data_4085 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-lethal Determined by Multidimensional Heteronuclear Magnetic Resonance ; _BMRB_accession_number 4085 _BMRB_flat_file_name bmr4085.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 Lee Andrew L. . 2 Kanaar Roland . . 3 Rio Donald C. . 4 Wemmer David E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 500 "13C chemical shifts" 288 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-16 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 ; Lee, A. L., Kannar, R., Rio, D. C., and Wemmer, D. E., "Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-lethal Determined by Multidimensional Heteronuclear Magnetic Resonance," Biochemistry 33, 13775-13786 (1994). ; _Citation_title ; Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-lethal Determined by Multidimensional Heteronuclear Magnetic Resonance ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7524663 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Andrew L. . 2 Kanaar Roland . . 3 Rio Donald C. . 4 Wemmer David E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 33 _Journal_issue 46 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13775 _Page_last 13786 _Year 1994 _Details . loop_ _Keyword 'Drosophila melanogaster' NMR 'Nuclear Magnetic Resonance' 'Sex-lethal protein (Sxl)' 'Sxl RNA binding domain 2 (Sxl-RBD2)' stop_ save_ ################################## # Molecular system description # ################################## save_system_Sxl-RBD2 _Saveframe_category molecular_system _Mol_system_name 'Sex-lethal protein RNA binding domain 2' _Abbreviation_common Sxl-RBD2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Sxl-RBD2 $Sxl-RBD2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'regulates sexual differentiation in Drosophila' Sxl-RBD2 stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sxl-RBD2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sex-lethal protein RNA binding domain 2' _Name_variant RNP-2 _Abbreviation_common Sxl-RBD2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; MSYARPGGESIKDTNLYVTN LPRTITDDQLDTIFGKYGSI VQKNILRDKLTGRPRGVAFV RYNKREEAQEAISALNNVIP EGGSQPLSVRLAEEHGK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 SER 3 3 TYR 4 4 ALA 5 5 ARG 6 6 PRO 7 7 GLY 8 8 GLY 9 9 GLU 10 10 SER 11 11 ILE 12 12 LYS 13 13 ASP 14 14 THR 15 15 ASN 16 16 LEU 17 17 TYR 18 18 VAL 19 19 THR 20 20 ASN 21 21 LEU 22 22 PRO 23 23 ARG 24 24 THR 25 25 ILE 26 26 THR 27 27 ASP 28 28 ASP 29 29 GLN 30 30 LEU 31 31 ASP 32 32 THR 33 33 ILE 34 34 PHE 35 35 GLY 36 36 LYS 37 37 TYR 38 38 GLY 39 39 SER 40 40 ILE 41 41 VAL 42 42 GLN 43 43 LYS 44 44 ASN 45 45 ILE 46 46 LEU 47 47 ARG 48 48 ASP 49 49 LYS 50 50 LEU 51 51 THR 52 52 GLY 53 53 ARG 54 54 PRO 55 55 ARG 56 56 GLY 57 57 VAL 58 58 ALA 59 59 PHE 60 60 VAL 61 61 ARG 62 62 TYR 63 63 ASN 64 64 LYS 65 65 ARG 66 66 GLU 67 67 GLU 68 68 ALA 69 69 GLN 70 70 GLU 71 71 ALA 72 72 ILE 73 73 SER 74 74 ALA 75 75 LEU 76 76 ASN 77 77 ASN 78 78 VAL 79 79 ILE 80 80 PRO 81 81 GLU 82 82 GLY 83 83 GLY 84 84 SER 85 85 GLN 86 86 PRO 87 87 LEU 88 88 SER 89 89 VAL 90 90 ARG 91 91 LEU 92 92 ALA 93 93 GLU 94 94 GLU 95 95 HIS 96 96 GLY 97 97 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1SXL "Resonance Assignments And Solution Structure Of The Second Rna-Binding Domain Of Sex-Lethal Determined By Multidimensional Hete" 100.00 97 100.00 100.00 1.64e-63 GB AAS15801 "sex lethal, partial [Drosophila melanogaster]" 60.82 59 98.31 100.00 3.80e-33 GB AAS15802 "sex lethal, partial [Drosophila melanogaster]" 60.82 59 98.31 100.00 3.80e-33 GB AAS15803 "sex lethal, partial [Drosophila melanogaster]" 60.82 59 98.31 100.00 3.80e-33 GB AAS15804 "sex lethal, partial [Drosophila melanogaster]" 60.82 59 98.31 100.00 3.80e-33 GB AAS15805 "sex lethal, partial [Drosophila melanogaster]" 60.82 59 98.31 100.00 3.80e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sxl-RBD2 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Sxl-RBD2 'recombinant technology' 'E. coli' Escherichia coli BL21-(DE3)pLysS plasmid pAR-Sxl-RNAP-2 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sxl-RBD2 . mM 1.5 2.0 [U-15N] NaCL 25 mM . . . d4-acetic_acid 25 mM . . . NaN3 0.01 % . . . D20 99.996 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sxl-RBD2 . mM 1.5 2.0 [U-15N] NaCL 25 mM . . . d4-acetic_acid 25 mM . . . NaN3 0.01 % . . . H20 10 % . . . D20 90 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sxl-RBD2 . mM 1.5 2.0 '[U-13C; U-15N]' NaCL 25 mM . . . d4-acetic_acid 25 mM . . . NaN3 0.01 % . . . D20 99.996 % . . . stop_ save_ save_sample_four _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sxl-RBD2 . mM 1.5 2.0 '[U-13C; U-15N]' NaCL 25 mM . . . d4-acetic_acid 25 mM . . . NaN3 0.01 % . . . H20 10 % . . . D20 90 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . 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 carbons' ppm 0.00 . . . . . TSP H 1 'methyl protons' ppm 0.00 . . . . . 'liquid NH3' N 15 nitrogen ppm 0.00 . . . . . 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_four stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name Sxl-RBD2 _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 . 4 ALA H H 8.09 . 1 2 . 4 ALA HA H 4.29 . 1 3 . 4 ALA HB H 1.30 . 1 4 . 4 ALA CA C 51.8 . 1 5 . 4 ALA CB C 19.4 . 1 6 . 4 ALA N N 125.6 . 1 7 . 5 ARG H H 8.22 . 1 8 . 5 ARG N N 126.6 . 1 9 . 6 PRO HA H 4.45 . 1 10 . 6 PRO HD2 H 3.67 . 2 11 . 6 PRO HD3 H 3.84 . 2 12 . 6 PRO CD C 50.7 . 1 13 . 7 GLY H H 8.63 . 1 14 . 7 GLY N N 109.9 . 1 15 . 8 GLY H H 8.32 . 1 16 . 8 GLY N N 108.6 . 1 17 . 9 GLU H H 8.50 . 1 18 . 9 GLU HA H 4.34 . 1 19 . 9 GLU HB2 H 1.97 . 2 20 . 9 GLU HB3 H 2.11 . 2 21 . 9 GLU HG2 H 2.32 . 1 22 . 9 GLU HG3 H 2.37 . 2 23 . 9 GLU CA C 56.5 . 1 24 . 9 GLU CG C 35.9 . 1 25 . 9 GLU N N 120.4 . 1 26 . 10 SER H H 8.48 . 1 27 . 10 SER HA H 4.48 . 1 28 . 10 SER HB2 H 3.90 . 2 29 . 10 SER HB3 H 3.95 . 2 30 . 10 SER CA C 58.3 . 1 31 . 10 SER CB C 63.6 . 1 32 . 10 SER N N 116.2 . 1 33 . 11 ILE H H 8.29 . 1 34 . 11 ILE HA H 4.20 . 1 35 . 11 ILE HB H 1.94 . 1 36 . 11 ILE HG12 H 1.20 . 2 37 . 11 ILE HG13 H 1.45 . 2 38 . 11 ILE HG2 H 0.94 . 1 39 . 11 ILE HD1 H 0.86 . 1 40 . 11 ILE CA C 63.0 . 1 41 . 11 ILE CB C 38.2 . 1 42 . 11 ILE CG1 C 27.6 . 1 43 . 11 ILE CG2 C 17.4 . 1 44 . 11 ILE CD1 C 13.2 . 1 45 . 11 ILE N N 122.6 . 1 46 . 12 LYS H H 8.18 . 1 47 . 12 LYS HA H 4.28 . 1 48 . 12 LYS HB2 H 1.81 . 1 49 . 12 LYS HB3 H 1.81 . 1 50 . 12 LYS HG2 H 1.43 . 1 51 . 12 LYS HG3 H 1.43 . 1 52 . 12 LYS HD2 H 1.66 . 1 53 . 12 LYS HD3 H 1.66 . 1 54 . 12 LYS HE2 H 3.00 . 1 55 . 12 LYS HE3 H 3.00 . 1 56 . 12 LYS CA C 57.4 . 1 57 . 12 LYS CB C 32.8 . 1 58 . 12 LYS CG C 24.8 . 1 59 . 12 LYS CD C 29.1 . 1 60 . 12 LYS CE C 41.9 . 1 61 . 12 LYS N N 123.7 . 1 62 . 13 ASP H H 8.29 . 1 63 . 13 ASP HA H 4.75 . 1 64 . 13 ASP HB2 H 2.88 . 1 65 . 13 ASP HB3 H 2.88 . 1 66 . 13 ASP CA C 55.1 . 1 67 . 13 ASP N N 116.8 . 1 68 . 14 THR H H 7.61 . 1 69 . 14 THR HA H 4.40 . 1 70 . 14 THR HB H 4.75 . 1 71 . 14 THR HG2 H 0.87 . 1 72 . 14 THR CA C 61.2 . 1 73 . 14 THR N N 103.7 . 1 74 . 15 ASN H H 7.98 . 1 75 . 15 ASN HA H 5.36 . 1 76 . 15 ASN HB2 H 2.54 . 2 77 . 15 ASN HB3 H 3.12 . 2 78 . 15 ASN HD21 H 6.00 . 2 79 . 15 ASN HD22 H 7.43 . 2 80 . 15 ASN CA C 52.2 . 1 81 . 15 ASN CB C 41.0 . 1 82 . 15 ASN N N 120.7 . 1 83 . 15 ASN ND2 N 109.2 . 1 84 . 16 LEU H H 9.64 . 1 85 . 16 LEU HA H 5.06 . 1 86 . 16 LEU HB2 H 1.17 . 2 87 . 16 LEU HB3 H 2.07 . 2 88 . 16 LEU HG H 1.96 . 1 89 . 16 LEU HD1 H 0.84 . 2 90 . 16 LEU HD2 H 1.11 . 2 91 . 16 LEU CA C 53.7 . 1 92 . 16 LEU CB C 44.1 . 1 93 . 16 LEU CG C 27.0 . 1 94 . 16 LEU CD1 C 24.8 . 2 95 . 16 LEU CD2 C 27.3 . 2 96 . 16 LEU N N 127.1 . 1 97 . 17 TYR H H 9.31 . 1 98 . 17 TYR HA H 4.79 . 1 99 . 17 TYR HB2 H 2.63 . 2 100 . 17 TYR HB3 H 2.71 . 2 101 . 17 TYR HD1 H 6.34 . 1 102 . 17 TYR HD2 H 6.34 . 1 103 . 17 TYR HE1 H 6.37 . 1 104 . 17 TYR HE2 H 6.37 . 1 105 . 17 TYR CA C 55.9 . 1 106 . 17 TYR CB C 40.8 . 1 107 . 17 TYR CD1 C 132.6 . 1 108 . 17 TYR CD2 C 132.6 . 1 109 . 17 TYR CE1 C 117.7 . 1 110 . 17 TYR CE2 C 117.7 . 1 111 . 17 TYR N N 122.1 . 1 112 . 18 VAL H H 8.75 . 1 113 . 18 VAL HA H 5.05 . 1 114 . 18 VAL HB H 1.81 . 1 115 . 18 VAL HG1 H 0.77 . 2 116 . 18 VAL HG2 H 1.06 . 2 117 . 18 VAL CA C 60.0 . 1 118 . 18 VAL CB C 34.3 . 1 119 . 18 VAL CG1 C 21.2 . 2 120 . 18 VAL CG2 C 22.1 . 2 121 . 18 VAL N N 129.8 . 1 122 . 19 THR H H 8.82 . 1 123 . 19 THR HA H 5.04 . 1 124 . 19 THR HB H 4.21 . 1 125 . 19 THR HG2 H 0.79 . 1 126 . 19 THR CA C 59.3 . 1 127 . 19 THR CB C 71.5 . 1 128 . 19 THR CG2 C 22.5 . 1 129 . 19 THR N N 114.6 . 1 130 . 20 ASN H H 8.33 . 1 131 . 20 ASN HA H 4.32 . 1 132 . 20 ASN HB2 H 3.17 . 1 133 . 20 ASN HB3 H 3.17 . 1 134 . 20 ASN CA C 53.6 . 1 135 . 20 ASN CB C 37.1 . 1 136 . 20 ASN N N 113.0 . 1 137 . 21 LEU H H 8.22 . 1 138 . 21 LEU HA H 4.14 . 1 139 . 21 LEU HB2 H 1.18 . 2 140 . 21 LEU HB3 H 1.23 . 2 141 . 21 LEU HG H 1.46 . 1 142 . 21 LEU HD1 H 0.89 . 2 143 . 21 LEU HD2 H 0.60 . 2 144 . 21 LEU CA C 53.7 . 1 145 . 21 LEU CB C 41.0 . 1 146 . 21 LEU CG C 26.8 . 1 147 . 21 LEU CD1 C 24.1 . 2 148 . 21 LEU CD2 C 27.2 . 2 149 . 21 LEU N N 117.3 . 1 150 . 22 PRO HA H 4.54 . 1 151 . 22 PRO HB2 H 1.91 . 2 152 . 22 PRO HB3 H 2.44 . 2 153 . 22 PRO HG2 H 2.04 . 1 154 . 22 PRO HG3 H 2.04 . 1 155 . 22 PRO HD2 H 3.40 . 2 156 . 22 PRO HD3 H 3.82 . 2 157 . 22 PRO CA C 62.5 . 1 158 . 22 PRO CB C 32.2 . 1 159 . 22 PRO CD C 49.4 . 1 160 . 23 ARG H H 8.92 . 1 161 . 23 ARG HA H 3.94 . 1 162 . 23 ARG HB2 H 1.82 . 2 163 . 23 ARG HB3 H 2.08 . 2 164 . 23 ARG HG2 H 1.60 . 2 165 . 23 ARG HG3 H 1.82 . 2 166 . 23 ARG HD2 H 3.17 . 1 167 . 23 ARG HD3 H 3.17 . 1 168 . 23 ARG HE H 7.28 . 1 169 . 23 ARG CA C 57.8 . 1 170 . 23 ARG CB C 28.9 . 1 171 . 23 ARG CG C 27.9 . 1 172 . 23 ARG CD C 42.8 . 1 173 . 23 ARG N N 120.1 . 1 174 . 23 ARG NE N 113.2 . 1 175 . 24 THR H H 7.06 . 1 176 . 24 THR HA H 4.27 . 1 177 . 24 THR HB H 4.65 . 1 178 . 24 THR HG2 H 1.18 . 1 179 . 24 THR CA C 60.1 . 1 180 . 24 THR CB C 68.5 . 1 181 . 24 THR CG2 C 21.5 . 1 182 . 24 THR N N 103.5 . 1 183 . 25 ILE H H 7.22 . 1 184 . 25 ILE HA H 4.35 . 1 185 . 25 ILE HB H 2.06 . 1 186 . 25 ILE HG12 H 1.28 . 2 187 . 25 ILE HG13 H 1.68 . 2 188 . 25 ILE HG2 H 0.88 . 1 189 . 25 ILE HD1 H 0.97 . 1 190 . 25 ILE CA C 59.1 . 1 191 . 25 ILE CB C 39.2 . 1 192 . 25 ILE CG1 C 28.5 . 1 193 . 25 ILE CG2 C 16.6 . 1 194 . 25 ILE CD1 C 14.8 . 1 195 . 25 ILE N N 121.9 . 1 196 . 26 THR H H 6.91 . 1 197 . 26 THR HA H 4.71 . 1 198 . 26 THR HB H 4.67 . 1 199 . 26 THR HG2 H 1.35 . 1 200 . 26 THR CA C 58.4 . 1 201 . 26 THR CB C 73.1 . 1 202 . 26 THR CG2 C 21.8 . 1 203 . 26 THR N N 113.3 . 1 204 . 27 ASP H H 8.95 . 1 205 . 27 ASP HA H 4.17 . 1 206 . 27 ASP HB2 H 2.64 . 1 207 . 27 ASP HB3 H 2.64 . 1 208 . 27 ASP CA C 58.5 . 1 209 . 27 ASP CB C 40.6 . 1 210 . 27 ASP N N 122.2 . 1 211 . 28 ASP H H 8.37 . 1 212 . 28 ASP HA H 4.45 . 1 213 . 28 ASP HB2 H 2.60 . 2 214 . 28 ASP HB3 H 2.70 . 2 215 . 28 ASP CA C 57.0 . 1 216 . 28 ASP CB C 40.4 . 1 217 . 28 ASP N N 116.6 . 1 218 . 29 GLN H H 7.77 . 1 219 . 29 GLN HA H 4.18 . 1 220 . 29 GLN HB2 H 2.06 . 2 221 . 29 GLN HB3 H 2.23 . 2 222 . 29 GLN HG2 H 2.41 . 2 223 . 29 GLN HG3 H 2.52 . 2 224 . 29 GLN HE21 H 6.62 . 2 225 . 29 GLN HE22 H 7.45 . 2 226 . 29 GLN CA C 58.4 . 1 227 . 29 GLN CB C 29.0 . 1 228 . 29 GLN CG C 33.8 . 1 229 . 29 GLN N N 120.2 . 1 230 . 29 GLN NE2 N 109.1 . 1 231 . 30 LEU H H 8.31 . 1 232 . 30 LEU HA H 4.22 . 1 233 . 30 LEU HB2 H 1.57 . 2 234 . 30 LEU HB3 H 1.97 . 2 235 . 30 LEU HG H 1.76 . 1 236 . 30 LEU HD1 H 0.74 . 2 237 . 30 LEU HD2 H 0.75 . 2 238 . 30 LEU CA C 58.5 . 1 239 . 30 LEU CB C 42.0 . 1 240 . 30 LEU CG C 26.6 . 1 241 . 30 LEU CD1 C 24.6 . 2 242 . 30 LEU CD2 C 26.3 . 2 243 . 30 LEU N N 119.6 . 1 244 . 31 ASP H H 8.16 . 1 245 . 31 ASP HA H 4.37 . 1 246 . 31 ASP HB2 H 2.75 . 2 247 . 31 ASP HB3 H 2.95 . 2 248 . 31 ASP CA C 57.7 . 1 249 . 31 ASP CB C 40.3 . 1 250 . 31 ASP N N 119.5 . 1 251 . 32 THR H H 8.05 . 1 252 . 32 THR HA H 3.94 . 1 253 . 32 THR HB H 4.38 . 1 254 . 32 THR HG2 H 1.24 . 1 255 . 32 THR CA C 66.6 . 1 256 . 32 THR CB C 68.7 . 1 257 . 32 THR CG2 C 21.8 . 1 258 . 32 THR N N 117.4 . 1 259 . 33 ILE H H 8.12 . 1 260 . 33 ILE HA H 3.74 . 1 261 . 33 ILE HB H 1.75 . 1 262 . 33 ILE HG12 H 1.02 . 2 263 . 33 ILE HG13 H 1.95 . 2 264 . 33 ILE HG2 H 0.40 . 1 265 . 33 ILE HD1 H 0.83 . 1 266 . 33 ILE CA C 65.0 . 1 267 . 33 ILE CB C 40.0 . 1 268 . 33 ILE CG1 C 28.5 . 1 269 . 33 ILE CG2 C 18.0 . 1 270 . 33 ILE CD1 C 13.5 . 1 271 . 33 ILE N N 119.8 . 1 272 . 34 PHE H H 8.71 . 1 273 . 34 PHE HA H 4.46 . 1 274 . 34 PHE HB2 H 3.01 . 2 275 . 34 PHE HB3 H 3.38 . 2 276 . 34 PHE HD1 H 7.80 . 1 277 . 34 PHE HD2 H 7.80 . 1 278 . 34 PHE HE1 H 7.01 . 1 279 . 34 PHE HE2 H 7.01 . 1 280 . 34 PHE CA C 61.0 . 1 281 . 34 PHE CB C 38.4 . 1 282 . 34 PHE CD1 C 132.3 . 1 283 . 34 PHE CD2 C 132.3 . 1 284 . 34 PHE CE1 C 130.4 . 1 285 . 34 PHE CE2 C 130.4 . 1 286 . 34 PHE N N 112.1 . 1 287 . 35 GLY H H 9.05 . 1 288 . 35 GLY HA2 H 4.29 . 2 289 . 35 GLY HA3 H 4.37 . 2 290 . 35 GLY CA C 46.6 . 1 291 . 35 GLY N N 114.8 . 1 292 . 36 LYS H H 6.70 . 1 293 . 36 LYS HA H 3.95 . 1 294 . 36 LYS HB2 H 1.08 . 2 295 . 36 LYS HB3 H 1.18 . 2 296 . 36 LYS HG2 H 0.93 . 2 297 . 36 LYS HG3 H 0.95 . 2 298 . 36 LYS HD2 H 1.54 . 1 299 . 36 LYS HD3 H 1.54 . 1 300 . 36 LYS HE2 H 2.92 . 1 301 . 36 LYS HE3 H 2.92 . 1 302 . 36 LYS CA C 57.2 . 1 303 . 36 LYS CB C 32.1 . 1 304 . 36 LYS CG C 24.1 . 1 305 . 36 LYS CD C 28.8 . 1 306 . 36 LYS CE C 41.6 . 1 307 . 36 LYS N N 115.7 . 1 308 . 37 TYR H H 6.86 . 1 309 . 37 TYR HA H 4.41 . 1 310 . 37 TYR HB2 H 2.59 . 2 311 . 37 TYR HB3 H 3.36 . 2 312 . 37 TYR HD1 H 7.15 . 1 313 . 37 TYR HD2 H 7.15 . 1 314 . 37 TYR HE1 H 6.77 . 1 315 . 37 TYR HE2 H 6.77 . 1 316 . 37 TYR CA C 58.4 . 1 317 . 37 TYR CB C 38.7 . 1 318 . 37 TYR CD1 C 132.4 . 1 319 . 37 TYR CD2 C 132.4 . 1 320 . 37 TYR CE1 C 118.7 . 1 321 . 37 TYR CE2 C 118.7 . 1 322 . 37 TYR N N 113.5 . 1 323 . 38 GLY H H 7.34 . 1 324 . 38 GLY HA2 H 3.97 . 2 325 . 38 GLY HA3 H 4.23 . 2 326 . 38 GLY CA C 44.7 . 1 327 . 38 GLY N N 103.5 . 1 328 . 39 SER H H 8.30 . 1 329 . 39 SER HA H 4.57 . 1 330 . 39 SER HB2 H 3.94 . 1 331 . 39 SER HB3 H 3.94 . 1 332 . 39 SER CA C 57.6 . 1 333 . 39 SER CB C 63.3 . 1 334 . 39 SER N N 114.1 . 1 335 . 40 ILE H H 8.79 . 1 336 . 40 ILE HA H 3.82 . 1 337 . 40 ILE HB H 1.68 . 1 338 . 40 ILE HG2 H 0.57 . 1 339 . 40 ILE HD1 H 0.72 . 1 340 . 40 ILE CA C 61.5 . 1 341 . 40 ILE CB C 38.2 . 1 342 . 40 ILE CG2 C 17.9 . 1 343 . 40 ILE CD1 C 14.2 . 1 344 . 40 ILE N N 127.5 . 1 345 . 41 VAL H H 9.02 . 1 346 . 41 VAL HA H 4.21 . 1 347 . 41 VAL HB H 1.92 . 1 348 . 41 VAL HG1 H 0.74 . 2 349 . 41 VAL HG2 H 0.88 . 2 350 . 41 VAL CA C 61.9 . 1 351 . 41 VAL CB C 32.7 . 1 352 . 41 VAL CG1 C 19.7 . 2 353 . 41 VAL CG2 C 20.9 . 2 354 . 41 VAL N N 125.7 . 1 355 . 42 GLN H H 7.48 . 1 356 . 42 GLN HA H 4.49 . 1 357 . 42 GLN HB2 H 1.87 . 2 358 . 42 GLN HB3 H 1.99 . 2 359 . 42 GLN HG2 H 2.22 . 2 360 . 42 GLN HG3 H 2.34 . 2 361 . 42 GLN HE21 H 6.79 . 2 362 . 42 GLN HE22 H 7.55 . 2 363 . 42 GLN CA C 55.8 . 1 364 . 42 GLN CB C 32.5 . 1 365 . 42 GLN CG C 33.8 . 1 366 . 42 GLN N N 119.0 . 1 367 . 42 GLN NE2 N 111.6 . 1 368 . 43 LYS H H 8.61 . 1 369 . 43 LYS HA H 5.08 . 1 370 . 43 LYS HB2 H 1.62 . 2 371 . 43 LYS HB3 H 1.70 . 2 372 . 43 LYS HG2 H 1.34 . 2 373 . 43 LYS HG3 H 1.40 . 2 374 . 43 LYS HD2 H 1.57 . 1 375 . 43 LYS HD3 H 1.57 . 1 376 . 43 LYS HE2 H 2.88 . 2 377 . 43 LYS HE3 H 3.04 . 2 378 . 43 LYS CA C 54.8 . 1 379 . 43 LYS CB C 35.2 . 1 380 . 43 LYS CG C 23.6 . 1 381 . 43 LYS CD C 29.6 . 1 382 . 43 LYS CE C 41.1 . 1 383 . 43 LYS N N 121.7 . 1 384 . 44 ASN H H 8.87 . 1 385 . 44 ASN HA H 4.98 . 1 386 . 44 ASN HB2 H 2.72 . 2 387 . 44 ASN HB3 H 2.87 . 2 388 . 44 ASN HD21 H 6.68 . 2 389 . 44 ASN HD22 H 7.39 . 2 390 . 44 ASN CA C 52.8 . 1 391 . 44 ASN CB C 41.2 . 1 392 . 44 ASN N N 118.3 . 1 393 . 44 ASN ND2 N 109.7 . 1 394 . 45 ILE H H 8.97 . 1 395 . 45 ILE HA H 4.03 . 1 396 . 45 ILE HB H 1.80 . 1 397 . 45 ILE HG12 H 0.63 . 2 398 . 45 ILE HG13 H 1.64 . 2 399 . 45 ILE HG2 H 0.83 . 1 400 . 45 ILE HD1 H 0.75 . 1 401 . 45 ILE CA C 61.8 . 1 402 . 45 ILE CB C 38.9 . 1 403 . 45 ILE CG1 C 29.8 . 1 404 . 45 ILE CG2 C 17.4 . 1 405 . 45 ILE CD1 C 13.5 . 1 406 . 45 ILE N N 126.4 . 1 407 . 46 LEU H H 7.69 . 1 408 . 46 LEU HA H 4.54 . 1 409 . 46 LEU HB2 H 1.59 . 1 410 . 46 LEU HB3 H 1.59 . 1 411 . 46 LEU HG H 1.69 . 1 412 . 46 LEU HD1 H 0.98 . 2 413 . 46 LEU HD2 H 1.03 . 2 414 . 46 LEU CA C 55.6 . 1 415 . 46 LEU CB C 41.2 . 1 416 . 46 LEU CG C 28.4 . 1 417 . 46 LEU CD1 C 23.1 . 2 418 . 46 LEU CD2 C 25.0 . 2 419 . 46 LEU N N 127.1 . 1 420 . 47 ARG H H 9.09 . 1 421 . 47 ARG CB C 33.4 . 1 422 . 47 ARG N N 123.3 . 1 423 . 48 ASP H H 8.66 . 1 424 . 48 ASP HA H 4.54 . 1 425 . 48 ASP HB2 H 2.61 . 2 426 . 48 ASP HB3 H 2.97 . 2 427 . 48 ASP CA C 54.3 . 1 428 . 48 ASP CB C 42.9 . 1 429 . 48 ASP N N 123.2 . 1 430 . 49 LYS H H 8.97 . 1 431 . 49 LYS HA H 4.04 . 1 432 . 49 LYS HB2 H 1.90 . 1 433 . 49 LYS HB3 H 1.90 . 1 434 . 49 LYS HG2 H 1.51 . 1 435 . 49 LYS HG3 H 1.51 . 1 436 . 49 LYS HD2 H 1.73 . 1 437 . 49 LYS HD3 H 1.73 . 1 438 . 49 LYS HE3 H 3.04 . 1 439 . 49 LYS CA C 58.5 . 1 440 . 49 LYS CB C 32.5 . 1 441 . 49 LYS CG C 24.9 . 1 442 . 49 LYS CD C 29.1 . 1 443 . 49 LYS CE C 41.9 . 1 444 . 49 LYS N N 127.8 . 1 445 . 50 LEU H H 8.47 . 1 446 . 50 LEU HA H 4.39 . 1 447 . 50 LEU HB2 H 1.69 . 2 448 . 50 LEU HB3 H 1.93 . 2 449 . 50 LEU HG H 1.64 . 1 450 . 50 LEU HD1 H 0.91 . 2 451 . 50 LEU HD2 H 0.98 . 2 452 . 50 LEU CA C 56.9 . 1 453 . 50 LEU CB C 42.1 . 1 454 . 50 LEU CG C 27.3 . 1 455 . 50 LEU CD1 C 23.4 . 2 456 . 50 LEU CD2 C 24.4 . 2 457 . 50 LEU N N 117.8 . 1 458 . 51 THR H H 8.20 . 1 459 . 51 THR HA H 4.45 . 1 460 . 51 THR HB H 4.38 . 1 461 . 51 THR HG2 H 1.25 . 1 462 . 51 THR CA C 61.7 . 1 463 . 51 THR CB C 71.3 . 1 464 . 51 THR CG2 C 21.0 . 1 465 . 51 THR N N 106.4 . 1 466 . 52 GLY H H 8.26 . 1 467 . 52 GLY HA2 H 3.86 . 2 468 . 52 GLY HA3 H 4.25 . 2 469 . 52 GLY CA C 45.6 . 1 470 . 52 GLY N N 110.7 . 1 471 . 53 ARG H H 7.88 . 1 472 . 53 ARG HA H 4.66 . 1 473 . 53 ARG HB2 H 1.71 . 2 474 . 53 ARG HB3 H 1.91 . 2 475 . 53 ARG HG2 H 1.73 . 1 476 . 53 ARG HG3 H 1.73 . 1 477 . 53 ARG HD2 H 3.24 . 1 478 . 53 ARG HD3 H 3.24 . 1 479 . 53 ARG CA C 54.5 . 1 480 . 53 ARG CB C 30.2 . 1 481 . 53 ARG CG C 27.2 . 1 482 . 53 ARG CD C 43.2 . 1 483 . 53 ARG N N 120.8 . 1 484 . 54 PRO HA H 4.45 . 1 485 . 54 PRO HB2 H 1.96 . 2 486 . 54 PRO HB3 H 2.33 . 2 487 . 54 PRO HG2 H 2.04 . 2 488 . 54 PRO HG3 H 2.08 . 2 489 . 54 PRO HD2 H 3.67 . 2 490 . 54 PRO HD3 H 3.85 . 2 491 . 54 PRO CA C 63.5 . 1 492 . 54 PRO CB C 32.1 . 1 493 . 54 PRO CG C 27.4 . 1 494 . 55 ARG H H 8.27 . 1 495 . 55 ARG HA H 4.42 . 1 496 . 55 ARG HB2 H 1.53 . 2 497 . 55 ARG HB3 H 2.05 . 2 498 . 55 ARG HG2 H 1.53 . 2 499 . 55 ARG HG3 H 1.71 . 2 500 . 55 ARG HD2 H 3.01 . 2 501 . 55 ARG HD3 H 3.21 . 2 502 . 55 ARG CA C 56.2 . 1 503 . 55 ARG CB C 32.0 . 1 504 . 55 ARG CG C 27.5 . 1 505 . 55 ARG CD C 43.6 . 1 506 . 55 ARG N N 119.4 . 1 507 . 56 GLY H H 8.64 . 1 508 . 56 GLY HA2 H 3.40 . 2 509 . 56 GLY HA3 H 4.37 . 2 510 . 56 GLY CA C 45.6 . 1 511 . 56 GLY N N 106.8 . 1 512 . 57 VAL H H 6.98 . 1 513 . 57 VAL HA H 5.24 . 1 514 . 57 VAL HB H 1.69 . 1 515 . 57 VAL HG1 H 0.85 . 2 516 . 57 VAL HG2 H 0.74 . 2 517 . 57 VAL CA C 58.8 . 1 518 . 57 VAL CB C 35.4 . 1 519 . 57 VAL CG1 C 20.8 . 2 520 . 57 VAL CG2 C 21.9 . 2 521 . 57 VAL N N 114.7 . 1 522 . 58 ALA H H 9.21 . 1 523 . 58 ALA HA H 5.19 . 1 524 . 58 ALA HB H 0.98 . 1 525 . 58 ALA CA C 50.7 . 1 526 . 58 ALA CB C 23.8 . 1 527 . 58 ALA N N 126.7 . 1 528 . 59 PHE H H 8.38 . 1 529 . 59 PHE HA H 5.86 . 1 530 . 59 PHE HB2 H 2.78 . 2 531 . 59 PHE HB3 H 3.25 . 2 532 . 59 PHE HD1 H 7.23 . 1 533 . 59 PHE HD2 H 7.23 . 1 534 . 59 PHE HE1 H 7.28 . 1 535 . 59 PHE HE2 H 7.28 . 1 536 . 59 PHE CA C 56.3 . 1 537 . 59 PHE CB C 41.9 . 1 538 . 59 PHE CD1 C 132.2 . 1 539 . 59 PHE CD2 C 132.2 . 1 540 . 59 PHE CE1 C 131.1 . 1 541 . 59 PHE CE2 C 131.1 . 1 542 . 59 PHE N N 116.1 . 1 543 . 60 VAL H H 8.49 . 1 544 . 60 VAL HA H 4.13 . 1 545 . 60 VAL HB H 1.33 . 1 546 . 60 VAL HG1 H 0.05 . 2 547 . 60 VAL HG2 H 0.22 . 2 548 . 60 VAL CA C 61.9 . 1 549 . 60 VAL CB C 36.0 . 1 550 . 60 VAL CG1 C 20.3 . 2 551 . 60 VAL CG2 C 20.8 . 2 552 . 60 VAL N N 121.5 . 1 553 . 61 ARG H H 8.85 . 1 554 . 61 ARG HA H 5.59 . 1 555 . 61 ARG HD2 H 3.03 . 1 556 . 61 ARG HD3 H 3.03 . 1 557 . 61 ARG CA C 54.3 . 1 558 . 61 ARG CB C 35.9 . 1 559 . 61 ARG CD C 44.2 . 1 560 . 61 ARG N N 127.5 . 1 561 . 62 TYR H H 8.29 . 1 562 . 62 TYR HA H 5.28 . 1 563 . 62 TYR HB2 H 2.58 . 2 564 . 62 TYR HB3 H 4.10 . 2 565 . 62 TYR HD1 H 6.94 . 1 566 . 62 TYR HD2 H 6.94 . 1 567 . 62 TYR HE1 H 6.64 . 1 568 . 62 TYR HE2 H 6.64 . 1 569 . 62 TYR CA C 58.4 . 1 570 . 62 TYR CB C 42.1 . 1 571 . 62 TYR CD1 C 132.7 . 1 572 . 62 TYR CD2 C 132.7 . 1 573 . 62 TYR CE1 C 117.2 . 1 574 . 62 TYR CE2 C 117.2 . 1 575 . 62 TYR N N 125.7 . 1 576 . 63 ASN H H 8.75 . 1 577 . 63 ASN HA H 4.61 . 1 578 . 63 ASN HB2 H 2.85 . 2 579 . 63 ASN HB3 H 3.36 . 2 580 . 63 ASN HD21 H 6.98 . 2 581 . 63 ASN HD22 H 8.24 . 2 582 . 63 ASN CA C 55.6 . 1 583 . 63 ASN CB C 40.3 . 1 584 . 63 ASN N N 118.0 . 1 585 . 63 ASN ND2 N 114.3 . 1 586 . 64 LYS H H 8.27 . 1 587 . 64 LYS HA H 4.88 . 1 588 . 64 LYS HB2 H 1.60 . 2 589 . 64 LYS HB3 H 2.26 . 2 590 . 64 LYS HG2 H 1.48 . 1 591 . 64 LYS HG3 H 1.48 . 1 592 . 64 LYS HD2 H 1.74 . 1 593 . 64 LYS HD3 H 1.74 . 1 594 . 64 LYS HE2 H 3.03 . 1 595 . 64 LYS HE3 H 3.03 . 1 596 . 64 LYS CA C 53.9 . 1 597 . 64 LYS CB C 36.1 . 1 598 . 64 LYS CG C 24.9 . 1 599 . 64 LYS CD C 29.1 . 1 600 . 64 LYS CE C 41.8 . 1 601 . 64 LYS N N 113.0 . 1 602 . 65 ARG H H 9.31 . 1 603 . 65 ARG HA H 3.98 . 1 604 . 65 ARG HD3 H 3.27 . 1 605 . 65 ARG HE H 7.51 . 1 606 . 65 ARG CA C 59.3 . 1 607 . 65 ARG CB C 29.8 . 1 608 . 65 ARG CD C 43.4 . 1 609 . 65 ARG N N 125.0 . 1 610 . 65 ARG NE N 114.9 . 1 611 . 66 GLU H H 10.05 . 1 612 . 66 GLU HA H 4.04 . 1 613 . 66 GLU HG2 H 2.35 . 1 614 . 66 GLU HG3 H 2.53 . 2 615 . 66 GLU CA C 60.1 . 1 616 . 66 GLU CB C 28.5 . 1 617 . 66 GLU CG C 36.7 . 1 618 . 66 GLU N N 119.5 . 1 619 . 67 GLU H H 6.85 . 1 620 . 67 GLU HA H 3.92 . 1 621 . 67 GLU CA C 58.1 . 1 622 . 67 GLU CB C 29.3 . 1 623 . 67 GLU N N 119.1 . 1 624 . 68 ALA H H 6.72 . 1 625 . 68 ALA HA H 3.85 . 1 626 . 68 ALA HB H 1.59 . 1 627 . 68 ALA CA C 54.9 . 1 628 . 68 ALA CB C 17.7 . 1 629 . 68 ALA N N 118.3 . 1 630 . 69 GLN H H 8.00 . 1 631 . 69 GLN HA H 3.92 . 1 632 . 69 GLN HB2 H 2.10 . 1 633 . 69 GLN HB3 H 2.10 . 1 634 . 69 GLN HG2 H 2.45 . 1 635 . 69 GLN HG3 H 2.45 . 1 636 . 69 GLN CA C 58.4 . 1 637 . 69 GLN CB C 28.4 . 1 638 . 69 GLN CG C 33.7 . 1 639 . 69 GLN N N 113.6 . 1 640 . 70 GLU H H 7.76 . 1 641 . 70 GLU HA H 4.01 . 1 642 . 70 GLU HB2 H 2.18 . 2 643 . 70 GLU HB3 H 2.31 . 2 644 . 70 GLU HG2 H 2.54 . 1 645 . 70 GLU HG3 H 2.54 . 1 646 . 70 GLU CA C 58.9 . 1 647 . 70 GLU CB C 28.3 . 1 648 . 70 GLU CG C 35.0 . 1 649 . 70 GLU N N 120.8 . 1 650 . 71 ALA H H 7.89 . 1 651 . 71 ALA HA H 3.09 . 1 652 . 71 ALA HB H 1.57 . 1 653 . 71 ALA CA C 55.2 . 1 654 . 71 ALA CB C 19.0 . 1 655 . 71 ALA N N 121.9 . 1 656 . 72 ILE H H 7.96 . 1 657 . 72 ILE HA H 3.29 . 1 658 . 72 ILE HG12 H 1.67 . 1 659 . 72 ILE HG13 H 1.67 . 1 660 . 72 ILE HG2 H 0.92 . 1 661 . 72 ILE HD1 H 0.81 . 1 662 . 72 ILE CA C 66.4 . 1 663 . 72 ILE CB C 38.6 . 1 664 . 72 ILE CG1 C 28.2 . 1 665 . 72 ILE CG2 C 17.3 . 1 666 . 72 ILE CD1 C 14.0 . 1 667 . 72 ILE N N 116.7 . 1 668 . 73 SER H H 7.80 . 1 669 . 73 SER HA H 4.11 . 1 670 . 73 SER HB2 H 3.90 . 1 671 . 73 SER HB3 H 3.90 . 1 672 . 73 SER CA C 61.2 . 1 673 . 73 SER CB C 63.0 . 1 674 . 73 SER N N 112.5 . 1 675 . 74 ALA H H 7.88 . 1 676 . 74 ALA HA H 4.19 . 1 677 . 74 ALA HB H 1.10 . 1 678 . 74 ALA CA C 53.8 . 1 679 . 74 ALA CB C 20.4 . 1 680 . 74 ALA N N 120.4 . 1 681 . 75 LEU H H 7.87 . 1 682 . 75 LEU HA H 4.47 . 1 683 . 75 LEU HD1 H 0.66 . 2 684 . 75 LEU HD2 H 0.21 . 2 685 . 75 LEU CA C 54.7 . 1 686 . 75 LEU CB C 44.9 . 1 687 . 75 LEU CD1 C 22.4 . 2 688 . 75 LEU CD2 C 27.3 . 2 689 . 75 LEU N N 113.4 . 1 690 . 76 ASN H H 8.02 . 1 691 . 76 ASN HA H 4.34 . 1 692 . 76 ASN HB2 H 2.92 . 2 693 . 76 ASN HB3 H 3.03 . 2 694 . 76 ASN HD21 H 7.03 . 2 695 . 76 ASN HD22 H 7.96 . 2 696 . 76 ASN CA C 56.2 . 1 697 . 76 ASN CB C 38.9 . 1 698 . 76 ASN N N 116.0 . 1 699 . 76 ASN ND2 N 115.3 . 1 700 . 77 ASN H H 8.97 . 1 701 . 77 ASN HA H 4.39 . 1 702 . 77 ASN HB2 H 2.95 . 2 703 . 77 ASN HB3 H 3.17 . 2 704 . 77 ASN HD21 H 6.81 . 2 705 . 77 ASN HD22 H 7.62 . 2 706 . 77 ASN CA C 55.1 . 1 707 . 77 ASN CB C 37.7 . 1 708 . 77 ASN N N 119.4 . 1 709 . 77 ASN ND2 N 112.8 . 1 710 . 78 VAL H H 7.70 . 1 711 . 78 VAL HA H 4.22 . 1 712 . 78 VAL HB H 2.03 . 1 713 . 78 VAL HG1 H 0.85 . 1 714 . 78 VAL HG2 H 0.85 . 1 715 . 78 VAL CA C 61.4 . 1 716 . 78 VAL CB C 34.3 . 1 717 . 78 VAL CG1 C 21.1 . 1 718 . 78 VAL CG2 C 21.1 . 1 719 . 78 VAL N N 119.8 . 1 720 . 79 ILE H H 8.64 . 1 721 . 79 ILE HA H 4.41 . 1 722 . 79 ILE HB H 1.69 . 1 723 . 79 ILE HG12 H 0.30 . 2 724 . 79 ILE HG13 H 1.57 . 2 725 . 79 ILE HG2 H 0.67 . 1 726 . 79 ILE HD1 H 0.78 . 1 727 . 79 ILE CA C 58.9 . 1 728 . 79 ILE CG1 C 27.9 . 1 729 . 79 ILE CG2 C 16.6 . 1 730 . 79 ILE CD1 C 13.2 . 1 731 . 79 ILE N N 128.4 . 1 732 . 80 PRO HA H 4.45 . 1 733 . 80 PRO CA C 62.2 . 1 734 . 80 PRO CB C 32.1 . 1 735 . 81 GLU H H 8.64 . 1 736 . 81 GLU HA H 4.06 . 1 737 . 81 GLU HB2 H 1.91 . 2 738 . 81 GLU HB3 H 2.01 . 2 739 . 81 GLU HG2 H 2.30 . 1 740 . 81 GLU HG3 H 2.30 . 1 741 . 81 GLU CA C 58.2 . 1 742 . 81 GLU CB C 28.9 . 1 743 . 81 GLU CG C 35.5 . 1 744 . 81 GLU N N 121.6 . 1 745 . 82 GLY H H 8.84 . 1 746 . 82 GLY HA2 H 3.73 . 2 747 . 82 GLY HA3 H 4.21 . 2 748 . 82 GLY CA C 45.1 . 1 749 . 82 GLY N N 113.9 . 1 750 . 83 GLY H H 8.52 . 1 751 . 83 GLY HA2 H 3.56 . 2 752 . 83 GLY HA3 H 4.56 . 2 753 . 83 GLY CA C 43.6 . 1 754 . 83 GLY N N 107.9 . 1 755 . 84 SER H H 8.99 . 1 756 . 84 SER HA H 4.72 . 1 757 . 84 SER HB2 H 3.79 . 2 758 . 84 SER HB3 H 3.93 . 2 759 . 84 SER CA C 58.1 . 1 760 . 84 SER CB C 65.0 . 1 761 . 84 SER N N 110.4 . 1 762 . 85 GLN H H 7.83 . 1 763 . 85 GLN HA H 4.92 . 1 764 . 85 GLN HB2 H 1.90 . 2 765 . 85 GLN HB3 H 2.11 . 2 766 . 85 GLN HG2 H 2.35 . 1 767 . 85 GLN HG3 H 2.35 . 1 768 . 85 GLN HE21 H 6.79 . 2 769 . 85 GLN HE22 H 7.41 . 2 770 . 85 GLN CA C 52.6 . 1 771 . 85 GLN CG C 33.2 . 1 772 . 85 GLN N N 120.3 . 1 773 . 85 GLN NE2 N 111.6 . 1 774 . 86 PRO HA H 4.14 . 1 775 . 86 PRO HB2 H 1.78 . 1 776 . 86 PRO HB3 H 1.78 . 1 777 . 86 PRO CA C 62.0 . 1 778 . 86 PRO CB C 31.3 . 1 779 . 87 LEU H H 8.47 . 1 780 . 87 LEU HA H 4.39 . 1 781 . 87 LEU HB2 H 1.29 . 2 782 . 87 LEU HB3 H 2.23 . 2 783 . 87 LEU HG H 0.86 . 1 784 . 87 LEU HD1 H 0.83 . 2 785 . 87 LEU HD2 H 0.85 . 2 786 . 87 LEU CA C 55.1 . 1 787 . 87 LEU CB C 43.4 . 1 788 . 87 LEU CG C 21.9 . 1 789 . 87 LEU CD1 C 24.2 . 2 790 . 87 LEU CD2 C 26.1 . 2 791 . 87 LEU N N 122.2 . 1 792 . 88 SER H H 7.73 . 1 793 . 88 SER HA H 5.17 . 1 794 . 88 SER HB2 H 3.71 . 2 795 . 88 SER HB3 H 3.96 . 2 796 . 88 SER CA C 56.9 . 1 797 . 88 SER CB C 63.1 . 1 798 . 88 SER N N 115.6 . 1 799 . 89 VAL H H 8.82 . 1 800 . 89 VAL HA H 4.66 . 1 801 . 89 VAL HB H 1.93 . 1 802 . 89 VAL HG1 H 1.02 . 1 803 . 89 VAL HG2 H 1.02 . 1 804 . 89 VAL CA C 61.5 . 1 805 . 89 VAL CB C 34.9 . 1 806 . 89 VAL CG1 C 21.8 . 2 807 . 89 VAL CG2 C 24.3 . 2 808 . 89 VAL N N 126.6 . 1 809 . 90 ARG H H 8.25 . 1 810 . 90 ARG HA H 4.55 . 1 811 . 90 ARG HB2 H 1.89 . 2 812 . 90 ARG HB3 H 1.97 . 2 813 . 90 ARG HG2 H 1.67 . 1 814 . 90 ARG HG3 H 1.67 . 1 815 . 90 ARG HD2 H 3.23 . 1 816 . 90 ARG HD3 H 3.23 . 1 817 . 90 ARG CA C 53.7 . 1 818 . 90 ARG CB C 30.5 . 1 819 . 90 ARG CG C 26.8 . 1 820 . 90 ARG CD C 43.3 . 1 821 . 90 ARG N N 121.6 . 1 822 . 91 LEU H H 8.99 . 1 823 . 91 LEU HA H 4.54 . 1 824 . 91 LEU HB2 H 1.68 . 1 825 . 91 LEU HB3 H 1.68 . 1 826 . 91 LEU HD1 H 0.82 . 2 827 . 91 LEU HD2 H 0.95 . 2 828 . 91 LEU CA C 56.1 . 1 829 . 91 LEU CB C 41.7 . 1 830 . 91 LEU CD1 C 23.1 . 2 831 . 91 LEU CD2 C 25.4 . 2 832 . 91 LEU N N 126.1 . 1 833 . 92 ALA H H 8.82 . 1 834 . 92 ALA HA H 4.24 . 1 835 . 92 ALA HB H 1.48 . 1 836 . 92 ALA CA C 53.2 . 1 837 . 92 ALA CB C 19.4 . 1 838 . 92 ALA N N 121.7 . 1 839 . 93 GLU H H 8.58 . 1 840 . 93 GLU HA H 4.33 . 1 841 . 93 GLU HB2 H 1.92 . 2 842 . 93 GLU HB3 H 2.03 . 2 843 . 93 GLU HG2 H 2.27 . 1 844 . 93 GLU HG3 H 2.27 . 1 845 . 93 GLU CA C 55.9 . 1 846 . 93 GLU CB C 30.2 . 1 847 . 93 GLU CG C 35.7 . 1 848 . 93 GLU N N 119.5 . 1 849 . 94 GLU H H 8.39 . 1 850 . 94 GLU HA H 4.35 . 1 851 . 94 GLU HB2 H 1.88 . 2 852 . 94 GLU HB3 H 1.98 . 2 853 . 94 GLU HG2 H 2.19 . 1 854 . 94 GLU HG3 H 2.23 . 2 855 . 94 GLU CA C 56.3 . 1 856 . 94 GLU CB C 30.5 . 1 857 . 94 GLU CG C 35.8 . 1 858 . 94 GLU N N 122.2 . 1 859 . 95 HIS H H 8.61 . 1 860 . 95 HIS HA H 4.70 . 1 861 . 95 HIS HB2 H 3.14 . 2 862 . 95 HIS HB3 H 3.28 . 2 863 . 95 HIS HD2 H 7.27 . 1 864 . 95 HIS HE1 H 8.53 . 1 865 . 95 HIS CA C 55.2 . 1 866 . 95 HIS CB C 29.1 . 1 867 . 95 HIS CD2 C 119.9 . 1 868 . 95 HIS CE1 C 136.4 . 1 869 . 95 HIS N N 119.1 . 1 870 . 96 GLY H H 8.49 . 1 871 . 96 GLY N N 110.4 . 1 872 . 97 LYS H H 7.90 . 1 873 . 97 LYS HA H 4.17 . 1 874 . 97 LYS HB2 H 1.70 . 2 875 . 97 LYS HB3 H 1.82 . 2 876 . 97 LYS HG2 H 1.37 . 1 877 . 97 LYS HG3 H 1.37 . 1 878 . 97 LYS HD2 H 1.64 . 1 879 . 97 LYS HD3 H 1.64 . 1 880 . 97 LYS HE2 H 2.98 . 1 881 . 97 LYS HE3 H 2.98 . 1 882 . 97 LYS CA C 57.5 . 1 883 . 97 LYS CB C 33.6 . 1 884 . 97 LYS CG C 24.8 . 1 885 . 97 LYS CD C 29.1 . 1 886 . 97 LYS CE C 41.8 . 1 887 . 97 LYS N N 125.8 . 1 stop_ save_