 329 . 37 VAL HG2 H 1.19 . 1 330 . 37 VAL CG2 C 20.74 . 1 331 . 38 THR H H 8.71 . 1 332 . 38 THR N N 118.00 . 1 333 . 38 THR HA H 4.23 . 1 334 . 38 THR CA C 64.87 . 1 335 . 38 THR HB H 4.39 . 1 336 . 38 THR CB C 67.15 . 1 337 . 38 THR HG2 H 1.42 . 1 338 . 38 THR CG2 C 19.81 . 1 339 . 39 HIS H H 8.30 . 1 340 . 39 HIS N N 122.40 . 1 341 . 39 HIS HA H 4.62 . 1 342 . 39 HIS CA C 57.96 . 1 343 . 39 HIS HB2 H 3.69 . 1 344 . 39 HIS HB3 H 3.33 . 1 345 . 39 HIS CB C 26.70 . 1 346 . 39 HIS HD2 H 6.87 . 1 347 . 39 HIS HE1 H 8.61 . 1 348 . 40 PHE H H 9.11 . 1 349 . 40 PHE N N 121.00 . 1 350 . 40 PHE HA H 3.90 . 1 351 . 40 PHE CA C 60.58 . 1 352 . 40 PHE HB2 H 3.82 . 1 353 . 40 PHE HB3 H 2.95 . 1 354 . 40 PHE CB C 36.86 . 1 355 . 41 GLU H H 8.76 . 1 356 . 41 GLU N N 122.40 . 1 357 . 41 GLU HA H 3.65 . 1 358 . 41 GLU CA C 58.95 . 1 359 . 41 GLU HB2 H 2.69 . 1 360 . 41 GLU CB C 27.47 . 1 361 . 41 GLU HG2 H 3.05 . 1 362 . 41 GLU HG3 H 2.09 . 1 363 . 41 GLU CG C 35.38 . 1 364 . 42 GLU H H 8.54 . 1 365 . 42 GLU N N 120.90 . 1 366 . 42 GLU HA H 4.04 . 1 367 . 42 GLU CA C 56.91 . 1 368 . 42 GLU HB2 H 2.28 . 1 369 . 42 GLU CB C 27.97 . 1 370 . 42 GLU HG2 H 2.63 . 1 371 . 42 GLU CG C 34.32 . 1 372 . 43 MET H H 8.86 . 1 373 . 43 MET N N 115.10 . 1 374 . 43 MET HA H 4.51 . 1 375 . 43 MET CA C 53.93 . 1 376 . 43 MET HB2 H 2.08 . 1 377 . 43 MET HB3 H 1.46 . 1 378 . 43 MET CB C 34.26 . 1 379 . 43 MET HG2 H 2.17 . 1 380 . 43 MET HG3 H 1.86 . 1 381 . 43 MET CG C 31.24 . 1 382 . 43 MET HE H 1.97 . 1 383 . 43 MET CE C 18.80 . 1 384 . 44 THR H H 7.88 . 1 385 . 44 THR N N 106.10 . 1 386 . 44 THR HA H 3.54 . 1 387 . 44 THR CA C 63.63 . 1 388 . 44 THR HB H 3.80 . 1 389 . 44 THR CB C 67.57 . 1 390 . 44 THR HG2 H 0.77 . 1 391 . 44 THR CG2 C 20.86 . 1 392 . 45 GLU H H 7.36 . 1 393 . 45 GLU N N 111.90 . 1 394 . 45 GLU HA H 3.89 . 1 395 . 45 GLU CA C 55.56 . 1 396 . 45 GLU HB2 H 2.47 . 1 397 . 45 GLU CB C 27.03 . 1 398 . 45 GLU HG2 H 2.25 . 1 399 . 45 GLU HG3 H 2.19 . 1 400 . 45 GLU CG C 35.80 . 1 401 . 46 HIS H H 7.47 . 1 402 . 46 HIS N N 120.40 . 1 403 . 46 HIS HA H 2.99 . 1 404 . 46 HIS CA C 53.78 . 1 405 . 46 HIS HB2 H 2.66 . 1 406 . 46 HIS CB C 29.58 . 1 407 . 46 HIS HD2 H 6.18 . 1 408 . 46 HIS HE1 H 7.60 . 1 409 . 47 PRO HA H 4.24 . 1 410 . 47 PRO CA C 62.83 . 1 411 . 47 PRO HB2 H 2.28 . 1 412 . 47 PRO HB3 H 1.90 . 1 413 . 47 PRO CB C 29.99 . 1 414 . 47 PRO HG2 H 1.83 . 1 415 . 47 PRO HG3 H 1.66 . 1 416 . 47 PRO CG C 24.78 . 1 417 . 47 PRO HD2 H 2.70 . 1 418 . 47 PRO HD3 H 1.12 . 1 419 . 47 PRO CD C 48.34 . 1 420 . 48 SER H H 11.07 . 1 421 . 48 SER N N 118.70 . 1 422 . 48 SER HA H 4.59 . 1 423 . 48 SER CA C 58.11 . 1 424 . 48 SER HB2 H 3.93 . 1 425 . 48 SER HB3 H 3.88 . 1 426 . 48 SER CB C 61.33 . 1 427 . 49 GLY H H 8.19 . 1 428 . 49 GLY N N 109.40 . 1 429 . 49 GLY HA2 H 4.14 . 1 430 . 49 GLY HA3 H 3.87 . 1 431 . 49 GLY CA C 45.14 . 1 432 . 50 SER H H 10.14 . 1 433 . 50 SER N N 121.05 . 1 434 . 50 SER HA H 4.08 . 1 435 . 50 SER CA C 58.69 . 1 436 . 50 SER HB2 H 4.32 . 1 437 . 50 SER HB3 H 4.06 . 1 438 . 50 SER CB C 61.10 . 1 439 . 51 ASP H H 8.78 . 1 440 . 51 ASP N N 127.40 . 1 441 . 51 ASP HA H 4.63 . 1 442 . 51 ASP CA C 55.45 . 1 443 . 51 ASP HB2 H 3.22 . 1 444 . 51 ASP HB3 H 2.87 . 1 445 . 51 ASP CB C 37.17 . 1 446 . 52 LEU H H 7.41 . 1 447 . 52 LEU N N 115.50 . 1 448 . 52 LEU HA H 3.90 . 1 449 . 52 LEU CA C 55.42 . 1 450 . 52 LEU HB2 H 1.65 . 1 451 . 52 LEU HB3 H 1.38 . 1 452 . 52 LEU CB C 41.51 . 1 453 . 52 LEU HG H 1.51 . 1 454 . 52 LEU CG C 24.73 . 1 455 . 52 LEU HD1 H 0.51 . 1 456 . 52 LEU HD2 H 0.37 . 1 457 . 52 LEU CD1 C 20.43 . 1 458 . 52 LEU CD2 C 22.97 . 1 459 . 53 ILE H H 6.89 . 1 460 . 53 ILE N N 112.00 . 1 461 . 53 ILE HA H 3.54 . 1 462 . 53 ILE CA C 60.27 . 1 463 . 53 ILE HB H 1.10 . 1 464 . 53 ILE CB C 37.74 . 1 465 . 53 ILE HG12 H 0.88 . 1 466 . 53 ILE HG13 H 0.35 . 1 467 . 53 ILE CG1 C 26.02 . 1 468 . 53 ILE HG2 H -0.07 . 1 469 . 53 ILE CG2 C 14.35 . 1 470 . 53 ILE HD1 H -0.15 . 1 471 . 53 ILE CD1 C 10.90 . 1 472 . 54 TYR H H 7.39 . 1 473 . 54 TYR N N 114.70 . 1 474 . 54 TYR HA H 4.20 . 1 475 . 54 TYR CA C 58.50 . 1 476 . 54 TYR HB2 H 2.69 . 1 477 . 54 TYR HB3 H 2.56 . 1 478 . 54 TYR CB C 38.05 . 1 479 . 54 TYR HD1 H 7.14 . 1 480 . 54 TYR HD2 H 7.14 . 1 481 . 54 TYR HE1 H 6.71 . 1 482 . 54 TYR HE2 H 6.71 . 1 483 . 55 TYR H H 8.81 . 1 484 . 55 TYR N N 118.30 . 1 485 . 55 TYR HA H 4.98 . 1 486 . 55 TYR CA C 53.65 . 1 487 . 55 TYR HB2 H 3.20 . 1 488 . 55 TYR HB3 H 2.56 . 1 489 . 55 TYR CB C 37.54 . 1 490 . 55 TYR HD1 H 7.20 . 1 491 . 55 TYR HD2 H 7.20 . 1 492 . 55 TYR HE1 H 6.82 . 1 493 . 55 TYR HE2 H 6.82 . 1 494 . 56 PRO HA H 4.37 . 1 495 . 56 PRO CA C 60.98 . 1 496 . 56 PRO HB2 H 2.25 . 1 497 . 56 PRO CB C 29.41 . 1 498 . 56 PRO HG2 H 1.96 . 1 499 . 56 PRO HG3 H 1.93 . 1 500 . 56 PRO CG C 25.26 . 1 501 . 56 PRO HD2 H 3.42 . 1 502 . 56 PRO HD3 H 3.15 . 1 503 . 56 PRO CD C 48.27 . 1 504 . 57 LYS H H 8.86 . 1 505 . 57 LYS N N 123.40 . 1 506 . 57 LYS HA H 4.31 . 1 507 . 57 LYS CA C 53.33 . 1 508 . 57 LYS HB2 H 1.81 . 1 509 . 57 LYS CB C 30.76 . 1 510 . 57 LYS HG2 H 1.57 . 1 511 . 57 LYS CG C 22.67 . 1 512 . 57 LYS HD2 H 1.75 . 1 513 . 57 LYS CD C 26.68 . 1 514 . 57 LYS HE2 H 3.11 . 1 515 . 57 LYS HE3 H 3.11 . 1 516 . 57 LYS CE C 40.26 . 1 517 . 58 GLU H H 8.71 . 1 518 . 58 GLU N N 124.20 . 1 519 . 58 GLU HA H 4.08 . 1 520 . 58 GLU CA C 56.35 . 1 521 . 58 GLU HB2 H 2.06 . 1 522 . 58 GLU HB3 H 1.98 . 1 523 . 58 GLU CB C 27.15 . 1 524 . 58 GLU HG2 H 2.31 . 1 525 . 58 GLU CG C 33.97 . 1 526 . 59 GLY H H 8.94 . 1 527 . 59 GLY N N 115.10 . 1 528 . 59 GLY HA2 H 4.31 . 1 529 . 59 GLY HA3 H 3.75 . 1 530 . 59 GLY CA C 43.14 . 1 531 . 60 ASP H H 8.04 . 1 532 . 60 ASP N N 122.50 . 1 533 . 60 ASP HA H 4.71 . 1 534 . 60 ASP CA C 52.12 . 1 535 . 60 ASP HB2 H 2.89 . 1 536 . 60 ASP HB3 H 2.62 . 1 537 . 60 ASP CB C 38.60 . 1 538 . 61 ASP H H 8.69 . 1 539 . 61 ASP N N 122.00 . 1 540 . 61 ASP HA H 4.63 . 1 541 . 61 ASP CA C 51.64 . 1 542 . 62 ASP H H 8.41 . 1 543 . 62 ASP N N 126.10 . 1 544 . 62 ASP HA H 4.48 . 1 545 . 62 ASP CA C 50.92 . 1 546 . 62 ASP HB2 H 2.98 . 1 547 . 62 ASP HB3 H 2.37 . 1 548 . 62 ASP CB C 37.97 . 1 549 . 63 SER H H 8.16 . 1 550 . 63 SER N N 116.30 . 1 551 . 63 SER HA H 4.63 . 1 552 . 63 SER CA C 55.45 . 1 553 . 63 SER HB2 H 4.23 . 1 554 . 63 SER HB3 H 4.12 . 1 555 . 63 SER CB C 61.10 . 1 556 . 64 PRO HA H 4.09 . 1 557 . 64 PRO CA C 64.69 . 1 558 . 64 PRO HB2 H 2.07 . 1 559 . 64 PRO HB3 H 1.96 . 1 560 . 64 PRO CB C 30.35 . 1 561 . 64 PRO HG2 H 2.08 . 1 562 . 64 PRO CG C 26.54 . 1 563 . 64 PRO HD2 H 3.93 . 1 564 . 64 PRO HD3 H 3.89 . 1 565 . 64 PRO CD C 47.20 . 1 566 . 65 SER H H 8.31 . 1 567 . 65 SER N N 110.50 . 1 568 . 65 SER HA H 4.03 . 1 569 . 65 SER CA C 59.73 . 1 570 . 65 SER HB2 H 3.91 . 1 571 . 65 SER HB3 H 3.84 . 1 572 . 65 SER CB C 60.42 . 1 573 . 66 GLY H H 8.11 . 1 574 . 66 GLY N N 115.60 . 1 575 . 66 GLY HA2 H 3.90 . 1 576 . 66 GLY HA3 H 3.82 . 1 577 . 66 GLY CA C 45.04 . 1 578 . 67 ILE H H 8.82 . 1 579 . 67 ILE N N 125.90 . 1 580 . 67 ILE HA H 3.90 . 1 581 . 67 ILE CA C 63.47 . 1 582 . 67 ILE HB H 1.89 . 1 583 . 67 ILE CB C 36.37 . 1 584 . 67 ILE HG12 H 1.73 . 1 585 . 67 ILE HG13 H 1.73 . 1 586 . 67 ILE CG1 C 27.26 . 1 587 . 67 ILE HG2 H 0.87 . 1 588 . 67 ILE CG2 C 15.60 . 1 589 . 67 ILE HD1 H 0.46 . 1 590 . 67 ILE CD1 C 13.16 . 1 591 . 68 VAL H H 8.40 . 1 592 . 68 VAL N N 119.92 . 1 593 . 68 VAL HA H 3.65 . 1 594 . 68 VAL CA C 66.67 . 1 595 . 68 VAL HB H 2.41 . 1 596 . 68 VAL CB C 29.19 . 1 597 . 68 VAL HG1 H 1.27 . 1 598 . 68 VAL CG1 C 23.16 . 1 599 . 68 VAL HG2 H 1.23 . 1 600 . 68 VAL CG2 C 20.28 . 1 601 . 69 ASN H H 8.40 . 1 602 . 69 ASN N N 119.40 . 1 603 . 69 ASN HA H 4.61 . 1 604 . 69 ASN CA C 55.21 . 1 605 . 69 ASN HB2 H 3.07 . 1 606 . 69 ASN HB3 H 3.01 . 1 607 . 69 ASN CB C 36.29 . 1 608 . 69 ASN HD21 H 7.90 . 1 609 . 69 ASN HD22 H 7.03 . 1 610 . 69 ASN ND2 N 114.40 . 1 611 . 70 THR H H 8.87 . 1 612 . 70 THR N N 121.10 . 1 613 . 70 THR HA H 4.06 . 1 614 . 70 THR CA C 65.61 . 1 615 . 70 THR HB H 4.54 . 1 616 . 70 THR CB C 66.27 . 1 617 . 70 THR HG2 H 1.24 . 1 618 . 70 THR CG2 C 20.47 . 1 619 . 71 VAL H H 8.61 . 1 620 . 71 VAL N N 122.60 . 1 621 . 71 VAL HA H 3.66 . 1 622 . 71 VAL CA C 66.24 . 1 623 . 71 VAL HB H 2.55 . 1 624 . 71 VAL CB C 29.99 . 1 625 . 71 VAL HG1 H 1.14 . 1 626 . 71 VAL CG1 C 21.20 . 1 627 . 71 VAL HG2 H 0.81 . 1 628 . 71 VAL CG2 C 18.84 . 1 629 . 72 LYS H H 9.27 . 1 630 . 72 LYS N N 121.40 . 1 631 . 72 LYS HA H 3.98 . 1 632 . 72 LYS CA C 57.92 . 1 633 . 72 LYS HB2 H 2.19 . 1 634 . 72 LYS CB C 31.49 . 1 635 . 72 LYS HG2 H 1.78 . 1 636 . 72 LYS HG3 H 1.63 . 1 637 . 72 LYS CG C 22.94 . 1 638 . 72 LYS HD2 H 1.93 . 1 639 . 72 LYS CD C 28.25 . 1 640 . 72 LYS HE2 H 3.16 . 1 641 . 72 LYS HE3 H 3.16 . 1 642 . 72 LYS CE C 40.01 . 1 643 . 73 GLN H H 8.80 . 1 644 . 73 GLN N N 118.80 . 1 645 . 73 GLN HA H 4.23 . 1 646 . 73 GLN CA C 56.59 . 1 647 . 73 GLN HB2 H 2.30 . 1 648 . 73 GLN HB3 H 2.30 . 1 649 . 73 GLN CB C 26.30 . 1 650 . 73 GLN HG2 H 2.72 . 1 651 . 73 GLN HG3 H 2.59 . 1 652 . 73 GLN CG C 31.84 . 1 653 . 73 GLN HE21 H 7.68 . 1 654 . 73 GLN HE22 H 7.03 . 1 655 . 73 GLN NE2 N 92.49 . 1 656 . 74 TRP H H 8.57 . 1 657 . 74 TRP N N 122.50 . 1 658 . 74 TRP HA H 4.26 . 1 659 . 74 TRP CA C 61.10 . 1 660 . 74 TRP HB2 H 3.68 . 1 661 . 74 TRP HB3 H 3.54 . 1 662 . 74 TRP CB C 26.95 . 1 663 . 74 TRP HD1 H 7.29 . 1 664 . 74 TRP HE1 H 10.21 . 1 665 . 74 TRP HE3 H 7.38 . 1 666 . 74 TRP HZ2 H 7.32 . 1 667 . 74 TRP HZ3 H 7.02 . 1 668 . 74 TRP HH2 H 7.02 . 1 669 . 75 ARG H H 9.08 . 1 670 . 75 ARG N N 119.60 . 1 671 . 75 ARG HA H 3.30 . 1 672 . 75 ARG CA C 59.17 . 1 673 . 75 ARG HB2 H 2.37 . 1 674 . 75 ARG HB3 H 1.82 . 1 675 . 75 ARG CB C 27.83 . 1 676 . 75 ARG HD2 H 3.32 . 1 677 . 75 ARG HD3 H 3.10 . 1 678 . 75 ARG CD C 40.09 . 1 679 . 75 ARG HE H 7.51 . 1 680 . 75 ARG HH21 H 6.85 . 1 681 . 75 ARG HH22 H 6.85 . 1 682 . 76 ALA H H 7.79 . 1 683 . 76 ALA N N 121.10 . 1 684 . 76 ALA HA H 4.20 . 1 685 . 76 ALA CA C 53.11 . 1 686 . 76 ALA HB H 1.50 . 1 687 . 76 ALA CB C 15.90 . 1 688 . 77 ALA H H 8.10 . 1 689 . 77 ALA N N 120.50 . 1 690 . 77 ALA HA H 4.17 . 1 691 . 77 ALA CA C 51.90 . 1 692 . 77 ALA HB H 1.43 . 1 693 . 77 ALA CB C 16.32 . 1 694 . 78 ASN H H 7.13 . 1 695 . 78 ASN N N 114.30 . 1 696 . 78 ASN HA H 4.56 . 1 697 . 78 ASN CA C 51.22 . 1 698 . 78 ASN HB2 H 2.33 . 1 699 . 78 ASN HB3 H 1.30 . 1 700 . 78 ASN CB C 36.98 . 1 701 . 78 ASN HD21 H 6.53 . 1 702 . 78 ASN HD22 H 6.46 . 1 703 . 78 ASN ND2 N 116.40 . 1 704 . 79 GLY H H 7.66 . 1 705 . 79 GLY N N 108.50 . 1 706 . 79 GLY HA2 H 3.87 . 1 707 . 79 GLY HA3 H 3.87 . 1 708 . 79 GLY CA C 45.03 . 1 709 . 80 LYS H H 8.11 . 1 710 . 80 LYS N N 118.80 . 1 711 . 80 LYS HA H 4.57 . 1 712 . 80 LYS CA C 52.08 . 1 713 . 80 LYS HB2 H 2.00 . 1 714 . 80 LYS HB3 H 1.39 . 1 715 . 80 LYS CB C 31.67 . 1 716 . 80 LYS HG2 H 1.31 . 1 717 . 80 LYS HG3 H 1.13 . 1 718 . 80 LYS CG C 23.19 . 1 719 . 80 LYS HD2 H 1.67 . 1 720 . 80 LYS HD3 H 1.47 . 1 721 . 80 LYS CD C 26.88 . 1 722 . 80 LYS HE2 H 3.17 . 1 723 . 80 LYS HE3 H 2.87 . 1 724 . 80 LYS CE C 40.47 . 1 725 . 81 SER H H 8.73 . 1 726 . 81 SER N N 118.40 . 1 727 . 81 SER HB2 H 3.97 . 1 728 . 81 SER CB C 61.99 . 1 729 . 82 GLY H H 8.40 . 1 730 . 82 GLY N N 119.90 . 1 731 . 82 GLY HA2 H 4.27 . 1 732 . 82 GLY HA3 H 3.58 . 1 733 . 82 GLY CA C 41.13 . 1 734 . 83 PHE H H 7.88 . 1 735 . 83 PHE N N 116.80 . 1 736 . 83 PHE HA H 4.69 . 1 737 . 83 PHE CA C 56.58 . 1 738 . 83 PHE HB2 H 3.70 . 1 739 . 83 PHE HB3 H 2.69 . 1 740 . 83 PHE CB C 37.84 . 1 741 . 84 LYS H H 8.66 . 1 742 . 84 LYS N N 124.60 . 1 743 . 84 LYS HA H 4.25 . 1 744 . 84 LYS CA C 55.19 . 1 745 . 84 LYS HB2 H 1.49 . 1 746 . 84 LYS CB C 30.66 . 1 747 . 84 LYS HG2 H 1.49 . 1 748 . 84 LYS CG C 22.43 . 1 749 . 84 LYS HE2 H 3.02 . 1 750 . 84 LYS HE3 H 3.02 . 1 751 . 84 LYS CE C 40.27 . 1 752 . 85 GLN H H 8.80 . 1 753 . 85 GLN N N 126.20 . 1 754 . 85 GLN HA H 4.36 . 1 755 . 85 GLN CA C 54.33 . 1 756 . 85 GLN HB2 H 2.11 . 1 757 . 85 GLN HB3 H 2.22 . 1 758 . 85 GLN HG2 H 2.53 . 1 759 . 86 GLY H H 8.17 . 1 760 . 86 GLY N N 117.50 . 1 761 . 86 GLY HA2 H 3.87 . 1 762 . 86 GLY HA3 H 3.87 . 1 763 . 86 GLY CA C 44.06 . 1 stop_ save_