data_4084 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian hnRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy ; _BMRB_accession_number 4084 _BMRB_flat_file_name bmr4084.str _Entry_type update _Submission_date 1997-12-23 _Accession_date 1997-12-23 _Entry_origination BMRB _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 Garrett Daniel S. . 2 Lodi Patricia J. . 3 Shamoo Yousif . . 4 Williams Kenneth R. . 5 Clore G. Marius . 6 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 495 "13C chemical shifts" 274 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-17 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 ; Garrett, D. S., Lodi, P. J., Shamoo, Y., Williams, K. R., Clore, G. M., and Gronenborn, A. M., "Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian nhRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy," Biochemistry 33, 2852-2858, (1994). ; _Citation_title ; Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian nhRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Garrett Daniel S. . 2 Lodi Patricia J. . 3 Shamoo Yousif . . 4 Williams Kenneth R. . 5 Clore G. Marius . 6 Gronenborn Angela M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 33 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2852 _Page_last 2858 _Year 1994 _Details . loop_ _Keyword 'heterogenous nuclear ribonucleoprotein' hnRNP NMR 'nuclear magnetic resonance' 'small nuclear ribonucleoprotein' snRNP stop_ save_ ################################## # Molecular system description # ################################## save_system_hnRNP(A1) _Saveframe_category molecular_system _Mol_system_name hnRNP(A1) _Abbreviation_common hnRNP(A1) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hnRNP(A1) $hnRNP(A1) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hnRNP(A1) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human hnRNP A1' _Abbreviation_common 'hnRNP A1' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; MSKSESPKEPEQLRKLFIGG LSFETTDESLRSHFEQWGTL TDCVVMRDPNTKRSRGFGFV TYATVEEVDAAMNARPHKVD GRVVEPKRAVSRE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 SER 3 2 LYS 4 3 SER 5 4 GLU 6 5 SER 7 6 PRO 8 7 LYS 9 8 GLU 10 9 PRO 11 10 GLU 12 11 GLN 13 12 LEU 14 13 ARG 15 14 LYS 16 15 LEU 17 16 PHE 18 17 ILE 19 18 GLY 20 19 GLY 21 20 LEU 22 21 SER 23 22 PHE 24 23 GLU 25 24 THR 26 25 THR 27 26 ASP 28 27 GLU 29 28 SER 30 29 LEU 31 30 ARG 32 31 SER 33 32 HIS 34 33 PHE 35 34 GLU 36 35 GLN 37 36 TRP 38 37 GLY 39 38 THR 40 39 LEU 41 40 THR 42 41 ASP 43 42 CYS 44 43 VAL 45 44 VAL 46 45 MET 47 46 ARG 48 47 ASP 49 48 PRO 50 49 ASN 51 50 THR 52 51 LYS 53 52 ARG 54 53 SER 55 54 ARG 56 55 GLY 57 56 PHE 58 57 GLY 59 58 PHE 60 59 VAL 61 60 THR 62 61 TYR 63 62 ALA 64 63 THR 65 64 VAL 66 65 GLU 67 66 GLU 68 67 VAL 69 70 ASP 70 69 ALA 71 70 ALA 72 71 MET 73 72 ASN 74 73 ALA 75 74 ARG 76 75 PRO 77 76 HIS 78 77 LYS 79 78 VAL 80 79 ASP 81 80 GLY 82 81 ARG 83 82 VAL 84 83 VAL 85 84 GLU 86 85 PRO 87 86 LYS 88 87 ARG 89 88 ALA 90 89 VAL 91 90 SER 92 91 ARG 93 92 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 BAG60447 "unnamed protein product [Homo sapiens]" 100.00 208 100.00 100.00 9.51e-61 DBJ BAG64377 "unnamed protein product [Homo sapiens]" 100.00 254 100.00 100.00 1.38e-61 GB AAP78702 "hnRNP core protein A1, partial [Equus caballus]" 65.59 61 100.00 100.00 4.58e-36 GB ELK35268 "Heterogeneous nuclear ribonucleoprotein A1 [Myotis davidii]" 94.62 168 100.00 100.00 1.27e-56 REF XP_004274506 "PREDICTED: LOW QUALITY PROTEIN: heterogeneous nuclear ribonucleoprotein A1 [Orcinus orca]" 79.57 235 100.00 100.00 6.28e-47 REF XP_007659907 "PREDICTED: heterogeneous nuclear ribonucleoprotein A1, partial [Ornithorhynchus anatinus]" 100.00 132 100.00 100.00 9.22e-61 REF XP_012323839 "PREDICTED: polyadenylate-binding protein 4-like [Aotus nancymaae]" 100.00 386 98.92 98.92 1.20e-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 $hnRNP(A1) human 9606 Eukaryota Metazoa homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $hnRNP(A1) 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pYS45 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 $hnRNP(A1) 2 mM [U-15N] D2O 10 % . H2O 90 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hnRNP(A1) 2 mM '[U-13C; U-15N]' D2O 10 % . H2O 90 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hnRNP(A1) 2 mM [U-15N] D2O 99.996 % . stop_ save_ save_sample_four _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hnRNP(A1) 2 mM '[U-13C; U-15N]' D2O 99.996 % . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label . loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $hnRNP(A1) 97 % 'Mass Spectrometry' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details 'Conditions used for all four samples are the same' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.7 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 TSP C 13 'methyl protons' ppm 0.00 . . . . . TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 'liquid ammonia' N 15 nitrogen ppm 0.00 external . . . . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name hnRNP(A1) _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 . 1 MET HA H 4.14 . 1 2 . 1 MET HB2 H 2.04 . 2 3 . 1 MET HB3 H 1.87 . 2 4 . 1 MET HG2 H 2.19 . 1 5 . 1 MET HG3 H 2.19 . 1 6 . 1 MET CA C 58.1 . 1 7 . 1 MET CB C 31.2 . 1 8 . 1 MET CG C 36.5 . 1 9 . 2 SER H H 8.38 . 1 10 . 2 SER HA H 4.53 . 1 11 . 2 SER HB2 H 3.92 . 1 12 . 2 SER HB3 H 3.92 . 1 13 . 2 SER CA C 58.2 . 1 14 . 2 SER CB C 64.0 . 1 15 . 2 SER N N 119.5 . 1 16 . 3 LYS H H 8.36 . 1 17 . 3 LYS HA H 4.41 . 1 18 . 3 LYS HB2 H 1.87 . 2 19 . 3 LYS HB3 H 1.80 . 2 20 . 3 LYS HG2 H 1.46 . 1 21 . 3 LYS HG3 H 1.46 . 1 22 . 3 LYS HD2 H 1.69 . 1 23 . 3 LYS HD3 H 1.69 . 1 24 . 3 LYS HE2 H 3.0 . 1 25 . 3 LYS HE3 H 3.0 . 1 26 . 3 LYS CA C 56.4 . 1 27 . 3 LYS CB C 33.3 . 1 28 . 3 LYS CG C 24.8 . 1 29 . 3 LYS CD C 29.0 . 1 30 . 3 LYS CE C 41.9 . 1 31 . 3 LYS N N 121.7 . 1 32 . 4 SER H H 8.46 . 1 33 . 4 SER HA H 4.46 . 1 34 . 4 SER HB2 H 3.85 . 1 35 . 4 SER HB3 H 3.85 . 1 36 . 4 SER CA C 58.4 . 1 37 . 4 SER CB C 63.8 . 1 38 . 4 SER N N 117.4 . 1 39 . 5 GLU H H 8.42 . 1 40 . 5 GLU HA H 4.39 . 1 41 . 5 GLU HB2 H 2.06 . 2 42 . 5 GLU HB3 H 1.92 . 2 43 . 5 GLU HG2 H 2.26 . 1 44 . 5 GLU HG3 H 2.26 . 1 45 . 5 GLU CA C 56.2 . 1 46 . 5 GLU CB C 30.7 . 1 47 . 5 GLU CG C 35.9 . 1 48 . 5 GLU N N 122.7 . 1 49 . 6 SER H H 8.42 . 1 50 . 6 SER HA H 4.75 . 1 51 . 6 SER HB2 H 3.90 . 2 52 . 6 SER HB3 H 3.81 . 2 53 . 6 SER CA C 56.6 . 1 54 . 6 SER CB C 63.2 . 1 55 . 6 SER N N 118.5 . 1 56 . 7 PRO HA H 4.46 . 1 57 . 7 PRO HB2 H 2.36 . 2 58 . 7 PRO HB3 H 1.91 . 2 59 . 7 PRO HG2 H 2.06 . 1 60 . 7 PRO HG3 H 2.06 . 1 61 . 7 PRO HD2 H 3.87 . 2 62 . 7 PRO HD3 H 3.72 . 2 63 . 7 PRO CA C 63.3 . 1 64 . 7 PRO CB C 32.2 . 1 65 . 7 PRO CG C 27.6 . 1 66 . 7 PRO CD C 50.8 . 1 67 . 8 LYS H H 8.49 . 1 68 . 8 LYS HA H 4.31 . 1 69 . 8 LYS HB2 H 1.85 . 2 70 . 8 LYS HB3 H 1.79 . 2 71 . 8 LYS HG2 H 1.53 . 1 72 . 8 LYS HG3 H 1.53 . 1 73 . 8 LYS HD2 H 1.71 . 1 74 . 8 LYS HD3 H 1.71 . 1 75 . 8 LYS HE2 H 3.11 . 1 76 . 8 LYS HE3 H 3.11 . 1 77 . 8 LYS CA C 56.4 . 1 78 . 8 LYS CB C 33.4 . 1 79 . 8 LYS CG C 25.0 . 1 80 . 8 LYS CD C 29.0 . 1 81 . 8 LYS CE C 43.3 . 1 82 . 8 LYS N N 121.5 . 1 83 . 9 GLU H H 8.36 . 1 84 . 9 GLU HA H 4.67 . 1 85 . 9 GLU HB2 H 1.96 . 1 86 . 9 GLU HB3 H 1.96 . 1 87 . 9 GLU HG2 H 2.35 . 1 88 . 9 GLU HG3 H 2.35 . 1 89 . 9 GLU CA C 54.5 . 1 90 . 9 GLU CB C 29.6 . 1 91 . 9 GLU CG C 35.9 . 1 92 . 9 GLU N N 121.1 . 1 93 . 10 PRO HA H 4.36 . 1 94 . 10 PRO HB2 H 2.42 . 2 95 . 10 PRO HB3 H 1.91 . 2 96 . 10 PRO HG2 H 2.10 . 1 97 . 10 PRO HG3 H 2.10 . 1 98 . 10 PRO HD2 H 3.91 . 2 99 . 10 PRO HD3 H 3.68 . 2 100 . 10 PRO CA C 63.7 . 1 101 . 10 PRO CB C 32.4 . 1 102 . 10 PRO CG C 27.7 . 1 103 . 10 PRO CD C 50.8 . 1 104 . 11 GLU H H 8.74 . 1 105 . 11 GLU HA H 3.74 . 1 106 . 11 GLU HB2 H 2.03 . 2 107 . 11 GLU HB3 H 1.96 . 2 108 . 11 GLU HG2 H 2.19 . 1 109 . 11 GLU HG3 H 2.19 . 1 110 . 11 GLU CA C 59.6 . 1 111 . 11 GLU CB C 29.9 . 1 112 . 11 GLU CG C 36.6 . 1 113 . 11 GLU N N 122.5 . 1 114 . 12 GLN H H 8.65 . 1 115 . 12 GLN HA H 4.03 . 1 116 . 12 GLN HB2 H 2.06 . 1 117 . 12 GLN HB3 H 2.06 . 1 118 . 12 GLN HG2 H 2.43 . 2 119 . 12 GLN HG3 H 2.36 . 2 120 . 12 GLN HE21 H 7.50 . 2 121 . 12 GLN HE22 H 6.87 . 2 122 . 12 GLN CA C 58.4 . 1 123 . 12 GLN CB C 28.2 . 1 124 . 12 GLN CG C 33.6 . 1 125 . 12 GLN N N 116.0 . 1 126 . 12 GLN NE2 N 110.9 . 1 127 . 13 LEU H H 7.52 . 1 128 . 13 LEU HA H 4.31 . 1 129 . 13 LEU HB2 H 1.71 . 2 130 . 13 LEU HB3 H 1.69 . 2 131 . 13 LEU HG H 1.68 . 1 132 . 13 LEU HD1 H 0.99 . 2 133 . 13 LEU HD2 H 0.91 . 2 134 . 13 LEU CA C 56.0 . 1 135 . 13 LEU CB C 42.4 . 1 136 . 13 LEU CG C 27.5 . 1 137 . 13 LEU CD1 C 25.3 . 1 138 . 13 LEU CD2 C 22.9 . 1 139 . 13 LEU N N 116.4 . 1 140 . 14 ARG H H 7.64 . 1 141 . 14 ARG HA H 4.46 . 1 142 . 14 ARG HB2 H 2.62 . 1 143 . 14 ARG HB3 H 2.62 . 1 144 . 14 ARG CA C 56.2 . 1 145 . 14 ARG CB C 31.0 . 1 146 . 14 ARG N N 116.8 . 1 147 . 15 LYS H H 7.00 . 1 148 . 15 LYS HA H 5.23 . 1 149 . 15 LYS HB2 H 1.69 . 1 150 . 15 LYS HB3 H 1.69 . 1 151 . 15 LYS HG2 H 1.49 . 2 152 . 15 LYS HG3 H 1.15 . 2 153 . 15 LYS HD2 H 1.31 . 1 154 . 15 LYS HD3 H 1.31 . 1 155 . 15 LYS HE2 H 2.40 . 1 156 . 15 LYS HE3 H 2.40 . 1 157 . 15 LYS CA C 55.4 . 1 158 . 15 LYS CB C 35.9 . 1 159 . 15 LYS CG C 24.7 . 1 160 . 15 LYS CD C 29.5 . 1 161 . 15 LYS CE C 41.2 . 1 162 . 15 LYS N N 119.7 . 1 163 . 16 LEU H H 9.65 . 1 164 . 16 LEU HA H 5.06 . 1 165 . 16 LEU HB2 H 1.56 . 2 166 . 16 LEU HB3 H 1.11 . 2 167 . 16 LEU HG H 1.62 . 1 168 . 16 LEU HD1 H 0.77 . 1 169 . 16 LEU HD2 H 0.82 . 1 170 . 16 LEU CA C 53.2 . 1 171 . 16 LEU CB C 45.0 . 1 172 . 16 LEU CG C 26.6 . 1 173 . 16 LEU CD1 C 25.2 . 1 174 . 16 LEU CD2 C 24.6 . 1 175 . 16 LEU N N 125.8 . 1 176 . 17 PHE H H 9.06 . 1 177 . 17 PHE HA H 4.62 . 1 178 . 17 PHE HB2 H 3.04 . 2 179 . 17 PHE HB3 H 2.95 . 2 180 . 17 PHE CA C 57.3 . 1 181 . 17 PHE CB C 40.7 . 1 182 . 17 PHE N N 123.3 . 1 183 . 18 ILE H H 8.52 . 1 184 . 18 ILE HA H 4.06 . 1 185 . 18 ILE HB H 1.55 . 1 186 . 18 ILE HG12 H 1.00 . 2 187 . 18 ILE HG13 H 0.85 . 2 188 . 18 ILE HG2 H 0.64 . 1 189 . 18 ILE HD1 H 0.17 . 1 190 . 18 ILE CA C 59.3 . 1 191 . 18 ILE CB C 37.0 . 1 192 . 18 ILE CG1 C 26.6 . 1 193 . 18 ILE CG2 C 19.7 . 1 194 . 18 ILE CD1 C 12.6 . 1 195 . 18 ILE N N 126.7 . 1 196 . 19 GLY H H 8.00 . 1 197 . 19 GLY HA2 H 4.48 . 2 198 . 19 GLY HA3 H 3.79 . 2 199 . 19 GLY CA C 43.6 . 1 200 . 19 GLY N N 112.7 . 1 201 . 20 GLY H H 8.58 . 1 202 . 20 GLY HA2 H 3.97 . 2 203 . 20 GLY HA3 H 3.80 . 2 204 . 20 GLY CA C 46.6 . 1 205 . 20 GLY N N 107.2 . 1 206 . 21 LEU H H 7.53 . 1 207 . 21 LEU HA H 4.06 . 1 208 . 21 LEU HB2 H 1.29 . 2 209 . 21 LEU HB3 H 0.96 . 2 210 . 21 LEU HG H 1.34 . 1 211 . 21 LEU HD1 H 0.51 . 1 212 . 21 LEU HD2 H 0.67 . 1 213 . 21 LEU CA C 54.2 . 1 214 . 21 LEU CB C 42.9 . 1 215 . 21 LEU CG C 27.0 . 1 216 . 21 LEU CD1 C 26.6 . 1 217 . 21 LEU CD2 C 23.9 . 1 218 . 21 LEU N N 115.0 . 1 219 . 22 SER H H 9.14 . 1 220 . 22 SER HA H 4.16 . 1 221 . 22 SER HB2 H 3.96 . 1 222 . 22 SER HB3 H 3.96 . 1 223 . 22 SER CA C 57.6 . 1 224 . 22 SER CB C 63.1 . 1 225 . 22 SER N N 114.4 . 1 226 . 23 PHE H H 9.11 . 1 227 . 23 PHE HA H 4.35 . 1 228 . 23 PHE HB2 H 3.35 . 2 229 . 23 PHE HB3 H 3.10 . 2 230 . 23 PHE CA C 60.3 . 1 231 . 23 PHE CB C 37.6 . 1 232 . 23 PHE N N 128.0 . 1 233 . 24 GLU H H 8.33 . 1 234 . 24 GLU HA H 4.29 . 1 235 . 24 GLU HB2 H 2.15 . 2 236 . 24 GLU HB3 H 1.84 . 2 237 . 24 GLU HG2 H 2.22 . 1 238 . 24 GLU HG3 H 2.22 . 1 239 . 24 GLU CA C 56.7 . 1 240 . 24 GLU CB C 30.0 . 1 241 . 24 GLU CG C 36.6 . 1 242 . 24 GLU N N 115.8 . 1 243 . 25 THR H H 7.32 . 1 244 . 25 THR HA H 4.15 . 1 245 . 25 THR HB H 4.02 . 1 246 . 25 THR HG2 H 1.22 . 1 247 . 25 THR CA C 64.9 . 1 248 . 25 THR CB C 68.7 . 1 249 . 25 THR CG2 C 23.7 . 1 250 . 25 THR N N 118.5 . 1 251 . 26 THR H H 8.46 . 1 252 . 26 THR HA H 4.52 . 1 253 . 26 THR HB H 4.78 . 1 254 . 26 THR HG2 H 1.34 . 1 255 . 26 THR CA C 59.3 . 1 256 . 26 THR CB C 73.1 . 1 257 . 26 THR CG2 C 21.7 . 1 258 . 26 THR N N 119.1 . 1 259 . 27 ASP H H 8.84 . 1 260 . 27 ASP HA H 3.95 . 1 261 . 27 ASP HB2 H 2.80 . 2 262 . 27 ASP HB3 H 2.65 . 2 263 . 27 ASP CA C 58.2 . 1 264 . 27 ASP CB C 40.0 . 1 265 . 27 ASP N N 120.1 . 1 266 . 28 GLU H H 8.47 . 1 267 . 28 GLU HA H 4.02 . 1 268 . 28 GLU HB2 H 2.12 . 2 269 . 28 GLU HB3 H 1.99 . 2 270 . 28 GLU CA C 60.3 . 1 271 . 28 GLU CB C 29.2 . 1 272 . 28 GLU N N 116.2 . 1 273 . 29 SER H H 8.42 . 1 274 . 29 SER HA H 4.34 . 1 275 . 29 SER HB2 H 3.91 . 1 276 . 29 SER HB3 H 3.91 . 1 277 . 29 SER CA C 61.7 . 1 278 . 29 SER CB C 62.2 . 1 279 . 29 SER N N 120.2 . 1 280 . 30 LEU H H 8.54 . 1 281 . 30 LEU HA H 4.10 . 1 282 . 30 LEU HB2 H 1.75 . 2 283 . 30 LEU HB3 H 1.18 . 2 284 . 30 LEU HG H 1.54 . 1 285 . 30 LEU HD1 H 0.61 . 1 286 . 30 LEU HD2 H 0.97 . 1 287 . 30 LEU CA C 58.2 . 1 288 . 30 LEU CB C 42.6 . 1 289 . 30 LEU CG C 26.8 . 1 290 . 30 LEU CD1 C 26.1 . 1 291 . 30 LEU CD2 C 25.3 . 1 292 . 30 LEU N N 126.5 . 1 293 . 31 ARG H H 8.07 . 1 294 . 31 ARG HA H 3.89 . 1 295 . 31 ARG HB2 H 2.27 . 2 296 . 31 ARG HB3 H 1.92 . 2 297 . 31 ARG HG2 H 1.46 . 1 298 . 31 ARG HG3 H 1.46 . 1 299 . 31 ARG HD2 H 3.46 . 2 300 . 31 ARG HD3 H 3.13 . 2 301 . 31 ARG CA C 59.7 . 1 302 . 31 ARG CB C 30.7 . 1 303 . 31 ARG CG C 28.1 . 1 304 . 31 ARG CD C 43.3 . 1 305 . 31 ARG N N 121.2 . 1 306 . 32 SER H H 8.36 . 1 307 . 32 SER HA H 4.16 . 1 308 . 32 SER HB2 H 4.01 . 2 309 . 32 SER HB3 H 3.97 . 2 310 . 32 SER CA C 61.3 . 1 311 . 32 SER CB C 62.9 . 1 312 . 32 SER N N 112.6 . 1 313 . 33 HIS H H 7.43 . 1 314 . 33 HIS HA H 4.44 . 1 315 . 33 HIS HB2 H 3.32 . 2 316 . 33 HIS HB3 H 3.16 . 2 317 . 33 HIS CA C 60.1 . 1 318 . 33 HIS CB C 29.3 . 1 319 . 33 HIS N N 114.7 . 1 320 . 34 PHE H H 8.29 . 1 321 . 34 PHE HA H 4.57 . 1 322 . 34 PHE HB2 H 3.69 . 2 323 . 34 PHE HB3 H 2.84 . 2 324 . 34 PHE CA C 64.2 . 1 325 . 34 PHE CB C 38.5 . 1 326 . 34 PHE N N 113.2 . 1 327 . 35 GLU H H 9.30 . 1 328 . 35 GLU HA H 4.99 . 1 329 . 35 GLU HB2 H 2.28 . 2 330 . 35 GLU HB3 H 2.16 . 2 331 . 35 GLU HG2 H 2.59 . 1 332 . 35 GLU HG3 H 2.44 . 2 333 . 35 GLU CA C 58.0 . 1 334 . 35 GLU CB C 28.7 . 1 335 . 35 GLU CG C 36.5 . 1 336 . 35 GLU N N 124.3 . 1 337 . 36 GLN H H 6.98 . 1 338 . 36 GLN HA H 3.76 . 1 339 . 36 GLN HB2 H 0.70 . 1 340 . 36 GLN HB3 H 0.70 . 1 341 . 36 GLN HG2 H 2.01 . 2 342 . 36 GLN HG3 H 1.60 . 2 343 . 36 GLN HE21 H 7.03 . 2 344 . 36 GLN HE22 H 6.77 . 2 345 . 36 GLN CA C 58.0 . 1 346 . 36 GLN CB C 27.6 . 1 347 . 36 GLN CG C 34.3 . 1 348 . 36 GLN N N 116.4 . 1 349 . 36 GLN NE2 N 110.8 . 1 350 . 37 TRP H H 7.05 . 1 351 . 37 TRP HA H 4.51 . 1 352 . 37 TRP HB2 H 3.60 . 2 353 . 37 TRP HB3 H 3.08 . 2 354 . 37 TRP HE1 H 10.16 . 1 355 . 37 TRP CA C 61.6 . 1 356 . 37 TRP CB C 29.0 . 1 357 . 37 TRP N N 114.3 . 1 358 . 37 TRP NE1 N 130.9 . 1 359 . 38 GLY H H 7.34 . 1 360 . 38 GLY HA2 H 4.56 . 2 361 . 38 GLY HA3 H 3.97 . 2 362 . 38 GLY CA C 45.5 . 1 363 . 38 GLY N N 104.8 . 1 364 . 39 THR H H 8.67 . 1 365 . 39 THR HA H 4.27 . 1 366 . 39 THR HB H 4.18 . 1 367 . 39 THR HG2 H 1.18 . 1 368 . 39 THR CA C 63.0 . 1 369 . 39 THR CB C 69.9 . 1 370 . 39 THR CG2 C 21.5 . 1 371 . 39 THR N N 116.6 . 1 372 . 40 LEU H H 8.87 . 1 373 . 40 LEU HA H 4.98 . 1 374 . 40 LEU HB2 H 1.68 . 2 375 . 40 LEU HB3 H 1.14 . 2 376 . 40 LEU HG H 1.59 . 1 377 . 40 LEU HD1 H 0.85 . 1 378 . 40 LEU HD2 H 0.15 . 1 379 . 40 LEU CA C 53.0 . 1 380 . 40 LEU CB C 41.8 . 1 381 . 40 LEU CG C 26.9 . 1 382 . 40 LEU CD1 C 28.4 . 1 383 . 40 LEU CD2 C 24.5 . 1 384 . 40 LEU N N 126.3 . 1 385 . 41 THR H H 8.95 . 1 386 . 41 THR HA H 4.23 . 1 387 . 41 THR CA C 62.8 . 1 388 . 41 THR CB C 67.7 . 1 389 . 41 THR N N 117.0 . 1 390 . 42 ASP H H 7.53 . 1 391 . 42 ASP HA H 4.66 . 1 392 . 42 ASP HB2 H 2.61 . 2 393 . 42 ASP HB3 H 2.41 . 2 394 . 42 ASP CA C 54.2 . 1 395 . 42 ASP CB C 44.3 . 1 396 . 42 ASP N N 118.4 . 1 397 . 43 CYS H H 8.50 . 1 398 . 43 CYS HA H 4.88 . 1 399 . 43 CYS HB2 H 2.81 . 2 400 . 43 CYS HB3 H 2.68 . 2 401 . 43 CYS CA C 59.5 . 1 402 . 43 CYS CB C 26.4 . 1 403 . 43 CYS N N 123.4 . 1 404 . 44 VAL H H 8.77 . 1 405 . 44 VAL HA H 4.62 . 1 406 . 44 VAL HB H 1.81 . 1 407 . 44 VAL HG1 H 0.89 . 1 408 . 44 VAL HG2 H 0.89 . 1 409 . 44 VAL CA C 60.2 . 1 410 . 44 VAL CB C 36.6 . 1 411 . 44 VAL CG1 C 21.2 . 1 412 . 44 VAL CG2 C 21.2 . 1 413 . 44 VAL N N 126.4 . 1 414 . 45 VAL H H 8.31 . 1 415 . 45 VAL HA H 3.75 . 1 416 . 45 VAL HB H 1.84 . 1 417 . 45 VAL HG1 H 0.58 . 1 418 . 45 VAL HG2 H 0.71 . 1 419 . 45 VAL CA C 62.5 . 1 420 . 45 VAL CB C 33.1 . 1 421 . 45 VAL CG1 C 22.7 . 1 422 . 45 VAL CG2 C 20.6 . 1 423 . 45 VAL N N 125.2 . 1 424 . 46 MET H H 8.48 . 1 425 . 46 MET HA H 4.48 . 1 426 . 46 MET HB2 H 1.45 . 2 427 . 46 MET HB3 H 1.05 . 2 428 . 46 MET HG2 H 2.60 . 2 429 . 46 MET HG3 H 2.29 . 2 430 . 46 MET CA C 54.8 . 1 431 . 46 MET CB C 30.4 . 1 432 . 46 MET CG C 33.3 . 1 433 . 46 MET N N 126.6 . 1 434 . 47 ARG H H 8.36 . 1 435 . 47 ARG HA H 4.87 . 1 436 . 47 ARG HB2 H 1.40 . 2 437 . 47 ARG HB3 H 1.20 . 2 438 . 47 ARG CA C 54.3 . 1 439 . 47 ARG CB C 34.0 . 1 440 . 47 ARG N N 120.3 . 1 441 . 48 ASP H H 8.62 . 1 442 . 48 ASP HA H 4.73 . 1 443 . 48 ASP HB2 H 3.05 . 2 444 . 48 ASP HB3 H 2.56 . 2 445 . 48 ASP CA C 52.1 . 1 446 . 48 ASP CB C 42.9 . 1 447 . 48 ASP N N 124.9 . 1 448 . 49 PRO HA H 4.34 . 1 449 . 49 PRO HB2 H 2.33 . 2 450 . 49 PRO HB3 H 1.96 . 2 451 . 49 PRO HG2 H 2.11 . 2 452 . 49 PRO HG3 H 2.03 . 2 453 . 49 PRO HD2 H 3.98 . 2 454 . 49 PRO HD3 H 3.87 . 2 455 . 49 PRO CA C 64.6 . 1 456 . 49 PRO CB C 32.3 . 1 457 . 49 PRO CG C 27.2 . 1 458 . 49 PRO CD C 50.9 . 1 459 . 50 ASN H H 8.59 . 1 460 . 50 ASN HA H 4.77 . 1 461 . 50 ASN HB2 H 2.97 . 2 462 . 50 ASN HB3 H 2.85 . 2 463 . 50 ASN HD21 H 7.93 . 2 464 . 50 ASN HD22 H 7.07 . 2 465 . 50 ASN CA C 55.4 . 1 466 . 50 ASN CB C 39.5 . 1 467 . 50 ASN N N 115.2 . 1 468 . 50 ASN ND2 N 114.0 . 1 469 . 51 THR H H 8.33 . 1 470 . 51 THR HA H 4.32 . 1 471 . 51 THR HB H 4.37 . 1 472 . 51 THR HG2 H 1.22 . 1 473 . 51 THR CA C 62.1 . 1 474 . 51 THR CB C 70.7 . 1 475 . 51 THR CG2 C 20.9 . 1 476 . 51 THR N N 108.5 . 1 477 . 52 LYS H H 8.12 . 1 478 . 52 LYS HA H 3.95 . 1 479 . 52 LYS HB2 H 2.21 . 2 480 . 52 LYS HB3 H 2.08 . 2 481 . 52 LYS HG2 H 1.37 . 2 482 . 52 LYS HG3 H 1.30 . 2 483 . 52 LYS HD2 H 1.64 . 2 484 . 52 LYS HD3 H 1.59 . 2 485 . 52 LYS HE2 H 3.00 . 1 486 . 52 LYS HE3 H 3.00 . 1 487 . 52 LYS CA C 58.0 . 1 488 . 52 LYS CB C 29.3 . 1 489 . 52 LYS CG C 25.2 . 1 490 . 52 LYS CD C 28.6 . 1 491 . 52 LYS CE C 42.4 . 1 492 . 52 LYS N N 114.3 . 1 493 . 53 ARG H H 7.89 . 1 494 . 53 ARG HA H 4.20 . 1 495 . 53 ARG HB2 H 1.80 . 2 496 . 53 ARG HB3 H 1.64 . 2 497 . 53 ARG HG2 H 1.68 . 2 498 . 53 ARG HG3 H 1.45 . 2 499 . 53 ARG HD2 H 3.15 . 1 500 . 53 ARG HD3 H 3.15 . 1 501 . 53 ARG CA C 56.3 . 1 502 . 53 ARG CB C 31.1 . 1 503 . 53 ARG CG C 27.8 . 1 504 . 53 ARG CD C 43.2 . 1 505 . 53 ARG N N 120.1 . 1 506 . 54 SER H H 8.86 . 1 507 . 54 SER HA H 4.21 . 1 508 . 54 SER HB2 H 4.04 . 2 509 . 54 SER HB3 H 3.85 . 2 510 . 54 SER CA C 58.6 . 1 511 . 54 SER CB C 63.8 . 1 512 . 54 SER N N 116.6 . 1 513 . 55 ARG H H 9.02 . 1 514 . 55 ARG HA H 4.43 . 1 515 . 55 ARG HB2 H 2.25 . 2 516 . 55 ARG HB3 H 0.93 . 2 517 . 55 ARG CA C 56.1 . 1 518 . 55 ARG CB C 31.4 . 1 519 . 55 ARG N N 123.2 . 1 520 . 56 GLY H H 9.42 . 1 521 . 56 GLY HA2 H 4.14 . 2 522 . 56 GLY HA3 H 3.13 . 2 523 . 56 GLY CA C 45.7 . 1 524 . 56 GLY N N 107.1 . 1 525 . 57 PHE H H 7.07 . 1 526 . 57 PHE HA H 5.23 . 1 527 . 57 PHE HB2 H 3.19 . 2 528 . 57 PHE HB3 H 2.73 . 2 529 . 57 PHE CA C 54.9 . 1 530 . 57 PHE CB C 41.8 . 1 531 . 57 PHE N N 112.1 . 1 532 . 58 GLY H H 8.37 . 1 533 . 58 GLY HA2 H 4.18 . 2 534 . 58 GLY HA3 H 3.95 . 2 535 . 58 GLY CA C 45.3 . 1 536 . 58 GLY N N 106.5 . 1 537 . 59 PHE H H 8.93 . 1 538 . 59 PHE HA H 5.69 . 1 539 . 59 PHE HB2 H 2.87 . 2 540 . 59 PHE HB3 H 2.60 . 2 541 . 59 PHE CA C 56.5 . 1 542 . 59 PHE CB C 44.1 . 1 543 . 59 PHE N N 114.8 . 1 544 . 60 VAL H H 8.59 . 1 545 . 60 VAL HA H 4.58 . 1 546 . 60 VAL HB H 1.71 . 1 547 . 60 VAL HG1 H 0.54 . 1 548 . 60 VAL HG2 H 0.32 . 1 549 . 60 VAL CA C 59.5 . 1 550 . 60 VAL CB C 34.7 . 1 551 . 60 VAL CG1 C 22.3 . 1 552 . 60 VAL CG2 C 20.1 . 1 553 . 60 VAL N N 114.9 . 1 554 . 61 THR H H 8.21 . 1 555 . 61 THR HA H 5.12 . 1 556 . 61 THR HB H 3.77 . 1 557 . 61 THR HG2 H 1.08 . 1 558 . 61 THR CA C 60.9 . 1 559 . 61 THR CB C 70.2 . 1 560 . 61 THR CG2 C 22.6 . 1 561 . 61 THR N N 119.8 . 1 562 . 62 TYR H H 8.41 . 1 563 . 62 TYR HA H 5.38 . 1 564 . 62 TYR HB2 H 3.77 . 2 565 . 62 TYR HB3 H 2.80 . 2 566 . 62 TYR CA C 58.4 . 1 567 . 62 TYR CB C 42.3 . 1 568 . 62 TYR N N 124.9 . 1 569 . 63 ALA H H 8.77 . 1 570 . 63 ALA HA H 4.09 . 1 571 . 63 ALA HB H 1.68 . 1 572 . 63 ALA CA C 55.3 . 1 573 . 63 ALA CB C 19.1 . 1 574 . 63 ALA N N 121.2 . 1 575 . 64 THR H H 7.99 . 1 576 . 64 THR HA H 4.94 . 1 577 . 64 THR HB H 4.73 . 1 578 . 64 THR HG2 H 1.22 . 1 579 . 64 THR CA C 59.1 . 1 580 . 64 THR CB C 73.2 . 1 581 . 64 THR CG2 C 21.6 . 1 582 . 64 THR N N 104.8 . 1 583 . 65 VAL H H 8.99 . 1 584 . 65 VAL HA H 3.70 . 1 585 . 65 VAL HB H 2.06 . 1 586 . 65 VAL HG1 H 0.96 . 1 587 . 65 VAL HG2 H 0.96 . 1 588 . 65 VAL CA C 65.7 . 1 589 . 65 VAL CB C 31.6 . 1 590 . 65 VAL CG1 C 21.8 . 1 591 . 65 VAL CG2 C 21.8 . 1 592 . 65 VAL N N 120.6 . 1 593 . 66 GLU H H 8.72 . 1 594 . 66 GLU HA H 4.08 . 1 595 . 66 GLU HB2 H 2.11 . 2 596 . 66 GLU HB3 H 1.99 . 2 597 . 66 GLU HG2 H 2.47 . 1 598 . 66 GLU HG3 H 2.37 . 2 599 . 66 GLU CA C 60.4 . 1 600 . 66 GLU CB C 28.9 . 1 601 . 66 GLU CG C 36.8 . 1 602 . 66 GLU N N 120.5 . 1 603 . 67 GLU H H 7.51 . 1 604 . 67 GLU HA H 3.90 . 1 605 . 67 GLU HB2 H 2.31 . 2 606 . 67 GLU HB3 H 1.78 . 2 607 . 67 GLU HG2 H 2.44 . 1 608 . 67 GLU HG3 H 2.33 . 2 609 . 67 GLU CA C 59.3 . 1 610 . 67 GLU CB C 29.2 . 1 611 . 67 GLU CG C 36.7 . 1 612 . 67 GLU N N 120.4 . 1 613 . 68 VAL H H 6.91 . 1 614 . 68 VAL HA H 3.19 . 1 615 . 68 VAL HB H 2.45 . 1 616 . 68 VAL HG1 H 1.29 . 1 617 . 68 VAL HG2 H 1.02 . 1 618 . 68 VAL CA C 66.4 . 1 619 . 68 VAL CB C 31.2 . 1 620 . 68 VAL CG1 C 24.4 . 1 621 . 68 VAL CG2 C 22.3 . 1 622 . 68 VAL N N 118.1 . 1 623 . 69 ASP H H 8.15 . 1 624 . 69 ASP HA H 4.16 . 1 625 . 69 ASP HB2 H 2.76 . 2 626 . 69 ASP HB3 H 2.55 . 2 627 . 69 ASP CA C 57.4 . 1 628 . 69 ASP CB C 39.9 . 1 629 . 69 ASP N N 119.0 . 1 630 . 70 ALA H H 7.76 . 1 631 . 70 ALA HA H 4.11 . 1 632 . 70 ALA HB H 1.73 . 1 633 . 70 ALA CA C 55.2 . 1 634 . 70 ALA CB C 18.2 . 1 635 . 70 ALA N N 122.6 . 1 636 . 71 ALA H H 8.14 . 1 637 . 71 ALA HA H 3.00 . 1 638 . 71 ALA HB H 1.40 . 1 639 . 71 ALA CA C 55.4 . 1 640 . 71 ALA CB C 18.2 . 1 641 . 71 ALA N N 121.1 . 1 642 . 72 MET H H 8.72 . 1 643 . 72 MET HA H 4.44 . 1 644 . 72 MET HB2 H 2.24 . 2 645 . 72 MET HB3 H 2.04 . 2 646 . 72 MET HG2 H 2.56 . 2 647 . 72 MET HG3 H 2.50 . 2 648 . 72 MET CA C 56.3 . 1 649 . 72 MET CB C 30.7 . 1 650 . 72 MET CG C 33.1 . 1 651 . 72 MET N N 117.7 . 1 652 . 73 ASN H H 8.06 . 1 653 . 73 ASN HA H 4.66 . 1 654 . 73 ASN HB2 H 2.88 . 2 655 . 73 ASN HB3 H 2.80 . 2 656 . 73 ASN HD21 H 7.54 . 2 657 . 73 ASN HD22 H 6.90 . 2 658 . 73 ASN CA C 54.3 . 1 659 . 73 ASN CB C 38.6 . 1 660 . 73 ASN N N 118.6 . 1 661 . 73 ASN ND2 N 112.0 . 1 662 . 74 ALA H H 6.98 . 1 663 . 74 ALA HA H 4.36 . 1 664 . 74 ALA HB H 0.92 . 1 665 . 74 ALA CA C 51.3 . 1 666 . 74 ALA CB C 19.0 . 1 667 . 74 ALA N N 122.3 . 1 668 . 75 ARG H H 6.94 . 1 669 . 75 ARG HA H 3.71 . 1 670 . 75 ARG HB2 H 1.86 . 1 671 . 75 ARG HB3 H 1.86 . 1 672 . 75 ARG HG2 H 1.84 . 1 673 . 75 ARG HG3 H 1.84 . 1 674 . 75 ARG HD2 H 3.37 . 1 675 . 75 ARG HD3 H 3.37 . 1 676 . 75 ARG CA C 54.9 . 1 677 . 75 ARG CB C 30.4 . 1 678 . 75 ARG CG C 27.3 . 1 679 . 75 ARG CD C 43.6 . 1 680 . 75 ARG N N 116.7 . 1 681 . 76 PRO HA H 4.50 . 1 682 . 76 PRO HB2 H 2.41 . 2 683 . 76 PRO HB3 H 1.89 . 2 684 . 76 PRO HG2 H 1.97 . 1 685 . 76 PRO HG3 H 1.97 . 1 686 . 76 PRO HD2 H 3.63 . 2 687 . 76 PRO HD3 H 3.49 . 2 688 . 76 PRO CA C 61.8 . 1 689 . 76 PRO CB C 35.1 . 1 690 . 76 PRO CG C 31.1 . 1 691 . 76 PRO CD C 50.1 . 1 692 . 77 HIS H H 9.46 . 1 693 . 77 HIS HA H 4.56 . 1 694 . 77 HIS HB2 H 2.99 . 2 695 . 77 HIS HB3 H 2.38 . 2 696 . 77 HIS CA C 56.2 . 1 697 . 77 HIS CB C 32.1 . 1 698 . 77 HIS N N 121.2 . 1 699 . 78 LYS H H 8.51 . 1 700 . 78 LYS HA H 5.01 . 1 701 . 78 LYS HB2 H 1.61 . 2 702 . 78 LYS HB3 H 1.48 . 2 703 . 78 LYS HG2 H 1.06 . 1 704 . 78 LYS HG3 H 1.06 . 1 705 . 78 LYS HD2 H 1.58 . 1 706 . 78 LYS HD3 H 1.58 . 1 707 . 78 LYS HE2 H 2.81 . 1 708 . 78 LYS HE3 H 2.81 . 1 709 . 78 LYS CA C 54.7 . 1 710 . 78 LYS CB C 33.5 . 1 711 . 78 LYS CG C 25.4 . 1 712 . 78 LYS CD C 29.4 . 1 713 . 78 LYS CE C 41.6 . 1 714 . 78 LYS N N 125.0 . 1 715 . 79 VAL H H 8.66 . 1 716 . 79 VAL HA H 4.01 . 1 717 . 79 VAL HB H 1.76 . 1 718 . 79 VAL HG1 H 0.76 . 1 719 . 79 VAL HG2 H 0.19 . 1 720 . 79 VAL CA C 60.8 . 1 721 . 79 VAL CB C 33.4 . 1 722 . 79 VAL CG1 C 21.7 . 1 723 . 79 VAL CG2 C 21.0 . 1 724 . 79 VAL N N 123.9 . 1 725 . 80 ASP H H 9.59 . 1 726 . 80 ASP HA H 4.27 . 1 727 . 80 ASP HB2 H 2.79 . 2 728 . 80 ASP HB3 H 2.47 . 2 729 . 80 ASP CA C 56.0 . 1 730 . 80 ASP CB C 39.8 . 1 731 . 80 ASP N N 128.4 . 1 732 . 81 GLY H H 8.54 . 1 733 . 81 GLY HA2 H 4.19 . 2 734 . 81 GLY HA3 H 3.49 . 2 735 . 81 GLY CA C 45.5 . 1 736 . 81 GLY N N 101.4 . 1 737 . 82 ARG H H 7.58 . 1 738 . 82 ARG HA H 4.68 . 1 739 . 82 ARG HB2 H 1.82 . 2 740 . 82 ARG HB3 H 1.65 . 2 741 . 82 ARG HG2 H 1.60 . 1 742 . 82 ARG HG3 H 1.60 . 1 743 . 82 ARG HD2 H 3.21 . 1 744 . 82 ARG HD3 H 3.21 . 1 745 . 82 ARG CA C 53.2 . 1 746 . 82 ARG CB C 32.5 . 1 747 . 82 ARG CG C 26.1 . 1 748 . 82 ARG CD C 42.7 . 1 749 . 82 ARG N N 120.0 . 1 750 . 83 VAL H H 8.69 . 1 751 . 83 VAL HA H 4.53 . 1 752 . 83 VAL HB H 2.00 . 1 753 . 83 VAL HG1 H 0.96 . 1 754 . 83 VAL HG2 H 0.96 . 1 755 . 83 VAL CA C 63.2 . 1 756 . 83 VAL CB C 31.0 . 1 757 . 83 VAL CG1 C 22.0 . 1 758 . 83 VAL CG2 C 22.0 . 1 759 . 83 VAL N N 124.5 . 1 760 . 84 VAL H H 8.44 . 1 761 . 84 VAL HA H 4.73 . 1 762 . 84 VAL HB H 2.22 . 1 763 . 84 VAL HG1 H 0.82 . 1 764 . 84 VAL HG2 H 0.70 . 1 765 . 84 VAL CA C 59.6 . 1 766 . 84 VAL CB C 32.8 . 1 767 . 84 VAL CG1 C 22.5 . 1 768 . 84 VAL CG2 C 19.2 . 1 769 . 84 VAL N N 122.5 . 1 770 . 85 GLU H H 8.74 . 1 771 . 85 GLU HA H 5.12 . 1 772 . 85 GLU HB2 H 2.02 . 2 773 . 85 GLU HB3 H 1.82 . 2 774 . 85 GLU HG2 H 2.19 . 1 775 . 85 GLU HG3 H 2.15 . 2 776 . 85 GLU CA C 53.0 . 1 777 . 85 GLU CB C 31.4 . 1 778 . 85 GLU CG C 35.7 . 1 779 . 85 GLU N N 120.9 . 1 780 . 86 PRO HA H 5.34 . 1 781 . 86 PRO HB2 H 2.07 . 2 782 . 86 PRO HB3 H 1.86 . 2 783 . 86 PRO HG2 H 2.18 . 2 784 . 86 PRO HG3 H 1.69 . 2 785 . 86 PRO HD2 H 4.03 . 2 786 . 86 PRO HD3 H 3.98 . 2 787 . 86 PRO CA C 61.6 . 1 788 . 86 PRO CB C 32.8 . 1 789 . 86 PRO CD C 51.0 . 1 790 . 87 LYS H H 9.40 . 1 791 . 87 LYS HA H 4.70 . 1 792 . 87 LYS HB2 H 1.92 . 2 793 . 87 LYS HB3 H 1.79 . 2 794 . 87 LYS HG2 H 1.52 . 1 795 . 87 LYS HG3 H 1.52 . 1 796 . 87 LYS HD2 H 1.66 . 1 797 . 87 LYS HD3 H 1.66 . 1 798 . 87 LYS HE2 H 2.89 . 1 799 . 87 LYS HE3 H 2.89 . 1 800 . 87 LYS CA C 55.0 . 1 801 . 87 LYS CB C 36.7 . 1 802 . 87 LYS CG C 24.6 . 1 803 . 87 LYS CD C 29.3 . 1 804 . 87 LYS CE C 42.0 . 1 805 . 87 LYS N N 120.8 . 1 806 . 88 ARG H H 8.88 . 1 807 . 88 ARG HA H 4.39 . 1 808 . 88 ARG HB2 H 2.04 . 2 809 . 88 ARG HB3 H 1.69 . 2 810 . 88 ARG HG2 H 1.59 . 1 811 . 88 ARG HG3 H 1.59 . 1 812 . 88 ARG HD2 H 3.31 . 2 813 . 88 ARG HD3 H 3.18 . 2 814 . 88 ARG CA C 57.3 . 1 815 . 88 ARG CB C 30.3 . 1 816 . 88 ARG CG C 27.1 . 1 817 . 88 ARG CD C 43.3 . 1 818 . 88 ARG N N 122.6 . 1 819 . 89 ALA H H 8.46 . 1 820 . 89 ALA HA H 4.30 . 1 821 . 89 ALA HB H 1.49 . 1 822 . 89 ALA CA C 53.7 . 1 823 . 89 ALA CB C 18.9 . 1 824 . 89 ALA N N 126.0 . 1 825 . 90 VAL H H 7.94 . 1 826 . 90 VAL HA H 4.21 . 1 827 . 90 VAL HB H 2.06 . 1 828 . 90 VAL HG1 H 0.89 . 1 829 . 90 VAL HG2 H 0.89 . 1 830 . 90 VAL CA C 61.6 . 1 831 . 90 VAL CB C 33.3 . 1 832 . 90 VAL CG1 C 21.1 . 1 833 . 90 VAL CG2 C 20.2 . 1 834 . 90 VAL N N 115.4 . 1 835 . 91 SER H H 8.23 . 1 836 . 91 SER HA H 4.46 . 1 837 . 91 SER HB2 H 3.85 . 1 838 . 91 SER HB3 H 3.85 . 1 839 . 91 SER CA C 58.2 . 1 840 . 91 SER CB C 64.0 . 1 841 . 91 SER N N 118.6 . 1 842 . 92 ARG H H 8.36 . 1 843 . 92 ARG HA H 4.33 . 1 844 . 92 ARG HB2 H 1.87 . 2 845 . 92 ARG HB3 H 1.71 . 2 846 . 92 ARG HG2 H 1.59 . 1 847 . 92 ARG HG3 H 1.59 . 1 848 . 92 ARG HD2 H 3.10 . 1 849 . 92 ARG HD3 H 3.10 . 1 850 . 92 ARG CA C 56.2 . 1 851 . 92 ARG CB C 31.0 . 1 852 . 92 ARG CG C 26.9 . 1 853 . 92 ARG CD C 43.2 . 1 854 . 92 ARG N N 123.3 . 1 855 . 93 GLU H H 8.00 . 1 856 . 93 GLU HA H 4.11 . 1 857 . 93 GLU HB2 H 2.03 . 2 858 . 93 GLU HB3 H 1.86 . 2 859 . 93 GLU CA C 58.0 . 1 860 . 93 GLU CB C 31.1 . 1 861 . 93 GLU N N 127.0 . 1 stop_ save_