data_4045 #Corrected using PDB structure: 1YUA_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 6 A HA 4.62 3.71 # 10 E HA 4.36 5.73 # 38 L HA 5.15 4.33 # 39 A HA 5.48 4.15 # 43 F HA 4.99 3.92 # 68 L HA 4.80 3.86 # 76 Q HA 3.66 4.51 # 78 D HA 3.06 4.28 # 97 V HA 5.32 4.55 # 99 S HA 5.32 4.59 #105 A HA 4.53 3.71 #107 G HA 4.13 5.04 #112 Y HA 4.31 3.39 #115 G HA 3.51 4.38 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 78 D CB 39.08 44.16 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 10 E N 122.25 133.03 #107 G N 110.25 126.38 #114 D N 127.35 113.27 #115 G N 101.15 115.10 #118 V N 124.65 113.70 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 13 V H 8.30 5.45 # 22 K H 9.18 6.86 # 39 A H 8.96 6.88 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.02 0.04 0.18 N/A 0.25 -0.16 # #bmr4045.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4045.str file): #HA CA CB CO N HN #N/A +0.11 +0.11 N/A +0.25 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.16 +/-0.17 N/A +/-0.46 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.637 0.952 0.991 N/A 0.661 0.408 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.176 0.884 0.897 N/A 2.338 0.422 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the C-Terminal Single-Stranded DNA-Binding Domain of Escherichia Coli Topoisomerase I ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yu Liping . . 2 Zhu Chang-Xi . . 3 Tse-Dinh Yuk-Ching . . 4 Fesik Stephen W. . stop_ _BMRB_accession_number 4045 _BMRB_flat_file_name bmr4045.str _Entry_type reformat _Submission_date 1997-07-17 _Accession_date 1997-07-17 _Entry_origination BMRB _NMR_STAR_version 2.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 741 '13C chemical shifts' 441 '15N chemical shifts' 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-2-15 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Yu, L., Zhu, C-X., Tse-Dinh, Y-C., and Fesik, S. W., "Solution Structure of the C-Terminal Single-Stranded DNA-Binding Domain of Escherichia coli Topoisomerase I," Biochemistry 34, 7622-7628 (1995). ; _Citation_title ; Solution Structure of the C-Terminal Single-Stranded DNA-Binding Domain of Escherichia coli Topoisomerase I ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 95298771 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yu Liping . . 2 Zhu Chang-Xi . . 3 Tse-Dinh Yuk-Ching . . 4 Fesik Stephen W. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 34 _Journal_issue 23 _Page_first 7622 _Page_last 7628 _Year 1995 loop_ _Keyword NMR 'nuclear magnetic resonance' protein 'resonance assignments' 'DNA Topoisomerase I' stop_ save_ ################################## # Molecular system description # ################################## save_DNA_Topoisomerase_I _Saveframe_category molecular_system _Mol_system_name 'DNA Topoisomerase I' _Abbreviation_common 'DNA TopoI' loop_ _Mol_system_component_name _Mol_label 'DNA Topoisomerase I' $DNA_TopoI stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1yua 'DNA TOPOISOMERASE I' ? stop_ save_ ######################## # Monomeric polymers # ######################## save_DNA_TopoI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA Topoisomerase I' _Name_variant . _Abbreviation_common 'DNA TopoI' _Enzyme_commission_number 5.99.1.2 ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MNGEVAPPKEDPVPLPELPC EKSDAYFVLRDGAAGVFLAA NTFPKSRETRAPLVEELYRF RDRLPEKLRYLADAPQQDPE GNKTMVRFSRKTKQQYVSSE KDGKATGWSAFYVDGKWVEG KK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASN 3 3 GLY 4 4 GLU 5 5 VAL 6 6 ALA 7 7 PRO 8 8 PRO 9 9 LYS 10 10 GLU 11 11 ASP 12 12 PRO 13 13 VAL 14 14 PRO 15 15 LEU 16 16 PRO 17 17 GLU 18 18 LEU 19 19 PRO 20 20 CYS 21 21 GLU 22 22 LYS 23 23 SER 24 24 ASP 25 25 ALA 26 26 TYR 27 27 PHE 28 28 VAL 29 29 LEU 30 30 ARG 31 31 ASP 32 32 GLY 33 33 ALA 34 34 ALA 35 35 GLY 36 36 VAL 37 37 PHE 38 38 LEU 39 39 ALA 40 40 ALA 41 41 ASN 42 42 THR 43 43 PHE 44 44 PRO 45 45 LYS 46 46 SER 47 47 ARG 48 48 GLU 49 49 THR 50 50 ARG 51 51 ALA 52 52 PRO 53 53 LEU 54 54 VAL 55 55 GLU 56 56 GLU 57 57 LEU 58 58 TYR 59 59 ARG 60 60 PHE 61 61 ARG 62 62 ASP 63 63 ARG 64 64 LEU 65 65 PRO 66 66 GLU 67 67 LYS 68 68 LEU 69 69 ARG 70 70 TYR 71 71 LEU 72 72 ALA 73 73 ASP 74 74 ALA 75 75 PRO 76 76 GLN 77 77 GLN 78 78 ASP 79 79 PRO 80 80 GLU 81 81 GLY 82 82 ASN 83 83 LYS 84 84 THR 85 85 MET 86 86 VAL 87 87 ARG 88 88 PHE 89 89 SER 90 90 ARG 91 91 LYS 92 92 THR 93 93 LYS 94 94 GLN 95 95 GLN 96 96 TYR 97 97 VAL 98 98 SER 99 99 SER 100 100 GLU 101 101 LYS 102 102 ASP 103 103 GLY 104 104 LYS 105 105 ALA 106 106 THR 107 107 GLY 108 108 TRP 109 109 SER 110 110 ALA 111 111 PHE 112 112 TYR 113 113 VAL 114 114 ASP 115 115 GLY 116 116 LYS 117 117 TRP 118 118 VAL 119 119 GLU 120 120 GLY 121 121 LYS 122 122 LYS stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 PDB 1YUA "C-Terminal Domain Of Escherichia ColiTopoisomerase I" 100.00 122 100 100 3e-67 DBJ BAA14811.1 "DNA topoisomerase I (EC 5.99.1.2)(w-protein) (Relaxing enzyme) (Untwisting enzyme)(Swivelase). [Escherichia coli]" 14.10 865 100 100 1e-66 DBJ BAA14826.1 "DNA topoisomerase I (EC 5.99.1.2)(w-protein) (Relaxing enzyme) (Untwisting enzyme)(Swivelase). [Escherichia coli]" 14.10 865 100 100 1e-66 DBJ BAB35269.1 "DNA topoisomerase type I omega protein[Escherichia coli O157:H7]" 14.10 865 100 100 1e-66 EMBL CAA28164.1 "unnamed protein product [Escherichiacoli]" 14.10 865 100 100 1e-66 GenBank AAC74356.1 "DNA topoisomerase type I, omega protein[Escherichia coli K12]" 14.10 865 100 100 1e-66 GenBank AAG56541.1 "DNA topoisomerase type I, omega protein[Escherichia coli O157:H7 EDL933]" 14.10 865 100 100 1e-66 GenBank AAP16774.1 "DNA topoisomerase type I, omega protein[Shigella flexneri 2a str. 2457T]" 14.10 865 100 100 1e-66 GenBank AAN80207.1 "DNA topoisomerase I [Escherichia coliCFT073]" 13.88 879 100 100 1e-66 GenBank AAN42888.1 "DNA topoisomerase type I, omega protein[Shigella flexneri 2a str. 301]" 13.88 879 99 100 3e-66 PIR A85760 "DNA topoisomerase type I, omega protein[imported] - Escherichia coli (strain O157:H7, substrainEDL933)" 14.10 865 100 100 1e-66 PIR F90859 "DNA topoisomerase type I omega protein[imported] - Escherichia coli (strain O157:H7, substrainRIMD 0509952)" 14.10 865 100 100 1e-66 PIR ISECTP "DNA topoisomerase (EC 5.99.1.2) -Escherichia coli (strain K-12)" 14.10 865 100 100 1e-66 REF NP_287925.1 "DNA topoisomerase type I, omegaprotein [Escherichia coli O157:H7 EDL933]" 14.10 865 100 100 1e-66 REF NP_309873.1 "DNA topoisomerase type I omega protein[Escherichia coli O157:H7]" 14.10 865 100 100 1e-66 REF NP_415790.1 "DNA topoisomerase type I, omegaprotein [Escherichia coli K12]" 14.10 865 100 100 1e-66 REF NP_836967.1 "DNA topoisomerase type I, omegaprotein [Shigella flexneri 2a str. 2457T]" 14.10 865 100 100 1e-66 REF NP_753645.1 "DNA topoisomerase I [Escherichia coliCFT073]" 13.88 879 100 100 1e-66 SWISS-PROT P06612 "TOP1_ECOLI DNA topoisomerase I (Omega-protein)(Relaxing enzyme) (Untwisting enzyme) (Swivelase)" 14.10 865 100 100 1e-66 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DNA_TopoI '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 _Details $DNA_TopoI 'recombinant technology' 'E. coli' Escherichia coli ; The 14 K fragment of E. coli DNA topoisomeraseI was cloned, expressed and purified as described in: Zhu, C.X., Samuel, M., Pound, A., Ahumada, A., and Tse-Dinh, Y.C., Biochem. Mol. Biol. Int. 35, 375-385 (1995). ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DNA_Topoisomerase_I 3 mM '[U-15N]' dithiothreitol-d10 5 mM . KH2PO4 200 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DNA_Topoisomerase_I 3 mM '[U-13C; U-15N]' dithiothreitol-d10 5 mM . KH2PO4 200 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type . H 1 . ppm . . . . C 13 . ppm . . . . N 15 . ppm . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name 'DNA Topoisomerase I' loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET HA H 4.23 . 1 2 1 MET HB2 H 2.10 . 1 3 1 MET HB3 H 2.10 . 1 4 1 MET HG2 H 2.59 . 1 5 1 MET HG3 H 2.59 . 1 6 1 MET HE H 2.05 . 1 7 1 MET CA C 56.21 . 1 8 1 MET CB C 34.91 . 1 9 1 MET CG C 30.81 . 1 10 1 MET CE C 16.81 . 1 11 2 ASN HA H 4.02 . 1 12 2 ASN HB2 H 2.89 . 2 13 2 ASN HB3 H 3.00 . 2 14 2 ASN CA C 53.81 . 1 15 2 ASN CB C 37.91 . 1 16 3 GLY H H 8.34 . 1 17 3 GLY HA2 H 3.93 . 1 18 3 GLY HA3 H 3.93 . 1 19 3 GLY CA C 45.41 . 1 20 3 GLY N N 114.45 . 1 21 4 GLU H H 8.44 . 1 22 4 GLU HA H 4.29 . 1 23 4 GLU HB2 H 1.93 . 2 24 4 GLU HB3 H 2.01 . 2 25 4 GLU HG2 H 2.24 . 1 26 4 GLU HG3 H 2.24 . 1 27 4 GLU CA C 56.81 . 1 28 4 GLU CB C 30.21 . 1 29 4 GLU CG C 36.31 . 1 30 4 GLU N N 121.15 . 1 31 5 VAL H H 8.16 . 1 32 5 VAL HA H 4.09 . 1 33 5 VAL HB H 2.03 . 1 34 5 VAL HG1 H 0.91 . 1 35 5 VAL HG2 H 0.91 . 1 36 5 VAL CA C 63.11 . 1 37 5 VAL CB C 32.71 . 1 38 5 VAL CG1 C 20.71 . 1 39 5 VAL CG2 C 20.71 . 1 40 5 VAL N N 121.65 . 1 41 6 ALA H H 8.31 . 1 42 6 ALA HA H 4.60 . 1 43 6 ALA HB H 1.36 . 1 44 6 ALA CA C 50.41 . 1 45 6 ALA CB C 18.21 . 1 46 6 ALA N N 129.65 . 1 47 7 PRO HA H 4.69 . 1 48 7 PRO HB2 H 1.89 . 2 49 7 PRO HB3 H 2.35 . 2 50 7 PRO HG2 H 2.03 . 1 51 7 PRO HG3 H 2.03 . 1 52 7 PRO HD2 H 3.62 . 2 53 7 PRO HD3 H 3.82 . 2 54 7 PRO CA C 61.21 . 1 55 7 PRO CB C 30.81 . 1 56 7 PRO CG C 27.21 . 1 57 7 PRO CD C 50.21 . 1 58 8 PRO HA H 4.41 . 1 59 8 PRO HB2 H 1.90 . 2 60 8 PRO HB3 H 2.29 . 2 61 8 PRO HG2 H 2.01 . 1 62 8 PRO HG3 H 2.01 . 1 63 8 PRO HD2 H 3.62 . 2 64 8 PRO HD3 H 3.81 . 2 65 8 PRO CA C 63.11 . 1 66 8 PRO CB C 32.21 . 1 67 8 PRO CG C 27.21 . 1 68 8 PRO CD C 50.21 . 1 69 9 LYS H H 8.34 . 1 70 9 LYS HA H 4.27 . 1 71 9 LYS HB2 H 1.75 . 2 72 9 LYS HB3 H 1.83 . 2 73 9 LYS HG2 H 1.43 . 1 74 9 LYS HG3 H 1.43 . 1 75 9 LYS HD2 H 1.66 . 1 76 9 LYS HD3 H 1.66 . 1 77 9 LYS HE2 H 2.97 . 1 78 9 LYS HE3 H 2.97 . 1 79 9 LYS CA C 56.31 . 1 80 9 LYS CB C 33.01 . 1 81 9 LYS CG C 24.51 . 1 82 9 LYS CD C 28.91 . 1 83 9 LYS CE C 41.71 . 1 84 9 LYS N N 121.85 . 1 85 10 GLU H H 8.59 . 1 86 10 GLU HA H 4.34 . 1 87 10 GLU HB2 H 1.83 . 2 88 10 GLU HB3 H 2.02 . 2 89 10 GLU HG2 H 2.24 . 1 90 10 GLU HG3 H 2.24 . 1 91 10 GLU CA C 55.81 . 1 92 10 GLU CB C 30.51 . 1 93 10 GLU CG C 36.31 . 1 94 10 GLU N N 122.25 . 1 95 11 ASP H H 8.47 . 1 96 11 ASP HA H 4.87 . 1 97 11 ASP HB2 H 2.48 . 2 98 11 ASP HB3 H 2.70 . 2 99 11 ASP CA C 53.01 . 1 100 11 ASP CB C 40.11 . 1 101 11 ASP N N 123.55 . 1 102 12 PRO HA H 4.55 . 1 103 12 PRO HB2 H 1.62 . 2 104 12 PRO HB3 H 1.98 . 2 105 12 PRO HG2 H 1.90 . 2 106 12 PRO HG3 H 1.98 . 2 107 12 PRO HD2 H 3.66 . 2 108 12 PRO HD3 H 3.81 . 2 109 12 PRO CA C 62.51 . 1 110 12 PRO CB C 32.71 . 1 111 12 PRO CG C 27.21 . 1 112 12 PRO CD C 50.51 . 1 113 13 VAL H H 8.46 . 1 114 13 VAL HA H 4.52 . 1 115 13 VAL HB H 2.12 . 1 116 13 VAL HG1 H 0.81 . 2 117 13 VAL HG2 H 1.02 . 2 118 13 VAL CA C 59.51 . 1 119 13 VAL CB C 33.81 . 1 120 13 VAL CG1 C 20.91 . 2 121 13 VAL CG2 C 20.71 . 2 122 13 VAL N N 122.15 . 1 123 14 PRO HA H 4.50 . 1 124 14 PRO HB2 H 2.01 . 2 125 14 PRO HB3 H 2.49 . 2 126 14 PRO HG2 H 2.01 . 2 127 14 PRO HG3 H 2.26 . 2 128 14 PRO HD2 H 3.81 . 2 129 14 PRO HD3 H 3.98 . 2 130 14 PRO CA C 63.91 . 1 131 14 PRO CB C 32.71 . 1 132 14 PRO CG C 27.51 . 1 133 14 PRO CD C 51.01 . 1 134 15 LEU H H 8.44 . 1 135 15 LEU HA H 4.36 . 1 136 15 LEU HB2 H 0.60 . 2 137 15 LEU HB3 H 1.96 . 2 138 15 LEU HG H 1.52 . 1 139 15 LEU HD1 H 0.19 . 2 140 15 LEU HD2 H 0.55 . 2 141 15 LEU CA C 52.01 . 1 142 15 LEU CB C 41.21 . 1 143 15 LEU CG C 24.81 . 1 144 15 LEU CD1 C 23.41 . 2 145 15 LEU CD2 C 27.01 . 2 146 15 LEU N N 122.85 . 1 147 16 PRO HA H 3.40 . 1 148 16 PRO HB2 H 1.00 . 2 149 16 PRO HB3 H 1.34 . 2 150 16 PRO HG2 H 1.30 . 2 151 16 PRO HG3 H 1.54 . 2 152 16 PRO HD2 H 2.85 . 2 153 16 PRO HD3 H 3.33 . 2 154 16 PRO CA C 64.11 . 1 155 16 PRO CB C 30.51 . 1 156 16 PRO CG C 27.01 . 1 157 16 PRO CD C 49.71 . 1 158 17 GLU H H 8.90 . 1 159 17 GLU HA H 3.98 . 1 160 17 GLU HB2 H 1.86 . 2 161 17 GLU HB3 H 2.22 . 2 162 17 GLU HG2 H 2.16 . 1 163 17 GLU HG3 H 2.58 . 2 164 17 GLU CA C 58.41 . 1 165 17 GLU CB C 29.21 . 1 166 17 GLU CG C 36.81 . 1 167 17 GLU N N 116.15 . 1 168 18 LEU H H 8.57 . 1 169 18 LEU HA H 5.11 . 1 170 18 LEU HB2 H 1.88 . 2 171 18 LEU HB3 H 2.02 . 2 172 18 LEU HG H 1.63 . 1 173 18 LEU HD1 H 0.96 . 1 174 18 LEU HD2 H 0.96 . 1 175 18 LEU CA C 51.21 . 1 176 18 LEU CB C 42.61 . 1 177 18 LEU CG C 26.41 . 1 178 18 LEU CD1 C 24.21 . 2 179 18 LEU CD2 C 25.91 . 2 180 18 LEU N N 123.15 . 1 181 19 PRO HA H 4.59 . 1 182 19 PRO HB2 H 2.08 . 2 183 19 PRO HB3 H 2.39 . 2 184 19 PRO HG2 H 1.99 . 1 185 19 PRO HG3 H 1.99 . 1 186 19 PRO HD2 H 3.89 . 1 187 19 PRO HD3 H 3.89 . 1 188 19 PRO CA C 62.71 . 1 189 19 PRO CB C 32.71 . 1 190 19 PRO CG C 27.21 . 1 191 19 PRO CD C 51.01 . 1 192 20 CYS H H 7.97 . 1 193 20 CYS HA H 3.86 . 1 194 20 CYS HB2 H 2.00 . 2 195 20 CYS HB3 H 3.33 . 2 196 20 CYS CA C 60.01 . 1 197 20 CYS CB C 26.41 . 1 198 20 CYS N N 119.45 . 1 199 21 GLU H H 10.11 . 1 200 21 GLU HA H 4.32 . 1 201 21 GLU HB2 H 2.10 . 1 202 21 GLU HB3 H 2.10 . 1 203 21 GLU HG2 H 2.33 . 1 204 21 GLU HG3 H 2.38 . 2 205 21 GLU CA C 58.81 . 1 206 21 GLU CB C 31.31 . 1 207 21 GLU CG C 37.11 . 1 208 21 GLU N N 122.25 . 1 209 22 LYS H H 9.34 . 1 210 22 LYS HA H 4.43 . 1 211 22 LYS HB2 H 1.66 . 2 212 22 LYS HB3 H 1.80 . 2 213 22 LYS HG2 H 1.40 . 1 214 22 LYS HG3 H 1.40 . 1 215 22 LYS HD2 H 1.66 . 1 216 22 LYS HD3 H 1.66 . 1 217 22 LYS HE2 H 2.96 . 1 218 22 LYS HE3 H 2.96 . 1 219 22 LYS CA C 55.91 . 1 220 22 LYS CB C 33.81 . 1 221 22 LYS CG C 24.51 . 1 222 22 LYS CD C 28.91 . 1 223 22 LYS CE C 39.61 . 1 224 22 LYS N N 118.25 . 1 225 23 SER H H 7.49 . 1 226 23 SER HA H 4.48 . 1 227 23 SER HB2 H 3.72 . 2 228 23 SER HB3 H 3.87 . 2 229 23 SER CA C 57.71 . 1 230 23 SER CB C 64.51 . 1 231 23 SER N N 112.25 . 1 232 24 ASP H H 8.35 . 1 233 24 ASP HA H 4.66 . 1 234 24 ASP HB2 H 2.65 . 2 235 24 ASP HB3 H 2.72 . 2 236 24 ASP CA C 53.91 . 1 237 24 ASP CB C 39.01 . 1 238 24 ASP N N 118.55 . 1 239 25 ALA H H 7.49 . 1 240 25 ALA HA H 4.52 . 1 241 25 ALA HB H 1.29 . 1 242 25 ALA CA C 51.51 . 1 243 25 ALA CB C 21.51 . 1 244 25 ALA N N 124.35 . 1 245 26 TYR H H 7.82 . 1 246 26 TYR HA H 5.21 . 1 247 26 TYR HB2 H 2.71 . 2 248 26 TYR HB3 H 3.28 . 2 249 26 TYR HD1 H 7.03 . 1 250 26 TYR HD2 H 7.03 . 1 251 26 TYR HE1 H 6.53 . 1 252 26 TYR HE2 H 6.53 . 1 253 26 TYR CA C 55.61 . 1 254 26 TYR CB C 40.61 . 1 255 26 TYR CD1 C 134.81 . 1 256 26 TYR CD2 C 134.81 . 1 257 26 TYR CE1 C 117.81 . 1 258 26 TYR CE2 C 117.81 . 1 259 26 TYR N N 116.85 . 1 260 27 PHE H H 8.55 . 1 261 27 PHE HA H 4.59 . 1 262 27 PHE HB2 H 2.75 . 2 263 27 PHE HB3 H 2.92 . 2 264 27 PHE HD1 H 6.91 . 1 265 27 PHE HD2 H 6.91 . 1 266 27 PHE HE1 H 7.17 . 1 267 27 PHE HE2 H 7.17 . 1 268 27 PHE HZ H 7.48 . 1 269 27 PHE CA C 60.61 . 1 270 27 PHE CB C 41.71 . 1 271 27 PHE CD1 C 132.91 . 1 272 27 PHE CD2 C 132.91 . 1 273 27 PHE CE1 C 131.41 . 1 274 27 PHE CE2 C 131.41 . 1 275 27 PHE CZ C 130.31 . 1 276 27 PHE N N 118.55 . 1 277 28 VAL H H 8.93 . 1 278 28 VAL HA H 4.55 . 1 279 28 VAL HB H 1.87 . 1 280 28 VAL HG1 H 0.72 . 2 281 28 VAL HG2 H 0.82 . 2 282 28 VAL CA C 59.61 . 1 283 28 VAL CB C 34.41 . 1 284 28 VAL CG1 C 21.51 . 2 285 28 VAL CG2 C 20.91 . 2 286 28 VAL N N 115.65 . 1 287 29 LEU H H 8.84 . 1 288 29 LEU HA H 4.60 . 1 289 29 LEU HB2 H 1.04 . 2 290 29 LEU HB3 H 1.85 . 2 291 29 LEU HG H 1.29 . 1 292 29 LEU HD1 H 0.58 . 2 293 29 LEU HD2 H 0.59 . 2 294 29 LEU CA C 55.31 . 1 295 29 LEU CB C 42.81 . 1 296 29 LEU CG C 27.01 . 1 297 29 LEU CD1 C 24.81 . 2 298 29 LEU CD2 C 26.41 . 2 299 29 LEU N N 127.15 . 1 300 30 ARG H H 8.59 . 1 301 30 ARG HA H 4.36 . 1 302 30 ARG HB2 H 0.12 . 2 303 30 ARG HB3 H 1.23 . 2 304 30 ARG HG2 H 1.07 . 1 305 30 ARG HG3 H 1.07 . 1 306 30 ARG HD2 H 2.72 . 1 307 30 ARG HD3 H 2.72 . 1 308 30 ARG CA C 54.41 . 1 309 30 ARG CB C 33.01 . 1 310 30 ARG CG C 28.11 . 1 311 30 ARG CD C 42.61 . 1 312 30 ARG N N 127.85 . 1 313 31 ASP H H 8.16 . 1 314 31 ASP HA H 4.79 . 1 315 31 ASP HB2 H 2.29 . 2 316 31 ASP HB3 H 2.61 . 2 317 31 ASP CA C 52.51 . 1 318 31 ASP CB C 43.11 . 1 319 31 ASP N N 119.15 . 1 320 32 GLY H H 7.74 . 1 321 32 GLY HA2 H 4.03 . 2 322 32 GLY HA3 H 4.19 . 2 323 32 GLY CA C 45.51 . 1 324 32 GLY N N 109.85 . 1 325 33 ALA HA H 4.00 . 1 326 33 ALA HB H 1.36 . 1 327 33 ALA CA C 54.61 . 1 328 33 ALA CB C 18.51 . 1 329 34 ALA H H 8.36 . 1 330 34 ALA HA H 3.69 . 1 331 34 ALA HB H 0.99 . 1 332 34 ALA CA C 49.61 . 1 333 34 ALA CB C 17.71 . 1 334 34 ALA N N 122.05 . 1 335 35 GLY H H 6.81 . 1 336 35 GLY HA2 H 3.50 . 2 337 35 GLY HA3 H 3.88 . 2 338 35 GLY CA C 44.31 . 1 339 35 GLY N N 105.65 . 1 340 36 VAL H H 8.53 . 1 341 36 VAL HA H 5.20 . 1 342 36 VAL HB H 1.93 . 1 343 36 VAL HG1 H 0.77 . 2 344 36 VAL HG2 H 0.90 . 2 345 36 VAL CA C 60.81 . 1 346 36 VAL CB C 33.01 . 1 347 36 VAL CG1 C 19.91 . 2 348 36 VAL CG2 C 22.31 . 2 349 36 VAL N N 114.05 . 1 350 37 PHE H H 8.65 . 1 351 37 PHE HA H 4.60 . 1 352 37 PHE HB2 H 2.63 . 2 353 37 PHE HB3 H 3.17 . 2 354 37 PHE HD1 H 7.02 . 1 355 37 PHE HD2 H 7.02 . 1 356 37 PHE HE1 H 6.80 . 1 357 37 PHE HE2 H 6.80 . 1 358 37 PHE HZ H 6.92 . 1 359 37 PHE CA C 56.71 . 1 360 37 PHE CB C 39.81 . 1 361 37 PHE CD1 C 133.21 . 1 362 37 PHE CD2 C 133.21 . 1 363 37 PHE CE1 C 130.81 . 1 364 37 PHE CE2 C 130.81 . 1 365 37 PHE CZ C 129.81 . 1 366 37 PHE N N 117.55 . 1 367 38 LEU H H 8.64 . 1 368 38 LEU HA H 5.13 . 1 369 38 LEU HB2 H 0.70 . 2 370 38 LEU HB3 H 1.34 . 2 371 38 LEU HG H 1.09 . 1 372 38 LEU HD1 H 0.20 . 2 373 38 LEU HD2 H 0.48 . 2 374 38 LEU CA C 52.81 . 1 375 38 LEU CB C 42.31 . 1 376 38 LEU CG C 26.11 . 1 377 38 LEU CD1 C 25.31 . 2 378 38 LEU CD2 C 23.41 . 2 379 38 LEU N N 118.35 . 1 380 39 ALA H H 9.12 . 1 381 39 ALA HA H 5.46 . 1 382 39 ALA HB H 1.18 . 1 383 39 ALA CA C 50.01 . 1 384 39 ALA CB C 23.41 . 1 385 39 ALA N N 123.25 . 1 386 40 ALA H H 8.23 . 1 387 40 ALA HA H 3.81 . 1 388 40 ALA HB H 1.28 . 1 389 40 ALA CA C 52.91 . 1 390 40 ALA CB C 20.11 . 1 391 40 ALA N N 123.85 . 1 392 41 ASN H H 9.64 . 1 393 41 ASN HA H 4.12 . 1 394 41 ASN HB2 H 1.80 . 2 395 41 ASN HB3 H 2.36 . 2 396 41 ASN CA C 57.11 . 1 397 41 ASN CB C 36.01 . 1 398 41 ASN N N 121.85 . 1 399 42 THR H H 6.81 . 1 400 42 THR HA H 4.19 . 1 401 42 THR HB H 4.42 . 1 402 42 THR HG2 H 1.10 . 1 403 42 THR CA C 60.41 . 1 404 42 THR CB C 68.61 . 1 405 42 THR CG2 C 21.81 . 1 406 42 THR N N 105.35 . 1 407 43 PHE H H 7.69 . 1 408 43 PHE HA H 4.97 . 1 409 43 PHE HB2 H 3.07 . 2 410 43 PHE HB3 H 3.48 . 2 411 43 PHE HD1 H 7.24 . 1 412 43 PHE HD2 H 7.24 . 1 413 43 PHE HE1 H 7.37 . 1 414 43 PHE HE2 H 7.37 . 1 415 43 PHE HZ H 7.37 . 1 416 43 PHE CA C 57.21 . 1 417 43 PHE CB C 39.81 . 1 418 43 PHE CD1 C 132.41 . 1 419 43 PHE CD2 C 132.41 . 1 420 43 PHE CE1 C 131.71 . 1 421 43 PHE CE2 C 131.71 . 1 422 43 PHE CZ C 131.71 . 1 423 43 PHE N N 126.25 . 1 424 44 PRO HA H 3.31 . 1 425 44 PRO HB2 H 1.05 . 2 426 44 PRO HB3 H 1.82 . 2 427 44 PRO HG2 H 1.45 . 2 428 44 PRO HG3 H 1.76 . 2 429 44 PRO HD2 H 3.41 . 1 430 44 PRO HD3 H 3.41 . 1 431 44 PRO CA C 64.01 . 1 432 44 PRO CB C 32.71 . 1 433 44 PRO CG C 24.01 . 1 434 44 PRO CD C 49.71 . 1 435 45 LYS H H 8.71 . 1 436 45 LYS HA H 3.87 . 1 437 45 LYS HB2 H 1.77 . 1 438 45 LYS HB3 H 1.77 . 1 439 45 LYS HG2 H 1.34 . 2 440 45 LYS HG3 H 1.45 . 2 441 45 LYS HD2 H 1.63 . 1 442 45 LYS HD3 H 1.63 . 1 443 45 LYS HE2 H 2.94 . 1 444 45 LYS HE3 H 2.94 . 1 445 45 LYS CA C 60.01 . 1 446 45 LYS CB C 31.31 . 1 447 45 LYS CG C 25.11 . 1 448 45 LYS CD C 28.91 . 1 449 45 LYS CE C 41.71 . 1 450 45 LYS N N 128.15 . 1 451 46 SER H H 6.08 . 1 452 46 SER HA H 4.43 . 1 453 46 SER HB2 H 3.20 . 2 454 46 SER HB3 H 3.57 . 2 455 46 SER CA C 55.81 . 1 456 46 SER CB C 63.41 . 1 457 46 SER N N 107.25 . 1 458 47 ARG H H 8.51 . 1 459 47 ARG HA H 4.54 . 1 460 47 ARG HB2 H 1.57 . 2 461 47 ARG HB3 H 2.20 . 2 462 47 ARG HG2 H 1.29 . 2 463 47 ARG HG3 H 1.57 . 2 464 47 ARG HD2 H 3.07 . 1 465 47 ARG HD3 H 3.07 . 1 466 47 ARG CA C 54.31 . 1 467 47 ARG CB C 29.21 . 1 468 47 ARG CG C 27.51 . 1 469 47 ARG CD C 42.61 . 1 470 47 ARG N N 124.25 . 1 471 48 GLU H H 7.78 . 1 472 48 GLU HA H 4.22 . 1 473 48 GLU HB2 H 1.87 . 1 474 48 GLU HB3 H 1.87 . 1 475 48 GLU HG2 H 2.21 . 1 476 48 GLU HG3 H 2.35 . 2 477 48 GLU CA C 58.81 . 1 478 48 GLU CB C 30.21 . 1 479 48 GLU CG C 35.71 . 1 480 48 GLU N N 123.05 . 1 481 49 THR H H 8.03 . 1 482 49 THR HA H 5.74 . 1 483 49 THR HB H 4.34 . 1 484 49 THR HG2 H 1.27 . 1 485 49 THR CA C 59.61 . 1 486 49 THR CB C 73.21 . 1 487 49 THR CG2 C 21.21 . 1 488 49 THR N N 117.65 . 1 489 50 ARG H H 8.75 . 1 490 50 ARG HA H 4.71 . 1 491 50 ARG HB2 H 1.68 . 2 492 50 ARG HB3 H 2.18 . 2 493 50 ARG HG2 H 0.86 . 1 494 50 ARG HG3 H 0.86 . 1 495 50 ARG HD2 H 2.95 . 2 496 50 ARG HD3 H 3.03 . 2 497 50 ARG CA C 55.91 . 1 498 50 ARG CB C 32.41 . 1 499 50 ARG CG C 25.11 . 1 500 50 ARG CD C 43.11 . 1 501 50 ARG N N 116.55 . 1 502 51 ALA H H 8.40 . 1 503 51 ALA HA H 4.91 . 1 504 51 ALA HB H 1.42 . 1 505 51 ALA CA C 50.01 . 1 506 51 ALA CB C 17.91 . 1 507 51 ALA N N 123.05 . 1 508 52 PRO HA H 4.44 . 1 509 52 PRO HB2 H 1.71 . 1 510 52 PRO HB3 H 1.71 . 1 511 52 PRO HG2 H 1.59 . 2 512 52 PRO HG3 H 1.84 . 2 513 52 PRO HD2 H 3.57 . 2 514 52 PRO HD3 H 3.80 . 2 515 52 PRO CA C 61.71 . 1 516 52 PRO CB C 30.51 . 1 517 52 PRO CG C 26.71 . 1 518 52 PRO CD C 49.41 . 1 519 53 LEU H H 8.96 . 1 520 53 LEU HA H 4.80 . 1 521 53 LEU HB2 H 1.53 . 2 522 53 LEU HB3 H 1.74 . 2 523 53 LEU HG H 1.75 . 1 524 53 LEU HD1 H 0.82 . 2 525 53 LEU HD2 H 0.90 . 2 526 53 LEU CA C 54.31 . 1 527 53 LEU CB C 42.31 . 1 528 53 LEU CG C 28.11 . 1 529 53 LEU CD1 C 23.41 . 2 530 53 LEU CD2 C 25.91 . 2 531 53 LEU N N 121.05 . 1 532 54 VAL H H 8.05 . 1 533 54 VAL HA H 3.17 . 1 534 54 VAL HB H 1.84 . 1 535 54 VAL HG1 H 0.52 . 2 536 54 VAL HG2 H 0.61 . 2 537 54 VAL CA C 68.11 . 1 538 54 VAL CB C 30.51 . 1 539 54 VAL CG1 C 24.51 . 2 540 54 VAL CG2 C 21.31 . 2 541 54 VAL N N 125.55 . 1 542 55 GLU H H 9.31 . 1 543 55 GLU HA H 3.83 . 1 544 55 GLU HB2 H 1.94 . 2 545 55 GLU HB3 H 2.03 . 2 546 55 GLU HG2 H 2.13 . 1 547 55 GLU HG3 H 2.34 . 2 548 55 GLU CA C 59.71 . 1 549 55 GLU CB C 29.41 . 1 550 55 GLU CG C 35.71 . 1 551 55 GLU N N 116.25 . 1 552 56 GLU H H 6.74 . 1 553 56 GLU HA H 3.91 . 1 554 56 GLU HB2 H 1.75 . 2 555 56 GLU HB3 H 2.71 . 2 556 56 GLU HG2 H 2.34 . 1 557 56 GLU HG3 H 2.45 . 2 558 56 GLU CA C 59.31 . 1 559 56 GLU CB C 29.21 . 1 560 56 GLU CG C 37.61 . 1 561 56 GLU N N 118.35 . 1 562 57 LEU H H 7.22 . 1 563 57 LEU HA H 3.88 . 1 564 57 LEU HB2 H 1.10 . 2 565 57 LEU HB3 H 1.90 . 2 566 57 LEU HG H 1.72 . 1 567 57 LEU HD1 H 0.61 . 1 568 57 LEU HD2 H 0.61 . 1 569 57 LEU CA C 57.81 . 1 570 57 LEU CB C 39.81 . 1 571 57 LEU CG C 26.11 . 1 572 57 LEU CD1 C 21.81 . 2 573 57 LEU CD2 C 27.81 . 2 574 57 LEU N N 116.25 . 1 575 58 TYR H H 8.68 . 1 576 58 TYR HA H 3.93 . 1 577 58 TYR HB2 H 2.79 . 2 578 58 TYR HB3 H 3.19 . 2 579 58 TYR HD1 H 7.15 . 1 580 58 TYR HD2 H 7.15 . 1 581 58 TYR HE1 H 6.79 . 1 582 58 TYR HE2 H 6.79 . 1 583 58 TYR CA C 62.71 . 1 584 58 TYR CB C 37.91 . 1 585 58 TYR CD1 C 133.31 . 1 586 58 TYR CD2 C 133.31 . 1 587 58 TYR CE1 C 118.51 . 1 588 58 TYR CE2 C 118.51 . 1 589 58 TYR N N 116.25 . 1 590 59 ARG H H 7.78 . 1 591 59 ARG HA H 3.60 . 1 592 59 ARG HB2 H 1.30 . 2 593 59 ARG HB3 H 1.70 . 2 594 59 ARG HG2 H 0.49 . 2 595 59 ARG HG3 H 1.30 . 2 596 59 ARG HD2 H 2.74 . 2 597 59 ARG HD3 H 2.86 . 2 598 59 ARG CA C 59.21 . 1 599 59 ARG CB C 29.71 . 1 600 59 ARG CG C 26.11 . 1 601 59 ARG CD C 43.91 . 1 602 59 ARG N N 121.15 . 1 603 60 PHE H H 7.05 . 1 604 60 PHE HA H 4.89 . 1 605 60 PHE HB2 H 2.36 . 2 606 60 PHE HB3 H 3.28 . 2 607 60 PHE HD1 H 7.21 . 1 608 60 PHE HD2 H 7.21 . 1 609 60 PHE HE1 H 7.10 . 1 610 60 PHE HE2 H 7.10 . 1 611 60 PHE HZ H 6.96 . 1 612 60 PHE CA C 56.41 . 1 613 60 PHE CB C 38.21 . 1 614 60 PHE CD1 C 132.61 . 1 615 60 PHE CD2 C 132.61 . 1 616 60 PHE CE1 C 130.31 . 1 617 60 PHE CE2 C 130.31 . 1 618 60 PHE CZ C 129.11 . 1 619 60 PHE N N 114.85 . 1 620 61 ARG H H 6.95 . 1 621 61 ARG HA H 3.77 . 1 622 61 ARG HB2 H 1.64 . 1 623 61 ARG HB3 H 1.64 . 1 624 61 ARG HG2 H 1.19 . 2 625 61 ARG HG3 H 1.64 . 2 626 61 ARG HD2 H 2.74 . 2 627 61 ARG HD3 H 2.80 . 2 628 61 ARG CA C 60.11 . 1 629 61 ARG CB C 30.01 . 1 630 61 ARG CG C 25.91 . 1 631 61 ARG CD C 43.11 . 1 632 61 ARG N N 121.05 . 1 633 62 ASP H H 8.40 . 1 634 62 ASP HA H 4.36 . 1 635 62 ASP HB2 H 2.58 . 2 636 62 ASP HB3 H 2.65 . 2 637 62 ASP CA C 55.71 . 1 638 62 ASP CB C 39.61 . 1 639 62 ASP N N 115.65 . 1 640 63 ARG H H 8.10 . 1 641 63 ARG HA H 4.33 . 1 642 63 ARG HB2 H 1.80 . 2 643 63 ARG HB3 H 1.96 . 2 644 63 ARG HG2 H 1.68 . 2 645 63 ARG HG3 H 1.80 . 2 646 63 ARG HD2 H 2.86 . 2 647 63 ARG HD3 H 3.23 . 2 648 63 ARG CA C 55.51 . 1 649 63 ARG CB C 31.31 . 1 650 63 ARG CG C 27.01 . 1 651 63 ARG CD C 43.71 . 1 652 63 ARG N N 116.85 . 1 653 64 LEU H H 7.26 . 1 654 64 LEU HA H 4.34 . 1 655 64 LEU HB2 H 1.18 . 2 656 64 LEU HB3 H 1.80 . 2 657 64 LEU HG H 2.00 . 1 658 64 LEU HD1 H 0.67 . 2 659 64 LEU HD2 H 0.81 . 2 660 64 LEU CA C 52.91 . 1 661 64 LEU CB C 40.61 . 1 662 64 LEU CG C 26.11 . 1 663 64 LEU CD1 C 22.61 . 2 664 64 LEU CD2 C 26.11 . 2 665 64 LEU N N 117.35 . 1 666 65 PRO HA H 4.58 . 1 667 65 PRO HB2 H 1.91 . 2 668 65 PRO HB3 H 2.46 . 2 669 65 PRO HG2 H 1.91 . 2 670 65 PRO HG3 H 2.19 . 2 671 65 PRO HD2 H 3.37 . 2 672 65 PRO HD3 H 3.83 . 2 673 65 PRO CA C 63.01 . 1 674 65 PRO CB C 31.91 . 1 675 65 PRO CG C 27.51 . 1 676 65 PRO CD C 50.21 . 1 677 66 GLU H H 8.88 . 1 678 66 GLU HA H 3.73 . 1 679 66 GLU HB2 H 2.02 . 2 680 66 GLU HB3 H 2.10 . 2 681 66 GLU HG2 H 2.33 . 1 682 66 GLU HG3 H 2.33 . 1 683 66 GLU CA C 60.81 . 1 684 66 GLU CB C 29.41 . 1 685 66 GLU CG C 36.01 . 1 686 66 GLU N N 124.05 . 1 687 67 LYS H H 8.68 . 1 688 67 LYS HA H 4.25 . 1 689 67 LYS HB2 H 1.80 . 2 690 67 LYS HB3 H 2.02 . 2 691 67 LYS HG2 H 1.47 . 1 692 67 LYS HG3 H 1.47 . 1 693 67 LYS HD2 H 1.72 . 1 694 67 LYS HD3 H 1.72 . 1 695 67 LYS HE2 H 2.96 . 1 696 67 LYS HE3 H 2.96 . 1 697 67 LYS CA C 58.71 . 1 698 67 LYS CB C 32.21 . 1 699 67 LYS CG C 24.81 . 1 700 67 LYS CD C 29.21 . 1 701 67 LYS CE C 41.71 . 1 702 67 LYS N N 115.15 . 1 703 68 LEU H H 7.63 . 1 704 68 LEU HA H 4.78 . 1 705 68 LEU HB2 H 1.54 . 1 706 68 LEU HB3 H 1.54 . 1 707 68 LEU HG H 1.54 . 1 708 68 LEU HD1 H 0.77 . 2 709 68 LEU HD2 H 0.90 . 2 710 68 LEU CA C 54.01 . 1 711 68 LEU CB C 44.21 . 1 712 68 LEU CG C 27.21 . 1 713 68 LEU CD1 C 25.91 . 2 714 68 LEU CD2 C 22.31 . 2 715 68 LEU N N 114.35 . 1 716 69 ARG H H 7.53 . 1 717 69 ARG HA H 3.70 . 1 718 69 ARG HB2 H 1.89 . 1 719 69 ARG HB3 H 1.89 . 1 720 69 ARG HG2 H 1.64 . 1 721 69 ARG HG3 H 1.64 . 1 722 69 ARG HD2 H 3.19 . 1 723 69 ARG HD3 H 3.19 . 1 724 69 ARG CA C 60.71 . 1 725 69 ARG CB C 29.21 . 1 726 69 ARG CG C 28.91 . 1 727 69 ARG CD C 43.41 . 1 728 69 ARG N N 120.55 . 1 729 70 TYR H H 8.64 . 1 730 70 TYR HA H 4.47 . 1 731 70 TYR HB2 H 2.53 . 2 732 70 TYR HB3 H 2.92 . 2 733 70 TYR HD1 H 6.32 . 1 734 70 TYR HD2 H 6.32 . 1 735 70 TYR HE1 H 6.73 . 1 736 70 TYR HE2 H 6.73 . 1 737 70 TYR CA C 60.01 . 1 738 70 TYR CB C 35.71 . 1 739 70 TYR CD1 C 133.41 . 1 740 70 TYR CD2 C 133.41 . 1 741 70 TYR CE1 C 117.81 . 1 742 70 TYR CE2 C 117.81 . 1 743 70 TYR N N 117.45 . 1 744 71 LEU H H 6.85 . 1 745 71 LEU HA H 3.67 . 1 746 71 LEU HB2 H 0.92 . 2 747 71 LEU HB3 H 1.55 . 2 748 71 LEU HG H 0.57 . 1 749 71 LEU HD1 H 0.57 . 2 750 71 LEU HD2 H 0.74 . 2 751 71 LEU CA C 57.21 . 1 752 71 LEU CB C 42.61 . 1 753 71 LEU CG C 22.61 . 1 754 71 LEU CD1 C 22.61 . 2 755 71 LEU CD2 C 26.41 . 2 756 71 LEU N N 122.15 . 1 757 72 ALA H H 7.10 . 1 758 72 ALA HA H 3.91 . 1 759 72 ALA HB H 1.29 . 1 760 72 ALA CA C 53.01 . 1 761 72 ALA CB C 18.81 . 1 762 72 ALA N N 114.85 . 1 763 73 ASP H H 7.07 . 1 764 73 ASP HA H 4.75 . 1 765 73 ASP HB2 H 2.90 . 2 766 73 ASP HB3 H 3.18 . 2 767 73 ASP CA C 54.51 . 1 768 73 ASP CB C 41.21 . 1 769 73 ASP N N 115.35 . 1 770 74 ALA H H 6.39 . 1 771 74 ALA HA H 3.12 . 1 772 74 ALA HB H 0.07 . 1 773 74 ALA CA C 50.41 . 1 774 74 ALA CB C 16.81 . 1 775 74 ALA N N 123.55 . 1 776 75 PRO HA H 4.25 . 1 777 75 PRO HB2 H 1.80 . 2 778 75 PRO HB3 H 2.39 . 2 779 75 PRO HG2 H 2.03 . 2 780 75 PRO HG3 H 2.19 . 2 781 75 PRO HD2 H 2.84 . 2 782 75 PRO HD3 H 3.45 . 2 783 75 PRO CA C 62.91 . 1 784 75 PRO CB C 31.31 . 1 785 75 PRO CG C 28.31 . 1 786 75 PRO CD C 49.11 . 1 787 76 GLN H H 8.66 . 1 788 76 GLN HA H 3.64 . 1 789 76 GLN HB2 H 1.60 . 2 790 76 GLN HB3 H 2.15 . 2 791 76 GLN HG2 H 1.71 . 2 792 76 GLN HG3 H 2.37 . 2 793 76 GLN CA C 57.61 . 1 794 76 GLN CB C 29.21 . 1 795 76 GLN CG C 34.61 . 1 796 76 GLN N N 121.85 . 1 797 77 GLN H H 7.43 . 1 798 77 GLN HA H 5.01 . 1 799 77 GLN HB2 H 1.49 . 2 800 77 GLN HB3 H 1.83 . 2 801 77 GLN HG2 H 1.99 . 1 802 77 GLN HG3 H 1.99 . 1 803 77 GLN CA C 53.91 . 1 804 77 GLN CB C 32.71 . 1 805 77 GLN CG C 33.31 . 1 806 77 GLN N N 115.55 . 1 807 78 ASP H H 8.16 . 1 808 78 ASP HA H 3.04 . 1 809 78 ASP HB2 H 1.37 . 2 810 78 ASP HB3 H 1.84 . 2 811 78 ASP CA C 51.81 . 1 812 78 ASP CB C 39.01 . 1 813 78 ASP N N 121.65 . 1 814 79 PRO HA H 4.14 . 1 815 79 PRO HB2 H 1.71 . 2 816 79 PRO HB3 H 2.38 . 2 817 79 PRO HG2 H 1.87 . 2 818 79 PRO HG3 H 2.11 . 2 819 79 PRO HD2 H 2.38 . 2 820 79 PRO HD3 H 2.75 . 2 821 79 PRO CA C 65.51 . 1 822 79 PRO CB C 31.61 . 1 823 79 PRO CG C 28.11 . 1 824 79 PRO CD C 50.01 . 1 825 80 GLU H H 7.35 . 1 826 80 GLU HA H 4.24 . 1 827 80 GLU HB2 H 1.74 . 2 828 80 GLU HB3 H 2.13 . 2 829 80 GLU HG2 H 2.13 . 1 830 80 GLU HG3 H 2.13 . 1 831 80 GLU CA C 55.51 . 1 832 80 GLU CB C 30.21 . 1 833 80 GLU CG C 37.11 . 1 834 80 GLU N N 114.35 . 1 835 81 GLY H H 7.90 . 1 836 81 GLY HA2 H 3.43 . 2 837 81 GLY HA3 H 4.16 . 2 838 81 GLY CA C 45.11 . 1 839 81 GLY N N 107.55 . 1 840 82 ASN H H 8.22 . 1 841 82 ASN HA H 4.60 . 1 842 82 ASN HB2 H 2.62 . 2 843 82 ASN HB3 H 2.75 . 2 844 82 ASN CA C 53.11 . 1 845 82 ASN CB C 37.91 . 1 846 82 ASN N N 120.25 . 1 847 83 LYS H H 8.93 . 1 848 83 LYS HA H 4.40 . 1 849 83 LYS HB2 H 1.85 . 2 850 83 LYS HB3 H 1.94 . 2 851 83 LYS HG2 H 1.54 . 2 852 83 LYS HG3 H 1.66 . 2 853 83 LYS HD2 H 1.66 . 1 854 83 LYS HD3 H 1.66 . 1 855 83 LYS HE2 H 2.97 . 1 856 83 LYS HE3 H 2.97 . 1 857 83 LYS CA C 57.51 . 1 858 83 LYS CB C 32.21 . 1 859 83 LYS CG C 25.61 . 1 860 83 LYS CD C 28.91 . 1 861 83 LYS CE C 41.71 . 1 862 83 LYS N N 122.55 . 1 863 84 THR H H 7.21 . 1 864 84 THR HA H 4.73 . 1 865 84 THR HB H 4.02 . 1 866 84 THR HG2 H 0.69 . 1 867 84 THR CA C 59.51 . 1 868 84 THR CB C 70.21 . 1 869 84 THR CG2 C 24.51 . 1 870 84 THR N N 109.55 . 1 871 85 MET H H 8.97 . 1 872 85 MET HA H 5.03 . 1 873 85 MET HB2 H 1.83 . 1 874 85 MET HB3 H 1.83 . 1 875 85 MET HG2 H 2.23 . 2 876 85 MET HG3 H 2.31 . 2 877 85 MET HE H 1.89 . 1 878 85 MET CA C 54.21 . 1 879 85 MET CB C 36.01 . 1 880 85 MET CG C 30.81 . 1 881 85 MET CE C 16.81 . 1 882 85 MET N N 120.25 . 1 883 86 VAL H H 7.53 . 1 884 86 VAL HA H 4.01 . 1 885 86 VAL HB H 1.71 . 1 886 86 VAL HG1 H 0.69 . 2 887 86 VAL HG2 H 0.92 . 2 888 86 VAL CA C 63.41 . 1 889 86 VAL CB C 32.41 . 1 890 86 VAL CG1 C 22.51 . 2 891 86 VAL CG2 C 23.41 . 2 892 86 VAL N N 119.65 . 1 893 87 ARG H H 8.71 . 1 894 87 ARG HA H 4.58 . 1 895 87 ARG HB2 H 0.05 . 2 896 87 ARG HB3 H 1.40 . 2 897 87 ARG HG2 H 1.25 . 2 898 87 ARG HG3 H 1.33 . 2 899 87 ARG HD2 H 3.03 . 2 900 87 ARG HD3 H 3.11 . 2 901 87 ARG CA C 53.21 . 1 902 87 ARG CB C 33.51 . 1 903 87 ARG CG C 26.41 . 1 904 87 ARG CD C 42.81 . 1 905 87 ARG N N 125.35 . 1 906 88 PHE H H 8.88 . 1 907 88 PHE HA H 5.11 . 1 908 88 PHE HB2 H 2.87 . 2 909 88 PHE HB3 H 2.94 . 2 910 88 PHE HD1 H 6.83 . 1 911 88 PHE HD2 H 6.83 . 1 912 88 PHE HE1 H 7.20 . 1 913 88 PHE HE2 H 7.20 . 1 914 88 PHE HZ H 7.13 . 1 915 88 PHE CA C 57.51 . 1 916 88 PHE CB C 43.71 . 1 917 88 PHE CD1 C 131.11 . 1 918 88 PHE CD2 C 131.11 . 1 919 88 PHE CE1 C 131.41 . 1 920 88 PHE CE2 C 131.41 . 1 921 88 PHE CZ C 129.31 . 1 922 88 PHE N N 123.65 . 1 923 89 SER H H 8.26 . 1 924 89 SER HA H 5.00 . 1 925 89 SER HB2 H 3.82 . 2 926 89 SER HB3 H 3.90 . 2 927 89 SER CA C 55.21 . 1 928 89 SER CB C 63.81 . 1 929 89 SER N N 122.25 . 1 930 90 ARG H H 9.43 . 1 931 90 ARG HA H 4.04 . 1 932 90 ARG HB2 H 1.98 . 1 933 90 ARG HB3 H 1.98 . 1 934 90 ARG HG2 H 1.89 . 1 935 90 ARG HG3 H 1.89 . 1 936 90 ARG HD2 H 3.32 . 1 937 90 ARG HD3 H 3.32 . 1 938 90 ARG CA C 59.11 . 1 939 90 ARG CB C 29.71 . 1 940 90 ARG CG C 27.81 . 1 941 90 ARG CD C 43.41 . 1 942 90 ARG N N 129.75 . 1 943 91 LYS H H 8.19 . 1 944 91 LYS HA H 4.11 . 1 945 91 LYS HB2 H 1.67 . 2 946 91 LYS HB3 H 1.82 . 2 947 91 LYS HG2 H 1.35 . 2 948 91 LYS HG3 H 1.49 . 2 949 91 LYS HD2 H 1.66 . 1 950 91 LYS HD3 H 1.66 . 1 951 91 LYS HE2 H 2.93 . 1 952 91 LYS HE3 H 2.93 . 1 953 91 LYS CA C 59.11 . 1 954 91 LYS CB C 32.71 . 1 955 91 LYS CG C 25.11 . 1 956 91 LYS CD C 28.91 . 1 957 91 LYS CE C 41.71 . 1 958 91 LYS N N 118.05 . 1 959 92 THR H H 7.33 . 1 960 92 THR HA H 4.33 . 1 961 92 THR HB H 4.28 . 1 962 92 THR HG2 H 1.00 . 1 963 92 THR CA C 61.11 . 1 964 92 THR CB C 69.71 . 1 965 92 THR CG2 C 21.81 . 1 966 92 THR N N 105.05 . 1 967 93 LYS H H 7.86 . 1 968 93 LYS HA H 3.60 . 1 969 93 LYS HB2 H 2.09 . 1 970 93 LYS HB3 H 2.09 . 1 971 93 LYS HG2 H 1.42 . 1 972 93 LYS HG3 H 1.42 . 1 973 93 LYS HD2 H 1.78 . 1 974 93 LYS HD3 H 1.78 . 1 975 93 LYS HE2 H 3.09 . 1 976 93 LYS HE3 H 3.09 . 1 977 93 LYS CA C 57.31 . 1 978 93 LYS CB C 28.91 . 1 979 93 LYS CG C 25.31 . 1 980 93 LYS CD C 29.21 . 1 981 93 LYS CE C 42.31 . 1 982 93 LYS N N 119.05 . 1 983 94 GLN H H 6.85 . 1 984 94 GLN HA H 4.86 . 1 985 94 GLN HB2 H 1.93 . 2 986 94 GLN HB3 H 2.24 . 2 987 94 GLN HG2 H 2.33 . 2 988 94 GLN HG3 H 2.43 . 2 989 94 GLN CA C 54.21 . 1 990 94 GLN CB C 32.41 . 1 991 94 GLN CG C 33.31 . 1 992 94 GLN N N 113.85 . 1 993 95 GLN H H 8.94 . 1 994 95 GLN HA H 5.53 . 1 995 95 GLN HB2 H 2.12 . 2 996 95 GLN HB3 H 2.49 . 2 997 95 GLN HG2 H 2.66 . 2 998 95 GLN HG3 H 2.94 . 2 999 95 GLN CA C 55.11 . 1 1000 95 GLN CB C 29.41 . 1 1001 95 GLN CG C 33.01 . 1 1002 95 GLN N N 119.15 . 1 1003 96 TYR H H 9.07 . 1 1004 96 TYR HA H 5.17 . 1 1005 96 TYR HB2 H 2.78 . 2 1006 96 TYR HB3 H 3.04 . 2 1007 96 TYR HD1 H 6.74 . 1 1008 96 TYR HD2 H 6.74 . 1 1009 96 TYR HE1 H 6.49 . 1 1010 96 TYR HE2 H 6.49 . 1 1011 96 TYR CA C 56.61 . 1 1012 96 TYR CB C 39.61 . 1 1013 96 TYR CD1 C 134.41 . 1 1014 96 TYR CD2 C 134.41 . 1 1015 96 TYR CE1 C 117.71 . 1 1016 96 TYR CE2 C 117.71 . 1 1017 96 TYR N N 120.55 . 1 1018 97 VAL H H 8.54 . 1 1019 97 VAL HA H 5.30 . 1 1020 97 VAL HB H 1.75 . 1 1021 97 VAL HG1 H 0.49 . 2 1022 97 VAL HG2 H 0.56 . 2 1023 97 VAL CA C 59.41 . 1 1024 97 VAL CB C 35.21 . 1 1025 97 VAL CG1 C 21.21 . 2 1026 97 VAL CG2 C 20.41 . 2 1027 97 VAL N N 113.25 . 1 1028 98 SER H H 8.50 . 1 1029 98 SER HA H 5.35 . 1 1030 98 SER HB2 H 3.72 . 2 1031 98 SER HB3 H 4.18 . 2 1032 98 SER CA C 56.91 . 1 1033 98 SER CB C 65.81 . 1 1034 98 SER N N 115.85 . 1 1035 99 SER H H 8.29 . 1 1036 99 SER HA H 5.30 . 1 1037 99 SER HB2 H 3.52 . 2 1038 99 SER HB3 H 3.66 . 2 1039 99 SER CA C 56.51 . 1 1040 99 SER CB C 66.41 . 1 1041 99 SER N N 113.65 . 1 1042 100 GLU H H 8.02 . 1 1043 100 GLU HA H 5.00 . 1 1044 100 GLU HB2 H 1.66 . 2 1045 100 GLU HB3 H 1.73 . 2 1046 100 GLU HG2 H 1.94 . 1 1047 100 GLU HG3 H 2.12 . 2 1048 100 GLU CA C 54.61 . 1 1049 100 GLU CB C 34.41 . 1 1050 100 GLU CG C 36.01 . 1 1051 100 GLU N N 119.05 . 1 1052 101 LYS H H 8.64 . 1 1053 101 LYS HA H 4.41 . 1 1054 101 LYS HB2 H 1.45 . 2 1055 101 LYS HB3 H 1.66 . 2 1056 101 LYS HG2 H 1.21 . 2 1057 101 LYS HG3 H 1.33 . 2 1058 101 LYS HD2 H 1.69 . 1 1059 101 LYS HD3 H 1.69 . 1 1060 101 LYS HE2 H 2.95 . 1 1061 101 LYS HE3 H 2.95 . 1 1062 101 LYS CA C 55.91 . 1 1063 101 LYS CB C 34.91 . 1 1064 101 LYS CG C 24.81 . 1 1065 101 LYS CD C 28.91 . 1 1066 101 LYS CE C 41.71 . 1 1067 101 LYS N N 121.15 . 1 1068 102 ASP H H 9.44 . 1 1069 102 ASP HA H 4.28 . 1 1070 102 ASP HB2 H 2.65 . 2 1071 102 ASP HB3 H 2.92 . 2 1072 102 ASP CA C 55.61 . 1 1073 102 ASP CB C 39.81 . 1 1074 102 ASP N N 128.25 . 1 1075 103 GLY H H 8.63 . 1 1076 103 GLY HA2 H 3.64 . 2 1077 103 GLY HA3 H 4.05 . 2 1078 103 GLY CA C 45.61 . 1 1079 103 GLY N N 103.35 . 1 1080 104 LYS H H 7.66 . 1 1081 104 LYS HA H 4.67 . 1 1082 104 LYS HB2 H 1.78 . 2 1083 104 LYS HB3 H 1.86 . 2 1084 104 LYS HG2 H 1.44 . 1 1085 104 LYS HG3 H 1.44 . 1 1086 104 LYS HD2 H 1.70 . 1 1087 104 LYS HD3 H 1.70 . 1 1088 104 LYS HE2 H 3.02 . 1 1089 104 LYS HE3 H 3.02 . 1 1090 104 LYS CA C 54.11 . 1 1091 104 LYS CB C 34.61 . 1 1092 104 LYS CG C 24.21 . 1 1093 104 LYS CD C 28.91 . 1 1094 104 LYS CE C 42.01 . 1 1095 104 LYS N N 119.75 . 1 1096 105 ALA H H 8.68 . 1 1097 105 ALA HA H 4.51 . 1 1098 105 ALA HB H 1.56 . 1 1099 105 ALA CA C 53.51 . 1 1100 105 ALA CB C 18.51 . 1 1101 105 ALA N N 126.55 . 1 1102 106 THR H H 8.16 . 1 1103 106 THR HA H 4.25 . 1 1104 106 THR HB H 4.43 . 1 1105 106 THR HG2 H 1.16 . 1 1106 106 THR CA C 62.71 . 1 1107 106 THR CB C 70.21 . 1 1108 106 THR CG2 C 21.21 . 1 1109 106 THR N N 112.75 . 1 1110 107 GLY H H 8.64 . 1 1111 107 GLY HA2 H 3.80 . 2 1112 107 GLY HA3 H 4.42 . 2 1113 107 GLY CA C 45.41 . 1 1114 107 GLY N N 110.25 . 1 1115 108 TRP H H 8.58 . 1 1116 108 TRP HA H 4.60 . 1 1117 108 TRP HB2 H 3.10 . 2 1118 108 TRP HB3 H 3.48 . 2 1119 108 TRP HD1 H 7.36 . 1 1120 108 TRP HE1 H 10.66 . 1 1121 108 TRP HE3 H 7.32 . 1 1122 108 TRP HZ2 H 7.40 . 3 1123 108 TRP HZ3 H 6.45 . 3 1124 108 TRP HH2 H 6.63 . 1 1125 108 TRP CA C 59.41 . 1 1126 108 TRP CB C 29.41 . 1 1127 108 TRP CD1 C 127.51 . 1 1128 108 TRP CE3 C 120.41 . 1 1129 108 TRP CZ2 C 114.01 . 3 1130 108 TRP CZ3 C 121.11 . 3 1131 108 TRP CH2 C 123.41 . 1 1132 108 TRP N N 125.05 . 1 1133 108 TRP NE1 N 130.80 . 1 1134 109 SER H H 7.32 . 1 1135 109 SER HA H 4.93 . 1 1136 109 SER HB2 H 3.55 . 2 1137 109 SER HB3 H 3.79 . 2 1138 109 SER CA C 57.71 . 1 1139 109 SER CB C 67.21 . 1 1140 109 SER N N 121.85 . 1 1141 110 ALA H H 8.36 . 1 1142 110 ALA HA H 4.89 . 1 1143 110 ALA HB H 1.12 . 1 1144 110 ALA CA C 51.41 . 1 1145 110 ALA CB C 22.01 . 1 1146 110 ALA N N 119.25 . 1 1147 111 PHE H H 8.81 . 1 1148 111 PHE HA H 5.07 . 1 1149 111 PHE HB2 H 2.63 . 2 1150 111 PHE HB3 H 3.02 . 2 1151 111 PHE HD1 H 7.12 . 1 1152 111 PHE HD2 H 7.12 . 1 1153 111 PHE HE1 H 6.77 . 1 1154 111 PHE HE2 H 6.77 . 1 1155 111 PHE HZ H 6.63 . 1 1156 111 PHE CA C 57.21 . 1 1157 111 PHE CB C 43.11 . 1 1158 111 PHE CD1 C 131.91 . 1 1159 111 PHE CD2 C 131.91 . 1 1160 111 PHE CE1 C 131.01 . 1 1161 111 PHE CE2 C 131.01 . 1 1162 111 PHE CZ C 129.21 . 1 1163 111 PHE N N 119.25 . 1 1164 112 TYR H H 9.26 . 1 1165 112 TYR HA H 4.29 . 1 1166 112 TYR HB2 H 0.70 . 2 1167 112 TYR HB3 H 2.54 . 2 1168 112 TYR HD1 H 5.60 . 1 1169 112 TYR HD2 H 5.60 . 1 1170 112 TYR HE1 H 6.32 . 1 1171 112 TYR HE2 H 6.32 . 1 1172 112 TYR CA C 57.01 . 1 1173 112 TYR CB C 37.41 . 1 1174 112 TYR CD1 C 133.61 . 1 1175 112 TYR CD2 C 133.61 . 1 1176 112 TYR CE1 C 117.21 . 1 1177 112 TYR CE2 C 117.21 . 1 1178 112 TYR N N 126.65 . 1 1179 113 VAL H H 8.77 . 1 1180 113 VAL HA H 3.95 . 1 1181 113 VAL HB H 1.77 . 1 1182 113 VAL HG1 H 0.73 . 1 1183 113 VAL HG2 H 0.73 . 1 1184 113 VAL CA C 61.41 . 1 1185 113 VAL CB C 34.61 . 1 1186 113 VAL CG1 C 20.41 . 1 1187 113 VAL CG2 C 20.41 . 1 1188 113 VAL N N 129.75 . 1 1189 114 ASP H H 8.82 . 1 1190 114 ASP HA H 4.02 . 1 1191 114 ASP HB2 H 2.39 . 2 1192 114 ASP HB3 H 2.78 . 2 1193 114 ASP CA C 55.11 . 1 1194 114 ASP CB C 39.81 . 1 1195 114 ASP N N 127.35 . 1 1196 115 GLY H H 7.17 . 1 1197 115 GLY HA2 H 3.14 . 2 1198 115 GLY HA3 H 3.83 . 2 1199 115 GLY CA C 45.51 . 1 1200 115 GLY N N 101.15 . 1 1201 116 LYS H H 6.99 . 1 1202 116 LYS HA H 4.58 . 1 1203 116 LYS HB2 H 1.61 . 2 1204 116 LYS HB3 H 1.71 . 2 1205 116 LYS HG2 H 1.30 . 1 1206 116 LYS HG3 H 1.30 . 1 1207 116 LYS HD2 H 1.66 . 1 1208 116 LYS HD3 H 1.66 . 1 1209 116 LYS HE2 H 2.97 . 1 1210 116 LYS HE3 H 2.97 . 1 1211 116 LYS CA C 54.41 . 1 1212 116 LYS CB C 35.71 . 1 1213 116 LYS CG C 24.01 . 1 1214 116 LYS CD C 28.91 . 1 1215 116 LYS CE C 42.01 . 1 1216 116 LYS N N 118.35 . 1 1217 117 TRP H H 8.76 . 1 1218 117 TRP HA H 5.18 . 1 1219 117 TRP HB2 H 2.92 . 2 1220 117 TRP HB3 H 3.33 . 2 1221 117 TRP HD1 H 7.33 . 1 1222 117 TRP HE1 H 9.84 . 1 1223 117 TRP HE3 H 7.27 . 1 1224 117 TRP HZ2 H 7.03 . 3 1225 117 TRP HZ3 H 7.24 . 3 1226 117 TRP HH2 H 6.75 . 1 1227 117 TRP CA C 57.61 . 1 1228 117 TRP CB C 29.41 . 1 1229 117 TRP CD1 C 126.91 . 1 1230 117 TRP CE3 C 120.21 . 1 1231 117 TRP CZ2 C 115.31 . 3 1232 117 TRP CZ3 C 122.81 . 3 1233 117 TRP CH2 C 123.31 . 1 1234 117 TRP N N 121.65 . 1 1235 117 TRP NE1 N 129.00 . 1 1236 118 VAL H H 9.86 . 1 1237 118 VAL HA H 4.57 . 1 1238 118 VAL HB H 2.06 . 1 1239 118 VAL HG1 H 0.90 . 2 1240 118 VAL HG2 H 0.96 . 2 1241 118 VAL CA C 60.81 . 1 1242 118 VAL CB C 34.91 . 1 1243 118 VAL CG1 C 20.71 . 2 1244 118 VAL CG2 C 21.21 . 2 1245 118 VAL N N 124.65 . 1 1246 119 GLU H H 8.82 . 1 1247 119 GLU HA H 4.43 . 1 1248 119 GLU HB2 H 2.13 . 1 1249 119 GLU HB3 H 2.13 . 1 1250 119 GLU HG2 H 2.41 . 1 1251 119 GLU HG3 H 2.41 . 1 1252 119 GLU CA C 57.01 . 1 1253 119 GLU CB C 31.11 . 1 1254 119 GLU CG C 37.11 . 1 1255 119 GLU N N 126.05 . 1 1256 120 GLY H H 8.32 . 1 1257 120 GLY HA2 H 3.77 . 2 1258 120 GLY HA3 H 4.05 . 2 1259 120 GLY CA C 45.51 . 1 1260 120 GLY N N 110.35 . 1 1261 121 LYS H H 8.07 . 1 1262 121 LYS HA H 4.46 . 1 1263 121 LYS HB2 H 1.66 . 2 1264 121 LYS HB3 H 1.78 . 2 1265 121 LYS HG2 H 1.37 . 1 1266 121 LYS HG3 H 1.37 . 1 1267 121 LYS HD2 H 1.65 . 1 1268 121 LYS HD3 H 1.65 . 1 1269 121 LYS HE2 H 2.96 . 1 1270 121 LYS HE3 H 2.96 . 1 1271 121 LYS CA C 55.91 . 1 1272 121 LYS CB C 33.81 . 1 1273 121 LYS CG C 24.81 . 1 1274 121 LYS CD C 28.91 . 1 1275 121 LYS CE C 41.71 . 1 1276 121 LYS N N 121.35 . 1 1277 122 LYS H H 7.91 . 1 1278 122 LYS HA H 4.06 . 1 1279 122 LYS HB2 H 1.62 . 2 1280 122 LYS HB3 H 1.73 . 2 1281 122 LYS HG2 H 1.34 . 1 1282 122 LYS HG3 H 1.34 . 1 1283 122 LYS HD2 H 1.62 . 1 1284 122 LYS HD3 H 1.62 . 1 1285 122 LYS HE2 H 2.92 . 1 1286 122 LYS HE3 H 2.92 . 1 1287 122 LYS CA C 57.91 . 1 1288 122 LYS CB C 33.51 . 1 1289 122 LYS CG C 24.81 . 1 1290 122 LYS CD C 28.91 . 1 1291 122 LYS CE C 41.71 . 1 1292 122 LYS N N 128.75 . 1 stop_ save_