data_4022 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential NMR Assignment of 1H, 13C, and 15N Resonances of Human Carbonic Anhydrase I (HCAI) by Triple-Resonance NMR Techniques and Extensive Amino Acid Specific 15N Labeling ; _BMRB_accession_number 4022 _BMRB_flat_file_name bmr4022.str _Entry_type update _Submission_date 1996-10-20 _Accession_date 1997-04-25 _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 Sethson Ingmar . . 2 Edlund Ulf . . 3 Holak Tadeusz A. . 4 Ross Alfred . . 5 Jonsson Bengt-Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 825 "13C chemical shifts" 743 "15N chemical shifts" 243 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-15 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Sethson, I., Edlund, U., Holak, T.A., Ross, A., and Johnson, B-H., "Sequential Assignment of 1H, 13C and 15N Resonances of Human Carbonic Anhydrase I by Triple-resonance NMR Techniques and Extensive Amino Acid-Specific 15N-Labeling," J. Biomol. NMR 8, 417-428 (1996). ; _Citation_title ; Sequential Assignment of 1H, 13C and 15N Resonances of Human Carbonic Anhydrase I by Triple-Resonance NMR Techniques and Extensive Amino Acid-Specific 15N-Labeling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 97161090 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sethson Ingmar . . 2 Edlund Ulf . . 3 Holak Tadeusz A. . 4 Ross Alfred . . 5 Jonsson Bengt-Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 8 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 417 _Page_last 428 _Year 1996 _Details . save_ ################################## # Molecular system description # ################################## save_system_HCA_I _Saveframe_category molecular_system _Mol_system_name 'human carbonic anhydrase I' _Abbreviation_common 'HCA I' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HCA I' $HCA_I stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully reduced' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HCA_I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human carbonic anhydrase I' _Name_variant 'human carbonic anhydrase B' _Abbreviation_common 'HCA I' _Molecular_mass 29500 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 260 _Mol_residue_sequence ; ASPDWGYDDKNGPEQWSKLY PIANGNNQSPVDIKTSETKH DTSLKPISVSYNPATAKEII NVGHSFHVNFEDNDNRSVLK GGPFSDSYRLFQFHFHWGST NEHGSEHTVDGVKYSAELHV AHWNSAKYSSLAEAASKADG LAVIGVLMKVGEANPKLQKV LDALQAIKTKGKRAPFTNFD PSTLLPSSLDFWTYPGSLTH PPLYESVTWIICKESISVSS EQLAQFRSLLSNVEGDNAVP MQHNNRPTQPLKGRTVRASF ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 PRO 4 ASP 5 TRP 6 GLY 7 TYR 8 ASP 9 ASP 10 LYS 11 ASN 12 GLY 13 PRO 14 GLU 15 GLN 16 TRP 17 SER 18 LYS 19 LEU 20 TYR 21 PRO 22 ILE 23 ALA 24 ASN 25 GLY 26 ASN 27 ASN 28 GLN 29 SER 30 PRO 31 VAL 32 ASP 33 ILE 34 LYS 35 THR 36 SER 37 GLU 38 THR 39 LYS 40 HIS 41 ASP 42 THR 43 SER 44 LEU 45 LYS 46 PRO 47 ILE 48 SER 49 VAL 50 SER 51 TYR 52 ASN 53 PRO 54 ALA 55 THR 56 ALA 57 LYS 58 GLU 59 ILE 60 ILE 61 ASN 62 VAL 63 GLY 64 HIS 65 SER 66 PHE 67 HIS 68 VAL 69 ASN 70 PHE 71 GLU 72 ASP 73 ASN 74 ASP 75 ASN 76 ARG 77 SER 78 VAL 79 LEU 80 LYS 81 GLY 82 GLY 83 PRO 84 PHE 85 SER 86 ASP 87 SER 88 TYR 89 ARG 90 LEU 91 PHE 92 GLN 93 PHE 94 HIS 95 PHE 96 HIS 97 TRP 98 GLY 99 SER 100 THR 101 ASN 102 GLU 103 HIS 104 GLY 105 SER 106 GLU 107 HIS 108 THR 109 VAL 110 ASP 111 GLY 112 VAL 113 LYS 114 TYR 115 SER 116 ALA 117 GLU 118 LEU 119 HIS 120 VAL 121 ALA 122 HIS 123 TRP 124 ASN 125 SER 126 ALA 127 LYS 128 TYR 129 SER 130 SER 131 LEU 132 ALA 133 GLU 134 ALA 135 ALA 136 SER 137 LYS 138 ALA 139 ASP 140 GLY 141 LEU 142 ALA 143 VAL 144 ILE 145 GLY 146 VAL 147 LEU 148 MET 149 LYS 150 VAL 151 GLY 152 GLU 153 ALA 154 ASN 155 PRO 156 LYS 157 LEU 158 GLN 159 LYS 160 VAL 161 LEU 162 ASP 163 ALA 164 LEU 165 GLN 166 ALA 167 ILE 168 LYS 169 THR 170 LYS 171 GLY 172 LYS 173 ARG 174 ALA 175 PRO 176 PHE 177 THR 178 ASN 179 PHE 180 ASP 181 PRO 182 SER 183 THR 184 LEU 185 LEU 186 PRO 187 SER 188 SER 189 LEU 190 ASP 191 PHE 192 TRP 193 THR 194 TYR 195 PRO 196 GLY 197 SER 198 LEU 199 THR 200 HIS 201 PRO 202 PRO 203 LEU 204 TYR 205 GLU 206 SER 207 VAL 208 THR 209 TRP 210 ILE 211 ILE 212 CYS 213 LYS 214 GLU 215 SER 216 ILE 217 SER 218 VAL 219 SER 220 SER 221 GLU 222 GLN 223 LEU 224 ALA 225 GLN 226 PHE 227 ARG 228 SER 229 LEU 230 LEU 231 SER 232 ASN 233 VAL 234 GLU 235 GLY 236 ASP 237 ASN 238 ALA 239 VAL 240 PRO 241 MET 242 GLN 243 HIS 244 ASN 245 ASN 246 ARG 247 PRO 248 THR 249 GLN 250 PRO 251 LEU 252 LYS 253 GLY 254 ARG 255 THR 256 VAL 257 ARG 258 ALA 259 SER 260 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 1AZM "Drug-Protein Interactions: Structure Of Sulfonamide Drug Complexed With Human Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 1BZM "Drug-Protein Interactions: Structure Of Sulfonamide Drug Complexed With Human Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 1CRM "Structure And Function Of Carbonic Anhydrases" 100.00 260 99.23 99.62 0.00e+00 PDB 1CZM "Drug-Protein Interactions: Structure Of Sulfonamide Drug Complexed With Human Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 1HCB "Enzyme-Substrate Interactions: Structure Of Human Carbonic Anhydrase I Complexed With Bicarbonate" 100.00 260 100.00 100.00 0.00e+00 PDB 1HUG "Differences In Anionic Inhibition Of Human Carbonic Anhydrase I Revealed From The Structures Of Iodide And Gold Cyanide Inhibit" 100.00 260 100.00 100.00 0.00e+00 PDB 1HUH "Differences In Anionic Inhibition Of Human Carbonic Anhydrase I Revealed From The Structures Of Iodide And Gold Cyanide Inhibit" 100.00 260 100.00 100.00 0.00e+00 PDB 1J9W "Solution Structure Of The Cai Michigan 1 Variant" 100.00 260 99.62 99.62 0.00e+00 PDB 1JV0 "The Crystal Structure Of The Zinc(Ii) Adduct Of The Cai Michigan 1 Variant" 100.00 260 99.62 99.62 0.00e+00 PDB 2CAB "Structure, Refinement And Function Of Carbonic Anhydrase Isozymes. Refinement Of Human Carbonic Anhydrase I" 100.00 260 99.23 99.62 0.00e+00 PDB 2FOY "Human Carbonic Anhydrase I Complexed With A Two-Prong Inhibitor" 100.00 260 100.00 100.00 0.00e+00 PDB 2FW4 "Carbonic Anhydrase Activators. The First X-ray Crystallographic Study Of An Activator Of Isoform I, Structure With L-histidine." 100.00 260 100.00 100.00 0.00e+00 PDB 2IT4 "X Ray Structure Of The Complex Between Carbonic Anhydrase I And The Phosphonate Antiviral Drug Foscarnet" 98.46 256 100.00 100.00 0.00e+00 PDB 2NMX "Structure Of Inhibitor Binding To Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 2NN1 "Structure Of Inhibitor Binding To Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 2NN7 "Structure Of Inhibitor Binding To Carbonic Anhydrase I" 100.00 260 100.00 100.00 0.00e+00 PDB 3LXE "Human Carbonic Anhydrase I In Complex With Topiramate" 100.00 260 100.00 100.00 0.00e+00 PDB 3W6H "Crystal Structure Of 19f Probe-labeled Hcai In Complex With Acetazolamide" 100.00 260 100.00 100.00 0.00e+00 PDB 3W6I "Crystal Structure Of 19f Probe-labeled Hcai" 100.00 260 100.00 100.00 0.00e+00 PDB 4WR7 "Crystal Structure Of Human Carbonic Anhydrase Isozyme I With 2,3,5,6- Tetrafluoro-4-(propylthio)benzenesulfonamide." 99.62 260 100.00 100.00 0.00e+00 PDB 4WUP "Crystal Structure Of Human Carbonic Anhydrase Isozyme I With 4-[(2- Hydroxyethyl)thio]benzenesulfonamide" 99.62 260 100.00 100.00 0.00e+00 PDB 4WUQ "Crystal Structure Of Human Carbonic Anhydrase Isozyme I With 2,3,5,6- Tetrafluoro-4-piperidin-1-ylbenzenesulfonamide" 99.62 260 100.00 100.00 0.00e+00 EMBL CAA28663 "unnamed protein product [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 GB AAA51910 "carbonic anhydrase I (EC 4.2.1.1) [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 GB AAH27890 "CA1 protein [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 GB ABM81856 "carbonic anhydrase I [synthetic construct]" 100.00 261 100.00 100.00 0.00e+00 GB ABM85017 "carbonic anhydrase I [synthetic construct]" 100.00 261 100.00 100.00 0.00e+00 GB ACJ13649 "epididymis secretory protein Li 11 [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 REF NP_001122301 "carbonic anhydrase 1 isoform a [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 REF NP_001122302 "carbonic anhydrase 1 isoform a [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 REF NP_001122303 "carbonic anhydrase 1 isoform a [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 REF NP_001158302 "carbonic anhydrase 1 isoform a [Homo sapiens]" 100.00 261 100.00 100.00 0.00e+00 REF NP_001182062 "carbonic anhydrase 1 [Pan troglodytes]" 100.00 261 99.23 100.00 0.00e+00 SP P00915 "RecName: Full=Carbonic anhydrase 1; AltName: Full=Carbonate dehydratase I; AltName: Full=Carbonic anhydrase B; Short=CAB; AltNa" 100.00 261 100.00 100.00 0.00e+00 SP Q7M316 "RecName: Full=Carbonic anhydrase 1; AltName: Full=Carbonate dehydratase I; AltName: Full=Carbonic anhydrase I; Short=CA-I" 100.00 261 98.08 98.85 0.00e+00 SP Q7M317 "RecName: Full=Carbonic anhydrase 1; AltName: Full=Carbonate dehydratase I; AltName: Full=Carbonic anhydrase I; Short=CA-I" 100.00 261 99.23 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $HCA_I human 9606 Eukaryota Metazoa Homo sapiens generic 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 $HCA_I 'recombinant technology' 'E. coli' Escherichia coli BL21 (DE3) plasmid pHCAI 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 $HCA_I 0.8 mM [U-15N] D2O 5 % . H2O 95 % . 'phosphate buffer' 40 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HCA_I 0.8 mM [U-13C] D2O 5 % . H2O 95 % . 'phosphate buffer' 40 mM . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details ; 15N residue selective labeling of the following amino acids: Ala,Gly, His, Ile, Leu, Lys, Phe, Ser, Trp and Val listed below ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HCA_I 0.8 mM ; [15N]-Ala;[15N]-Gly;[15N]-His;[15N]-Ile;[15N]-Leu;[15N]-Lys;[15N]-Phe; [15N]-Ser;[15N]-Trp;[15N]-Val ; D2O 5 % . H2O 95 % . 'phosphate buffer' 40 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . na temperature 303 . 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 H2O H 1 protons ppm 4.72 . direct . . . . 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_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'HCA I' _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 ALA H H 8.27 0.01 1 2 . 1 ALA N N 124.5 0.2 1 3 . 1 ALA CA C 51.9 0.2 1 4 . 1 ALA CB C 19.4 0.2 1 5 . 1 ALA C C 173.9 0.2 1 6 . 1 ALA HA H 4.13 0.01 1 7 . 2 SER H H 8.25 0.01 1 8 . 2 SER N N 116.5 0.2 1 9 . 2 SER CA C 57.5 0.2 1 10 . 2 SER CB C 63.3 0.2 1 11 . 2 SER C C 170.2 0.2 1 12 . 2 SER HA H 4.00 0.01 1 13 . 3 PRO CA C 63.1 0.2 1 14 . 3 PRO CB C 32.2 0.2 1 15 . 3 PRO C C 176.6 0.2 1 16 . 3 PRO HA H 4.46 0.01 1 17 . 3 PRO HB2 H 2.21 0.01 2 18 . 3 PRO HB3 H 1.83 0.01 2 19 . 4 ASP H H 8.44 0.01 1 20 . 4 ASP N N 121.7 0.2 1 21 . 4 ASP CA C 54.6 0.2 1 22 . 4 ASP CB C 41.3 0.2 1 23 . 4 ASP C C 174.6 0.2 1 24 . 4 ASP HA H 4.55 0.01 1 25 . 4 ASP HB2 H 2.63 0.01 1 26 . 4 ASP HB3 H 2.63 0.01 1 27 . 5 TRP H H 7.4 0.01 1 28 . 5 TRP N N 115.9 0.2 1 29 . 5 TRP CA C 54.7 0.2 1 30 . 5 TRP CB C 31.4 0.2 1 31 . 5 TRP C C 173.9 0.2 1 32 . 5 TRP HA H 4.96 0.01 1 33 . 5 TRP HB2 H 3.26 0.01 2 34 . 5 TRP HB3 H 2.99 0.01 2 35 . 6 GLY H H 8.26 0.01 1 36 . 6 GLY N N 109.9 0.2 1 37 . 6 GLY CA C 45.4 0.2 1 38 . 6 GLY C C 171.6 0.2 1 39 . 6 GLY HA2 H 3.71 0.01 2 40 . 6 GLY HA3 H 3.66 0.01 2 41 . 7 TYR H H 9.06 0.01 1 42 . 7 TYR N N 118.5 0.2 1 43 . 7 TYR CA C 58.6 0.2 1 44 . 7 TYR CB C 39.7 0.2 1 45 . 7 TYR C C 175.5 0.2 1 46 . 7 TYR HA H 4.89 0.01 1 47 . 7 TYR HB2 H 3.2 0.01 2 48 . 7 TYR HB3 H 2.38 0.01 2 49 . 8 ASP H H 8.29 0.01 1 50 . 8 ASP N N 122.4 0.2 1 51 . 8 ASP CA C 53.9 0.2 1 52 . 8 ASP CB C 42.2 0.2 1 53 . 8 ASP C C 175.6 0.2 1 54 . 8 ASP HA H 5.07 0.01 1 55 . 8 ASP HB2 H 2.9 0.01 1 56 . 8 ASP HB3 H 2.9 0.01 1 57 . 9 ASP H H 8.45 0.01 1 58 . 9 ASP N N 117.3 0.2 1 59 . 9 ASP CA C 56.9 0.2 1 60 . 9 ASP CB C 40.5 0.2 1 61 . 9 ASP C C 177.9 0.2 1 62 . 9 ASP HA H 4.35 0.01 1 63 . 9 ASP HB2 H 2.65 0.01 1 64 . 9 ASP HB3 H 2.65 0.01 1 65 . 10 LYS H H 8.38 0.01 1 66 . 10 LYS N N 116.7 0.2 1 67 . 10 LYS CA C 57.3 0.2 1 68 . 10 LYS CB C 32.7 0.2 1 69 . 10 LYS C C 177.00 0.2 1 70 . 10 LYS HA H 4.25 0.01 1 71 . 10 LYS HB2 H 1.8 0.01 1 72 . 10 LYS HB3 H 1.8 0.01 1 73 . 11 ASN H H 7.94 0.01 1 74 . 11 ASN N N 118.1 0.2 1 75 . 11 ASN CA C 52.2 0.2 1 76 . 11 ASN CB C 38.8 0.2 1 77 . 11 ASN C C 176.00 0.2 1 78 . 11 ASN HA H 4.79 0.01 1 79 . 11 ASN HB2 H 3.13 0.01 2 80 . 11 ASN HB3 H 2.73 0.01 2 81 . 12 GLY H H 7.52 0.01 1 82 . 12 GLY N N 109.1 0.2 1 83 . 12 GLY CA C 45.5 0.2 1 84 . 12 GLY HA2 H 4.94 0.01 2 85 . 12 GLY HA3 H 3.88 0.01 2 86 . 13 PRO CA C 64.2 0.2 1 87 . 13 PRO CB C 32.00 0.2 1 88 . 13 PRO HA H 3.58 0.01 1 89 . 13 PRO HB2 H 1.7 0.01 2 90 . 13 PRO HB3 H 1.41 0.01 2 91 . 14 GLU H H 8.69 0.01 1 92 . 14 GLU N N 116.9 0.2 1 93 . 14 GLU CA C 58.5 0.2 1 94 . 14 GLU CB C 28.7 0.2 1 95 . 14 GLU C C 177.00 0.2 1 96 . 14 GLU HA H 4.01 0.01 1 97 . 14 GLU HB2 H 2.05 0.01 2 98 . 14 GLU HB3 H 1.9 0.01 2 99 . 15 GLN H H 8.5 0.01 1 100 . 15 GLN N N 116.00 0.2 1 101 . 15 GLN CA C 55.1 0.2 1 102 . 15 GLN CB C 29.1 0.2 1 103 . 15 GLN C C 178.2 0.2 1 104 . 15 GLN HA H 4.55 0.01 1 105 . 15 GLN HB2 H 2.37 0.01 2 106 . 15 GLN HB3 H 2.01 0.01 2 107 . 16 TRP H H 7.42 0.01 1 108 . 16 TRP N N 120.7 0.2 1 109 . 16 TRP CA C 58.5 0.2 1 110 . 16 TRP CB C 29.2 0.2 1 111 . 16 TRP C C 178.00 0.2 1 112 . 16 TRP HA H 4.6 0.01 1 113 . 17 SER H H 9.01 0.01 1 114 . 17 SER N N 113.2 0.2 1 115 . 17 SER CA C 60.2 0.2 1 116 . 17 SER CB C 62.00 0.2 1 117 . 17 SER C C 174.9 0.2 1 118 . 17 SER HA H 4.27 0.01 1 119 . 17 SER HB2 H 3.81 0.01 1 120 . 17 SER HB3 H 3.81 0.01 1 121 . 18 LYS H H 7.45 0.01 1 122 . 18 LYS N N 120.4 0.2 1 123 . 18 LYS CA C 58.6 0.2 1 124 . 18 LYS CB C 32.3 0.2 1 125 . 18 LYS C C 177.3 0.2 1 126 . 18 LYS HA H 4.05 0.01 1 127 . 18 LYS HB2 H 1.91 0.01 1 128 . 18 LYS HB3 H 1.91 0.01 1 129 . 19 LEU H H 7.29 0.01 1 130 . 19 LEU N N 117.4 0.2 1 131 . 19 LEU CA C 55.2 0.2 1 132 . 19 LEU CB C 44.8 0.2 1 133 . 19 LEU C C 176.3 0.2 1 134 . 19 LEU HA H 4.19 0.01 1 135 . 19 LEU HB2 H 1.65 0.01 2 136 . 19 LEU HB3 H 1.03 0.01 2 137 . 20 TYR H H 8.39 0.01 1 138 . 20 TYR N N 116.4 0.2 1 139 . 20 TYR CA C 55.00 0.2 1 140 . 20 TYR CB C 39.00 0.2 1 141 . 21 PRO CA C 65.2 0.2 1 142 . 21 PRO CB C 31.8 0.2 1 143 . 21 PRO C C 178.4 0.2 1 144 . 21 PRO HA H 4.41 0.01 1 145 . 21 PRO HB2 H 2.37 0.01 2 146 . 21 PRO HB3 H 1.89 0.01 2 147 . 22 ILE H H 7.99 0.01 1 148 . 22 ILE N N 119.7 0.2 1 149 . 22 ILE CA C 60.7 0.2 1 150 . 22 ILE CB C 38.9 0.2 1 151 . 22 ILE C C 174.9 0.2 1 152 . 22 ILE HA H 4.13 0.01 1 153 . 22 ILE HB H 1.82 0.01 1 154 . 23 ALA H H 8.48 0.01 1 155 . 23 ALA N N 123.5 0.2 1 156 . 23 ALA CA C 53.7 0.2 1 157 . 23 ALA CB C 18.6 0.2 1 158 . 23 ALA C C 178.5 0.2 1 159 . 23 ALA HA H 4.1 0.01 1 160 . 23 ALA HB H 1.22 0.01 1 161 . 24 ASN H H 7.17 0.01 1 162 . 24 ASN N N 112.2 0.2 1 163 . 24 ASN CA C 52.2 0.2 1 164 . 24 ASN CB C 38.5 0.2 1 165 . 24 ASN C C 175.5 0.2 1 166 . 24 ASN HA H 5.03 0.01 1 167 . 24 ASN HB2 H 3.17 0.01 2 168 . 24 ASN HB3 H 2.59 0.01 2 169 . 25 GLY H H 8.35 0.01 1 170 . 25 GLY N N 108.7 0.2 1 171 . 25 GLY CA C 45.00 0.2 1 172 . 25 GLY C C 173.5 0.2 1 173 . 25 GLY HA2 H 4.26 0.01 2 174 . 25 GLY HA3 H 4.09 0.01 2 175 . 26 ASN H H 9.26 0.01 1 176 . 26 ASN N N 116.7 0.2 1 177 . 26 ASN CA C 54.1 0.2 1 178 . 26 ASN CB C 39.4 0.2 1 179 . 26 ASN C C 175.00 0.2 1 180 . 26 ASN HA H 4.69 0.01 1 181 . 26 ASN HB2 H 2.64 0.01 1 182 . 26 ASN HB3 H 2.64 0.01 1 183 . 27 ASN H H 8.78 0.01 1 184 . 27 ASN N N 119.4 0.2 1 185 . 27 ASN CA C 51.4 0.2 1 186 . 27 ASN CB C 39.8 0.2 1 187 . 27 ASN C C 174.5 0.2 1 188 . 27 ASN HA H 4.9 0.01 1 189 . 27 ASN HB2 H 2.71 0.01 2 190 . 27 ASN HB3 H 2.25 0.01 2 191 . 28 GLN H H 7.57 0.01 1 192 . 28 GLN N N 114.5 0.2 1 193 . 28 GLN CA C 55.5 0.2 1 194 . 28 GLN CB C 31.9 0.2 1 195 . 28 GLN HA H 4.44 0.01 1 196 . 29 SER H H 8.1 0.01 1 197 . 29 SER N N 117.5 0.2 1 198 . 29 SER CA C 57.00 0.2 1 199 . 29 SER CB C 63.2 0.2 1 200 . 29 SER C C 172.3 0.2 1 201 . 29 SER HA H 4.81 0.01 1 202 . 30 PRO CA C 61.8 0.2 1 203 . 30 PRO CB C 33.4 0.2 1 204 . 30 PRO C C 172.9 0.2 1 205 . 30 PRO HA H 3.7 0.01 1 206 . 31 VAL H H 6.13 0.01 1 207 . 31 VAL N N 107.1 0.2 1 208 . 31 VAL CA C 59.00 0.2 1 209 . 31 VAL CB C 35.5 0.2 1 210 . 31 VAL C C 173.1 0.2 1 211 . 31 VAL HA H 4.6 0.01 1 212 . 31 VAL HB H 1.79 0.01 1 213 . 32 ASP H H 8.41 0.01 1 214 . 32 ASP N N 119.2 0.2 1 215 . 32 ASP CA C 52.4 0.2 1 216 . 32 ASP CB C 42.3 0.2 1 217 . 32 ASP C C 175.1 0.2 1 218 . 32 ASP HA H 4.89 0.01 1 219 . 32 ASP HB2 H 2.3 0.01 2 220 . 32 ASP HB3 H 2.16 0.01 2 221 . 33 ILE H H 8.46 0.01 1 222 . 33 ILE N N 127.9 0.2 1 223 . 33 ILE CA C 61.6 0.2 1 224 . 33 ILE CB C 37.6 0.2 1 225 . 33 ILE C C 173.9 0.2 1 226 . 33 ILE HA H 3.31 0.01 1 227 . 33 ILE HB H 1.34 0.01 1 228 . 34 LYS H H 8.02 0.01 1 229 . 34 LYS N N 129.2 0.2 1 230 . 34 LYS CA C 54.2 0.2 1 231 . 34 LYS CB C 31.7 0.2 1 232 . 34 LYS C C 179.1 0.2 1 233 . 34 LYS HA H 4.84 0.01 1 234 . 34 LYS HB2 H 1.62 0.01 1 235 . 34 LYS HB3 H 1.62 0.01 1 236 . 35 THR H H 10.08 0.01 1 237 . 35 THR N N 123.4 0.2 1 238 . 35 THR CA C 66.2 0.2 1 239 . 35 THR CB C 68.9 0.2 1 240 . 35 THR C C 177.9 0.2 1 241 . 35 THR HA H 3.8 0.01 1 242 . 35 THR HB H 4.36 0.01 1 243 . 36 SER H H 8.78 0.01 1 244 . 36 SER N N 116.9 0.2 1 245 . 36 SER CA C 59.9 0.2 1 246 . 36 SER CB C 62.8 0.2 1 247 . 36 SER C C 175.2 0.2 1 248 . 36 SER HA H 4.35 0.01 1 249 . 36 SER HB2 H 4.05 0.01 2 250 . 36 SER HB3 H 3.87 0.01 2 251 . 37 GLU H H 7.64 0.01 1 252 . 37 GLU N N 119.00 0.2 1 253 . 37 GLU CA C 55.4 0.2 1 254 . 37 GLU CB C 30.8 0.2 1 255 . 37 GLU C C 177.2 0.2 1 256 . 37 GLU HA H 4.6 0.01 1 257 . 37 GLU HB2 H 2.37 0.01 2 258 . 37 GLU HB3 H 1.72 0.01 2 259 . 38 THR H H 7.26 0.01 1 260 . 38 THR N N 112.5 0.2 1 261 . 38 THR CA C 61.4 0.2 1 262 . 38 THR CB C 71.1 0.2 1 263 . 38 THR C C 174.00 0.2 1 264 . 38 THR HA H 4.58 0.01 1 265 . 38 THR HB H 3.94 0.01 1 266 . 39 LYS H H 8.35 0.01 1 267 . 39 LYS N N 121.4 0.2 1 268 . 39 LYS CA C 54.00 0.2 1 269 . 39 LYS CB C 34.6 0.2 1 270 . 39 LYS HA H 4.6 0.01 1 271 . 39 LYS HB2 H 1.7 0.01 1 272 . 39 LYS HB3 H 1.7 0.01 1 273 . 40 HIS H H 9.12 0.01 1 274 . 40 HIS N N 126.3 0.2 1 275 . 40 HIS CA C 55.3 0.2 1 276 . 40 HIS CB C 27.9 0.2 1 277 . 40 HIS C C 173.7 0.2 1 278 . 40 HIS HA H 4.61 0.01 1 279 . 40 HIS HB2 H 3.03 0.01 1 280 . 40 HIS HB3 H 3.03 0.01 1 281 . 41 ASP H H 8.05 0.01 1 282 . 41 ASP N N 127.7 0.2 1 283 . 41 ASP CA C 52.5 0.2 1 284 . 41 ASP CB C 42.00 0.2 1 285 . 41 ASP C C 176.4 0.2 1 286 . 41 ASP HA H 4.87 0.01 1 287 . 41 ASP HB2 H 2.3 0.01 1 288 . 41 ASP HB3 H 2.3 0.01 1 289 . 42 THR H H 8.38 0.01 1 290 . 42 THR N N 116.6 0.2 1 291 . 42 THR CA C 63.1 0.2 1 292 . 42 THR CB C 68.4 0.2 1 293 . 42 THR C C 175.00 0.2 1 294 . 42 THR HA H 3.98 0.01 1 295 . 42 THR HB H 4.39 0.01 1 296 . 43 SER H H 8.73 0.01 1 297 . 43 SER N N 117.4 0.2 1 298 . 43 SER CA C 59.4 0.2 1 299 . 43 SER CB C 63.7 0.2 1 300 . 43 SER C C 175.3 0.2 1 301 . 43 SER HA H 4.35 0.01 1 302 . 43 SER HB2 H 3.86 0.01 1 303 . 43 SER HB3 H 3.86 0.01 1 304 . 44 LEU H H 7.03 0.01 1 305 . 44 LEU N N 122.6 0.2 1 306 . 44 LEU CA C 55.1 0.2 1 307 . 44 LEU CB C 42.00 0.2 1 308 . 44 LEU C C 175.9 0.2 1 309 . 44 LEU HA H 3.98 0.01 1 310 . 44 LEU HB2 H 1.76 0.01 2 311 . 44 LEU HB3 H 1.11 0.01 2 312 . 45 LYS H H 7.42 0.01 1 313 . 45 LYS N N 124.4 0.2 1 314 . 45 LYS CA C 53.6 0.2 1 315 . 45 LYS CB C 31.8 0.2 1 316 . 45 LYS C C 173.6 0.2 1 317 . 45 LYS HA H 4.64 0.01 1 318 . 45 LYS HB2 H 1.71 0.01 1 319 . 45 LYS HB3 H 1.71 0.01 1 320 . 46 PRO CA C 63.00 0.2 1 321 . 46 PRO CB C 31.8 0.2 1 322 . 46 PRO C C 179.5 0.2 1 323 . 46 PRO HA H 4.62 0.01 1 324 . 46 PRO HB2 H 2.36 0.01 2 325 . 46 PRO HB3 H 1.72 0.01 2 326 . 47 ILE H H 8.55 0.01 1 327 . 47 ILE N N 120.6 0.2 1 328 . 47 ILE CA C 60.5 0.2 1 329 . 47 ILE CB C 38.8 0.2 1 330 . 47 ILE C C 175.1 0.2 1 331 . 47 ILE HA H 4.38 0.01 1 332 . 47 ILE HB H 1.58 0.01 1 333 . 48 SER H H 8.5 0.01 1 334 . 48 SER N N 118.9 0.2 1 335 . 48 SER CA C 56.5 0.2 1 336 . 48 SER CB C 64.4 0.2 1 337 . 48 SER C C 173.00 0.2 1 338 . 48 SER HA H 4.61 0.01 1 339 . 48 SER HB2 H 3.47 0.01 1 340 . 48 SER HB3 H 3.47 0.01 1 341 . 49 VAL H H 8.32 0.01 1 342 . 49 VAL N N 120.4 0.2 1 343 . 49 VAL CA C 59.2 0.2 1 344 . 49 VAL CB C 33.1 0.2 1 345 . 49 VAL C C 175.2 0.2 1 346 . 49 VAL HA H 4.42 0.01 1 347 . 49 VAL HB H 1.03 0.01 1 348 . 50 SER H H 7.98 0.01 1 349 . 50 SER N N 119.4 0.2 1 350 . 50 SER CA C 56.00 0.2 1 351 . 50 SER CB C 62.8 0.2 1 352 . 50 SER C C 172.7 0.2 1 353 . 50 SER HA H 4.39 0.01 1 354 . 50 SER HB2 H 3.78 0.01 2 355 . 50 SER HB3 H 3.49 0.01 2 356 . 51 TYR H H 9.00 0.01 1 357 . 51 TYR N N 125.1 0.2 1 358 . 51 TYR CA C 52.4 0.2 1 359 . 51 TYR CB C 38.00 0.2 1 360 . 51 TYR C C 174.2 0.2 1 361 . 51 TYR HA H 5.25 0.01 1 362 . 51 TYR HB2 H 3.27 0.01 2 363 . 51 TYR HB3 H 2.64 0.01 2 364 . 52 ASN H H 8.66 0.01 1 365 . 52 ASN N N 120.8 0.2 1 366 . 52 ASN CA C 49.2 0.2 1 367 . 52 ASN CB C 41.00 0.2 1 368 . 52 ASN C C 175.5 0.2 1 369 . 52 ASN HA H 5.29 0.01 1 370 . 53 PRO CA C 64.4 0.2 1 371 . 53 PRO CB C 32.00 0.2 1 372 . 53 PRO C C 177.3 0.2 1 373 . 53 PRO HA H 4.52 0.01 1 374 . 53 PRO HB2 H 2.05 0.01 1 375 . 53 PRO HB3 H 2.05 0.01 1 376 . 54 ALA H H 8.4 0.01 1 377 . 54 ALA N N 120.00 0.2 1 378 . 54 ALA CA C 53.8 0.2 1 379 . 54 ALA CB C 18.3 0.2 1 380 . 54 ALA C C 178.8 0.2 1 381 . 54 ALA HA H 4.6 0.01 1 382 . 54 ALA HB H 1.45 0.01 1 383 . 55 THR H H 8.17 0.01 1 384 . 55 THR N N 104.3 0.2 1 385 . 55 THR CA C 62.8 0.2 1 386 . 55 THR CB C 70.7 0.2 1 387 . 55 THR C C 175.3 0.2 1 388 . 55 THR HA H 4.36 0.01 1 389 . 55 THR HB H 5.03 0.01 1 390 . 56 ALA H H 7.39 0.01 1 391 . 56 ALA N N 127.5 0.2 1 392 . 56 ALA CA C 55.00 0.2 1 393 . 56 ALA CB C 17.9 0.2 1 394 . 56 ALA C C 176.00 0.2 1 395 . 56 ALA HA H 3.18 0.01 1 396 . 56 ALA HB H 1.51 0.01 1 397 . 57 LYS H H 8.18 0.01 1 398 . 57 LYS N N 123.2 0.2 1 399 . 57 LYS CA C 57.7 0.2 1 400 . 57 LYS CB C 37.00 0.2 1 401 . 57 LYS C C 177.1 0.2 1 402 . 57 LYS HA H 4.78 0.01 1 403 . 57 LYS HB2 H 1.67 0.01 1 404 . 57 LYS HB3 H 1.67 0.01 1 405 . 58 GLU H H 7.79 0.01 1 406 . 58 GLU N N 116.00 0.2 1 407 . 58 GLU CA C 55.4 0.2 1 408 . 58 GLU CB C 33.6 0.2 1 409 . 58 GLU C C 171.5 0.2 1 410 . 58 GLU HA H 5.22 0.01 1 411 . 58 GLU HB2 H 1.92 0.01 1 412 . 58 GLU HB3 H 1.92 0.01 1 413 . 59 ILE H H 9.18 0.01 1 414 . 59 ILE N N 123.1 0.2 1 415 . 59 ILE CA C 58.3 0.2 1 416 . 59 ILE CB C 42.3 0.2 1 417 . 59 ILE C C 172.8 0.2 1 418 . 59 ILE HA H 5.52 0.01 1 419 . 59 ILE HB H 1.07 0.01 1 420 . 60 ILE H H 8.8 0.01 1 421 . 60 ILE N N 122.9 0.2 1 422 . 60 ILE CA C 59.2 0.2 1 423 . 60 ILE CB C 43.00 0.2 1 424 . 60 ILE C C 174.00 0.2 1 425 . 60 ILE HA H 5.15 0.01 1 426 . 60 ILE HB H 1.54 0.01 1 427 . 61 ASN H H 8.37 0.01 1 428 . 61 ASN N N 125.4 0.2 1 429 . 61 ASN CA C 53.1 0.2 1 430 . 61 ASN CB C 38.2 0.2 1 431 . 61 ASN C C 176.7 0.2 1 432 . 61 ASN HA H 4.55 0.01 1 433 . 61 ASN HB2 H 3.12 0.01 1 434 . 61 ASN HB3 H 3.12 0.01 1 435 . 62 VAL H H 7.84 0.01 1 436 . 62 VAL N N 119.4 0.2 1 437 . 62 VAL CA C 59.8 0.2 1 438 . 62 VAL CB C 30.2 0.2 1 439 . 62 VAL C C 176.5 0.2 1 440 . 62 VAL HA H 4.52 0.01 1 441 . 62 VAL HB H 2.2 0.01 1 442 . 63 GLY H H 9.76 0.01 1 443 . 63 GLY N N 116.2 0.2 1 444 . 63 GLY CA C 47.1 0.2 1 445 . 63 GLY HA2 H 4.52 0.01 2 446 . 63 GLY HA3 H 3.42 0.01 2 447 . 64 HIS H H 6.86 0.01 1 448 . 64 HIS N N 113.5 0.2 1 449 . 64 HIS CA C 54.6 0.2 1 450 . 64 HIS CB C 31.00 0.2 1 451 . 64 HIS C C 174.2 0.2 1 452 . 64 HIS HA H 4.62 0.01 1 453 . 65 SER H H 6.74 0.01 1 454 . 65 SER N N 110.5 0.2 1 455 . 65 SER CA C 56.3 0.2 1 456 . 65 SER CB C 62.8 0.2 1 457 . 65 SER C C 174.2 0.2 1 458 . 65 SER HA H 4.31 0.01 1 459 . 66 PHE H H 7.87 0.01 1 460 . 66 PHE N N 113.7 0.2 1 461 . 66 PHE CA C 55.8 0.2 1 462 . 66 PHE CB C 42.4 0.2 1 463 . 66 PHE C C 172.8 0.2 1 464 . 66 PHE HA H 5.5 0.01 1 465 . 66 PHE HB2 H 2.73 0.01 1 466 . 66 PHE HB3 H 2.73 0.01 1 467 . 67 HIS H H 9.12 0.01 1 468 . 67 HIS N N 120.9 0.2 1 469 . 67 HIS CA C 52.2 0.2 1 470 . 67 HIS CB C 35.2 0.2 1 471 . 67 HIS C C 173.8 0.2 1 472 . 67 HIS HA H 5.03 0.01 1 473 . 67 HIS HB2 H 2.88 0.01 1 474 . 67 HIS HB3 H 2.88 0.01 1 475 . 68 VAL H H 8.04 0.01 1 476 . 68 VAL N N 120.9 0.2 1 477 . 68 VAL CA C 61.4 0.2 1 478 . 68 VAL CB C 30.4 0.2 1 479 . 68 VAL C C 174.8 0.2 1 480 . 68 VAL HA H 4.55 0.01 1 481 . 68 VAL HB H 0.34 0.01 1 482 . 69 ASN H H 8.88 0.01 1 483 . 69 ASN N N 123.5 0.2 1 484 . 69 ASN CA C 52.3 0.2 1 485 . 69 ASN CB C 41.5 0.2 1 486 . 69 ASN C C 175.1 0.2 1 487 . 69 ASN HA H 5.76 0.01 1 488 . 69 ASN HB2 H 3.00 0.01 2 489 . 69 ASN HB3 H 2.66 0.01 2 490 . 70 PHE H H 8.22 0.01 1 491 . 70 PHE N N 119.4 0.2 1 492 . 70 PHE CA C 56.4 0.2 1 493 . 70 PHE CB C 41.8 0.2 1 494 . 70 PHE C C 176.00 0.2 1 495 . 70 PHE HA H 4.93 0.01 1 496 . 70 PHE HB2 H 2.48 0.01 1 497 . 70 PHE HB3 H 2.48 0.01 1 498 . 71 GLU H H 9.77 0.01 1 499 . 71 GLU N N 122.7 0.2 1 500 . 71 GLU CA C 57.7 0.2 1 501 . 71 GLU CB C 30.8 0.2 1 502 . 71 GLU C C 177.9 0.2 1 503 . 71 GLU HA H 4.39 0.01 1 504 . 71 GLU HB2 H 2.23 0.01 1 505 . 71 GLU HB3 H 2.23 0.01 1 506 . 72 ASP H H 8.97 0.01 1 507 . 72 ASP N N 128.3 0.2 1 508 . 72 ASP CA C 53.5 0.2 1 509 . 72 ASP CB C 40.7 0.2 1 510 . 72 ASP C C 175.6 0.2 1 511 . 72 ASP HA H 5.08 0.01 1 512 . 73 ASN H H 8.18 0.01 1 513 . 73 ASN N N 117.4 0.2 1 514 . 73 ASN CA C 54.1 0.2 1 515 . 73 ASN CB C 39.1 0.2 1 516 . 73 ASN C C 174.2 0.2 1 517 . 73 ASN HA H 4.84 0.01 1 518 . 73 ASN HB2 H 2.9 0.01 1 519 . 73 ASN HB3 H 2.9 0.01 1 520 . 74 ASP H H 8.14 0.01 1 521 . 74 ASP N N 119.4 0.2 1 522 . 74 ASP CA C 52.8 0.2 1 523 . 74 ASP CB C 41.5 0.2 1 524 . 74 ASP C C 175.3 0.2 1 525 . 74 ASP HA H 4.49 0.01 1 526 . 75 ASN H H 8.2 0.01 1 527 . 75 ASN N N 116.4 0.2 1 528 . 75 ASN CA C 52.1 0.2 1 529 . 75 ASN CB C 37.5 0.2 1 530 . 75 ASN C C 174.1 0.2 1 531 . 75 ASN HA H 4.77 0.01 1 532 . 76 ARG H H 7.53 0.01 1 533 . 76 ARG N N 119.4 0.2 1 534 . 76 ARG CA C 60.4 0.2 1 535 . 76 ARG CB C 32.1 0.2 1 536 . 76 ARG C C 177.7 0.2 1 537 . 76 ARG HA H 4.00 0.01 1 538 . 77 SER H H 9.91 0.01 1 539 . 77 SER N N 117.00 0.2 1 540 . 77 SER CA C 55.9 0.2 1 541 . 77 SER CB C 65.6 0.2 1 542 . 77 SER C C 173.6 0.2 1 543 . 77 SER HA H 6.09 0.01 1 544 . 78 VAL H H 8.52 0.01 1 545 . 78 VAL N N 117.3 0.2 1 546 . 78 VAL CA C 58.9 0.2 1 547 . 78 VAL CB C 37.7 0.2 1 548 . 78 VAL C C 173.1 0.2 1 549 . 78 VAL HA H 5.57 0.01 1 550 . 78 VAL HB H 1.93 0.01 1 551 . 79 LEU H H 8.94 0.01 1 552 . 79 LEU N N 124.6 0.2 1 553 . 79 LEU CA C 53.4 0.2 1 554 . 79 LEU CB C 45.7 0.2 1 555 . 79 LEU C C 173.8 0.2 1 556 . 79 LEU HA H 4.74 0.01 1 557 . 80 LYS H H 8.66 0.01 1 558 . 80 LYS N N 122.6 0.2 1 559 . 80 LYS CA C 54.6 0.2 1 560 . 80 LYS CB C 36.6 0.2 1 561 . 80 LYS C C 174.8 0.2 1 562 . 80 LYS HA H 4.71 0.01 1 563 . 80 LYS HB2 H 1.85 0.01 2 564 . 80 LYS HB3 H 1.66 0.01 2 565 . 81 GLY H H 8.7 0.01 1 566 . 81 GLY N N 105.8 0.2 1 567 . 81 GLY CA C 43.9 0.2 1 568 . 81 GLY C C 174.00 0.2 1 569 . 81 GLY HA2 H 4.47 0.01 2 570 . 81 GLY HA3 H 3.49 0.01 2 571 . 82 GLY H H 6.99 0.01 1 572 . 82 GLY N N 109.4 0.2 1 573 . 82 GLY CA C 44.6 0.2 1 574 . 82 GLY HA2 H 4.45 0.01 2 575 . 82 GLY HA3 H 3.45 0.01 2 576 . 83 PRO CA C 62.7 0.2 1 577 . 83 PRO CB C 32.1 0.2 1 578 . 83 PRO C C 175.4 0.2 1 579 . 83 PRO HA H 4.57 0.01 1 580 . 83 PRO HB2 H 1.89 0.01 2 581 . 83 PRO HB3 H 1.65 0.01 2 582 . 84 PHE H H 7.7 0.01 1 583 . 84 PHE N N 120.9 0.2 1 584 . 84 PHE CA C 57.6 0.2 1 585 . 84 PHE CB C 39.9 0.2 1 586 . 84 PHE C C 176.1 0.2 1 587 . 84 PHE HA H 4.88 0.01 1 588 . 84 PHE HB2 H 3.63 0.01 2 589 . 84 PHE HB3 H 3.3 0.01 2 590 . 85 SER H H 9.11 0.01 1 591 . 85 SER N N 118.1 0.2 1 592 . 85 SER CA C 59.1 0.2 1 593 . 85 SER CB C 64.00 0.2 1 594 . 85 SER C C 173.6 0.2 1 595 . 85 SER HA H 4.57 0.01 1 596 . 85 SER HB2 H 3.87 0.01 1 597 . 85 SER HB3 H 3.87 0.01 1 598 . 86 ASP H H 7.64 0.01 1 599 . 86 ASP N N 122.2 0.2 1 600 . 86 ASP CA C 53.4 0.2 1 601 . 86 ASP CB C 44.00 0.2 1 602 . 86 ASP C C 174.6 0.2 1 603 . 86 ASP HA H 4.81 0.01 1 604 . 86 ASP HB2 H 2.63 0.01 2 605 . 86 ASP HB3 H 2.28 0.01 2 606 . 87 SER H H 7.71 0.01 1 607 . 87 SER N N 113.8 0.2 1 608 . 87 SER CA C 57.7 0.2 1 609 . 87 SER CB C 64.5 0.2 1 610 . 87 SER C C 172.7 0.2 1 611 . 87 SER HA H 4.84 0.01 1 612 . 87 SER HB2 H 3.58 0.01 1 613 . 87 SER HB3 H 3.58 0.01 1 614 . 88 TYR H H 8.67 0.01 1 615 . 88 TYR N N 120.9 0.2 1 616 . 88 TYR CA C 56.2 0.2 1 617 . 88 TYR CB C 41.4 0.2 1 618 . 88 TYR C C 174.6 0.2 1 619 . 88 TYR HA H 4.72 0.01 1 620 . 88 TYR HB2 H 2.27 0.01 1 621 . 88 TYR HB3 H 2.27 0.01 1 622 . 89 ARG H H 9.04 0.01 1 623 . 89 ARG N N 123.3 0.2 1 624 . 89 ARG CA C 55.5 0.2 1 625 . 89 ARG CB C 32.5 0.2 1 626 . 89 ARG C C 176.6 0.2 1 627 . 89 ARG HA H 4.71 0.01 1 628 . 90 LEU H H 8.06 0.01 1 629 . 90 LEU N N 128.4 0.2 1 630 . 90 LEU CA C 56.2 0.2 1 631 . 90 LEU CB C 41.9 0.2 1 632 . 90 LEU C C 175.8 0.2 1 633 . 90 LEU HA H 3.92 0.01 1 634 . 91 PHE H H 8.82 0.01 1 635 . 91 PHE N N 118.1 0.2 1 636 . 91 PHE CA C 57.8 0.2 1 637 . 91 PHE CB C 41.9 0.2 1 638 . 91 PHE C C 174.5 0.2 1 639 . 91 PHE HA H 5.49 0.01 1 640 . 91 PHE HB2 H 3.69 0.01 2 641 . 91 PHE HB3 H 3.25 0.01 2 642 . 92 GLN H H 6.99 0.01 1 643 . 92 GLN N N 121.9 0.2 1 644 . 92 GLN CA C 56.00 0.2 1 645 . 92 GLN CB C 35.8 0.2 1 646 . 92 GLN C C 174.5 0.2 1 647 . 92 GLN HA H 5.99 0.01 1 648 . 93 PHE H H 8.96 0.01 1 649 . 93 PHE N N 116.9 0.2 1 650 . 93 PHE CA C 57.1 0.2 1 651 . 93 PHE CB C 44.00 0.2 1 652 . 93 PHE C C 172.1 0.2 1 653 . 93 PHE HA H 5.64 0.01 1 654 . 93 PHE HB2 H 3.42 0.01 2 655 . 93 PHE HB3 H 2.67 0.01 2 656 . 94 HIS H H 8.8 0.01 1 657 . 94 HIS N N 114.8 0.2 1 658 . 94 HIS CA C 55.3 0.2 1 659 . 94 HIS CB C 32.00 0.2 1 660 . 94 HIS C C 170.5 0.2 1 661 . 94 HIS HA H 4.33 0.01 1 662 . 95 PHE H H 9.8 0.01 1 663 . 95 PHE N N 117.3 0.2 1 664 . 95 PHE CA C 55.9 0.2 1 665 . 95 PHE CB C 42.8 0.2 1 666 . 95 PHE C C 175.00 0.2 1 667 . 95 PHE HA H 5.68 0.01 1 668 . 96 HIS H H 9.37 0.01 1 669 . 96 HIS N N 116.4 0.2 1 670 . 96 HIS CA C 53.7 0.2 1 671 . 96 HIS CB C 32.3 0.2 1 672 . 96 HIS C C 172.7 0.2 1 673 . 96 HIS HA H 5.02 0.01 1 674 . 96 HIS HB2 H 2.57 0.01 1 675 . 96 HIS HB3 H 2.57 0.01 1 676 . 97 TRP H H 8.99 0.01 1 677 . 97 TRP N N 118.3 0.2 1 678 . 97 TRP CA C 57.4 0.2 1 679 . 97 TRP CB C 30.6 0.2 1 680 . 97 TRP C C 173.00 0.2 1 681 . 97 TRP HA H 5.09 0.01 1 682 . 97 TRP HB2 H 3.39 0.01 1 683 . 97 TRP HB3 H 3.39 0.01 1 684 . 98 GLY H H 9.1 0.01 1 685 . 98 GLY N N 107.9 0.2 1 686 . 98 GLY CA C 43.00 0.2 1 687 . 98 GLY C C 173.9 0.2 1 688 . 98 GLY HA2 H 5.09 0.01 2 689 . 98 GLY HA3 H 4.27 0.01 2 690 . 99 SER H H 8.83 0.01 1 691 . 99 SER N N 114.9 0.2 1 692 . 99 SER CA C 61.1 0.2 1 693 . 99 SER CB C 63.4 0.2 1 694 . 99 SER C C 174.4 0.2 1 695 . 99 SER HA H 4.52 0.01 1 696 . 99 SER HB2 H 3.87 0.01 1 697 . 99 SER HB3 H 3.87 0.01 1 698 . 100 THR H H 7.97 0.01 1 699 . 100 THR N N 109.00 0.2 1 700 . 100 THR CA C 58.8 0.2 1 701 . 100 THR CB C 71.6 0.2 1 702 . 100 THR C C 176.1 0.2 1 703 . 100 THR HA H 4.61 0.01 1 704 . 101 ASN H H 9.14 0.01 1 705 . 101 ASN N N 118.9 0.2 1 706 . 101 ASN CA C 54.8 0.2 1 707 . 101 ASN CB C 37.5 0.2 1 708 . 101 ASN C C 175.4 0.2 1 709 . 101 ASN HA H 4.37 0.01 1 710 . 102 GLU H H 8.15 0.01 1 711 . 102 GLU N N 116.9 0.2 1 712 . 102 GLU CA C 58.5 0.2 1 713 . 102 GLU CB C 29.7 0.2 1 714 . 102 GLU C C 176.00 0.2 1 715 . 102 GLU HA H 4.00 0.01 1 716 . 102 GLU HB2 H 1.77 0.01 1 717 . 102 GLU HB3 H 1.77 0.01 1 718 . 103 HIS H H 7.05 0.01 1 719 . 103 HIS N N 113.7 0.2 1 720 . 103 HIS CA C 53.9 0.2 1 721 . 103 HIS CB C 31.6 0.2 1 722 . 103 HIS C C 173.00 0.2 1 723 . 103 HIS HA H 4.92 0.01 1 724 . 103 HIS HB2 H 3.05 0.01 1 725 . 103 HIS HB3 H 3.05 0.01 1 726 . 104 GLY H H 9.18 0.01 1 727 . 104 GLY N N 111.6 0.2 1 728 . 104 GLY CA C 46.7 0.2 1 729 . 104 GLY C C 171.3 0.2 1 730 . 104 GLY HA2 H 4.1 0.01 1 731 . 104 GLY HA3 H 4.1 0.01 1 732 . 105 SER H H 7.4 0.01 1 733 . 105 SER N N 110.7 0.2 1 734 . 105 SER CA C 58.2 0.2 1 735 . 105 SER CB C 63.7 0.2 1 736 . 105 SER C C 171.8 0.2 1 737 . 105 SER HA H 4.11 0.01 1 738 . 106 GLU H H 8.37 0.01 1 739 . 106 GLU N N 117.8 0.2 1 740 . 106 GLU CA C 58.6 0.2 1 741 . 106 GLU CB C 30.1 0.2 1 742 . 106 GLU C C 176.8 0.2 1 743 . 106 GLU HA H 4.41 0.01 1 744 . 107 HIS H H 10.8 0.01 1 745 . 107 HIS N N 118.6 0.2 1 746 . 107 HIS CA C 60.3 0.2 1 747 . 107 HIS CB C 28.6 0.2 1 748 . 107 HIS C C 173.4 0.2 1 749 . 107 HIS HA H 4.09 0.01 1 750 . 108 THR H H 7.49 0.01 1 751 . 108 THR N N 109.8 0.2 1 752 . 108 THR CA C 59.6 0.2 1 753 . 108 THR CB C 71.1 0.2 1 754 . 108 THR HA H 4.76 0.01 1 755 . 108 THR HB H 3.78 0.01 1 756 . 109 VAL H H 7.65 0.01 1 757 . 109 VAL N N 117.9 0.2 1 758 . 109 VAL CA C 61.2 0.2 1 759 . 109 VAL CB C 34.2 0.2 1 760 . 109 VAL C C 177.2 0.2 1 761 . 109 VAL HA H 4.63 0.01 1 762 . 109 VAL HB H 2.06 0.01 1 763 . 110 ASP H H 10.00 0.01 1 764 . 110 ASP N N 131.1 0.2 1 765 . 110 ASP CA C 56.5 0.2 1 766 . 110 ASP CB C 39.3 0.2 1 767 . 110 ASP C C 176.1 0.2 1 768 . 110 ASP HA H 4.36 0.01 1 769 . 110 ASP HB2 H 3.01 0.01 2 770 . 110 ASP HB3 H 2.73 0.01 2 771 . 111 GLY H H 10.4 0.01 1 772 . 111 GLY N N 107.5 0.2 1 773 . 111 GLY CA C 45.00 0.2 1 774 . 111 GLY C C 174.1 0.2 1 775 . 111 GLY HA2 H 3.99 0.01 2 776 . 111 GLY HA3 H 3.27 0.01 2 777 . 112 VAL H H 8.16 0.01 1 778 . 112 VAL N N 124.1 0.2 1 779 . 112 VAL CA C 63.5 0.2 1 780 . 112 VAL CB C 31.9 0.2 1 781 . 112 VAL C C 174.8 0.2 1 782 . 112 VAL HA H 3.78 0.01 1 783 . 112 VAL HB H 2.33 0.01 1 784 . 113 LYS H H 8.22 0.01 1 785 . 113 LYS N N 126.4 0.2 1 786 . 113 LYS CA C 55.9 0.2 1 787 . 113 LYS CB C 33.5 0.2 1 788 . 113 LYS C C 176.1 0.2 1 789 . 113 LYS HA H 4.26 0.01 1 790 . 114 TYR H H 8.17 0.01 1 791 . 114 TYR N N 123.00 0.2 1 792 . 114 TYR CA C 57.5 0.2 1 793 . 114 TYR CB C 38.5 0.2 1 794 . 114 TYR C C 175.7 0.2 1 795 . 114 TYR HA H 4.97 0.01 1 796 . 115 SER H H 8.55 0.01 1 797 . 115 SER N N 118.7 0.2 1 798 . 115 SER CA C 62.5 0.2 1 799 . 115 SER CB C 64.00 0.2 1 800 . 115 SER HA H 4.58 0.01 1 801 . 116 ALA H H 8.49 0.01 1 802 . 116 ALA N N 118.9 0.2 1 803 . 116 ALA CA C 52.00 0.2 1 804 . 116 ALA CB C 22.5 0.2 1 805 . 116 ALA C C 174.9 0.2 1 806 . 116 ALA HA H 4.7 0.01 1 807 . 116 ALA HB H 1.91 0.01 1 808 . 117 GLU H H 9.21 0.01 1 809 . 117 GLU N N 121.7 0.2 1 810 . 117 GLU CA C 56.2 0.2 1 811 . 117 GLU CB C 36.00 0.2 1 812 . 117 GLU C C 172.9 0.2 1 813 . 117 GLU HA H 5.3 0.01 1 814 . 118 LEU H H 9.51 0.01 1 815 . 118 LEU N N 130.1 0.2 1 816 . 118 LEU CA C 53.8 0.2 1 817 . 118 LEU CB C 43.9 0.2 1 818 . 118 LEU C C 174.7 0.2 1 819 . 118 LEU HA H 4.66 0.01 1 820 . 118 LEU HB2 H 1.79 0.01 1 821 . 118 LEU HB3 H 1.79 0.01 1 822 . 119 HIS H H 9.25 0.01 1 823 . 119 HIS N N 125.9 0.2 1 824 . 119 HIS CA C 52.5 0.2 1 825 . 119 HIS CB C 33.6 0.2 1 826 . 119 HIS C C 174.2 0.2 1 827 . 119 HIS HA H 4.94 0.01 1 828 . 120 VAL H H 9.32 0.01 1 829 . 120 VAL N N 122.8 0.2 1 830 . 120 VAL CA C 61.8 0.2 1 831 . 120 VAL CB C 32.4 0.2 1 832 . 120 VAL C C 174.4 0.2 1 833 . 120 VAL HA H 4.22 0.01 1 834 . 120 VAL HB H 2.1 0.01 1 835 . 121 ALA H H 9.11 0.01 1 836 . 121 ALA N N 131.7 0.2 1 837 . 121 ALA CA C 52.6 0.2 1 838 . 121 ALA CB C 23.00 0.2 1 839 . 121 ALA C C 174.5 0.2 1 840 . 121 ALA HA H 4.8 0.01 1 841 . 121 ALA HB H 0.83 0.01 1 842 . 122 HIS H H 8.45 0.01 1 843 . 122 HIS N N 118.6 0.2 1 844 . 122 HIS CA C 54.8 0.2 1 845 . 122 HIS CB C 34.3 0.2 1 846 . 122 HIS C C 174.9 0.2 1 847 . 122 HIS HA H 6.05 0.01 1 848 . 123 TRP H H 9.57 0.01 1 849 . 123 TRP N N 119.7 0.2 1 850 . 123 TRP CA C 54.8 0.2 1 851 . 123 TRP CB C 34.3 0.2 1 852 . 123 TRP C C 176.1 0.2 1 853 . 123 TRP HA H 6.3 0.01 1 854 . 123 TRP HB2 H 3.15 0.01 1 855 . 123 TRP HB3 H 3.15 0.01 1 856 . 124 ASN H H 9.15 0.01 1 857 . 124 ASN N N 118.5 0.2 1 858 . 124 ASN CA C 53.4 0.2 1 859 . 124 ASN CB C 37.4 0.2 1 860 . 124 ASN C C 173.1 0.2 1 861 . 124 ASN HA H 3.45 0.01 1 862 . 124 ASN HB2 H 2.73 0.01 1 863 . 124 ASN HB3 H 2.73 0.01 1 864 . 125 SER H H 7.39 0.01 1 865 . 125 SER N N 120.4 0.2 1 866 . 125 SER CA C 57.9 0.2 1 867 . 125 SER CB C 62.5 0.2 1 868 . 125 SER C C 175.5 0.2 1 869 . 125 SER HA H 4.65 0.01 1 870 . 125 SER HB2 H 3.64 0.01 2 871 . 125 SER HB3 H 1.95 0.01 2 872 . 126 ALA H H 7.82 0.01 1 873 . 126 ALA N N 125.8 0.2 1 874 . 126 ALA CA C 53.4 0.2 1 875 . 126 ALA CB C 19.00 0.2 1 876 . 126 ALA C C 179.2 0.2 1 877 . 126 ALA HA H 4.23 0.01 1 878 . 126 ALA HB H 1.4 0.01 1 879 . 127 LYS H H 6.59 0.01 1 880 . 127 LYS N N 114.4 0.2 1 881 . 127 LYS CA C 55.9 0.2 1 882 . 127 LYS CB C 34.6 0.2 1 883 . 127 LYS C C 175.7 0.2 1 884 . 127 LYS HA H 3.93 0.01 1 885 . 127 LYS HB2 H 0.65 0.01 1 886 . 127 LYS HB3 H 0.65 0.01 1 887 . 128 TYR H H 7.28 0.01 1 888 . 128 TYR N N 116.00 0.2 1 889 . 128 TYR CA C 56.00 0.2 1 890 . 128 TYR CB C 40.6 0.2 1 891 . 128 TYR C C 175.5 0.2 1 892 . 128 TYR HA H 5.06 0.01 1 893 . 128 TYR HB2 H 3.2 0.01 2 894 . 128 TYR HB3 H 2.97 0.01 2 895 . 129 SER H H 8.97 0.01 1 896 . 129 SER N N 112.7 0.2 1 897 . 129 SER CA C 59.2 0.2 1 898 . 129 SER CB C 64.6 0.2 1 899 . 129 SER C C 174.00 0.2 1 900 . 129 SER HA H 4.61 0.01 1 901 . 129 SER HB2 H 3.99 0.01 1 902 . 129 SER HB3 H 3.99 0.01 1 903 . 130 SER H H 7.21 0.01 1 904 . 130 SER N N 113.8 0.2 1 905 . 130 SER CA C 56.8 0.2 1 906 . 130 SER CB C 65.5 0.2 1 907 . 130 SER C C 171.9 0.2 1 908 . 130 SER HA H 3.85 0.01 1 909 . 131 LEU H H 7.53 0.01 1 910 . 131 LEU N N 122.8 0.2 1 911 . 131 LEU CA C 56.9 0.2 1 912 . 131 LEU CB C 39.9 0.2 1 913 . 131 LEU C C 176.8 0.2 1 914 . 131 LEU HA H 2.5 0.01 1 915 . 131 LEU HB2 H 0.96 0.01 1 916 . 131 LEU HB3 H 0.96 0.01 1 917 . 132 ALA H H 7.52 0.01 1 918 . 132 ALA N N 116.9 0.2 1 919 . 132 ALA CA C 54.5 0.2 1 920 . 132 ALA CB C 17.8 0.2 1 921 . 132 ALA C C 180.00 0.2 1 922 . 132 ALA HA H 3.64 0.01 1 923 . 132 ALA HB H 1.15 0.01 1 924 . 133 GLU H H 7.24 0.01 1 925 . 133 GLU N N 116.9 0.2 1 926 . 133 GLU CA C 58.2 0.2 1 927 . 133 GLU CB C 30.8 0.2 1 928 . 133 GLU C C 176.9 0.2 1 929 . 133 GLU HA H 3.76 0.01 1 930 . 133 GLU HB2 H 1.92 0.01 1 931 . 133 GLU HB3 H 1.92 0.01 1 932 . 134 ALA H H 7.52 0.01 1 933 . 134 ALA N N 119.8 0.2 1 934 . 134 ALA CA C 54.3 0.2 1 935 . 134 ALA CB C 20.3 0.2 1 936 . 134 ALA C C 179.8 0.2 1 937 . 134 ALA HA H 3.09 0.01 1 938 . 134 ALA HB H 1.49 0.01 1 939 . 135 ALA H H 8.02 0.01 1 940 . 135 ALA N N 114.2 0.2 1 941 . 135 ALA CA C 55.6 0.2 1 942 . 135 ALA CB C 17.8 0.2 1 943 . 135 ALA C C 175.6 0.2 1 944 . 135 ALA HA H 3.62 0.01 1 945 . 135 ALA HB H 1.27 0.01 1 946 . 136 SER H H 6.85 0.01 1 947 . 136 SER N N 104.2 0.2 1 948 . 136 SER CA C 56.5 0.2 1 949 . 136 SER CB C 63.3 0.2 1 950 . 136 SER C C 174.9 0.2 1 951 . 136 SER HA H 3.69 0.01 1 952 . 136 SER HB2 H 3.46 0.01 2 953 . 136 SER HB3 H 2.63 0.01 2 954 . 137 LYS H H 7.5 0.01 1 955 . 137 LYS N N 124.1 0.2 1 956 . 137 LYS CA C 53.5 0.2 1 957 . 137 LYS CB C 33.3 0.2 1 958 . 137 LYS C C 177.8 0.2 1 959 . 137 LYS HA H 4.39 0.01 1 960 . 137 LYS HB2 H 1.66 0.01 1 961 . 137 LYS HB3 H 1.66 0.01 1 962 . 138 ALA H H 8.63 0.01 1 963 . 138 ALA N N 123.2 0.2 1 964 . 138 ALA CA C 55.5 0.2 1 965 . 138 ALA CB C 18.8 0.2 1 966 . 138 ALA C C 177.8 0.2 1 967 . 138 ALA HA H 4.31 0.01 1 968 . 138 ALA HB H 1.49 0.01 1 969 . 139 ASP H H 8.16 0.01 1 970 . 139 ASP N N 113.2 0.2 1 971 . 139 ASP CA C 52.4 0.2 1 972 . 139 ASP CB C 39.5 0.2 1 973 . 139 ASP C C 179.3 0.2 1 974 . 139 ASP HA H 5.07 0.01 1 975 . 139 ASP HB2 H 3.14 0.01 2 976 . 139 ASP HB3 H 2.61 0.01 2 977 . 140 GLY H H 8.52 0.01 1 978 . 140 GLY N N 109.1 0.2 1 979 . 140 GLY CA C 48.7 0.2 1 980 . 140 GLY C C 174.9 0.2 1 981 . 140 GLY HA2 H 4.92 0.01 2 982 . 140 GLY HA3 H 3.93 0.01 2 983 . 141 LEU H H 8.66 0.01 1 984 . 141 LEU N N 115.9 0.2 1 985 . 141 LEU CA C 53.4 0.2 1 986 . 141 LEU CB C 46.00 0.2 1 987 . 141 LEU C C 176.5 0.2 1 988 . 141 LEU HA H 5.86 0.01 1 989 . 142 ALA H H 8.53 0.01 1 990 . 142 ALA N N 123.3 0.2 1 991 . 142 ALA CA C 50.8 0.2 1 992 . 142 ALA CB C 23.2 0.2 1 993 . 142 ALA C C 177.00 0.2 1 994 . 142 ALA HA H 4.94 0.01 1 995 . 142 ALA HB H 0.08 0.01 1 996 . 143 VAL H H 7.44 0.01 1 997 . 143 VAL N N 125.00 0.2 1 998 . 143 VAL CA C 59.7 0.2 1 999 . 143 VAL CB C 33.1 0.2 1 1000 . 143 VAL C C 173.8 0.2 1 1001 . 143 VAL HA H 4.89 0.01 1 1002 . 143 VAL HB H 0.07 0.01 1 1003 . 144 ILE H H 8.9 0.01 1 1004 . 144 ILE N N 126.00 0.2 1 1005 . 144 ILE CA C 59.7 0.2 1 1006 . 144 ILE CB C 40.1 0.2 1 1007 . 144 ILE C C 175.7 0.2 1 1008 . 144 ILE HA H 5.2 0.01 1 1009 . 144 ILE HB H 1.7 0.01 1 1010 . 145 GLY H H 10.23 0.01 1 1011 . 145 GLY N N 115.9 0.2 1 1012 . 145 GLY CA C 43.9 0.2 1 1013 . 145 GLY C C 171.8 0.2 1 1014 . 145 GLY HA2 H 6.17 0.01 2 1015 . 145 GLY HA3 H 3.58 0.01 2 1016 . 146 VAL H H 9.59 0.01 1 1017 . 146 VAL N N 124.6 0.2 1 1018 . 146 VAL CA C 60.2 0.2 1 1019 . 146 VAL CB C 34.6 0.2 1 1020 . 146 VAL C C 175.4 0.2 1 1021 . 146 VAL HA H 4.78 0.01 1 1022 . 146 VAL HB H 2.13 0.01 1 1023 . 147 LEU H H 10.4 0.01 1 1024 . 147 LEU N N 131.1 0.2 1 1025 . 147 LEU CA C 55.3 0.2 1 1026 . 147 LEU CB C 41.1 0.2 1 1027 . 147 LEU C C 175.9 0.2 1 1028 . 147 LEU HA H 4.39 0.01 1 1029 . 147 LEU HB2 H 1.35 0.01 2 1030 . 147 LEU HB3 H 0.68 0.01 2 1031 . 148 MET H H 8.19 0.01 1 1032 . 148 MET N N 117.5 0.2 1 1033 . 148 MET CA C 54.00 0.2 1 1034 . 148 MET CB C 34.7 0.2 1 1035 . 148 MET C C 174.8 0.2 1 1036 . 148 MET HA H 5.44 0.01 1 1037 . 148 MET HB2 H 1.8 0.01 1 1038 . 148 MET HB3 H 1.8 0.01 1 1039 . 149 LYS H H 9.3 0.01 1 1040 . 149 LYS N N 126.00 0.2 1 1041 . 149 LYS CA C 54.00 0.2 1 1042 . 149 LYS CB C 36.5 0.2 1 1043 . 149 LYS C C 176.00 0.2 1 1044 . 149 LYS HA H 5.14 0.01 1 1045 . 149 LYS HB2 H 2.00 0.01 2 1046 . 149 LYS HB3 H 1.76 0.01 2 1047 . 150 VAL H H 8.19 0.01 1 1048 . 150 VAL N N 125.8 0.2 1 1049 . 150 VAL CA C 61.5 0.2 1 1050 . 150 VAL CB C 31.2 0.2 1 1051 . 150 VAL C C 176.3 0.2 1 1052 . 150 VAL HA H 4.91 0.01 1 1053 . 150 VAL HB H 2.03 0.01 1 1054 . 151 GLY H H 8.51 0.01 1 1055 . 151 GLY N N 116.2 0.2 1 1056 . 151 GLY CA C 46.7 0.2 1 1057 . 151 GLY C C 172.8 0.2 1 1058 . 151 GLY HA2 H 3.91 0.01 1 1059 . 151 GLY HA3 H 3.91 0.01 1 1060 . 152 GLU H H 8.69 0.01 1 1061 . 152 GLU N N 128.00 0.2 1 1062 . 152 GLU CA C 56.3 0.2 1 1063 . 152 GLU CB C 30.1 0.2 1 1064 . 152 GLU C C 175.8 0.2 1 1065 . 152 GLU HA H 4.16 0.01 1 1066 . 152 GLU HB2 H 1.95 0.01 1 1067 . 152 GLU HB3 H 1.95 0.01 1 1068 . 153 ALA H H 8.49 0.01 1 1069 . 153 ALA N N 122.6 0.2 1 1070 . 153 ALA CA C 52.8 0.2 1 1071 . 153 ALA CB C 18.4 0.2 1 1072 . 153 ALA C C 176.9 0.2 1 1073 . 153 ALA HA H 3.81 0.01 1 1074 . 153 ALA HB H 1.22 0.01 1 1075 . 154 ASN H H 8.76 0.01 1 1076 . 154 ASN N N 119.9 0.2 1 1077 . 154 ASN CA C 52.8 0.2 1 1078 . 154 ASN CB C 39.8 0.2 1 1079 . 155 PRO CA C 64.4 0.2 1 1080 . 155 PRO CB C 32.2 0.2 1 1081 . 155 PRO C C 179.3 0.2 1 1082 . 155 PRO HA H 4.58 0.01 1 1083 . 155 PRO HB2 H 2.41 0.01 1 1084 . 155 PRO HB3 H 2.41 0.01 1 1085 . 156 LYS H H 8.05 0.01 1 1086 . 156 LYS N N 116.9 0.2 1 1087 . 156 LYS CA C 57.4 0.2 1 1088 . 156 LYS CB C 31.3 0.2 1 1089 . 156 LYS C C 178.5 0.2 1 1090 . 156 LYS HA H 4.27 0.01 1 1091 . 156 LYS HB2 H 2.05 0.01 2 1092 . 156 LYS HB3 H 1.9 0.01 2 1093 . 157 LEU H H 7.23 0.01 1 1094 . 157 LEU N N 115.1 0.2 1 1095 . 157 LEU CA C 54.6 0.2 1 1096 . 157 LEU CB C 43.4 0.2 1 1097 . 157 LEU C C 178.2 0.2 1 1098 . 157 LEU HA H 4.31 0.01 1 1099 . 157 LEU HB2 H 1.65 0.01 1 1100 . 157 LEU HB3 H 1.65 0.01 1 1101 . 158 GLN H H 7.46 0.01 1 1102 . 158 GLN N N 120.00 0.2 1 1103 . 158 GLN CA C 59.9 0.2 1 1104 . 158 GLN CB C 28.9 0.2 1 1105 . 158 GLN C C 176.2 0.2 1 1106 . 158 GLN HA H 3.58 0.01 1 1107 . 159 LYS H H 8.65 0.01 1 1108 . 159 LYS N N 116.1 0.2 1 1109 . 159 LYS CA C 59.9 0.2 1 1110 . 159 LYS CB C 33.00 0.2 1 1111 . 159 LYS C C 179.9 0.2 1 1112 . 159 LYS HA H 4.13 0.01 1 1113 . 159 LYS HB2 H 2.06 0.01 2 1114 . 159 LYS HB3 H 1.76 0.01 2 1115 . 160 VAL H H 7.15 0.01 1 1116 . 160 VAL N N 115.5 0.2 1 1117 . 160 VAL CA C 65.6 0.2 1 1118 . 160 VAL CB C 31.9 0.2 1 1119 . 160 VAL C C 176.2 0.2 1 1120 . 160 VAL HA H 3.5 0.01 1 1121 . 160 VAL HB H 2.35 0.01 1 1122 . 161 LEU H H 7.48 0.01 1 1123 . 161 LEU N N 116.6 0.2 1 1124 . 161 LEU CA C 57.3 0.2 1 1125 . 161 LEU CB C 40.1 0.2 1 1126 . 161 LEU C C 180.4 0.2 1 1127 . 161 LEU HA H 3.68 0.01 1 1128 . 162 ASP H H 8.71 0.01 1 1129 . 162 ASP N N 119.00 0.2 1 1130 . 162 ASP CA C 56.8 0.2 1 1131 . 162 ASP CB C 40.5 0.2 1 1132 . 162 ASP C C 178.00 0.2 1 1133 . 162 ASP HA H 4.32 0.01 1 1134 . 162 ASP HB2 H 2.65 0.01 1 1135 . 162 ASP HB3 H 2.65 0.01 1 1136 . 163 ALA H H 7.3 0.01 1 1137 . 163 ALA N N 121.1 0.2 1 1138 . 163 ALA CA C 53.2 0.2 1 1139 . 163 ALA CB C 19.6 0.2 1 1140 . 163 ALA C C 178.6 0.2 1 1141 . 163 ALA HA H 4.3 0.01 1 1142 . 163 ALA HB H 1.63 0.01 1 1143 . 164 LEU H H 7.24 0.01 1 1144 . 164 LEU N N 114.1 0.2 1 1145 . 164 LEU CA C 56.8 0.2 1 1146 . 164 LEU CB C 40.00 0.2 1 1147 . 164 LEU C C 179.5 0.2 1 1148 . 164 LEU HA H 3.66 0.01 1 1149 . 164 LEU HB2 H 1.66 0.01 2 1150 . 164 LEU HB3 H 1.14 0.01 2 1151 . 165 GLN H H 7.39 0.01 1 1152 . 165 GLN N N 114.4 0.2 1 1153 . 165 GLN CA C 57.6 0.2 1 1154 . 165 GLN CB C 27.8 0.2 1 1155 . 165 GLN C C 176.7 0.2 1 1156 . 165 GLN HA H 3.89 0.01 1 1157 . 165 GLN HB2 H 2.08 0.01 1 1158 . 165 GLN HB3 H 2.08 0.01 1 1159 . 166 ALA H H 7.4 0.01 1 1160 . 166 ALA N N 118.9 0.2 1 1161 . 166 ALA CA C 52.5 0.2 1 1162 . 166 ALA CB C 20.1 0.2 1 1163 . 166 ALA C C 178.2 0.2 1 1164 . 166 ALA HA H 4.4 0.01 1 1165 . 166 ALA HB H 1.45 0.01 1 1166 . 167 ILE H H 7.28 0.01 1 1167 . 167 ILE N N 112.3 0.2 1 1168 . 167 ILE CA C 58.7 0.2 1 1169 . 167 ILE CB C 38.4 0.2 1 1170 . 167 ILE HA H 4.75 0.01 1 1171 . 167 ILE HG12 H 1.78 0.01 2 1172 . 167 ILE HG13 H 1.46 0.01 2 1173 . 168 LYS H H 7.6 0.01 1 1174 . 168 LYS N N 116.9 0.2 1 1175 . 168 LYS CA C 60.4 0.2 1 1176 . 168 LYS CB C 33.7 0.2 1 1177 . 168 LYS C C 175.2 0.2 1 1178 . 168 LYS HA H 3.85 0.01 1 1179 . 168 LYS HB2 H 1.82 0.01 1 1180 . 168 LYS HB3 H 1.82 0.01 1 1181 . 169 THR H H 6.39 0.01 1 1182 . 169 THR N N 97.7 0.2 1 1183 . 169 THR CA C 58.3 0.2 1 1184 . 169 THR CB C 71.00 0.2 1 1185 . 169 THR HA H 4.73 0.01 1 1186 . 170 LYS H H 7.29 0.01 1 1187 . 170 LYS N N 120.6 0.2 1 1188 . 170 LYS CA C 58.3 0.2 1 1189 . 170 LYS CB C 32.00 0.2 1 1190 . 170 LYS C C 177.7 0.2 1 1191 . 170 LYS HA H 3.57 0.01 1 1192 . 171 GLY H H 8.72 0.01 1 1193 . 171 GLY N N 116.3 0.2 1 1194 . 171 GLY CA C 44.3 0.2 1 1195 . 171 GLY C C 174.9 0.2 1 1196 . 171 GLY HA2 H 4.4 0.01 2 1197 . 171 GLY HA3 H 3.61 0.01 2 1198 . 172 LYS H H 7.84 0.01 1 1199 . 172 LYS N N 119.9 0.2 1 1200 . 172 LYS CA C 56.6 0.2 1 1201 . 172 LYS CB C 33.2 0.2 1 1202 . 172 LYS C C 174.3 0.2 1 1203 . 172 LYS HA H 4.4 0.01 1 1204 . 172 LYS HB2 H 1.99 0.01 1 1205 . 172 LYS HB3 H 1.99 0.01 1 1206 . 173 ARG H H 8.29 0.01 1 1207 . 173 ARG N N 117.9 0.2 1 1208 . 173 ARG CA C 53.6 0.2 1 1209 . 173 ARG CB C 34.6 0.2 1 1210 . 173 ARG C C 174.7 0.2 1 1211 . 173 ARG HA H 5.42 0.01 1 1212 . 173 ARG HB2 H 1.73 0.01 2 1213 . 173 ARG HB3 H 1.6 0.01 2 1214 . 174 ALA H H 9.07 0.01 1 1215 . 174 ALA N N 124.9 0.2 1 1216 . 174 ALA CA C 49.8 0.2 1 1217 . 174 ALA CB C 20.8 0.2 1 1218 . 174 ALA C C 173.4 0.2 1 1219 . 174 ALA HA H 4.93 0.01 1 1220 . 174 ALA HB H 1.24 0.01 1 1221 . 175 PRO CA C 63.00 0.2 1 1222 . 175 PRO CB C 32.00 0.2 1 1223 . 175 PRO C C 175.8 0.2 1 1224 . 175 PRO HA H 4.55 0.01 1 1225 . 175 PRO HB2 H 2.37 0.01 2 1226 . 175 PRO HB3 H 1.9 0.01 2 1227 . 176 PHE H H 7.6 0.01 1 1228 . 176 PHE N N 127.1 0.2 1 1229 . 176 PHE CA C 58.4 0.2 1 1230 . 176 PHE CB C 40.6 0.2 1 1231 . 176 PHE C C 171.6 0.2 1 1232 . 176 PHE HA H 4.34 0.01 1 1233 . 176 PHE HB2 H 2.67 0.01 2 1234 . 176 PHE HB3 H 2.54 0.01 2 1235 . 177 THR H H 7.4 0.01 1 1236 . 177 THR N N 110.6 0.2 1 1237 . 177 THR CA C 58.6 0.2 1 1238 . 177 THR CB C 72.00 0.2 1 1239 . 177 THR C C 174.8 0.2 1 1240 . 177 THR HA H 4.61 0.01 1 1241 . 177 THR HB H 4.24 0.01 1 1242 . 178 ASN H H 9.09 0.01 1 1243 . 178 ASN N N 116.5 0.2 1 1244 . 178 ASN CA C 53.7 0.2 1 1245 . 178 ASN CB C 37.00 0.2 1 1246 . 178 ASN C C 173.7 0.2 1 1247 . 178 ASN HA H 4.13 0.01 1 1248 . 178 ASN HB2 H 2.96 0.01 2 1249 . 178 ASN HB3 H 2.57 0.01 2 1250 . 179 PHE H H 7.67 0.01 1 1251 . 179 PHE N N 119.6 0.2 1 1252 . 179 PHE CA C 58.00 0.2 1 1253 . 179 PHE CB C 44.1 0.2 1 1254 . 179 PHE C C 171.9 0.2 1 1255 . 179 PHE HA H 4.7 0.01 1 1256 . 179 PHE HB2 H 2.61 0.01 1 1257 . 179 PHE HB3 H 2.61 0.01 1 1258 . 180 ASP H H 8.15 0.01 1 1259 . 180 ASP N N 125.5 0.2 1 1260 . 180 ASP CA C 48.8 0.2 1 1261 . 180 ASP CB C 42.2 0.2 1 1262 . 180 ASP C C 175.4 0.2 1 1263 . 180 ASP HA H 5.00 0.01 1 1264 . 181 PRO CA C 64.00 0.2 1 1265 . 181 PRO CB C 31.3 0.2 1 1266 . 181 PRO C C 177.00 0.2 1 1267 . 181 PRO HA H 4.11 0.01 1 1268 . 182 SER H H 9.4 0.01 1 1269 . 182 SER N N 116.9 0.2 1 1270 . 182 SER CA C 61.8 0.2 1 1271 . 182 SER C C 177.2 0.2 1 1272 . 182 SER HA H 4.08 0.01 1 1273 . 182 SER HB2 H 3.85 0.01 1 1274 . 182 SER HB3 H 3.85 0.01 1 1275 . 183 THR H H 7.48 0.01 1 1276 . 183 THR N N 113.2 0.2 1 1277 . 183 THR CA C 63.7 0.2 1 1278 . 183 THR CB C 70.00 0.2 1 1279 . 183 THR C C 174.9 0.2 1 1280 . 183 THR HA H 4.16 0.01 1 1281 . 184 LEU H H 7.23 0.01 1 1282 . 184 LEU N N 118.6 0.2 1 1283 . 184 LEU CA C 54.4 0.2 1 1284 . 184 LEU CB C 42.9 0.2 1 1285 . 184 LEU C C 175.7 0.2 1 1286 . 184 LEU HA H 4.39 0.01 1 1287 . 184 LEU HB2 H 1.71 0.01 2 1288 . 184 LEU HB3 H 1.44 0.01 2 1289 . 185 LEU H H 6.76 0.01 1 1290 . 185 LEU N N 113.9 0.2 1 1291 . 185 LEU CA C 52.9 0.2 1 1292 . 185 LEU CB C 39.7 0.2 1 1293 . 185 LEU C C 174.9 0.2 1 1294 . 185 LEU HA H 4.32 0.01 1 1295 . 185 LEU HB2 H 1.8 0.01 2 1296 . 185 LEU HB3 H 1.44 0.01 2 1297 . 186 PRO CA C 62.2 0.2 1 1298 . 186 PRO CB C 32.2 0.2 1 1299 . 186 PRO C C 174.7 0.2 1 1300 . 186 PRO HA H 4.46 0.01 1 1301 . 186 PRO HB2 H 2.23 0.01 2 1302 . 186 PRO HB3 H 2.08 0.01 2 1303 . 187 SER H H 8.15 0.01 1 1304 . 187 SER N N 112.4 0.2 1 1305 . 187 SER CA C 60.8 0.2 1 1306 . 187 SER CB C 63.1 0.2 1 1307 . 187 SER C C 174.8 0.2 1 1308 . 187 SER HA H 4.08 0.01 1 1309 . 187 SER HB2 H 3.91 0.01 1 1310 . 187 SER HB3 H 3.91 0.01 1 1311 . 188 SER H H 7.42 0.01 1 1312 . 188 SER N N 113.4 0.2 1 1313 . 188 SER CA C 56.3 0.2 1 1314 . 188 SER CB C 64.2 0.2 1 1315 . 188 SER C C 175.3 0.2 1 1316 . 188 SER HA H 4.58 0.01 1 1317 . 188 SER HB2 H 3.72 0.01 1 1318 . 188 SER HB3 H 3.72 0.01 1 1319 . 189 LEU H H 8.67 0.01 1 1320 . 189 LEU N N 125.5 0.2 1 1321 . 189 LEU CA C 53.6 0.2 1 1322 . 189 LEU CB C 40.5 0.2 1 1323 . 189 LEU C C 176.9 0.2 1 1324 . 189 LEU HA H 4.6 0.01 1 1325 . 190 ASP H H 7.28 0.01 1 1326 . 190 ASP N N 121.1 0.2 1 1327 . 190 ASP CA C 56.2 0.2 1 1328 . 190 ASP CB C 40.4 0.2 1 1329 . 190 ASP C C 177.1 0.2 1 1330 . 190 ASP HA H 4.32 0.01 1 1331 . 190 ASP HB2 H 1.95 0.01 1 1332 . 190 ASP HB3 H 1.95 0.01 1 1333 . 191 PHE H H 8.7 0.01 1 1334 . 191 PHE N N 118.7 0.2 1 1335 . 191 PHE CA C 56.8 0.2 1 1336 . 191 PHE CB C 43.00 0.2 1 1337 . 191 PHE C C 172.2 0.2 1 1338 . 191 PHE HA H 5.5 0.01 1 1339 . 192 TRP H H 9.5 0.01 1 1340 . 192 TRP N N 117.4 0.2 1 1341 . 192 TRP CA C 57.3 0.2 1 1342 . 192 TRP CB C 31.5 0.2 1 1343 . 192 TRP C C 177.3 0.2 1 1344 . 192 TRP HA H 5.83 0.01 1 1345 . 192 TRP HB2 H 3.09 0.01 1 1346 . 192 TRP HB3 H 3.09 0.01 1 1347 . 193 THR H H 9.78 0.01 1 1348 . 193 THR N N 115.6 0.2 1 1349 . 193 THR CA C 58.2 0.2 1 1350 . 193 THR CB C 70.6 0.2 1 1351 . 193 THR C C 170.9 0.2 1 1352 . 193 THR HA H 6.13 0.01 1 1353 . 193 THR HB H 4.27 0.01 1 1354 . 194 TYR H H 7.96 0.01 1 1355 . 194 TYR N N 126.7 0.2 1 1356 . 194 TYR CA C 55.9 0.2 1 1357 . 194 TYR CB C 39.9 0.2 1 1358 . 194 TYR C C 170.7 0.2 1 1359 . 194 TYR HA H 5.27 0.01 1 1360 . 195 PRO CA C 62.00 0.2 1 1361 . 195 PRO CB C 31.4 0.2 1 1362 . 195 PRO C C 173.1 0.2 1 1363 . 195 PRO HA H 4.98 0.01 1 1364 . 195 PRO HB2 H 2.21 0.01 1 1365 . 195 PRO HB3 H 2.21 0.01 1 1366 . 196 GLY H H 9.53 0.01 1 1367 . 196 GLY N N 111.1 0.2 1 1368 . 196 GLY CA C 46.3 0.2 1 1369 . 196 GLY HA2 H 4.59 0.01 2 1370 . 196 GLY HA3 H 3.68 0.01 2 1371 . 197 SER H H 8.5 0.01 1 1372 . 197 SER N N 118.9 0.2 1 1373 . 197 SER CA C 56.7 0.2 1 1374 . 197 SER CB C 70.8 0.2 1 1375 . 197 SER C C 175.9 0.2 1 1376 . 197 SER HA H 5.86 0.01 1 1377 . 198 LEU H H 7.78 0.01 1 1378 . 198 LEU N N 117.5 0.2 1 1379 . 198 LEU CA C 55.00 0.2 1 1380 . 198 LEU CB C 43.7 0.2 1 1381 . 198 LEU C C 180.3 0.2 1 1382 . 198 LEU HA H 4.55 0.01 1 1383 . 198 LEU HB2 H 1.19 0.01 1 1384 . 198 LEU HB3 H 1.19 0.01 1 1385 . 199 THR H H 8.55 0.01 1 1386 . 199 THR N N 111.2 0.2 1 1387 . 199 THR CA C 61.5 0.2 1 1388 . 199 THR CB C 67.8 0.2 1 1389 . 199 THR C C 173.1 0.2 1 1390 . 199 THR HA H 4.28 0.01 1 1391 . 199 THR HB H 4.55 0.01 1 1392 . 200 HIS H H 6.7 0.01 1 1393 . 200 HIS N N 115.4 0.2 1 1394 . 200 HIS CA C 51.9 0.2 1 1395 . 200 HIS CB C 28.8 0.2 1 1396 . 200 HIS C C 171.2 0.2 1 1397 . 200 HIS HA H 4.2 0.01 1 1398 . 202 PRO CA C 64.1 0.2 1 1399 . 202 PRO CB C 31.6 0.2 1 1400 . 203 LEU H H 8.14 0.01 1 1401 . 203 LEU N N 117.1 0.2 1 1402 . 203 LEU CA C 57.1 0.2 1 1403 . 203 LEU CB C 37.4 0.2 1 1404 . 203 LEU C C 173.2 0.2 1 1405 . 203 LEU HA H 3.4 0.01 1 1406 . 203 LEU HB2 H 1.92 0.01 1 1407 . 203 LEU HB3 H 1.92 0.01 1 1408 . 204 TYR H H 5.64 0.01 1 1409 . 204 TYR N N 110.1 0.2 1 1410 . 204 TYR CA C 56.2 0.2 1 1411 . 204 TYR CB C 38.7 0.2 1 1412 . 204 TYR C C 178.00 0.2 1 1413 . 204 TYR HA H 4.36 0.01 1 1414 . 204 TYR HB2 H 3.03 0.01 1 1415 . 204 TYR HB3 H 3.03 0.01 1 1416 . 205 GLU H H 8.75 0.01 1 1417 . 205 GLU N N 124.4 0.2 1 1418 . 205 GLU CA C 55.7 0.2 1 1419 . 205 GLU CB C 26.3 0.2 1 1420 . 205 GLU C C 177.3 0.2 1 1421 . 205 GLU HA H 4.49 0.01 1 1422 . 206 SER H H 7.74 0.01 1 1423 . 206 SER N N 114.3 0.2 1 1424 . 206 SER CA C 56.00 0.2 1 1425 . 206 SER CB C 66.9 0.2 1 1426 . 206 SER C C 173.4 0.2 1 1427 . 206 SER HA H 4.92 0.01 1 1428 . 207 VAL H H 7.44 0.01 1 1429 . 207 VAL N N 119.00 0.2 1 1430 . 207 VAL CA C 61.7 0.2 1 1431 . 207 VAL CB C 35.6 0.2 1 1432 . 207 VAL C C 175.9 0.2 1 1433 . 207 VAL HA H 4.02 0.01 1 1434 . 207 VAL HB H 1.19 0.01 1 1435 . 208 THR H H 8.07 0.01 1 1436 . 208 THR N N 124.6 0.2 1 1437 . 208 THR CA C 63.3 0.2 1 1438 . 208 THR CB C 68.2 0.2 1 1439 . 208 THR C C 173.3 0.2 1 1440 . 208 THR HA H 4.29 0.01 1 1441 . 208 THR HB H 4.05 0.01 1 1442 . 209 TRP H H 8.1 0.01 1 1443 . 209 TRP N N 128.6 0.2 1 1444 . 209 TRP CA C 58.2 0.2 1 1445 . 209 TRP CB C 31.6 0.2 1 1446 . 209 TRP C C 176.8 0.2 1 1447 . 209 TRP HA H 4.41 0.01 1 1448 . 210 ILE H H 9.05 0.01 1 1449 . 210 ILE N N 126.1 0.2 1 1450 . 210 ILE CA C 58.2 0.2 1 1451 . 210 ILE CB C 38.2 0.2 1 1452 . 210 ILE C C 173.9 0.2 1 1453 . 210 ILE HA H 4.81 0.01 1 1454 . 210 ILE HB H 1.98 0.01 1 1455 . 211 ILE H H 10.07 0.01 1 1456 . 211 ILE N N 126.8 0.2 1 1457 . 211 ILE CA C 56.9 0.2 1 1458 . 211 ILE CB C 37.1 0.2 1 1459 . 211 ILE C C 176.7 0.2 1 1460 . 211 ILE HA H 5.24 0.01 1 1461 . 211 ILE HB H 2.5 0.01 1 1462 . 212 CYS H H 8.66 0.01 1 1463 . 212 CYS N N 125.6 0.2 1 1464 . 212 CYS CA C 62.6 0.2 1 1465 . 212 CYS CB C 27.1 0.2 1 1466 . 212 CYS C C 174.2 0.2 1 1467 . 212 CYS HA H 4.44 0.01 1 1468 . 212 CYS HB2 H 3.68 0.01 1 1469 . 212 CYS HB3 H 3.68 0.01 1 1470 . 213 LYS H H 7.68 0.01 1 1471 . 213 LYS N N 124.3 0.2 1 1472 . 213 LYS CA C 57.8 0.2 1 1473 . 213 LYS CB C 33.00 0.2 1 1474 . 213 LYS C C 177.1 0.2 1 1475 . 213 LYS HA H 3.88 0.01 1 1476 . 213 LYS HB2 H 0.7 0.01 2 1477 . 213 LYS HB3 H 0.44 0.01 2 1478 . 214 GLU H H 8.76 0.01 1 1479 . 214 GLU N N 119.2 0.2 1 1480 . 214 GLU CA C 55.4 0.2 1 1481 . 214 GLU CB C 30.3 0.2 1 1482 . 214 GLU C C 176.3 0.2 1 1483 . 214 GLU HA H 4.4 0.01 1 1484 . 214 GLU HB2 H 2.07 0.01 2 1485 . 214 GLU HB3 H 1.82 0.01 2 1486 . 215 SER H H 8.11 0.01 1 1487 . 215 SER N N 117.4 0.2 1 1488 . 215 SER CA C 56.9 0.2 1 1489 . 215 SER CB C 66.3 0.2 1 1490 . 215 SER C C 174.9 0.2 1 1491 . 215 SER HA H 4.95 0.01 1 1492 . 215 SER HB2 H 3.79 0.01 1 1493 . 215 SER HB3 H 3.79 0.01 1 1494 . 216 ILE H H 8.25 0.01 1 1495 . 216 ILE N N 111.2 0.2 1 1496 . 216 ILE CA C 60.00 0.2 1 1497 . 216 ILE CB C 40.9 0.2 1 1498 . 216 ILE C C 174.8 0.2 1 1499 . 216 ILE HA H 4.9 0.01 1 1500 . 216 ILE HB H 2.08 0.01 1 1501 . 217 SER H H 8.57 0.01 1 1502 . 217 SER N N 116.6 0.2 1 1503 . 217 SER CA C 57.6 0.2 1 1504 . 217 SER CB C 65.9 0.2 1 1505 . 217 SER C C 172.6 0.2 1 1506 . 217 SER HA H 5.44 0.01 1 1507 . 217 SER HB2 H 3.91 0.01 2 1508 . 217 SER HB3 H 3.3 0.01 2 1509 . 218 VAL H H 7.64 0.01 1 1510 . 218 VAL N N 116.9 0.2 1 1511 . 218 VAL CA C 60.5 0.2 1 1512 . 218 VAL CB C 33.7 0.2 1 1513 . 218 VAL C C 172.5 0.2 1 1514 . 218 VAL HA H 4.46 0.01 1 1515 . 218 VAL HB H 1.33 0.01 1 1516 . 219 SER H H 8.73 0.01 1 1517 . 219 SER N N 120.4 0.2 1 1518 . 219 SER CA C 56.4 0.2 1 1519 . 219 SER CB C 66.1 0.2 1 1520 . 219 SER C C 176.7 0.2 1 1521 . 219 SER HA H 5.19 0.01 1 1522 . 219 SER HB2 H 3.61 0.01 1 1523 . 219 SER HB3 H 3.61 0.01 1 1524 . 220 SER H H 9.36 0.01 1 1525 . 220 SER N N 116.6 0.2 1 1526 . 220 SER CA C 56.4 0.2 1 1527 . 220 SER CB C 66.00 0.2 1 1528 . 220 SER C C 174.2 0.2 1 1529 . 220 SER HA H 4.83 0.01 1 1530 . 220 SER HB2 H 3.83 0.01 2 1531 . 220 SER HB3 H 3.57 0.01 2 1532 . 221 GLU H H 8.67 0.01 1 1533 . 221 GLU N N 120.3 0.2 1 1534 . 221 GLU CA C 59.9 0.2 1 1535 . 221 GLU CB C 28.7 0.2 1 1536 . 221 GLU C C 179.00 0.2 1 1537 . 221 GLU HA H 3.96 0.01 1 1538 . 221 GLU HB2 H 1.91 0.01 1 1539 . 221 GLU HB3 H 1.91 0.01 1 1540 . 222 GLN H H 7.53 0.01 1 1541 . 222 GLN N N 120.3 0.2 1 1542 . 222 GLN CA C 59.4 0.2 1 1543 . 222 GLN CB C 28.7 0.2 1 1544 . 222 GLN C C 177.4 0.2 1 1545 . 222 GLN HA H 3.75 0.01 1 1546 . 223 LEU H H 7.65 0.01 1 1547 . 223 LEU N N 117.4 0.2 1 1548 . 223 LEU CA C 57.6 0.2 1 1549 . 223 LEU CB C 41.5 0.2 1 1550 . 223 LEU C C 178.9 0.2 1 1551 . 223 LEU HA H 3.33 0.01 1 1552 . 224 ALA H H 7.67 0.01 1 1553 . 224 ALA N N 117.3 0.2 1 1554 . 224 ALA CA C 54.5 0.2 1 1555 . 224 ALA CB C 17.8 0.2 1 1556 . 224 ALA C C 180.3 0.2 1 1557 . 224 ALA HA H 3.85 0.01 1 1558 . 224 ALA HB H 1.38 0.01 1 1559 . 225 GLN H H 7.18 0.01 1 1560 . 225 GLN N N 116.4 0.2 1 1561 . 225 GLN CA C 59.00 0.2 1 1562 . 225 GLN CB C 28.2 0.2 1 1563 . 225 GLN C C 179.4 0.2 1 1564 . 225 GLN HA H 3.8 0.01 1 1565 . 225 GLN HB2 H 2.04 0.01 2 1566 . 225 GLN HB3 H 1.83 0.01 2 1567 . 226 PHE H H 6.8 0.01 1 1568 . 226 PHE N N 119.9 0.2 1 1569 . 226 PHE CA C 57.8 0.2 1 1570 . 226 PHE CB C 34.1 0.2 1 1571 . 226 PHE C C 175.3 0.2 1 1572 . 226 PHE HA H 3.8 0.01 1 1573 . 226 PHE HB2 H 2.06 0.01 1 1574 . 226 PHE HB3 H 2.06 0.01 1 1575 . 227 ARG H H 6.39 0.01 1 1576 . 227 ARG N N 109.1 0.2 1 1577 . 227 ARG CA C 56.5 0.2 1 1578 . 227 ARG CB C 30.3 0.2 1 1579 . 227 ARG C C 176.2 0.2 1 1580 . 227 ARG HA H 4.4 0.01 1 1581 . 227 ARG HB2 H 1.87 0.01 2 1582 . 227 ARG HB3 H 1.63 0.01 2 1583 . 228 SER H H 7.1 0.01 1 1584 . 228 SER N N 111.7 0.2 1 1585 . 228 SER CA C 58.9 0.2 1 1586 . 228 SER CB C 63.8 0.2 1 1587 . 228 SER C C 175.4 0.2 1 1588 . 228 SER HA H 4.35 0.01 1 1589 . 228 SER HB2 H 3.88 0.01 1 1590 . 228 SER HB3 H 3.88 0.01 1 1591 . 229 LEU H H 7.15 0.01 1 1592 . 229 LEU N N 123.00 0.2 1 1593 . 229 LEU CA C 55.5 0.2 1 1594 . 229 LEU CB C 42.8 0.2 1 1595 . 229 LEU C C 175.1 0.2 1 1596 . 229 LEU HA H 4.17 0.01 1 1597 . 229 LEU HB2 H 2.4 0.01 1 1598 . 229 LEU HB3 H 2.4 0.01 1 1599 . 230 LEU H H 8.46 0.01 1 1600 . 230 LEU N N 118.9 0.2 1 1601 . 230 LEU CA C 53.9 0.2 1 1602 . 230 LEU CB C 41.4 0.2 1 1603 . 230 LEU C C 176.3 0.2 1 1604 . 230 LEU HA H 4.95 0.01 1 1605 . 230 LEU HB2 H 1.91 0.01 1 1606 . 230 LEU HB3 H 1.91 0.01 1 1607 . 231 SER H H 9.06 0.01 1 1608 . 231 SER N N 113.5 0.2 1 1609 . 231 SER CA C 58.6 0.2 1 1610 . 231 SER CB C 66.1 0.2 1 1611 . 231 SER C C 174.2 0.2 1 1612 . 231 SER HA H 4.84 0.01 1 1613 . 231 SER HB2 H 3.81 0.01 1 1614 . 231 SER HB3 H 3.81 0.01 1 1615 . 232 ASN H H 8.18 0.01 1 1616 . 232 ASN N N 115.5 0.2 1 1617 . 232 ASN CA C 51.9 0.2 1 1618 . 232 ASN CB C 42.1 0.2 1 1619 . 232 ASN C C 175.2 0.2 1 1620 . 232 ASN HA H 4.77 0.01 1 1621 . 232 ASN HB2 H 2.49 0.01 1 1622 . 232 ASN HB3 H 2.49 0.01 1 1623 . 233 VAL H H 8.68 0.01 1 1624 . 233 VAL N N 115.9 0.2 1 1625 . 233 VAL CA C 61.5 0.2 1 1626 . 233 VAL CB C 33.1 0.2 1 1627 . 233 VAL C C 177.2 0.2 1 1628 . 233 VAL HA H 4.22 0.01 1 1629 . 233 VAL HB H 2.11 0.01 1 1630 . 234 GLU H H 8.41 0.01 1 1631 . 234 GLU N N 126.2 0.2 1 1632 . 234 GLU CA C 58.5 0.2 1 1633 . 234 GLU CB C 29.5 0.2 1 1634 . 234 GLU C C 176.4 0.2 1 1635 . 234 GLU HA H 3.96 0.01 1 1636 . 234 GLU HB2 H 2.05 0.01 1 1637 . 234 GLU HB3 H 2.05 0.01 1 1638 . 235 GLY H H 9.04 0.01 1 1639 . 235 GLY N N 116.2 0.2 1 1640 . 235 GLY CA C 45.1 0.2 1 1641 . 235 GLY C C 174.2 0.2 1 1642 . 235 GLY HA2 H 4.39 0.01 2 1643 . 235 GLY HA3 H 3.61 0.01 2 1644 . 236 ASP H H 7.54 0.01 1 1645 . 236 ASP N N 120.8 0.2 1 1646 . 236 ASP CA C 52.6 0.2 1 1647 . 236 ASP CB C 42.5 0.2 1 1648 . 236 ASP C C 175.3 0.2 1 1649 . 236 ASP HA H 4.97 0.01 1 1650 . 236 ASP HB2 H 2.87 0.01 1 1651 . 236 ASP HB3 H 2.87 0.01 1 1652 . 237 ASN H H 8.47 0.01 1 1653 . 237 ASN N N 118.2 0.2 1 1654 . 237 ASN CA C 54.00 0.2 1 1655 . 237 ASN CB C 38.5 0.2 1 1656 . 237 ASN C C 175.4 0.2 1 1657 . 237 ASN HA H 4.35 0.01 1 1658 . 237 ASN HB2 H 2.62 0.01 1 1659 . 237 ASN HB3 H 2.62 0.01 1 1660 . 238 ALA H H 8.1 0.01 1 1661 . 238 ALA N N 124.4 0.2 1 1662 . 238 ALA CA C 52.7 0.2 1 1663 . 238 ALA CB C 19.4 0.2 1 1664 . 238 ALA C C 178.7 0.2 1 1665 . 238 ALA HA H 4.22 0.01 1 1666 . 238 ALA HB H 1.3 0.01 1 1667 . 239 VAL H H 8.76 0.01 1 1668 . 239 VAL N N 125.5 0.2 1 1669 . 239 VAL CA C 59.5 0.2 1 1670 . 239 VAL CB C 34.6 0.2 1 1671 . 239 VAL C C 173.1 0.2 1 1672 . 239 VAL HA H 4.48 0.01 1 1673 . 239 VAL HB H 2.03 0.01 1 1674 . 240 PRO CA C 63.4 0.2 1 1675 . 240 PRO CB C 32.8 0.2 1 1676 . 240 PRO C C 176.8 0.2 1 1677 . 240 PRO HA H 4.86 0.01 1 1678 . 240 PRO HB2 H 2.49 0.01 2 1679 . 240 PRO HB3 H 1.94 0.01 2 1680 . 241 MET H H 8.76 0.01 1 1681 . 241 MET N N 127.2 0.2 1 1682 . 241 MET CA C 54.9 0.2 1 1683 . 241 MET CB C 32.5 0.2 1 1684 . 241 MET C C 175.1 0.2 1 1685 . 241 MET HA H 4.4 0.01 1 1686 . 242 GLN H H 7.68 0.01 1 1687 . 242 GLN N N 121.7 0.2 1 1688 . 242 GLN CA C 59.6 0.2 1 1689 . 242 GLN CB C 30.7 0.2 1 1690 . 242 GLN C C 174.4 0.2 1 1691 . 242 GLN HA H 4.09 0.01 1 1692 . 242 GLN HB2 H 2.14 0.01 1 1693 . 242 GLN HB3 H 2.14 0.01 1 1694 . 243 HIS H H 7.25 0.01 1 1695 . 243 HIS N N 105.1 0.2 1 1696 . 243 HIS CA C 53.8 0.2 1 1697 . 243 HIS CB C 31.2 0.2 1 1698 . 243 HIS C C 174.3 0.2 1 1699 . 243 HIS HA H 4.4 0.01 1 1700 . 244 ASN H H 8.12 0.01 1 1701 . 244 ASN N N 117.00 0.2 1 1702 . 244 ASN CA C 51.7 0.2 1 1703 . 244 ASN CB C 36.4 0.2 1 1704 . 244 ASN C C 175.1 0.2 1 1705 . 244 ASN HA H 4.83 0.01 1 1706 . 245 ASN H H 8.68 0.01 1 1707 . 245 ASN N N 115.7 0.2 1 1708 . 245 ASN CA C 51.8 0.2 1 1709 . 245 ASN CB C 39.00 0.2 1 1710 . 245 ASN C C 173.9 0.2 1 1711 . 245 ASN HA H 5.36 0.01 1 1712 . 245 ASN HB2 H 2.23 0.01 1 1713 . 245 ASN HB3 H 2.23 0.01 1 1714 . 246 ARG H H 10.7 0.01 1 1715 . 246 ARG N N 130.9 0.2 1 1716 . 246 ARG CA C 53.9 0.2 1 1717 . 247 PRO CA C 62.6 0.2 1 1718 . 247 PRO CB C 33.00 0.2 1 1719 . 247 PRO C C 176.2 0.2 1 1720 . 247 PRO HA H 4.47 0.01 1 1721 . 247 PRO HB2 H 2.37 0.01 2 1722 . 247 PRO HB3 H 1.64 0.01 2 1723 . 248 THR H H 7.62 0.01 1 1724 . 248 THR N N 111.1 0.2 1 1725 . 248 THR CA C 62.5 0.2 1 1726 . 248 THR CB C 70.2 0.2 1 1727 . 248 THR C C 174.00 0.2 1 1728 . 248 THR HA H 3.57 0.01 1 1729 . 248 THR HB H 3.86 0.01 1 1730 . 249 GLN H H 8.49 0.01 1 1731 . 249 GLN N N 120.9 0.2 1 1732 . 249 GLN CA C 51.4 0.2 1 1733 . 249 GLN CB C 29.2 0.2 1 1734 . 249 GLN C C 173.00 0.2 1 1735 . 249 GLN HA H 4.4 0.01 1 1736 . 250 PRO CA C 62.3 0.2 1 1737 . 250 PRO CB C 31.8 0.2 1 1738 . 250 PRO C C 177.5 0.2 1 1739 . 250 PRO HA H 4.33 0.01 1 1740 . 251 LEU H H 8.74 0.01 1 1741 . 251 LEU N N 123.9 0.2 1 1742 . 251 LEU CA C 57.9 0.2 1 1743 . 251 LEU CB C 42.3 0.2 1 1744 . 251 LEU C C 179.4 0.2 1 1745 . 251 LEU HA H 3.94 0.01 1 1746 . 251 LEU HB2 H 1.7 0.01 1 1747 . 251 LEU HB3 H 1.7 0.01 1 1748 . 252 LYS H H 9.01 0.01 1 1749 . 252 LYS N N 115.9 0.2 1 1750 . 252 LYS CA C 56.9 0.2 1 1751 . 252 LYS CB C 29.7 0.2 1 1752 . 252 LYS C C 177.00 0.2 1 1753 . 252 LYS HA H 3.85 0.01 1 1754 . 252 LYS HB2 H 2.18 0.01 2 1755 . 252 LYS HB3 H 1.98 0.01 2 1756 . 253 GLY H H 8.52 0.01 1 1757 . 253 GLY N N 106.00 0.2 1 1758 . 253 GLY CA C 45.5 0.2 1 1759 . 253 GLY C C 175.3 0.2 1 1760 . 253 GLY HA2 H 4.15 0.01 2 1761 . 253 GLY HA3 H 3.73 0.01 2 1762 . 254 ARG H H 7.18 0.01 1 1763 . 254 ARG N N 119.5 0.2 1 1764 . 254 ARG CA C 56.9 0.2 1 1765 . 254 ARG CB C 33.6 0.2 1 1766 . 254 ARG C C 175.1 0.2 1 1767 . 254 ARG HA H 4.33 0.01 1 1768 . 255 THR H H 8.71 0.01 1 1769 . 255 THR N N 116.5 0.2 1 1770 . 255 THR CA C 62.2 0.2 1 1771 . 255 THR CB C 70.8 0.2 1 1772 . 255 THR C C 173.5 0.2 1 1773 . 255 THR HA H 4.4 0.01 1 1774 . 255 THR HB H 3.95 0.01 1 1775 . 256 VAL H H 8.95 0.01 1 1776 . 256 VAL N N 128.2 0.2 1 1777 . 256 VAL CA C 61.7 0.2 1 1778 . 256 VAL CB C 31.5 0.2 1 1779 . 256 VAL C C 175.7 0.2 1 1780 . 256 VAL HA H 4.53 0.01 1 1781 . 256 VAL HB H 2.04 0.01 1 1782 . 257 ARG H H 8.86 0.01 1 1783 . 257 ARG N N 126.00 0.2 1 1784 . 257 ARG CA C 54.4 0.2 1 1785 . 257 ARG CB C 33.9 0.2 1 1786 . 257 ARG C C 175.1 0.2 1 1787 . 257 ARG HA H 5.34 0.01 1 1788 . 257 ARG HB2 H 1.7 0.01 1 1789 . 257 ARG HB3 H 1.7 0.01 1 1790 . 258 ALA H H 8.65 0.01 1 1791 . 258 ALA N N 123.1 0.2 1 1792 . 258 ALA CA C 49.7 0.2 1 1793 . 258 ALA CB C 23.00 0.2 1 1794 . 258 ALA C C 176.9 0.2 1 1795 . 258 ALA HA H 4.95 0.01 1 1796 . 258 ALA HB H 0.66 0.01 1 1797 . 259 SER H H 8.68 0.01 1 1798 . 259 SER N N 117.9 0.2 1 1799 . 259 SER CA C 58.6 0.2 1 1800 . 259 SER CB C 63.6 0.2 1 1801 . 259 SER C C 171.1 0.2 1 1802 . 259 SER HA H 3.98 0.01 1 1803 . 259 SER HB2 H 3.72 0.01 2 1804 . 259 SER HB3 H 1.88 0.01 2 1805 . 260 PHE H H 6.52 0.01 1 1806 . 260 PHE N N 125.00 0.2 1 1807 . 260 PHE CA C 55.8 0.2 1 1808 . 260 PHE CB C 40.7 0.2 1 1809 . 260 PHE HA H 4.27 0.01 1 1810 . 260 PHE HB2 H 2.88 0.01 2 1811 . 260 PHE HB3 H 2.47 0.01 2 stop_ save_