data_4251 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Triple Resonance Assignment for Abl SH(32) and One in the Complex with a Consolidated Ligand ; _BMRB_accession_number 4251 _BMRB_flat_file_name bmr4251.str _Entry_type original _Submission_date 1998-10-19 _Accession_date 1998-10-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Rong . . 2 Cahill Sean . . 3 Cowburn David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 781 "13C chemical shifts" 443 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-11-26 original BMRB . stop_ _Original_release_date 1998-10-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99356753 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Rong . . 2 Cahill Sean . . 3 Cowburn David . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 14 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 187 _Page_last 188 _Year 1999 _Details . loop_ _Keyword Abl_SH(32) NMR_assignment consolidated_ligand stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title . _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 Wishart D. . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Abl_SH(32) _Saveframe_category molecular_system _Mol_system_name 'Src homology domain 3 and 2' _Abbreviation_common 'Abl SH(32)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Abl SH(32)' $Abl_SH(32) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Abl_SH(32) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Src homology domain 3 and 2' _Name_variant 'Abl SH(32)' _Abbreviation_common 'Abl SH(32)' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; GSPGGSLFVALYDFVASGDN TLSITKGEKLRVLGYNHNGE WAEAQTKNGQGWVPSNYITP VNSLEKHSWYHGPVSRNAAE YLLSSGINGSFLVRESESSP GQRSISLRYEGRVYHYRINT ASDGKLYVSSESRFNTLAEL VHHHSTVADGLITTLHYPAP KRGIRD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 59 GLY 2 60 SER 3 61 PRO 4 62 GLY 5 63 GLY 6 64 SER 7 65 LEU 8 66 PHE 9 67 VAL 10 68 ALA 11 69 LEU 12 70 TYR 13 71 ASP 14 72 PHE 15 73 VAL 16 74 ALA 17 75 SER 18 76 GLY 19 77 ASP 20 78 ASN 21 79 THR 22 80 LEU 23 81 SER 24 82 ILE 25 83 THR 26 84 LYS 27 85 GLY 28 86 GLU 29 87 LYS 30 88 LEU 31 89 ARG 32 90 VAL 33 91 LEU 34 92 GLY 35 93 TYR 36 94 ASN 37 95 HIS 38 96 ASN 39 97 GLY 40 98 GLU 41 99 TRP 42 100 ALA 43 101 GLU 44 102 ALA 45 103 GLN 46 104 THR 47 105 LYS 48 106 ASN 49 107 GLY 50 108 GLN 51 109 GLY 52 110 TRP 53 111 VAL 54 112 PRO 55 113 SER 56 114 ASN 57 115 TYR 58 116 ILE 59 117 THR 60 118 PRO 61 119 VAL 62 120 ASN 63 121 SER 64 122 LEU 65 123 GLU 66 124 LYS 67 125 HIS 68 126 SER 69 127 TRP 70 128 TYR 71 129 HIS 72 130 GLY 73 131 PRO 74 132 VAL 75 133 SER 76 134 ARG 77 135 ASN 78 136 ALA 79 137 ALA 80 138 GLU 81 139 TYR 82 140 LEU 83 141 LEU 84 142 SER 85 143 SER 86 144 GLY 87 145 ILE 88 146 ASN 89 147 GLY 90 148 SER 91 149 PHE 92 150 LEU 93 151 VAL 94 152 ARG 95 153 GLU 96 154 SER 97 155 GLU 98 156 SER 99 157 SER 100 158 PRO 101 159 GLY 102 160 GLN 103 161 ARG 104 162 SER 105 163 ILE 106 164 SER 107 165 LEU 108 166 ARG 109 167 TYR 110 168 GLU 111 169 GLY 112 170 ARG 113 171 VAL 114 172 TYR 115 173 HIS 116 174 TYR 117 175 ARG 118 176 ILE 119 177 ASN 120 178 THR 121 179 ALA 122 180 SER 123 181 ASP 124 182 GLY 125 183 LYS 126 184 LEU 127 185 TYR 128 186 VAL 129 187 SER 130 188 SER 131 189 GLU 132 190 SER 133 191 ARG 134 192 PHE 135 193 ASN 136 194 THR 137 195 LEU 138 196 ALA 139 197 GLU 140 198 LEU 141 199 VAL 142 200 HIS 143 201 HIS 144 202 HIS 145 203 SER 146 204 THR 147 205 VAL 148 206 ALA 149 207 ASP 150 208 GLY 151 209 LEU 152 210 ILE 153 211 THR 154 212 THR 155 213 LEU 156 214 HIS 157 215 TYR 158 216 PRO 159 217 ALA 160 218 PRO 161 219 LYS 162 220 ARG 163 221 GLY 164 222 ILE 165 224 ARG 166 225 ASP stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4252 'Src homology domain 3 and 2' 100.00 166 100.00 100.00 1.04e-91 PDB 1AB2 'Three-Dimensional Solution Structure Of The Src Homology 2 Domain Of C-Abl' 63.86 109 99.06 99.06 1.80e-52 PDB 1OPK 'Structural Basis For The Auto-Inhibition Of C-Abl Tyrosine Kinase' 94.58 495 98.73 99.36 2.14e-86 PDB 1OPL 'Structural Basis For The Auto-Inhibition Of C-Abl Tyrosine Kinase' 94.58 537 98.73 99.36 3.04e-86 PDB 2ABL 'Sh3-Sh2 Domain Fragment Of Human Bcr-Abl Tyrosine Kinase' 93.37 163 98.71 99.35 4.28e-84 PDB 2FO0 'Organization Of The Sh3-Sh2 Unit In Active And Inactive Forms Of The C-Abl Tyrosine Kinase' 94.58 495 98.73 99.36 2.18e-86 DBJ BAC41088 'unnamed protein product [Mus musculus]' 93.98 1123 99.36 99.36 1.64e-88 DBJ BAD92693 'v-abl Abelson murine leukemia viral oncogene homolog 1 isoform b variant [Homo sapiens]' 93.98 1167 99.36 99.36 7.80e-88 DBJ BAG10808 'proto-oncogene tyrosine-protein kinase ABL1 [synthetic construct]' 93.98 1149 99.36 99.36 4.50e-88 EMBL CAA10376 'bcr-abl1 e14a2 chimeric protein [Homo sapiens]' 93.98 332 99.36 99.36 8.34e-87 EMBL CAA10377 'bcr-abl1 e13a2 chimeric protein [Homo sapiens]' 93.98 307 99.36 99.36 7.42e-87 EMBL CAA24781 'oncogene v-abl [Abelson murine leukemia virus]' 63.86 918 100.00 100.00 6.18e-56 EMBL CAA34438 'unnamed protein product [Homo sapiens]' 93.98 1130 99.36 99.36 3.56e-88 EMBL CAB56204 'unnamed protein product [Abelson murine leukemia virus]' 63.86 818 100.00 100.00 5.32e-56 GenBank AAA43042 'gag-abl-pol fusion polyprotein' 94.58 697 98.09 98.73 4.14e-86 GenBank AAA51561 'abl protein' 93.98 1130 98.08 98.08 2.23e-86 GenBank AAA88241 '125 kDa c-abl protein' 93.98 1123 99.36 99.36 1.77e-88 GenBank AAB60393 'proto-oncogene tyrosine-protein kinase [Homo sapiens]' 93.98 1149 99.36 99.36 4.50e-88 GenBank AAB60394 'proto-oncogene tyrosine-protein kinase [Homo sapiens]' 93.98 1130 99.36 99.36 3.56e-88 REF NP_001106174 'v-abl Abelson murine leukemia oncogene 1 isoform a [Mus musculus]' 93.98 1142 99.36 99.36 2.53e-88 REF NP_005148 'v-abl Abelson murine leukemia viral oncogene homolog 1 isoform a [Homo sapiens]' 93.98 1130 99.36 99.36 3.56e-88 REF NP_009297 'v-abl Abelson murine leukemia viral oncogene homolog 1 isoform b [Homo sapiens]' 93.98 1149 99.36 99.36 4.50e-88 REF NP_033724 'v-abl Abelson murine leukemia oncogene 1 isoform b [Mus musculus]' 93.98 1123 99.36 99.36 1.36e-88 REF NP_057866 'p120 Gag-Abl polyprotein [Abelson murine leukemia virus]' 63.86 981 100.00 100.00 2.47e-56 SWISS-PROT P00519 'Proto-oncogene tyrosine-protein kinase ABL1 (Abelson murine leukemia viral oncogene homolog 1) (c-ABL) (p150)' 93.98 1130 99.36 99.36 3.56e-88 SWISS-PROT P00520 'Proto-oncogene tyrosine-protein kinase ABL1 (Abelson murine leukemia viral oncogene homolog 1) (c-ABL) (p150)' 93.98 1123 99.36 99.36 1.36e-88 SWISS-PROT P00521 'Tyrosine-protein kinase transforming protein Abl (V-abl)' 63.86 746 100.00 100.00 1.57e-56 SWISS-PROT P10447 'Tyrosine-protein kinase transforming protein Abl (V-abl)' 94.58 439 98.09 98.73 1.28e-85 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Abl_SH(32) 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 _Vector_name $Abl_SH(32) 'recombinant technology' . . . . . 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 $Abl_SH(32) 0.8 mM . stop_ save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.5 n/a temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Abl SH(32)' _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 GLY CA C 45.1 . 1 2 . 2 SER N N 115.1 . 1 3 . 2 SER H H 8.31 . 1 4 . 2 SER CA C 58.3 . 1 5 . 2 SER HA H 4.71 . 1 6 . 2 SER CB C 64.6 . 1 7 . 2 SER HB2 H 4.04 . 2 8 . 2 SER HB3 H 3.97 . 2 9 . 3 PRO CA C 63.6 . 1 10 . 3 PRO HA H 4.47 . 1 11 . 3 PRO HB2 H 2.28 . 2 12 . 3 PRO HB3 H 1.94 . 2 13 . 3 PRO HG2 H 2.01 . 1 14 . 3 PRO HG3 H 2.01 . 1 15 . 3 PRO HD2 H 3.83 . 2 16 . 3 PRO HD3 H 3.73 . 2 17 . 6 SER N N 120.4 . 1 18 . 6 SER H H 8.24 . 1 19 . 6 SER CA C 58.2 . 1 20 . 6 SER CB C 64.3 . 1 21 . 7 LEU N N 124.0 . 1 22 . 7 LEU H H 8.39 . 1 23 . 7 LEU CA C 55.2 . 1 24 . 7 LEU HA H 4.97 . 1 25 . 7 LEU CB C 43.6 . 1 26 . 7 LEU HB2 H 1.62 . 1 27 . 7 LEU HB3 H 1.62 . 1 28 . 7 LEU CG C 27.2 . 1 29 . 7 LEU HG H 1.65 . 1 30 . 7 LEU HD1 H 0.94 . 2 31 . 7 LEU HD2 H 0.86 . 2 32 . 7 LEU CD1 C 24.5 . 1 33 . 7 LEU CD2 C 24.2 . 1 34 . 8 PHE N N 126.8 . 1 35 . 8 PHE H H 9.51 . 1 36 . 8 PHE CA C 56.0 . 1 37 . 8 PHE HA H 5.24 . 1 38 . 8 PHE CB C 44.5 . 1 39 . 8 PHE HB2 H 2.80 . 2 40 . 8 PHE HB3 H 2.63 . 2 41 . 9 VAL N N 117.1 . 1 42 . 9 VAL H H 9.42 . 1 43 . 9 VAL CA C 58.8 . 1 44 . 9 VAL HA H 5.22 . 1 45 . 9 VAL CB C 35.5 . 1 46 . 9 VAL HB H 1.68 . 1 47 . 9 VAL HG1 H 0.81 . 2 48 . 9 VAL HG2 H 0.77 . 2 49 . 9 VAL CG1 C 21.4 . 1 50 . 9 VAL CG2 C 20.1 . 1 51 . 10 ALA N N 126.7 . 1 52 . 10 ALA H H 8.41 . 1 53 . 10 ALA CA C 51.9 . 1 54 . 10 ALA HA H 4.70 . 1 55 . 10 ALA HB H 1.55 . 1 56 . 10 ALA CB C 19.6 . 1 57 . 11 LEU N N 126.8 . 1 58 . 11 LEU H H 9.48 . 1 59 . 11 LEU CA C 55.8 . 1 60 . 11 LEU HA H 3.90 . 1 61 . 11 LEU CB C 43.6 . 1 62 . 11 LEU HB2 H 0.97 . 2 63 . 11 LEU HB3 H 0.51 . 2 64 . 11 LEU CG C 26.5 . 1 65 . 11 LEU HG H 1.13 . 1 66 . 11 LEU CD1 C 25.0 . 1 67 . 11 LEU HD1 H 0.63 . 1 68 . 11 LEU HD2 H 0.63 . 1 69 . 12 TYR N N 111.9 . 1 70 . 12 TYR H H 6.98 . 1 71 . 12 TYR CA C 54.0 . 1 72 . 12 TYR HA H 4.73 . 1 73 . 12 TYR CB C 42.5 . 1 74 . 12 TYR HB2 H 3.10 . 2 75 . 12 TYR HB3 H 2.15 . 2 76 . 13 ASP N N 117.3 . 1 77 . 13 ASP H H 8.19 . 1 78 . 13 ASP CA C 54.4 . 1 79 . 13 ASP HA H 4.84 . 1 80 . 13 ASP CB C 41.7 . 1 81 . 13 ASP HB2 H 2.74 . 2 82 . 13 ASP HB3 H 2.62 . 2 83 . 14 PHE N N 121.9 . 1 84 . 14 PHE H H 8.94 . 1 85 . 14 PHE CA C 57.6 . 1 86 . 14 PHE HA H 4.98 . 1 87 . 14 PHE CB C 42.0 . 1 88 . 14 PHE HB2 H 3.21 . 2 89 . 14 PHE HB3 H 3.09 . 2 90 . 15 VAL N N 128.7 . 1 91 . 15 VAL H H 7.91 . 1 92 . 15 VAL CA C 60.8 . 1 93 . 15 VAL HA H 4.02 . 1 94 . 15 VAL CB C 32.4 . 1 95 . 15 VAL HB H 1.73 . 1 96 . 15 VAL HG1 H 0.86 . 2 97 . 15 VAL HG2 H 0.80 . 2 98 . 15 VAL CG1 C 20.9 . 1 99 . 15 VAL CG2 C 20.9 . 1 100 . 16 ALA N N 129.4 . 1 101 . 16 ALA H H 8.28 . 1 102 . 16 ALA CA C 53.0 . 1 103 . 16 ALA HA H 3.77 . 1 104 . 16 ALA HB H 1.30 . 1 105 . 16 ALA CB C 19.5 . 1 106 . 17 SER N N 115.6 . 1 107 . 17 SER H H 7.96 . 1 108 . 17 SER CA C 57.1 . 1 109 . 17 SER HA H 4.52 . 1 110 . 17 SER CB C 64.1 . 1 111 . 17 SER HB2 H 3.89 . 2 112 . 17 SER HB3 H 3.76 . 2 113 . 18 GLY N N 110.5 . 1 114 . 18 GLY H H 8.04 . 1 115 . 19 ASP CA C 55.5 . 1 116 . 19 ASP CB C 40.6 . 1 117 . 20 ASN N N 115.0 . 1 118 . 20 ASN H H 8.63 . 1 119 . 20 ASN CA C 53.8 . 1 120 . 20 ASN HA H 4.77 . 1 121 . 20 ASN CB C 38.2 . 1 122 . 20 ASN HB2 H 3.18 . 2 123 . 20 ASN HB3 H 2.96 . 2 124 . 21 THR N N 109.0 . 1 125 . 21 THR H H 7.71 . 1 126 . 21 THR CA C 60.9 . 1 127 . 21 THR HA H 5.14 . 1 128 . 21 THR CB C 71.7 . 1 129 . 21 THR HB H 4.58 . 1 130 . 21 THR HG2 H 1.24 . 1 131 . 21 THR CG2 C 22.7 . 1 132 . 22 LEU N N 125.3 . 1 133 . 22 LEU H H 8.22 . 1 134 . 22 LEU CA C 53.5 . 1 135 . 22 LEU HA H 4.60 . 1 136 . 22 LEU CB C 46.3 . 1 137 . 22 LEU HB2 H 1.55 . 2 138 . 22 LEU HB3 H 0.79 . 2 139 . 22 LEU CG C 26.0 . 1 140 . 22 LEU HG H 1.41 . 1 141 . 22 LEU HD1 H 0.66 . 2 142 . 22 LEU HD2 H 0.58 . 2 143 . 22 LEU CD1 C 22.9 . 1 144 . 22 LEU CD2 C 26.0 . 1 145 . 23 SER N N 120.1 . 1 146 . 23 SER H H 8.11 . 1 147 . 23 SER CA C 58.5 . 1 148 . 23 SER HA H 5.05 . 1 149 . 23 SER CB C 63.7 . 1 150 . 23 SER HB2 H 4.02 . 2 151 . 23 SER HB3 H 3.84 . 2 152 . 24 ILE N N 117.7 . 1 153 . 24 ILE H H 9.01 . 1 154 . 24 ILE CA C 59.4 . 1 155 . 24 ILE HA H 5.05 . 1 156 . 24 ILE CB C 42.7 . 1 157 . 24 ILE HB H 1.81 . 1 158 . 24 ILE HG2 H 0.86 . 1 159 . 24 ILE CG2 C 18.6 . 1 160 . 24 ILE CG1 C 26.0 . 1 161 . 24 ILE HG12 H 1.46 . 1 162 . 24 ILE HG13 H 1.46 . 1 163 . 24 ILE HD1 H 0.88 . 1 164 . 24 ILE CD1 C 13.3 . 1 165 . 25 THR N N 118.9 . 1 166 . 25 THR H H 9.00 . 1 167 . 25 THR CA C 59.8 . 1 168 . 25 THR HA H 4.91 . 1 169 . 25 THR CB C 71.6 . 1 170 . 25 THR HB H 3.92 . 1 171 . 25 THR HG2 H 1.28 . 1 172 . 26 LYS N N 124.5 . 1 173 . 26 LYS H H 8.95 . 1 174 . 26 LYS CA C 58.8 . 1 175 . 26 LYS HA H 3.27 . 1 176 . 26 LYS CB C 32.4 . 1 177 . 26 LYS HB2 H 1.65 . 2 178 . 26 LYS HB3 H 1.52 . 2 179 . 26 LYS CG C 24.1 . 1 180 . 26 LYS HG2 H 1.19 . 2 181 . 26 LYS HG3 H 1.12 . 2 182 . 26 LYS CD C 29.7 . 1 183 . 26 LYS HD2 H 1.67 . 1 184 . 26 LYS HD3 H 1.67 . 1 185 . 26 LYS CE C 41.7 . 1 186 . 26 LYS HE2 H 3.00 . 1 187 . 26 LYS HE3 H 3.00 . 1 188 . 27 GLY N N 114.9 . 1 189 . 27 GLY H H 8.97 . 1 190 . 27 GLY CA C 44.8 . 1 191 . 27 GLY HA2 H 4.36 . 2 192 . 27 GLY HA3 H 3.46 . 2 193 . 28 GLU N N 124.0 . 1 194 . 28 GLU H H 8.54 . 1 195 . 28 GLU CA C 57.2 . 1 196 . 28 GLU HA H 4.26 . 1 197 . 28 GLU CB C 31.5 . 1 198 . 28 GLU HB2 H 2.34 . 2 199 . 28 GLU HB3 H 2.08 . 2 200 . 28 GLU CG C 36.3 . 1 201 . 28 GLU HG2 H 2.48 . 2 202 . 28 GLU HG3 H 2.33 . 2 203 . 29 LYS N N 122.5 . 1 204 . 29 LYS H H 8.35 . 1 205 . 29 LYS CA C 55.4 . 1 206 . 29 LYS HA H 5.20 . 1 207 . 29 LYS CB C 33.3 . 1 208 . 29 LYS HB2 H 1.89 . 2 209 . 29 LYS HB3 H 1.81 . 2 210 . 29 LYS CG C 25.7 . 1 211 . 29 LYS HG2 H 1.65 . 2 212 . 29 LYS HG3 H 1.45 . 2 213 . 29 LYS CD C 28.7 . 1 214 . 29 LYS HD2 H 1.70 . 1 215 . 29 LYS HD3 H 1.70 . 1 216 . 29 LYS CE C 42.2 . 1 217 . 29 LYS HE2 H 2.98 . 1 218 . 29 LYS HE3 H 2.98 . 1 219 . 30 LEU N N 119.8 . 1 220 . 30 LEU H H 9.17 . 1 221 . 30 LEU CA C 53.9 . 1 222 . 30 LEU HA H 4.86 . 1 223 . 30 LEU CB C 45.1 . 1 224 . 30 LEU HB2 H 1.56 . 2 225 . 30 LEU HB3 H 1.29 . 2 226 . 30 LEU CG C 26.0 . 1 227 . 30 LEU HG H 1.56 . 1 228 . 30 LEU HD1 H 0.68 . 2 229 . 30 LEU HD2 H 0.61 . 2 230 . 30 LEU CD2 C 27.3 . 1 231 . 31 ARG N N 120.1 . 1 232 . 31 ARG H H 8.29 . 1 233 . 31 ARG CA C 54.2 . 1 234 . 31 ARG HA H 5.07 . 1 235 . 31 ARG CB C 32.2 . 1 236 . 31 ARG HB2 H 1.69 . 1 237 . 31 ARG HB3 H 1.69 . 1 238 . 31 ARG CG C 27.8 . 1 239 . 31 ARG HG2 H 1.63 . 2 240 . 31 ARG HG3 H 1.41 . 2 241 . 31 ARG CD C 43.1 . 1 242 . 31 ARG HD2 H 3.11 . 1 243 . 31 ARG HD3 H 3.11 . 1 244 . 32 VAL N N 124.6 . 1 245 . 32 VAL H H 8.77 . 1 246 . 32 VAL CA C 62.2 . 1 247 . 32 VAL HA H 4.14 . 1 248 . 32 VAL CB C 32.8 . 1 249 . 32 VAL HB H 1.45 . 1 250 . 32 VAL HG1 H 0.22 . 2 251 . 32 VAL HG2 H -0.21 . 2 252 . 32 VAL CG1 C 20.7 . 1 253 . 32 VAL CG2 C 22.4 . 1 254 . 33 LEU N N 128.5 . 1 255 . 33 LEU H H 9.21 . 1 256 . 33 LEU CA C 55.1 . 1 257 . 33 LEU HA H 4.20 . 1 258 . 33 LEU CB C 42.0 . 1 259 . 33 LEU HB2 H 1.20 . 2 260 . 33 LEU HB3 H 1.42 . 2 261 . 33 LEU CG C 27.5 . 1 262 . 33 LEU HG H 1.33 . 1 263 . 33 LEU HD1 H 0.56 . 2 264 . 33 LEU HD2 H 0.52 . 2 265 . 33 LEU CD1 C 22.4 . 1 266 . 33 LEU CD2 C 24.7 . 1 267 . 34 GLY N N 105.8 . 1 268 . 34 GLY H H 7.03 . 1 269 . 34 GLY CA C 44.8 . 1 270 . 34 GLY HA2 H 4.25 . 2 271 . 34 GLY HA3 H 3.79 . 2 272 . 35 TYR N N 116.0 . 1 273 . 35 TYR H H 8.65 . 1 274 . 35 TYR CA C 57.2 . 1 275 . 35 TYR HA H 5.70 . 1 276 . 35 TYR CB C 43.5 . 1 277 . 35 TYR HB2 H 3.29 . 2 278 . 35 TYR HB3 H 2.94 . 2 279 . 36 ASN N N 120.5 . 1 280 . 36 ASN H H 9.04 . 1 281 . 36 ASN CA C 52.3 . 1 282 . 36 ASN HA H 4.91 . 1 283 . 36 ASN CB C 37.8 . 1 284 . 36 ASN HB2 H 3.20 . 2 285 . 36 ASN HB3 H 2.42 . 2 286 . 37 HIS N N 120.4 . 1 287 . 37 HIS H H 8.98 . 1 288 . 37 HIS CA C 59.8 . 1 289 . 37 HIS HA H 4.29 . 1 290 . 37 HIS CB C 30.1 . 1 291 . 37 HIS HB2 H 3.12 . 1 292 . 37 HIS HB3 H 3.12 . 1 293 . 38 ASN N N 113.5 . 1 294 . 38 ASN H H 6.54 . 1 295 . 38 ASN CA C 51.0 . 1 296 . 38 ASN HA H 4.76 . 1 297 . 38 ASN CB C 37.9 . 1 298 . 38 ASN HB2 H 3.18 . 2 299 . 38 ASN HB3 H 2.45 . 2 300 . 39 GLY N N 107.4 . 1 301 . 39 GLY H H 7.60 . 1 302 . 39 GLY CA C 45.9 . 1 303 . 39 GLY HA2 H 4.11 . 2 304 . 39 GLY HA3 H 3.58 . 2 305 . 40 GLU N N 122.1 . 1 306 . 40 GLU H H 8.34 . 1 307 . 40 GLU CA C 58.5 . 1 308 . 40 GLU HA H 4.00 . 1 309 . 40 GLU CB C 30.5 . 1 310 . 40 GLU HB2 H 2.09 . 2 311 . 40 GLU HB3 H 1.96 . 2 312 . 40 GLU CG C 36.9 . 1 313 . 40 GLU HG2 H 2.14 . 2 314 . 40 GLU HG3 H 2.02 . 2 315 . 41 TRP N N 119.6 . 1 316 . 41 TRP H H 8.31 . 1 317 . 41 TRP CA C 56.1 . 1 318 . 41 TRP HA H 4.99 . 1 319 . 41 TRP CB C 32.6 . 1 320 . 41 TRP HB2 H 3.36 . 2 321 . 41 TRP HB3 H 2.43 . 2 322 . 42 ALA N N 124.9 . 1 323 . 42 ALA H H 9.78 . 1 324 . 42 ALA CA C 49.5 . 1 325 . 42 ALA HA H 4.92 . 1 326 . 42 ALA HB H 0.84 . 1 327 . 42 ALA CB C 21.8 . 1 328 . 43 GLU N N 126.6 . 1 329 . 43 GLU H H 8.38 . 1 330 . 43 GLU CA C 55.0 . 1 331 . 43 GLU HA H 3.40 . 1 332 . 43 GLU CB C 27.4 . 1 333 . 43 GLU HB2 H 1.06 . 2 334 . 43 GLU HB3 H -0.32 . 2 335 . 43 GLU CG C 36.1 . 1 336 . 43 GLU HG2 H 1.29 . 2 337 . 43 GLU HG3 H 0.67 . 2 338 . 44 ALA N N 130.7 . 1 339 . 44 ALA H H 8.97 . 1 340 . 44 ALA CA C 49.9 . 1 341 . 44 ALA HA H 5.25 . 1 342 . 44 ALA HB H 1.07 . 1 343 . 44 ALA CB C 24.3 . 1 344 . 45 GLN N N 117.5 . 1 345 . 45 GLN H H 8.82 . 1 346 . 45 GLN CA C 54.7 . 1 347 . 45 GLN HA H 5.14 . 1 348 . 45 GLN CB C 32.4 . 1 349 . 45 GLN HB2 H 1.77 . 2 350 . 45 GLN HB3 H 1.96 . 2 351 . 45 GLN CG C 34.5 . 1 352 . 45 GLN HG2 H 2.28 . 2 353 . 45 GLN HG3 H 2.19 . 2 354 . 46 THR N N 117.6 . 1 355 . 46 THR H H 9.09 . 1 356 . 46 THR CA C 59.1 . 1 357 . 46 THR HA H 4.93 . 1 358 . 46 THR CB C 72.2 . 1 359 . 46 THR HB H 4.91 . 1 360 . 46 THR HG2 H 1.22 . 1 361 . 46 THR CG2 C 21.9 . 1 362 . 47 LYS CA C 58.4 . 1 363 . 47 LYS HA H 4.21 . 1 364 . 47 LYS CB C 31.9 . 1 365 . 47 LYS HB2 H 1.94 . 2 366 . 47 LYS HB3 H 1.86 . 2 367 . 47 LYS CG C 24.2 . 1 368 . 47 LYS HG2 H 1.52 . 2 369 . 47 LYS HG3 H 1.44 . 2 370 . 47 LYS CD C 29.2 . 1 371 . 47 LYS HD2 H 1.72 . 1 372 . 47 LYS HD3 H 1.72 . 1 373 . 47 LYS CE C 42.0 . 1 374 . 47 LYS HE2 H 3.04 . 1 375 . 47 LYS HE3 H 3.04 . 1 376 . 48 ASN N N 113.9 . 1 377 . 48 ASN H H 8.25 . 1 378 . 48 ASN CA C 53.2 . 1 379 . 48 ASN HA H 4.86 . 1 380 . 48 ASN CB C 40.1 . 1 381 . 48 ASN HB2 H 2.89 . 2 382 . 48 ASN HB3 H 2.59 . 2 383 . 49 GLY N N 108.3 . 1 384 . 49 GLY H H 7.51 . 1 385 . 49 GLY CA C 45.2 . 1 386 . 49 GLY HA2 H 4.31 . 2 387 . 49 GLY HA3 H 3.86 . 2 388 . 50 GLN N N 119.6 . 1 389 . 50 GLN H H 8.20 . 1 390 . 50 GLN CA C 53.6 . 1 391 . 50 GLN HA H 5.56 . 1 392 . 50 GLN CB C 31.8 . 1 393 . 50 GLN HB2 H 1.80 . 2 394 . 50 GLN HB3 H 2.03 . 2 395 . 50 GLN CG C 33.3 . 1 396 . 50 GLN HG2 H 2.11 . 1 397 . 50 GLN HG3 H 2.11 . 1 398 . 51 GLY N N 112.2 . 1 399 . 51 GLY H H 8.75 . 1 400 . 51 GLY CA C 45.2 . 1 401 . 51 GLY HA2 H 4.07 . 2 402 . 51 GLY HA3 H 3.95 . 2 403 . 52 TRP N N 121.1 . 1 404 . 52 TRP H H 8.74 . 1 405 . 52 TRP CA C 57.1 . 1 406 . 52 TRP HA H 5.46 . 1 407 . 52 TRP CB C 30.6 . 1 408 . 52 TRP HB2 H 3.22 . 2 409 . 52 TRP HB3 H 2.83 . 2 410 . 53 VAL N N 115.7 . 1 411 . 53 VAL H H 9.76 . 1 412 . 53 VAL CA C 57.4 . 1 413 . 53 VAL HA H 4.87 . 1 414 . 53 VAL CB C 33.8 . 1 415 . 53 VAL HB H 1.74 . 1 416 . 53 VAL HG1 H 1.02 . 2 417 . 53 VAL HG2 H 0.61 . 2 418 . 53 VAL CG1 C 22.2 . 1 419 . 53 VAL CG2 C 19.3 . 1 420 . 54 PRO CA C 62.1 . 1 421 . 54 PRO CB C 30.8 . 1 422 . 55 SER N N 121.4 . 1 423 . 55 SER H H 8.46 . 1 424 . 55 SER CA C 60.8 . 1 425 . 55 SER HA H 4.01 . 1 426 . 55 SER CB C 62.8 . 1 427 . 55 SER HB2 H 3.94 . 2 428 . 55 SER HB3 H 3.84 . 2 429 . 56 ASN N N 114.2 . 1 430 . 56 ASN H H 8.39 . 1 431 . 56 ASN CA C 53.2 . 1 432 . 56 ASN HA H 4.84 . 1 433 . 56 ASN CB C 36.4 . 1 434 . 56 ASN HB2 H 3.03 . 2 435 . 56 ASN HB3 H 2.77 . 2 436 . 57 TYR N N 119.1 . 1 437 . 57 TYR H H 7.96 . 1 438 . 57 TYR CA C 57.5 . 1 439 . 57 TYR HA H 4.80 . 1 440 . 57 TYR CB C 37.8 . 1 441 . 57 TYR HB2 H 3.39 . 2 442 . 57 TYR HB3 H 3.21 . 2 443 . 58 ILE N N 111.7 . 1 444 . 58 ILE H H 7.41 . 1 445 . 58 ILE CA C 59.1 . 1 446 . 58 ILE HA H 5.45 . 1 447 . 58 ILE CB C 42.2 . 1 448 . 58 ILE HB H 1.73 . 1 449 . 58 ILE HG2 H 0.66 . 1 450 . 58 ILE CG2 C 18.1 . 1 451 . 58 ILE HG12 H 1.43 . 2 452 . 58 ILE HG13 H 1.28 . 2 453 . 58 ILE HD1 H 0.12 . 1 454 . 58 ILE CD1 C 13.8 . 1 455 . 59 THR N N 116.3 . 1 456 . 59 THR H H 8.73 . 1 457 . 59 THR CA C 58.8 . 1 458 . 59 THR HA H 5.23 . 1 459 . 59 THR CB C 72.7 . 1 460 . 59 THR HB H 3.92 . 1 461 . 59 THR HG2 H 1.05 . 1 462 . 59 THR CG2 C 20.1 . 1 463 . 60 PRO CA C 63.3 . 1 464 . 60 PRO HA H 4.79 . 1 465 . 60 PRO CB C 31.9 . 1 466 . 60 PRO HB2 H 2.28 . 2 467 . 60 PRO HB3 H 1.94 . 2 468 . 60 PRO HD2 H 3.58 . 2 469 . 60 PRO HD3 H 3.52 . 2 470 . 61 VAL N N 119.6 . 1 471 . 61 VAL H H 7.89 . 1 472 . 61 VAL CA C 62.4 . 1 473 . 61 VAL HA H 3.98 . 1 474 . 61 VAL CB C 32.7 . 1 475 . 61 VAL HB H 1.92 . 1 476 . 61 VAL HG1 H 0.85 . 1 477 . 61 VAL HG2 H 0.85 . 1 478 . 61 VAL CG1 C 21.4 . 1 479 . 61 VAL CG2 C 21.4 . 1 480 . 62 ASN N N 127.3 . 1 481 . 62 ASN H H 7.90 . 1 482 . 62 ASN CA C 54.7 . 1 483 . 62 ASN HA H 4.45 . 1 484 . 62 ASN CB C 40.7 . 1 485 . 62 ASN HB2 H 2.66 . 2 486 . 62 ASN HB3 H 2.55 . 2 487 . 63 SER N N 116.7 . 1 488 . 63 SER H H 7.22 . 1 489 . 63 SER CA C 55.7 . 1 490 . 63 SER HA H 4.64 . 1 491 . 63 SER HB2 H 3.77 . 1 492 . 63 SER HB3 H 3.77 . 1 493 . 64 LEU CA C 59.0 . 1 494 . 64 LEU HA H 4.20 . 1 495 . 64 LEU CB C 41.4 . 1 496 . 64 LEU HB2 H 1.52 . 2 497 . 64 LEU HD2 H 0.73 . 2 498 . 65 GLU N N 115.3 . 1 499 . 65 GLU H H 8.29 . 1 500 . 65 GLU CA C 58.3 . 1 501 . 65 GLU HA H 4.68 . 1 502 . 65 GLU CB C 29.0 . 1 503 . 65 GLU HB2 H 2.03 . 2 504 . 65 GLU HB3 H 1.88 . 2 505 . 65 GLU CG C 37.0 . 1 506 . 65 GLU HG2 H 2.25 . 1 507 . 65 GLU HG3 H 2.25 . 1 508 . 66 LYS N N 116.4 . 1 509 . 66 LYS H H 7.35 . 1 510 . 66 LYS CA C 56.5 . 1 511 . 66 LYS HA H 3.96 . 1 512 . 66 LYS CB C 31.8 . 1 513 . 66 LYS HB2 H 1.52 . 1 514 . 66 LYS HB3 H 1.52 . 1 515 . 66 LYS CG C 24.0 . 1 516 . 66 LYS HG2 H 1.11 . 2 517 . 66 LYS HG3 H 0.90 . 2 518 . 66 LYS CD C 28.8 . 1 519 . 66 LYS HD2 H 1.46 . 1 520 . 66 LYS HD3 H 1.46 . 1 521 . 66 LYS CE C 42.0 . 1 522 . 66 LYS HE2 H 2.80 . 1 523 . 66 LYS HE3 H 2.80 . 1 524 . 67 HIS N N 119.2 . 1 525 . 67 HIS H H 7.49 . 1 526 . 67 HIS CA C 55.5 . 1 527 . 67 HIS HA H 4.60 . 1 528 . 67 HIS CB C 31.0 . 1 529 . 67 HIS HB2 H 3.09 . 2 530 . 67 HIS HB3 H 3.01 . 2 531 . 68 SER CA C 60.7 . 1 532 . 68 SER HA H 3.51 . 1 533 . 68 SER CB C 62.4 . 1 534 . 68 SER HB2 H 3.79 . 2 535 . 68 SER HB3 H 3.87 . 2 536 . 69 TRP N N 111.0 . 1 537 . 69 TRP H H 6.42 . 1 538 . 69 TRP CA C 53.7 . 1 539 . 69 TRP HA H 4.51 . 1 540 . 69 TRP CB C 31.4 . 1 541 . 69 TRP HB2 H 3.55 . 1 542 . 69 TRP HB3 H 3.55 . 1 543 . 70 TYR N N 123.4 . 1 544 . 70 TYR H H 7.58 . 1 545 . 70 TYR CA C 58.6 . 1 546 . 70 TYR HA H 5.12 . 1 547 . 70 TYR CB C 37.5 . 1 548 . 70 TYR HB2 H 3.09 . 2 549 . 70 TYR HB3 H 2.43 . 2 550 . 71 HIS N N 127.1 . 1 551 . 71 HIS H H 8.91 . 1 552 . 71 HIS CA C 56.7 . 1 553 . 71 HIS HA H 4.48 . 1 554 . 71 HIS CB C 33.7 . 1 555 . 71 HIS HB2 H 3.26 . 2 556 . 71 HIS HB3 H 2.66 . 2 557 . 72 GLY N N 105.1 . 1 558 . 72 GLY H H 5.72 . 1 559 . 72 GLY CA C 45.3 . 1 560 . 72 GLY HA2 H 4.28 . 2 561 . 72 GLY HA3 H 3.43 . 2 562 . 73 PRO CA C 62.9 . 1 563 . 73 PRO HA H 4.87 . 1 564 . 73 PRO CB C 29.8 . 1 565 . 73 PRO HB2 H 2.15 . 2 566 . 73 PRO HB3 H 1.94 . 2 567 . 73 PRO HG2 H 2.04 . 1 568 . 73 PRO HG3 H 2.04 . 1 569 . 73 PRO HD2 H 3.81 . 2 570 . 73 PRO HD3 H 3.64 . 2 571 . 74 VAL N N 126.2 . 1 572 . 74 VAL H H 8.03 . 1 573 . 74 VAL CA C 61.3 . 1 574 . 74 VAL HA H 4.32 . 1 575 . 74 VAL CB C 35.4 . 1 576 . 74 VAL HB H 1.83 . 1 577 . 74 VAL HG1 H 1.03 . 2 578 . 74 VAL HG2 H 0.87 . 2 579 . 74 VAL CG1 C 22.1 . 1 580 . 74 VAL CG2 C 22.1 . 1 581 . 75 SER N N 122.5 . 1 582 . 75 SER H H 8.64 . 1 583 . 75 SER CA C 57.9 . 1 584 . 75 SER HA H 4.43 . 1 585 . 75 SER CB C 65.1 . 1 586 . 75 SER HB2 H 3.82 . 2 587 . 75 SER HB3 H 4.36 . 2 588 . 76 ARG N N 122.5 . 1 589 . 76 ARG H H 8.92 . 1 590 . 76 ARG CA C 60.5 . 1 591 . 76 ARG HA H 3.45 . 1 592 . 76 ARG CB C 30.1 . 1 593 . 76 ARG HB2 H 1.74 . 2 594 . 76 ARG HB3 H 1.57 . 2 595 . 76 ARG CG C 27.3 . 1 596 . 76 ARG HG2 H 1.01 . 2 597 . 76 ARG HG3 H 0.52 . 2 598 . 76 ARG CD C 43.3 . 1 599 . 76 ARG HD2 H 2.85 . 1 600 . 76 ARG HD3 H 2.85 . 1 601 . 77 ASN N N 115.3 . 1 602 . 77 ASN H H 8.50 . 1 603 . 77 ASN CA C 56.2 . 1 604 . 77 ASN HA H 4.31 . 1 605 . 77 ASN CB C 38.2 . 1 606 . 77 ASN HB2 H 2.67 . 1 607 . 77 ASN HB3 H 2.67 . 1 608 . 78 ALA N N 124.5 . 1 609 . 78 ALA H H 8.15 . 1 610 . 78 ALA CA C 54.9 . 1 611 . 78 ALA HA H 4.19 . 1 612 . 78 ALA HB H 1.49 . 1 613 . 78 ALA CB C 18.3 . 1 614 . 79 ALA N N 121.4 . 1 615 . 79 ALA H H 8.62 . 1 616 . 79 ALA CA C 54.9 . 1 617 . 79 ALA HA H 3.90 . 1 618 . 79 ALA HB H 1.47 . 1 619 . 79 ALA CB C 18.3 . 1 620 . 80 GLU N N 115.4 . 1 621 . 80 GLU H H 7.96 . 1 622 . 80 GLU CA C 60.3 . 1 623 . 80 GLU HA H 3.79 . 1 624 . 80 GLU CB C 27.9 . 1 625 . 80 GLU HB2 H 2.25 . 2 626 . 80 GLU HB3 H 2.11 . 2 627 . 80 GLU CG C 37.4 . 1 628 . 80 GLU HG2 H 2.88 . 2 629 . 80 GLU HG3 H 2.08 . 2 630 . 81 TYR N N 120.2 . 1 631 . 81 TYR H H 7.82 . 1 632 . 81 TYR CA C 61.2 . 1 633 . 81 TYR HA H 4.30 . 1 634 . 81 TYR CB C 37.5 . 1 635 . 81 TYR HB2 H 3.23 . 2 636 . 81 TYR HB3 H 3.15 . 2 637 . 82 LEU N N 123.0 . 1 638 . 82 LEU H H 8.56 . 1 639 . 82 LEU CA C 57.8 . 1 640 . 82 LEU HA H 3.89 . 1 641 . 82 LEU CB C 42.1 . 1 642 . 82 LEU HB2 H 1.87 . 2 643 . 82 LEU HB3 H 1.32 . 2 644 . 82 LEU CG C 27.3 . 1 645 . 82 LEU HG H 1.86 . 1 646 . 82 LEU HD2 H 0.99 . 2 647 . 82 LEU CD2 C 23.6 . 1 648 . 83 LEU N N 116.2 . 1 649 . 83 LEU H H 7.55 . 1 650 . 83 LEU CA C 54.3 . 1 651 . 83 LEU HA H 4.35 . 1 652 . 83 LEU CB C 42.0 . 1 653 . 83 LEU HB2 H 1.66 . 1 654 . 83 LEU HB3 H 1.66 . 1 655 . 83 LEU CG C 27.0 . 1 656 . 83 LEU HG H 1.69 . 1 657 . 83 LEU HD1 H 0.66 . 2 658 . 83 LEU HD2 H 0.59 . 2 659 . 83 LEU CD1 C 23.5 . 1 660 . 83 LEU CD2 C 27.0 . 1 661 . 84 SER N N 116.5 . 1 662 . 84 SER H H 7.54 . 1 663 . 84 SER CA C 61.1 . 1 664 . 84 SER HA H 4.19 . 1 665 . 84 SER CB C 63.1 . 1 666 . 84 SER HB2 H 3.99 . 1 667 . 84 SER HB3 H 3.99 . 1 668 . 85 SER CA C 57.1 . 1 669 . 85 SER HA H 4.82 . 1 670 . 85 SER CB C 64.1 . 1 671 . 85 SER HB2 H 3.88 . 2 672 . 85 SER HB3 H 3.82 . 2 673 . 86 GLY N N 108.8 . 1 674 . 86 GLY H H 7.87 . 1 675 . 86 GLY CA C 44.2 . 1 676 . 86 GLY HA2 H 4.33 . 2 677 . 87 ILE N N 113.9 . 1 678 . 87 ILE H H 8.18 . 1 679 . 87 ILE CA C 60.2 . 1 680 . 87 ILE HA H 4.46 . 1 681 . 87 ILE CB C 40.9 . 1 682 . 87 ILE HB H 1.97 . 1 683 . 87 ILE HG2 H 0.85 . 1 684 . 87 ILE CG2 C 17.7 . 1 685 . 87 ILE CG1 C 25.0 . 1 686 . 87 ILE HG12 H 1.30 . 2 687 . 87 ILE HG13 H 0.90 . 2 688 . 87 ILE HD1 H 0.59 . 1 689 . 87 ILE CD1 C 13.7 . 1 690 . 88 ASN N N 121.1 . 1 691 . 88 ASN H H 8.69 . 1 692 . 88 ASN CA C 54.3 . 1 693 . 88 ASN HA H 4.66 . 1 694 . 88 ASN CB C 37.8 . 1 695 . 88 ASN HB2 H 2.36 . 2 696 . 88 ASN HB3 H 2.27 . 2 697 . 89 GLY N N 109.1 . 1 698 . 89 GLY H H 9.33 . 1 699 . 89 GLY CA C 45.9 . 1 700 . 89 GLY HA2 H 3.88 . 2 701 . 90 SER N N 122.1 . 1 702 . 90 SER H H 8.71 . 1 703 . 90 SER CA C 60.3 . 1 704 . 90 SER HA H 6.07 . 1 705 . 90 SER CB C 63.8 . 1 706 . 90 SER HB2 H 3.98 . 1 707 . 90 SER HB3 H 3.98 . 1 708 . 91 PHE N N 120.5 . 1 709 . 91 PHE H H 8.78 . 1 710 . 91 PHE CA C 55.8 . 1 711 . 91 PHE HA H 5.98 . 1 712 . 91 PHE CB C 44.7 . 1 713 . 91 PHE HB2 H 3.03 . 2 714 . 91 PHE HB3 H 2.98 . 2 715 . 92 LEU N N 114.5 . 1 716 . 92 LEU H H 9.07 . 1 717 . 92 LEU CA C 54.5 . 1 718 . 92 LEU HA H 4.53 . 1 719 . 92 LEU CB C 43.6 . 1 720 . 92 LEU HB2 H 1.33 . 2 721 . 92 LEU HB3 H 1.01 . 2 722 . 92 LEU CG C 25.0 . 1 723 . 92 LEU HG H 1.55 . 1 724 . 92 LEU HD1 H 0.42 . 2 725 . 92 LEU HD2 H 0.55 . 2 726 . 92 LEU CD1 C 27.9 . 1 727 . 92 LEU CD2 C 25.9 . 1 728 . 93 VAL N N 120.9 . 1 729 . 93 VAL H H 9.22 . 1 730 . 93 VAL CA C 61.2 . 1 731 . 93 VAL HA H 5.21 . 1 732 . 93 VAL CB C 33.5 . 1 733 . 93 VAL HB H 2.56 . 1 734 . 93 VAL HG1 H 1.24 . 2 735 . 93 VAL HG2 H 1.12 . 2 736 . 93 VAL CG1 C 21.9 . 1 737 . 93 VAL CG2 C 22.4 . 1 738 . 94 ARG N N 122.9 . 1 739 . 94 ARG H H 9.22 . 1 740 . 94 ARG CA C 52.2 . 1 741 . 94 ARG HA H 5.28 . 1 742 . 94 ARG CB C 34.5 . 1 743 . 94 ARG HB2 H 2.16 . 2 744 . 94 ARG HG2 H 1.26 . 1 745 . 94 ARG HG3 H 1.26 . 1 746 . 94 ARG CD C 43.3 . 1 747 . 94 ARG HD2 H 3.34 . 1 748 . 94 ARG HD3 H 3.34 . 1 749 . 95 GLU N N 120.6 . 1 750 . 95 GLU H H 8.01 . 1 751 . 95 GLU CA C 54.5 . 1 752 . 95 GLU HA H 4.75 . 1 753 . 95 GLU CB C 31.0 . 1 754 . 95 GLU HB2 H 2.37 . 2 755 . 95 GLU HB3 H 2.01 . 2 756 . 96 SER N N 117.2 . 1 757 . 96 SER H H 8.30 . 1 758 . 96 SER CA C 57.9 . 1 759 . 96 SER HA H 4.30 . 1 760 . 96 SER CB C 63.5 . 1 761 . 96 SER HB2 H 3.87 . 2 762 . 96 SER HB3 H 3.95 . 2 763 . 97 GLU N N 127.1 . 1 764 . 97 GLU H H 9.19 . 1 765 . 97 GLU CA C 57.9 . 1 766 . 97 GLU HA H 4.14 . 1 767 . 97 GLU CB C 30.5 . 1 768 . 97 GLU HB2 H 2.01 . 1 769 . 97 GLU HB3 H 2.01 . 1 770 . 97 GLU CG C 36.8 . 1 771 . 97 GLU HG2 H 2.26 . 2 772 . 97 GLU HG3 H 2.15 . 2 773 . 98 SER N N 121.1 . 1 774 . 98 SER H H 9.03 . 1 775 . 98 SER CA C 59.3 . 1 776 . 98 SER HA H 4.22 . 1 777 . 98 SER CB C 63.9 . 1 778 . 98 SER HB2 H 3.88 . 2 779 . 98 SER HB3 H 3.81 . 2 780 . 99 SER N N 118.0 . 1 781 . 99 SER H H 7.66 . 1 782 . 99 SER CA C 54.7 . 1 783 . 99 SER HA H 4.84 . 1 784 . 99 SER CB C 63.6 . 1 785 . 99 SER HB2 H 3.77 . 2 786 . 99 SER HB3 H 3.57 . 2 787 . 100 PRO CA C 63.8 . 1 788 . 100 PRO HA H 4.32 . 1 789 . 100 PRO CB C 31.7 . 1 790 . 100 PRO HB2 H 2.26 . 2 791 . 100 PRO HB3 H 1.84 . 2 792 . 100 PRO CG C 27.5 . 1 793 . 100 PRO HG2 H 2.03 . 2 794 . 100 PRO HG3 H 1.94 . 2 795 . 100 PRO HD2 H 3.62 . 2 796 . 100 PRO HD3 H 3.53 . 2 797 . 101 GLY N N 111.8 . 1 798 . 101 GLY H H 9.23 . 1 799 . 101 GLY CA C 45.2 . 1 800 . 101 GLY HA2 H 4.04 . 2 801 . 102 GLN N N 120.5 . 1 802 . 102 GLN H H 8.11 . 1 803 . 102 GLN CA C 54.7 . 1 804 . 102 GLN HA H 4.70 . 1 805 . 102 GLN CB C 29.1 . 1 806 . 102 GLN HB2 H 2.25 . 2 807 . 102 GLN HB3 H 2.08 . 2 808 . 102 GLN CG C 34.1 . 1 809 . 102 GLN HG2 H 2.35 . 2 810 . 102 GLN HG3 H 2.27 . 2 811 . 103 ARG N N 124.7 . 1 812 . 103 ARG H H 9.15 . 1 813 . 103 ARG CA C 55.3 . 1 814 . 103 ARG HA H 5.40 . 1 815 . 103 ARG CB C 34.3 . 1 816 . 103 ARG HB2 H 1.76 . 1 817 . 103 ARG HB3 H 1.76 . 1 818 . 103 ARG CD C 43.8 . 1 819 . 103 ARG HD2 H 3.26 . 2 820 . 103 ARG HD3 H 3.09 . 2 821 . 104 SER N N 114.9 . 1 822 . 104 SER H H 9.09 . 1 823 . 104 SER CA C 57.6 . 1 824 . 104 SER HA H 5.49 . 1 825 . 104 SER CB C 67.1 . 1 826 . 104 SER HB2 H 3.31 . 2 827 . 104 SER HB3 H 3.71 . 2 828 . 105 ILE N N 122.6 . 1 829 . 105 ILE H H 9.49 . 1 830 . 105 ILE CA C 60.4 . 1 831 . 105 ILE HA H 4.94 . 1 832 . 105 ILE CB C 41.7 . 1 833 . 105 ILE HB H 1.70 . 1 834 . 105 ILE HG2 H 0.93 . 1 835 . 105 ILE CG2 C 17.9 . 1 836 . 105 ILE CG1 C 28.5 . 1 837 . 105 ILE HG12 H 1.75 . 2 838 . 105 ILE HG13 H 0.91 . 2 839 . 105 ILE HD1 H 0.50 . 1 840 . 105 ILE CD1 C 13.8 . 1 841 . 106 SER N N 124.1 . 1 842 . 106 SER H H 9.09 . 1 843 . 106 SER CA C 58.5 . 1 844 . 106 SER HA H 5.64 . 1 845 . 106 SER CB C 65.4 . 1 846 . 106 SER HB2 H 3.29 . 1 847 . 106 SER HB3 H 3.29 . 1 848 . 107 LEU N N 126.5 . 1 849 . 107 LEU H H 9.35 . 1 850 . 107 LEU CA C 53.7 . 1 851 . 107 LEU HA H 5.40 . 1 852 . 107 LEU CB C 48.2 . 1 853 . 107 LEU HB2 H 1.87 . 2 854 . 107 LEU HB3 H 1.37 . 2 855 . 107 LEU HD1 H 0.87 . 2 856 . 107 LEU HD2 H 0.76 . 2 857 . 107 LEU CD1 C 24.5 . 1 858 . 107 LEU CD2 C 28.2 . 1 859 . 108 ARG N N 127.0 . 1 860 . 108 ARG H H 9.21 . 1 861 . 108 ARG CA C 54.6 . 1 862 . 108 ARG HA H 5.29 . 1 863 . 108 ARG CB C 33.1 . 1 864 . 108 ARG HB2 H 2.19 . 1 865 . 108 ARG HB3 H 2.19 . 1 866 . 108 ARG HG2 H 1.46 . 1 867 . 108 ARG HG3 H 1.46 . 1 868 . 108 ARG CD C 43.0 . 1 869 . 108 ARG HD2 H 3.11 . 2 870 . 108 ARG HD3 H 2.70 . 2 871 . 109 TYR N N 125.6 . 1 872 . 109 TYR H H 9.48 . 1 873 . 109 TYR CA C 59.3 . 1 874 . 109 TYR HA H 4.66 . 1 875 . 109 TYR CB C 41.3 . 1 876 . 109 TYR HB2 H 2.85 . 2 877 . 109 TYR HB3 H 2.74 . 2 878 . 110 GLU N N 128.5 . 1 879 . 110 GLU H H 9.33 . 1 880 . 110 GLU CA C 56.1 . 1 881 . 110 GLU HA H 3.63 . 1 882 . 110 GLU CB C 27.6 . 1 883 . 110 GLU HB2 H 2.01 . 2 884 . 110 GLU HB3 H 1.48 . 2 885 . 110 GLU CG C 35.5 . 1 886 . 110 GLU HG2 H 1.67 . 2 887 . 110 GLU HG3 H 0.99 . 2 888 . 111 GLY N N 102.7 . 1 889 . 111 GLY H H 8.40 . 1 890 . 111 GLY CA C 45.5 . 1 891 . 111 GLY HA2 H 3.48 . 2 892 . 111 GLY HA3 H 4.10 . 2 893 . 112 ARG N N 120.3 . 1 894 . 112 ARG H H 7.81 . 1 895 . 112 ARG CA C 54.0 . 1 896 . 112 ARG HA H 4.62 . 1 897 . 112 ARG CB C 33.6 . 1 898 . 112 ARG HB2 H 1.76 . 2 899 . 112 ARG HB3 H 1.60 . 2 900 . 112 ARG CG C 27.4 . 1 901 . 112 ARG HG2 H 1.56 . 2 902 . 112 ARG HG3 H 1.37 . 2 903 . 113 VAL N N 120.6 . 1 904 . 113 VAL H H 8.23 . 1 905 . 113 VAL CA C 61.1 . 1 906 . 113 VAL HA H 4.71 . 1 907 . 113 VAL CB C 32.5 . 1 908 . 113 VAL HB H 1.67 . 1 909 . 113 VAL HG1 H 0.79 . 2 910 . 113 VAL CG1 C 23.1 . 1 911 . 114 TYR N N 128.8 . 1 912 . 114 TYR H H 9.40 . 1 913 . 114 TYR CA C 56.7 . 1 914 . 114 TYR HA H 4.22 . 1 915 . 114 TYR CB C 33.0 . 1 916 . 114 TYR HB2 H 2.72 . 1 917 . 114 TYR HB3 H 2.72 . 1 918 . 115 HIS N N 120.1 . 1 919 . 115 HIS H H 8.31 . 1 920 . 115 HIS CA C 54.2 . 1 921 . 115 HIS HA H 5.63 . 1 922 . 115 HIS CB C 33.3 . 1 923 . 115 HIS HB2 H 2.75 . 1 924 . 115 HIS HB3 H 2.75 . 1 925 . 116 TYR N N 121.7 . 1 926 . 116 TYR H H 9.69 . 1 927 . 116 TYR CA C 56.5 . 1 928 . 116 TYR HA H 4.78 . 1 929 . 116 TYR CB C 41.3 . 1 930 . 116 TYR HB2 H 2.82 . 2 931 . 116 TYR HB3 H 2.56 . 2 932 . 117 ARG N N 125.2 . 1 933 . 117 ARG H H 8.75 . 1 934 . 117 ARG CA C 56.3 . 1 935 . 117 ARG HA H 4.46 . 1 936 . 117 ARG CB C 30.5 . 1 937 . 117 ARG HB2 H 1.80 . 2 938 . 117 ARG HB3 H 1.72 . 2 939 . 117 ARG HG2 H 1.58 . 1 940 . 117 ARG HG3 H 1.58 . 1 941 . 117 ARG CD C 42.8 . 1 942 . 117 ARG HD2 H 3.22 . 1 943 . 117 ARG HD3 H 3.22 . 1 944 . 118 ILE N N 123.3 . 1 945 . 118 ILE H H 8.41 . 1 946 . 118 ILE CA C 61.3 . 1 947 . 118 ILE HA H 3.93 . 1 948 . 118 ILE CB C 37.3 . 1 949 . 118 ILE HB H 1.69 . 1 950 . 118 ILE HG2 H 0.79 . 1 951 . 118 ILE CG2 C 18.7 . 1 952 . 118 ILE HG12 H 1.59 . 2 953 . 118 ILE HG13 H 0.66 . 2 954 . 118 ILE HD1 H 0.71 . 1 955 . 118 ILE CD1 C 14.3 . 1 956 . 119 ASN N N 128.3 . 1 957 . 119 ASN H H 8.72 . 1 958 . 119 ASN CA C 52.6 . 1 959 . 119 ASN HA H 4.63 . 1 960 . 119 ASN CB C 40.3 . 1 961 . 119 ASN HB2 H 2.00 . 2 962 . 119 ASN HB3 H 1.02 . 2 963 . 120 THR N N 113.8 . 1 964 . 120 THR H H 8.31 . 1 965 . 120 THR CA C 60.9 . 1 966 . 120 THR HA H 5.04 . 1 967 . 120 THR CB C 69.9 . 1 968 . 120 THR HB H 3.94 . 1 969 . 120 THR HG2 H 1.27 . 1 970 . 120 THR CG2 C 21.1 . 1 971 . 121 ALA N N 129.5 . 1 972 . 121 ALA H H 9.67 . 1 973 . 121 ALA CA C 51.0 . 1 974 . 121 ALA HA H 4.78 . 1 975 . 121 ALA HB H 1.70 . 1 976 . 121 ALA CB C 21.4 . 1 977 . 122 SER CA C 61.2 . 1 978 . 122 SER HA H 3.86 . 1 979 . 122 SER CB C 62.7 . 1 980 . 122 SER HB2 H 3.75 . 1 981 . 122 SER HB3 H 3.75 . 1 982 . 123 ASP N N 118.0 . 1 983 . 123 ASP H H 7.84 . 1 984 . 123 ASP CA C 52.6 . 1 985 . 123 ASP HA H 4.61 . 1 986 . 123 ASP CB C 39.9 . 1 987 . 123 ASP HB2 H 3.06 . 2 988 . 123 ASP HB3 H 2.53 . 2 989 . 124 GLY N N 108.0 . 1 990 . 124 GLY H H 8.16 . 1 991 . 124 GLY CA C 44.9 . 1 992 . 124 GLY HA2 H 4.31 . 2 993 . 124 GLY HA3 H 3.54 . 2 994 . 125 LYS N N 119.1 . 1 995 . 125 LYS H H 7.52 . 1 996 . 125 LYS CA C 57.6 . 1 997 . 125 LYS HA H 4.37 . 1 998 . 125 LYS CB C 33.9 . 1 999 . 125 LYS HB2 H 1.77 . 2 1000 . 125 LYS HB3 H 1.59 . 2 1001 . 125 LYS CG C 26.5 . 1 1002 . 125 LYS HG2 H 1.42 . 2 1003 . 125 LYS HG3 H 1.12 . 2 1004 . 125 LYS CD C 29.4 . 1 1005 . 125 LYS HD2 H 1.43 . 2 1006 . 125 LYS HD3 H 1.23 . 2 1007 . 125 LYS CE C 42.2 . 1 1008 . 125 LYS HE2 H 2.85 . 1 1009 . 125 LYS HE3 H 2.85 . 1 1010 . 126 LEU N N 119.7 . 1 1011 . 126 LEU H H 9.21 . 1 1012 . 126 LEU CA C 53.5 . 1 1013 . 126 LEU HA H 5.53 . 1 1014 . 126 LEU CB C 45.8 . 1 1015 . 126 LEU HB2 H 1.57 . 2 1016 . 126 LEU HB3 H 1.34 . 2 1017 . 126 LEU CG C 27.3 . 1 1018 . 126 LEU HG H 1.81 . 1 1019 . 126 LEU HD1 H 0.86 . 2 1020 . 126 LEU HD2 H 0.82 . 2 1021 . 126 LEU CD1 C 24.3 . 1 1022 . 126 LEU CD2 C 25.8 . 1 1023 . 127 TYR N N 114.5 . 1 1024 . 127 TYR H H 8.72 . 1 1025 . 127 TYR CA C 57.7 . 1 1026 . 127 TYR HA H 5.13 . 1 1027 . 127 TYR CB C 41.0 . 1 1028 . 127 TYR HB3 H 3.07 . 2 1029 . 128 VAL N N 121.4 . 1 1030 . 128 VAL H H 10.20 . 1 1031 . 128 VAL CA C 64.1 . 1 1032 . 128 VAL HA H 4.29 . 1 1033 . 128 VAL CB C 32.9 . 1 1034 . 128 VAL HB H 1.92 . 1 1035 . 128 VAL HG1 H 0.76 . 2 1036 . 128 VAL HG2 H 0.61 . 2 1037 . 128 VAL CG1 C 20.9 . 1 1038 . 128 VAL CG2 C 21.4 . 1 1039 . 129 SER N N 117.5 . 1 1040 . 129 SER H H 9.22 . 1 1041 . 129 SER CA C 56.8 . 1 1042 . 129 SER HA H 4.89 . 1 1043 . 129 SER CB C 64.1 . 1 1044 . 129 SER HB2 H 4.04 . 1 1045 . 129 SER HB3 H 4.04 . 1 1046 . 130 SER CA C 60.6 . 1 1047 . 130 SER CB C 63.4 . 1 1048 . 131 GLU N N 116.7 . 1 1049 . 131 GLU H H 8.44 . 1 1050 . 131 GLU CA C 57.1 . 1 1051 . 131 GLU HA H 4.11 . 1 1052 . 131 GLU CB C 29.5 . 1 1053 . 131 GLU HB2 H 2.09 . 2 1054 . 131 GLU HB3 H 1.86 . 2 1055 . 131 GLU CG C 36.4 . 1 1056 . 131 GLU HG2 H 2.20 . 1 1057 . 131 GLU HG3 H 2.20 . 1 1058 . 132 SER N N 118.5 . 1 1059 . 132 SER H H 7.81 . 1 1060 . 132 SER CA C 56.6 . 1 1061 . 132 SER HA H 4.29 . 1 1062 . 132 SER CB C 63.5 . 1 1063 . 132 SER HB2 H 3.77 . 2 1064 . 132 SER HB3 H 3.36 . 2 1065 . 133 ARG N N 120.0 . 1 1066 . 133 ARG H H 7.60 . 1 1067 . 133 ARG CA C 53.1 . 1 1068 . 133 ARG HA H 5.06 . 1 1069 . 133 ARG CB C 32.9 . 1 1070 . 133 ARG HB2 H 1.43 . 2 1071 . 133 ARG HB3 H 1.32 . 2 1072 . 133 ARG CG C 26.5 . 1 1073 . 133 ARG HG2 H 1.29 . 2 1074 . 133 ARG HG3 H 0.99 . 2 1075 . 133 ARG CD C 43.8 . 1 1076 . 133 ARG HD2 H 2.81 . 2 1077 . 133 ARG HD3 H 2.63 . 2 1078 . 134 PHE N N 118.0 . 1 1079 . 134 PHE H H 9.16 . 1 1080 . 134 PHE CA C 57.6 . 1 1081 . 134 PHE HA H 4.84 . 1 1082 . 134 PHE CB C 44.7 . 1 1083 . 134 PHE HB2 H 3.41 . 2 1084 . 134 PHE HB3 H 2.53 . 2 1085 . 135 ASN N N 118.6 . 1 1086 . 135 ASN H H 9.59 . 1 1087 . 135 ASN CA C 55.8 . 1 1088 . 135 ASN HA H 4.69 . 1 1089 . 135 ASN CB C 39.4 . 1 1090 . 135 ASN HB2 H 3.20 . 2 1091 . 135 ASN HB3 H 2.88 . 2 1092 . 136 THR N N 104.7 . 1 1093 . 136 THR H H 7.43 . 1 1094 . 136 THR CA C 58.8 . 1 1095 . 136 THR HA H 4.92 . 1 1096 . 136 THR CB C 73.4 . 1 1097 . 136 THR HB H 4.71 . 1 1098 . 136 THR HG2 H 1.25 . 1 1099 . 136 THR CG2 C 21.7 . 1 1100 . 137 LEU N N 123.5 . 1 1101 . 137 LEU H H 9.15 . 1 1102 . 137 LEU CA C 57.2 . 1 1103 . 137 LEU HA H 4.00 . 1 1104 . 137 LEU CB C 41.9 . 1 1105 . 137 LEU HB2 H 1.77 . 1 1106 . 137 LEU HB3 H 1.77 . 1 1107 . 137 LEU CG C 27.0 . 1 1108 . 137 LEU HG H 1.83 . 1 1109 . 137 LEU HD1 H 1.07 . 2 1110 . 137 LEU HD2 H 1.02 . 2 1111 . 137 LEU CD1 C 26.3 . 1 1112 . 137 LEU CD2 C 25.0 . 1 1113 . 138 ALA N N 119.9 . 1 1114 . 138 ALA H H 8.93 . 1 1115 . 138 ALA CA C 55.5 . 1 1116 . 138 ALA HA H 3.95 . 1 1117 . 138 ALA HB H 1.49 . 1 1118 . 138 ALA CB C 17.7 . 1 1119 . 139 GLU N N 117.4 . 1 1120 . 139 GLU H H 7.63 . 1 1121 . 139 GLU CA C 59.0 . 1 1122 . 139 GLU HA H 3.87 . 1 1123 . 139 GLU CB C 31.2 . 1 1124 . 139 GLU HB2 H 2.25 . 1 1125 . 139 GLU HB3 H 2.25 . 1 1126 . 139 GLU CG C 37.9 . 1 1127 . 139 GLU HG2 H 2.32 . 1 1128 . 139 GLU HG3 H 2.32 . 1 1129 . 140 LEU N N 123.4 . 1 1130 . 140 LEU H H 7.26 . 1 1131 . 140 LEU CA C 58.6 . 1 1132 . 140 LEU HA H 2.92 . 1 1133 . 140 LEU CB C 42.2 . 1 1134 . 140 LEU HB2 H 2.04 . 2 1135 . 140 LEU HB3 H 1.49 . 2 1136 . 140 LEU CG C 27.3 . 1 1137 . 140 LEU HG H 1.77 . 1 1138 . 140 LEU HD1 H 1.15 . 2 1139 . 140 LEU HD2 H 0.67 . 2 1140 . 140 LEU CD1 C 28.2 . 1 1141 . 140 LEU CD2 C 25.2 . 1 1142 . 141 VAL N N 119.6 . 1 1143 . 141 VAL H H 8.20 . 1 1144 . 141 VAL CA C 66.3 . 1 1145 . 141 VAL HA H 2.87 . 1 1146 . 141 VAL CB C 31.2 . 1 1147 . 141 VAL HB H 1.17 . 1 1148 . 141 VAL HG1 H -0.14 . 2 1149 . 141 VAL HG2 H -0.26 . 2 1150 . 141 VAL CG1 C 19.9 . 1 1151 . 141 VAL CG2 C 21.7 . 1 1152 . 142 HIS N N 118.4 . 1 1153 . 142 HIS H H 7.96 . 1 1154 . 142 HIS CA C 59.8 . 1 1155 . 142 HIS HA H 4.08 . 1 1156 . 142 HIS CB C 30.0 . 1 1157 . 142 HIS HB3 H 3.03 . 2 1158 . 143 HIS N N 120.4 . 1 1159 . 143 HIS H H 7.95 . 1 1160 . 143 HIS CA C 60.3 . 1 1161 . 143 HIS HA H 3.99 . 1 1162 . 143 HIS CB C 31.3 . 1 1163 . 143 HIS HB2 H 2.69 . 2 1164 . 143 HIS HB3 H 2.59 . 2 1165 . 144 HIS N N 115.6 . 1 1166 . 144 HIS H H 7.76 . 1 1167 . 144 HIS CA C 57.3 . 1 1168 . 144 HIS HA H 4.97 . 1 1169 . 144 HIS CB C 27.5 . 1 1170 . 144 HIS HB2 H 3.06 . 2 1171 . 144 HIS HB3 H 2.54 . 2 1172 . 145 SER N N 115.5 . 1 1173 . 145 SER H H 7.58 . 1 1174 . 145 SER CA C 59.8 . 1 1175 . 145 SER HA H 4.68 . 1 1176 . 145 SER CB C 63.3 . 1 1177 . 145 SER HB2 H 3.88 . 2 1178 . 145 SER HB3 H 3.75 . 2 1179 . 146 THR N N 113.9 . 1 1180 . 146 THR H H 7.40 . 1 1181 . 146 THR CA C 63.1 . 1 1182 . 146 THR HA H 4.22 . 1 1183 . 146 THR CB C 70.1 . 1 1184 . 146 THR HB H 4.07 . 1 1185 . 146 THR HG2 H 1.02 . 1 1186 . 146 THR CG2 C 21.2 . 1 1187 . 147 VAL N N 120.8 . 1 1188 . 147 VAL H H 7.61 . 1 1189 . 147 VAL CA C 59.8 . 1 1190 . 147 VAL HA H 4.01 . 1 1191 . 147 VAL CB C 33.8 . 1 1192 . 147 VAL HB H 1.43 . 1 1193 . 147 VAL HG1 H 0.60 . 2 1194 . 147 VAL HG2 H 0.50 . 2 1195 . 147 VAL CG1 C 21.3 . 1 1196 . 147 VAL CG2 C 19.6 . 1 1197 . 148 ALA N N 127.8 . 1 1198 . 148 ALA H H 8.28 . 1 1199 . 148 ALA CA C 56.2 . 1 1200 . 148 ALA HA H 3.54 . 1 1201 . 148 ALA HB H 1.06 . 1 1202 . 148 ALA CB C 16.9 . 1 1203 . 149 ASP N N 116.4 . 1 1204 . 149 ASP H H 8.37 . 1 1205 . 149 ASP CA C 54.2 . 1 1206 . 149 ASP HA H 4.18 . 1 1207 . 149 ASP CB C 41.2 . 1 1208 . 149 ASP HB2 H 2.99 . 2 1209 . 149 ASP HB3 H 2.11 . 2 1210 . 150 GLY N N 105.4 . 1 1211 . 150 GLY H H 8.21 . 1 1212 . 150 GLY CA C 44.5 . 1 1213 . 150 GLY HA2 H 4.41 . 2 1214 . 150 GLY HA3 H 3.45 . 2 1215 . 151 LEU N N 119.7 . 1 1216 . 151 LEU H H 7.26 . 1 1217 . 151 LEU CA C 53.8 . 1 1218 . 151 LEU HA H 3.82 . 1 1219 . 151 LEU CB C 42.5 . 1 1220 . 151 LEU HB2 H 1.67 . 2 1221 . 151 LEU HB3 H 0.85 . 2 1222 . 151 LEU CG C 26.2 . 1 1223 . 151 LEU HG H 1.03 . 1 1224 . 151 LEU HD1 H 0.29 . 2 1225 . 151 LEU HD2 H -0.46 . 2 1226 . 151 LEU CD1 C 26.2 . 1 1227 . 151 LEU CD2 C 21.1 . 1 1228 . 152 ILE N N 118.2 . 1 1229 . 152 ILE H H 7.10 . 1 1230 . 152 ILE CA C 61.8 . 1 1231 . 152 ILE HA H 3.63 . 1 1232 . 152 ILE CB C 38.5 . 1 1233 . 152 ILE HB H 1.15 . 1 1234 . 152 ILE HG2 H 0.00 . 1 1235 . 152 ILE CG2 C 16.9 . 1 1236 . 152 ILE CG1 C 29.0 . 1 1237 . 152 ILE HG12 H 0.85 . 2 1238 . 152 ILE HG13 H 0.41 . 2 1239 . 152 ILE HD1 H 0.52 . 1 1240 . 152 ILE CD1 C 14.5 . 1 1241 . 153 THR N N 111.1 . 1 1242 . 153 THR H H 6.78 . 1 1243 . 153 THR CA C 58.9 . 1 1244 . 153 THR HA H 3.97 . 1 1245 . 153 THR CB C 68.5 . 1 1246 . 153 THR HB H 3.35 . 1 1247 . 153 THR HG2 H 1.04 . 1 1248 . 153 THR CG2 C 18.2 . 1 1249 . 154 THR N N 106.7 . 1 1250 . 154 THR H H 7.28 . 1 1251 . 154 THR CA C 60.2 . 1 1252 . 154 THR HA H 3.98 . 1 1253 . 154 THR CB C 69.6 . 1 1254 . 154 THR HB H 3.74 . 1 1255 . 154 THR HG2 H 0.67 . 1 1256 . 154 THR CG2 C 22.5 . 1 1257 . 155 LEU N N 117.9 . 1 1258 . 155 LEU H H 7.59 . 1 1259 . 155 LEU CA C 53.5 . 1 1260 . 155 LEU HA H 3.49 . 1 1261 . 155 LEU CB C 37.3 . 1 1262 . 155 LEU HB2 H 0.85 . 1 1263 . 155 LEU HB3 H 0.85 . 1 1264 . 155 LEU CG C 25.0 . 1 1265 . 155 LEU HG H 0.95 . 1 1266 . 155 LEU HD1 H 0.12 . 2 1267 . 155 LEU HD2 H 0.09 . 2 1268 . 155 LEU CD1 C 22.6 . 1 1269 . 155 LEU CD2 C 25.5 . 1 1270 . 156 HIS N N 123.1 . 1 1271 . 156 HIS H H 8.38 . 1 1272 . 156 HIS CA C 56.9 . 1 1273 . 156 HIS HA H 4.75 . 1 1274 . 156 HIS CB C 33.6 . 1 1275 . 156 HIS HB2 H 2.79 . 2 1276 . 156 HIS HB3 H 2.65 . 2 1277 . 157 TYR N N 119.3 . 1 1278 . 157 TYR H H 8.02 . 1 1279 . 157 TYR CA C 54.4 . 1 1280 . 157 TYR HA H 5.24 . 1 1281 . 157 TYR CB C 40.6 . 1 1282 . 157 TYR HB2 H 3.06 . 2 1283 . 157 TYR HB3 H 2.78 . 2 1284 . 158 PRO CA C 61.7 . 1 1285 . 158 PRO HA H 3.86 . 1 1286 . 158 PRO CB C 31.5 . 1 1287 . 158 PRO HB2 H 1.78 . 1 1288 . 158 PRO HB3 H 1.78 . 1 1289 . 158 PRO CG C 28.0 . 1 1290 . 158 PRO HG2 H 2.26 . 2 1291 . 158 PRO HG3 H 1.99 . 2 1292 . 158 PRO HD2 H 3.69 . 1 1293 . 158 PRO HD3 H 3.69 . 1 1294 . 159 ALA N N 129.8 . 1 1295 . 159 ALA H H 8.73 . 1 1296 . 159 ALA CA C 50.1 . 1 1297 . 159 ALA HA H 4.54 . 1 1298 . 159 ALA HB H 1.13 . 1 1299 . 159 ALA CB C 17.9 . 1 1300 . 160 PRO CA C 62.9 . 1 1301 . 160 PRO HA H 4.39 . 1 1302 . 160 PRO CB C 32.0 . 1 1303 . 160 PRO HB2 H 2.26 . 2 1304 . 160 PRO HB3 H 1.84 . 2 1305 . 160 PRO CG C 27.5 . 1 1306 . 160 PRO HG2 H 2.10 . 2 1307 . 160 PRO HG3 H 2.00 . 2 1308 . 160 PRO HD2 H 3.93 . 2 1309 . 160 PRO HD3 H 3.68 . 2 1310 . 161 LYS N N 121.9 . 1 1311 . 161 LYS H H 8.17 . 1 1312 . 161 LYS CA C 56.5 . 1 1313 . 161 LYS HA H 4.02 . 1 1314 . 161 LYS CB C 33.1 . 1 1315 . 161 LYS HB2 H 1.44 . 2 1316 . 161 LYS HB3 H 1.53 . 2 1317 . 161 LYS CG C 25.3 . 1 1318 . 161 LYS HG2 H 1.12 . 2 1319 . 161 LYS HG3 H 0.41 . 2 1320 . 161 LYS CD C 29.2 . 1 1321 . 161 LYS HD2 H 1.41 . 1 1322 . 161 LYS HD3 H 1.41 . 1 1323 . 161 LYS CE C 42.8 . 1 1324 . 161 LYS HE2 H 2.77 . 2 1325 . 161 LYS HE3 H 2.61 . 2 1326 . 162 ARG N N 121.1 . 1 1327 . 162 ARG H H 8.34 . 1 1328 . 162 ARG CA C 55.7 . 1 1329 . 162 ARG HA H 4.33 . 1 1330 . 162 ARG CB C 31.3 . 1 1331 . 162 ARG HB2 H 1.81 . 2 1332 . 162 ARG HB3 H 1.65 . 2 1333 . 162 ARG CG C 26.8 . 1 1334 . 162 ARG HG2 H 1.53 . 1 1335 . 162 ARG HG3 H 1.53 . 1 1336 . 162 ARG CD C 43.1 . 1 1337 . 162 ARG HD2 H 3.11 . 1 1338 . 162 ARG HD3 H 3.11 . 1 1339 . 163 GLY N N 109.6 . 1 1340 . 163 GLY H H 8.39 . 1 1341 . 163 GLY CA C 45.2 . 1 1342 . 163 GLY HA2 H 4.67 . 2 1343 . 164 ILE N N 119.5 . 1 1344 . 164 ILE H H 7.90 . 1 1345 . 164 ILE CA C 60.9 . 1 1346 . 164 ILE HA H 4.12 . 1 1347 . 164 ILE CB C 38.5 . 1 1348 . 164 ILE HB H 1.76 . 1 1349 . 164 ILE HG2 H 0.75 . 1 1350 . 164 ILE CG2 C 17.4 . 1 1351 . 164 ILE CG1 C 27.0 . 1 1352 . 164 ILE HG12 H 1.28 . 2 1353 . 164 ILE HG13 H 1.04 . 2 1354 . 164 ILE HD1 H 0.76 . 1 1355 . 164 ILE CD1 C 13.0 . 1 1356 . 165 ARG CA C 55.5 . 1 1357 . 165 ARG HA H 4.80 . 1 1358 . 165 ARG CB C 31.2 . 1 1359 . 165 ARG HB2 H 2.35 . 2 1360 . 165 ARG HB3 H 2.19 . 2 1361 . 165 ARG CG C 24.6 . 1 1362 . 165 ARG HG2 H 1.92 . 2 1363 . 165 ARG HG3 H 1.84 . 2 1364 . 165 ARG HD2 H 3.58 . 2 1365 . 165 ARG HD3 H 3.52 . 2 1366 . 166 ASP N N 127.2 . 1 1367 . 166 ASP H H 7.96 . 1 1368 . 166 ASP CA C 55.7 . 1 1369 . 166 ASP HA H 4.36 . 1 1370 . 166 ASP CB C 42.2 . 1 1371 . 166 ASP HB2 H 2.65 . 2 1372 . 166 ASP HB3 H 2.51 . 2 stop_ save_