data_4076 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C Chemical Shift Assignments of Outer Surface Protein A from Borrelia burgdorferi ; _BMRB_accession_number 4076 _BMRB_flat_file_name bmr4076.str _Entry_type original _Submission_date 1997-11-26 _Accession_date 1997-11-28 _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 Pham Thuy-Nga . . 2 Koide Shohei . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 908 "13C chemical shifts" 1041 "15N chemical shifts" 254 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-12-17 original author . stop_ _Original_release_date 1998-12-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Pham, T-N., and Koide, S., "NMR Studies of Borrelia burgdorferi OspA, a 28 KDa Protein Containing a Single-Layer Beta-sheet," J. Biomol. NMR 11, 407-414 (1998) ; _Citation_title ; NMR Studies of Borrelia burgdorferi OspA, a 28 kDa Protein Containing a Single-Layer Beta-sheet ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98356289 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pham Thuy-Nga . . 2 Koide Shohei . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 11 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 407 _Page_last 414 _Year 1998 _Details . loop_ _Keyword antigen beta-sheet 'large proteins' 'Lyme disease' 'Outer Surface Protein A' 'triple resonance' stop_ save_ ################################## # Molecular system description # ################################## save_system_OspA _Saveframe_category molecular_system _Mol_system_name 'Outer Surface Protein A' _Abbreviation_common OspA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OspA $OspA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OspA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Outer Surface Protein A' _Abbreviation_common OspA _Molecular_mass 27555 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 257 _Mol_residue_sequence ; AKQNVSSLDEKNSVSVDLPG EMKVLVSKEKNKDGKYDLIA TVDKLELKGTSDKNNGSGVL EGVKADKSKVKLTISDDLGQ TTLEVFKEDGKTLVSKKVTS KDKSSTEEKFNEKGEVSEKI ITRADGTRLEYTGIKSDGSG KAKEVLKGYVLEGTLTAEKT TLVVKEGTVTLSKNISKSGE VSVELNDTDSSAATKKTAAW NSGTSTLTITVNSKKTKDLV FTKENTITVQQYDSNGTKLE GSAVEITKLDEIKNALK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 17 ALA 2 18 LYS 3 19 GLN 4 20 ASN 5 21 VAL 6 22 SER 7 23 SER 8 24 LEU 9 25 ASP 10 26 GLU 11 27 LYS 12 28 ASN 13 29 SER 14 30 VAL 15 31 SER 16 32 VAL 17 33 ASP 18 34 LEU 19 35 PRO 20 36 GLY 21 37 GLU 22 38 MET 23 39 LYS 24 40 VAL 25 41 LEU 26 42 VAL 27 43 SER 28 44 LYS 29 45 GLU 30 46 LYS 31 47 ASN 32 48 LYS 33 49 ASP 34 50 GLY 35 51 LYS 36 52 TYR 37 53 ASP 38 54 LEU 39 55 ILE 40 56 ALA 41 57 THR 42 58 VAL 43 59 ASP 44 60 LYS 45 61 LEU 46 62 GLU 47 63 LEU 48 64 LYS 49 65 GLY 50 66 THR 51 67 SER 52 68 ASP 53 69 LYS 54 70 ASN 55 71 ASN 56 72 GLY 57 73 SER 58 74 GLY 59 75 VAL 60 76 LEU 61 77 GLU 62 78 GLY 63 79 VAL 64 80 LYS 65 81 ALA 66 82 ASP 67 83 LYS 68 84 SER 69 85 LYS 70 86 VAL 71 87 LYS 72 88 LEU 73 89 THR 74 90 ILE 75 91 SER 76 92 ASP 77 93 ASP 78 94 LEU 79 95 GLY 80 96 GLN 81 97 THR 82 98 THR 83 99 LEU 84 100 GLU 85 101 VAL 86 102 PHE 87 103 LYS 88 104 GLU 89 105 ASP 90 106 GLY 91 107 LYS 92 108 THR 93 109 LEU 94 110 VAL 95 111 SER 96 112 LYS 97 113 LYS 98 114 VAL 99 115 THR 100 116 SER 101 117 LYS 102 118 ASP 103 119 LYS 104 120 SER 105 121 SER 106 122 THR 107 123 GLU 108 124 GLU 109 125 LYS 110 126 PHE 111 127 ASN 112 128 GLU 113 129 LYS 114 130 GLY 115 131 GLU 116 132 VAL 117 133 SER 118 134 GLU 119 135 LYS 120 136 ILE 121 137 ILE 122 138 THR 123 139 ARG 124 140 ALA 125 141 ASP 126 142 GLY 127 143 THR 128 144 ARG 129 145 LEU 130 146 GLU 131 147 TYR 132 148 THR 133 149 GLY 134 150 ILE 135 151 LYS 136 152 SER 137 153 ASP 138 154 GLY 139 155 SER 140 156 GLY 141 157 LYS 142 158 ALA 143 159 LYS 144 160 GLU 145 161 VAL 146 162 LEU 147 163 LYS 148 164 GLY 149 165 TYR 150 166 VAL 151 167 LEU 152 168 GLU 153 169 GLY 154 170 THR 155 171 LEU 156 172 THR 157 173 ALA 158 174 GLU 159 175 LYS 160 176 THR 161 177 THR 162 178 LEU 163 179 VAL 164 180 VAL 165 181 LYS 166 182 GLU 167 183 GLY 168 184 THR 169 185 VAL 170 186 THR 171 187 LEU 172 188 SER 173 189 LYS 174 190 ASN 175 191 ILE 176 192 SER 177 193 LYS 178 194 SER 179 195 GLY 180 196 GLU 181 197 VAL 182 198 SER 183 199 VAL 184 200 GLU 185 201 LEU 186 202 ASN 187 203 ASP 188 204 THR 189 205 ASP 190 206 SER 191 207 SER 192 208 ALA 193 209 ALA 194 210 THR 195 211 LYS 196 212 LYS 197 213 THR 198 214 ALA 199 215 ALA 200 216 TRP 201 217 ASN 202 218 SER 203 219 GLY 204 220 THR 205 221 SER 206 222 THR 207 223 LEU 208 224 THR 209 225 ILE 210 226 THR 211 227 VAL 212 228 ASN 213 229 SER 214 230 LYS 215 231 LYS 216 232 THR 217 233 LYS 218 234 ASP 219 235 LEU 220 236 VAL 221 237 PHE 222 238 THR 223 239 LYS 224 240 GLU 225 241 ASN 226 242 THR 227 243 ILE 228 244 THR 229 245 VAL 230 246 GLN 231 247 GLN 232 248 TYR 233 249 ASP 234 250 SER 235 251 ASN 236 252 GLY 237 253 THR 238 254 LYS 239 255 LEU 240 256 GLU 241 257 GLY 242 258 SER 243 259 ALA 244 260 VAL 245 261 GLU 246 262 ILE 247 263 THR 248 264 LYS 249 265 LEU 250 266 ASP 251 267 GLU 252 268 ILE 253 269 LYS 254 270 ASN 255 271 ALA 256 272 LEU 257 273 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4077 "Outer Surface Protein A" 100.00 257 100.00 100.00 4.05e-171 PDB 1FJ1 "Lyme Disease Antigen Ospa In Complex With Neutralizing Antibody Fab La-2" 100.00 257 99.61 99.61 1.38e-170 PDB 1OSP "Crystal Structure Of Outer Surface Protein A Of Borrelia Burgdorferi Complexed With A Murine Monoclonal Antibody Fab" 100.00 257 99.61 99.61 1.38e-170 EMBL CAA32579 "ospA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA34487 "unnamed protein product [Borrelia burgdorferi ZS7]" 100.00 273 98.44 98.44 4.25e-167 EMBL CAA49314 "0spA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA56467 "ospA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA59729 "outer surface protein A [Borrelia burgdorferi 297]" 100.00 273 99.22 99.22 1.18e-168 GB AAA20947 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 GB AAA20949 "OspA, partial [Borrelia burgdorferi]" 97.28 250 99.20 99.20 6.94e-164 GB AAA20951 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 GB AAA20953 "OspA, partial [Borrelia burgdorferi]" 97.28 250 98.80 99.20 3.10e-163 GB AAA20955 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 REF NP_045688 "outer surface protein A [Borrelia burgdorferi B31]" 100.00 273 99.61 99.61 5.76e-170 REF WP_010258120 "outer surface protein A (ospA) [Borrelia burgdorferi]" 100.00 273 99.22 99.22 1.18e-168 REF WP_010890378 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 REF WP_012615002 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 98.44 98.44 4.25e-167 REF WP_012665570 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 98.83 98.83 6.93e-168 SP B7IZU3 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 98.44 98.44 4.25e-167 SP C6C2D6 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 98.83 98.83 6.93e-168 SP P0CL66 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 99.61 99.61 5.76e-170 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 $OspA spirochete 139 Eubacteria . Borrelia burgdorferi B31 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $OspA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET9-OspA 'natural source' 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 $OspA 1.5 mM '[U-99% 13C; U-98% 15N]' 'sodium phosphate' 10 mM . 'sodium chloride' 50 mM . EDTA 0.05 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 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 60 3 mM pH 6.0 0.05 n/a pressure 1.0 . atm temperature 318 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP C 13 methyl ppm 0.00 external indirect . . . 0.25144954 DSS H 1 methyl ppm 0.00 external direct . . . . DSS N 15 . ppm 0 external indirect . . . 0.10132900 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_OspA _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name OspA _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 . 2 LYS CA C 56.6 0.5 1 2 . 2 LYS HA H 4.33 0.06 1 3 . 2 LYS CB C 33.2 0.5 1 4 . 2 LYS HB2 H 1.79 0.06 2 5 . 2 LYS HB3 H 1.79 0.06 2 6 . 2 LYS CG C 24.6 0.5 1 7 . 2 LYS CD C 29.0 0.5 1 8 . 2 LYS CE C 42.0 0.5 1 9 . 2 LYS C C 176.13 0.09 1 10 . 3 GLN N N 122.9 0.1 1 11 . 3 GLN H H 8.40 0.007 1 12 . 3 GLN CA C 55.8 0.5 1 13 . 3 GLN HA H 4.35 0.06 1 14 . 3 GLN CB C 29.8 0.5 1 15 . 3 GLN HB2 H 2.04 0.06 2 16 . 3 GLN HB3 H 2.04 0.06 2 17 . 3 GLN CG C 33.8 0.5 1 18 . 3 GLN C C 175.46 0.09 1 19 . 4 ASN N N 121.6 0.1 1 20 . 4 ASN H H 8.47 0.007 1 21 . 4 ASN CA C 53.4 0.5 1 22 . 4 ASN HA H 4.72 0.06 1 23 . 4 ASN CB C 39.0 0.5 1 24 . 4 ASN HB2 H 2.79 0.06 2 25 . 4 ASN HB3 H 2.79 0.06 2 26 . 4 ASN C C 174.95 0.09 1 27 . 5 VAL N N 121.0 0.1 1 28 . 5 VAL H H 8.03 0.007 1 29 . 5 VAL CA C 62.1 0.5 1 30 . 5 VAL HA H 4.20 0.06 1 31 . 5 VAL CB C 33.1 0.5 1 32 . 5 VAL HB H 2.12 0.06 1 33 . 5 VAL CG1 C 21.2 0.5 2 34 . 5 VAL CG2 C 20.2 0.5 2 35 . 5 VAL C C 175.94 0.09 1 36 . 6 SER N N 120.5 0.1 1 37 . 6 SER H H 8.33 0.007 1 38 . 6 SER CA C 58.3 0.5 1 39 . 6 SER HA H 4.50 0.06 1 40 . 6 SER CB C 64.0 0.5 1 41 . 6 SER HB2 H 3.85 0.06 2 42 . 6 SER HB3 H 3.85 0.06 2 43 . 6 SER C C 174.45 0.09 1 44 . 7 SER N N 119.1 0.1 1 45 . 7 SER H H 8.26 0.007 1 46 . 7 SER CA C 58.5 0.5 1 47 . 7 SER HA H 4.43 0.06 1 48 . 7 SER CB C 63.8 0.5 1 49 . 7 SER HB2 H 3.84 0.06 2 50 . 7 SER HB3 H 3.84 0.06 2 51 . 7 SER C C 174.23 0.09 1 52 . 8 LEU N N 124.1 0.1 1 53 . 8 LEU H H 7.90 0.007 1 54 . 8 LEU CA C 54.9 0.5 1 55 . 8 LEU HA H 4.64 0.06 1 56 . 8 LEU CB C 42.5 0.5 1 57 . 8 LEU HB2 H 1.54 0.06 2 58 . 8 LEU HB3 H 1.54 0.06 2 59 . 8 LEU CG C 27.0 0.5 1 60 . 8 LEU CD1 C 23.5 0.5 2 61 . 8 LEU CD2 C 25.5 0.5 2 62 . 8 LEU C C 176.23 0.09 1 63 . 9 ASP N N 123.2 0.1 1 64 . 9 ASP H H 8.70 0.007 1 65 . 9 ASP CA C 53.6 0.5 1 66 . 9 ASP HA H 4.54 0.06 1 67 . 9 ASP CB C 41.8 0.5 1 68 . 9 ASP HB2 H 2.68 0.06 2 69 . 9 ASP HB3 H 2.80 0.06 2 70 . 9 ASP C C 176.81 0.09 1 71 . 10 GLU N N 121.0 0.1 1 72 . 10 GLU H H 8.62 0.007 1 73 . 10 GLU CA C 58.1 0.5 1 74 . 10 GLU HA H 4.21 0.06 1 75 . 10 GLU CB C 29.4 0.5 1 76 . 10 GLU HB2 H 2.05 0.06 2 77 . 10 GLU HB3 H 2.05 0.06 2 78 . 10 GLU CG C 36.3 0.5 1 79 . 10 GLU HG2 H 2.27 0.06 2 80 . 10 GLU HG3 H 2.27 0.06 2 81 . 10 GLU C C 177.14 0.09 1 82 . 11 LYS N N 119.7 0.1 1 83 . 11 LYS H H 8.34 0.007 1 84 . 11 LYS CA C 57.4 0.5 1 85 . 11 LYS HA H 4.33 0.06 1 86 . 11 LYS CB C 32.6 0.5 1 87 . 11 LYS HB2 H 1.88 0.06 2 88 . 11 LYS HB3 H 1.88 0.06 2 89 . 11 LYS CG C 25.0 0.5 1 90 . 11 LYS CD C 28.9 0.5 1 91 . 11 LYS C C 177.63 0.09 1 92 . 12 ASN N N 118.4 0.1 1 93 . 12 ASN H H 8.06 0.007 1 94 . 12 ASN CA C 52.7 0.5 1 95 . 12 ASN HA H 4.94 0.06 1 96 . 12 ASN CB C 39.3 0.5 1 97 . 12 ASN HB2 H 2.88 0.06 2 98 . 12 ASN HB3 H 3.05 0.06 2 99 . 12 ASN C C 175.04 0.09 1 100 . 13 SER N N 115.2 0.1 1 101 . 13 SER H H 7.75 0.007 1 102 . 13 SER CA C 58.0 0.5 1 103 . 13 SER HA H 5.21 0.06 1 104 . 13 SER CB C 67.3 0.5 1 105 . 13 SER HB2 H 3.57 0.06 2 106 . 13 SER HB3 H 3.73 0.06 2 107 . 13 SER C C 172.17 0.09 1 108 . 14 VAL N N 120.8 0.1 1 109 . 14 VAL H H 9.03 0.007 1 110 . 14 VAL CA C 61.1 0.5 1 111 . 14 VAL HA H 4.33 0.06 1 112 . 14 VAL CB C 34.5 0.5 1 113 . 14 VAL HB H 1.98 0.06 1 114 . 14 VAL CG1 C 20.7 0.5 2 115 . 14 VAL CG2 C 20.7 0.5 2 116 . 14 VAL C C 174.52 0.09 1 117 . 15 SER N N 120.0 0.1 1 118 . 15 SER H H 8.22 0.007 1 119 . 15 SER CA C 57.3 0.5 1 120 . 15 SER HA H 5.14 0.06 1 121 . 15 SER CB C 64.3 0.5 1 122 . 15 SER HB2 H 3.63 0.06 2 123 . 15 SER HB3 H 3.63 0.06 2 124 . 15 SER C C 174.45 0.09 1 125 . 16 VAL N N 130.3 0.1 1 126 . 16 VAL H H 9.29 0.007 1 127 . 16 VAL CA C 62.1 0.5 1 128 . 16 VAL HA H 4.15 0.06 1 129 . 16 VAL CB C 34.4 0.5 1 130 . 16 VAL HB H 2.00 0.06 1 131 . 16 VAL CG1 C 20.5 0.5 2 132 . 16 VAL CG2 C 20.5 0.5 2 133 . 16 VAL C C 174.97 0.09 1 134 . 17 ASP N N 127.4 0.1 1 135 . 17 ASP H H 8.20 0.007 1 136 . 17 ASP CA C 55.3 0.5 1 137 . 17 ASP HA H 4.76 0.06 1 138 . 17 ASP CB C 41.8 0.5 1 139 . 17 ASP HB2 H 2.51 0.06 2 140 . 17 ASP HB3 H 2.66 0.06 2 141 . 17 ASP C C 175.37 0.09 1 142 . 18 LEU N N 123.2 0.1 1 143 . 18 LEU H H 8.31 0.007 1 144 . 18 LEU CA C 51.8 0.5 1 145 . 18 LEU CB C 44.1 0.5 1 146 . 18 LEU CG C 33.8 0.5 1 147 . 18 LEU CD1 C 24.9 0.5 2 148 . 18 LEU CD2 C 24.9 0.5 2 149 . 19 PRO CA C 63.5 0.5 1 150 . 19 PRO HA H 4.36 0.06 1 151 . 19 PRO CB C 31.9 0.5 1 152 . 19 PRO HB2 H 1.55 0.06 2 153 . 19 PRO HB3 H 1.88 0.06 2 154 . 19 PRO CG C 27.9 0.5 1 155 . 19 PRO CD C 50.5 0.5 1 156 . 19 PRO C C 176.13 0.09 1 157 . 20 GLY N N 111.3 0.1 1 158 . 20 GLY H H 8.72 0.007 1 159 . 20 GLY CA C 45.7 0.5 1 160 . 20 GLY HA2 H 3.70 0.06 2 161 . 20 GLY HA3 H 3.94 0.06 2 162 . 20 GLY C C 174.37 0.09 1 163 . 21 GLU N N 115.7 0.1 1 164 . 21 GLU H H 8.32 0.007 1 165 . 21 GLU CA C 57.1 0.5 1 166 . 21 GLU HA H 4.04 0.06 1 167 . 21 GLU CB C 26.7 0.5 1 168 . 21 GLU HB2 H 2.19 0.06 2 169 . 21 GLU HB3 H 2.19 0.06 2 170 . 21 GLU CG C 36.7 0.5 1 171 . 21 GLU C C 175.33 0.09 1 172 . 22 MET N N 117.6 0.1 1 173 . 22 MET H H 6.79 0.007 1 174 . 22 MET CA C 54.4 0.5 1 175 . 22 MET HA H 4.76 0.06 1 176 . 22 MET CB C 36.4 0.5 1 177 . 22 MET HB2 H 1.82 0.06 2 178 . 22 MET HB3 H 1.82 0.06 2 179 . 22 MET CG C 32.3 0.5 1 180 . 22 MET C C 174.22 0.09 1 181 . 23 LYS N N 122.1 0.1 1 182 . 23 LYS H H 8.10 0.007 1 183 . 23 LYS CA C 59.0 0.5 1 184 . 23 LYS HA H 5.23 0.06 1 185 . 23 LYS CB C 36.2 0.5 1 186 . 23 LYS HB2 H 3.57 0.06 2 187 . 23 LYS HB3 H 1.62 0.06 2 188 . 23 LYS CG C 24.7 0.5 1 189 . 23 LYS CD C 29.3 0.5 1 190 . 23 LYS CE C 42.1 0.5 1 191 . 23 LYS C C 174.87 0.09 1 192 . 24 VAL N N 122.9 0.1 1 193 . 24 VAL H H 8.73 0.007 1 194 . 24 VAL CA C 59.0 0.5 1 195 . 24 VAL HA H 4.87 0.06 1 196 . 24 VAL CB C 35.8 0.5 1 197 . 24 VAL HB H 1.75 0.06 1 198 . 24 VAL CG1 C 22.6 0.5 2 199 . 24 VAL CG2 C 20.3 0.5 2 200 . 24 VAL C C 171.98 0.09 1 201 . 25 LEU N N 128.5 0.1 1 202 . 25 LEU H H 9.12 0.007 1 203 . 25 LEU CA C 53.6 0.5 1 204 . 25 LEU HA H 5.17 0.06 1 205 . 25 LEU CB C 42.8 0.5 1 206 . 25 LEU HB2 H 1.29 0.06 2 207 . 25 LEU HB3 H 1.77 0.06 2 208 . 25 LEU CG C 27.9 0.5 1 209 . 25 LEU CD1 C 24.3 0.5 2 210 . 25 LEU CD2 C 24.3 0.5 2 211 . 25 LEU C C 175.84 0.09 1 212 . 26 VAL N N 123.2 0.1 1 213 . 26 VAL H H 8.87 0.007 1 214 . 26 VAL CA C 59.4 0.5 1 215 . 26 VAL HA H 4.92 0.06 1 216 . 26 VAL CB C 34.3 0.5 1 217 . 26 VAL HB H 1.78 0.06 1 218 . 26 VAL CG1 C 19.5 0.5 2 219 . 26 VAL CG2 C 20.9 0.5 2 220 . 26 VAL C C 176.40 0.09 1 221 . 27 SER N N 124.4 0.1 1 222 . 27 SER H H 9.06 0.007 1 223 . 27 SER CA C 59.8 0.5 1 224 . 27 SER CB C 64.1 0.5 1 225 . 27 SER C C 173.91 0.09 1 226 . 28 LYS N N 121.3 0.1 1 227 . 28 LYS H H 8.16 0.007 1 228 . 28 LYS CA C 58.9 0.5 1 229 . 28 LYS HA H 4.17 0.06 1 230 . 28 LYS CB C 33.6 0.5 1 231 . 28 LYS HB2 H 1.67 0.06 2 232 . 28 LYS HB3 H 1.93 0.06 2 233 . 28 LYS CG C 26.9 0.5 1 234 . 28 LYS CD C 29.6 0.5 1 235 . 28 LYS CE C 42.8 0.5 1 236 . 28 LYS C C 177.35 0.09 1 237 . 29 GLU N N 116.3 0.1 1 238 . 29 GLU H H 8.09 0.007 1 239 . 29 GLU CA C 53.7 0.5 1 240 . 29 GLU HA H 4.75 0.06 1 241 . 29 GLU CB C 32.6 0.5 1 242 . 29 GLU HB2 H 1.83 0.06 2 243 . 29 GLU HB3 H 2.13 0.06 2 244 . 29 GLU CG C 35.9 0.5 1 245 . 29 GLU HG2 H 2.54 0.06 2 246 . 29 GLU HG3 H 2.54 0.06 2 247 . 29 GLU C C 176.61 0.09 1 248 . 30 LYS N N 124.0 0.1 1 249 . 30 LYS H H 8.47 0.007 1 250 . 30 LYS CA C 56.4 0.5 1 251 . 30 LYS HA H 3.53 0.06 1 252 . 30 LYS CB C 34.2 0.5 1 253 . 30 LYS HB2 H 1.24 0.06 2 254 . 30 LYS HB3 H 1.42 0.06 2 255 . 30 LYS CG C 25.6 0.5 1 256 . 30 LYS CD C 29.7 0.5 1 257 . 30 LYS CE C 42.0 0.5 1 258 . 30 LYS C C 176.67 0.09 1 259 . 31 ASN N N 121.0 0.1 1 260 . 31 ASN H H 9.16 0.007 1 261 . 31 ASN CA C 51.1 0.5 1 262 . 31 ASN HA H 4.59 0.06 1 263 . 31 ASN CB C 38.9 0.5 1 264 . 31 ASN HB2 H 3.19 0.06 2 265 . 31 ASN HB3 H 3.19 0.06 2 266 . 31 ASN C C 178.03 0.09 1 267 . 32 LYS N N 118.9 0.1 1 268 . 32 LYS H H 8.31 0.007 1 269 . 32 LYS CA C 58.8 0.5 1 270 . 32 LYS HA H 4.08 0.06 1 271 . 32 LYS CB C 31.7 0.5 1 272 . 32 LYS HB2 H 1.85 0.06 2 273 . 32 LYS HB3 H 1.85 0.06 2 274 . 32 LYS CG C 24.0 0.5 1 275 . 32 LYS CD C 28.9 0.5 1 276 . 32 LYS CE C 42.3 0.5 1 277 . 32 LYS C C 176.90 0.09 1 278 . 33 ASP N N 119.4 0.1 1 279 . 33 ASP H H 7.94 0.007 1 280 . 33 ASP CA C 54.5 0.5 1 281 . 33 ASP HA H 4.78 0.06 1 282 . 33 ASP CB C 41.8 0.5 1 283 . 33 ASP HB2 H 2.54 0.06 2 284 . 33 ASP HB3 H 2.84 0.06 2 285 . 33 ASP C C 176.29 0.09 1 286 . 34 GLY N N 108.8 0.1 1 287 . 34 GLY H H 8.22 0.007 1 288 . 34 GLY CA C 45.8 0.5 1 289 . 34 GLY HA2 H 3.54 0.06 2 290 . 34 GLY HA3 H 4.16 0.06 2 291 . 34 GLY C C 173.25 0.09 1 292 . 35 LYS N N 119.4 0.1 1 293 . 35 LYS H H 7.33 0.007 1 294 . 35 LYS CA C 53.8 0.5 1 295 . 35 LYS HA H 4.54 0.06 1 296 . 35 LYS CB C 36.0 0.5 1 297 . 35 LYS HB2 H 1.55 0.06 2 298 . 35 LYS HB3 H 1.85 0.06 2 299 . 35 LYS CG C 25.2 0.5 1 300 . 35 LYS CD C 28.9 0.5 1 301 . 35 LYS CE C 42.4 0.5 1 302 . 35 LYS C C 173.84 0.09 1 303 . 36 TYR N N 119.7 0.1 1 304 . 36 TYR H H 9.13 0.007 1 305 . 36 TYR CA C 59.3 0.5 1 306 . 36 TYR HA H 4.28 0.06 1 307 . 36 TYR CB C 38.6 0.5 1 308 . 36 TYR HB2 H 2.76 0.06 2 309 . 36 TYR HB3 H 2.88 0.06 2 310 . 36 TYR C C 175.73 0.09 1 311 . 37 ASP N N 123.2 0.1 1 312 . 37 ASP H H 8.48 0.007 1 313 . 37 ASP CA C 55.1 0.5 1 314 . 37 ASP HA H 5.05 0.06 1 315 . 37 ASP CB C 43.9 0.5 1 316 . 37 ASP HB2 H 2.51 0.06 2 317 . 37 ASP HB3 H 2.80 0.06 2 318 . 37 ASP C C 174.57 0.09 1 319 . 38 LEU N N 121.3 0.1 1 320 . 38 LEU H H 8.40 0.007 1 321 . 38 LEU CA C 53.7 0.5 1 322 . 38 LEU HA H 5.63 0.06 1 323 . 38 LEU CB C 46.3 0.5 1 324 . 38 LEU HB2 H 2.51 0.06 2 325 . 38 LEU HB3 H 1.20 0.06 2 326 . 38 LEU CG C 28.2 0.5 1 327 . 38 LEU CD1 C 25.5 0.5 2 328 . 38 LEU CD2 C 25.5 0.5 2 329 . 38 LEU C C 177.29 0.09 1 330 . 39 ILE N N 121.9 0.1 1 331 . 39 ILE H H 8.68 0.007 1 332 . 39 ILE CA C 60.1 0.5 1 333 . 39 ILE HA H 5.14 0.06 1 334 . 39 ILE CB C 42.6 0.5 1 335 . 39 ILE HB H 1.75 0.06 1 336 . 39 ILE CG1 C 27.9 0.5 2 337 . 39 ILE CD1 C 17.6 0.5 1 338 . 39 ILE C C 173.70 0.09 1 339 . 40 ALA N N 127.3 0.1 1 340 . 40 ALA H H 8.57 0.007 1 341 . 40 ALA CA C 51.2 0.5 1 342 . 40 ALA HA H 4.89 0.06 1 343 . 40 ALA CB C 23.6 0.5 1 344 . 40 ALA HB H 1.24 0.06 1 345 . 40 ALA C C 175.53 0.09 1 346 . 41 THR N N 117.9 0.1 1 347 . 41 THR H H 8.78 0.007 1 348 . 41 THR CA C 61.5 0.5 1 349 . 41 THR HA H 5.22 0.06 1 350 . 41 THR CB C 69.8 0.5 1 351 . 41 THR HB H 3.89 0.06 1 352 . 41 THR CG2 C 20.8 0.5 1 353 . 41 THR C C 174.44 0.09 1 354 . 42 VAL N N 127.7 0.1 1 355 . 42 VAL H H 8.64 0.007 1 356 . 42 VAL CA C 61.2 0.5 1 357 . 42 VAL HA H 4.22 0.06 1 358 . 42 VAL CB C 34.5 0.5 1 359 . 42 VAL HB H 1.83 0.06 1 360 . 42 VAL CG1 C 20.8 0.5 2 361 . 42 VAL CG2 C 20.8 0.5 2 362 . 42 VAL C C 175.28 0.09 1 363 . 43 ASP N N 129.8 0.1 1 364 . 43 ASP H H 9.15 0.007 1 365 . 43 ASP CA C 56.0 0.5 1 366 . 43 ASP HA H 4.17 0.06 1 367 . 43 ASP CB C 39.5 0.5 1 368 . 43 ASP HB2 H 2.54 0.06 2 369 . 43 ASP HB3 H 2.96 0.06 2 370 . 43 ASP C C 175.06 0.09 1 371 . 44 LYS N N 111.7 0.1 1 372 . 44 LYS H H 8.26 0.007 1 373 . 44 LYS CA C 57.9 0.5 1 374 . 44 LYS HA H 3.73 0.06 1 375 . 44 LYS CB C 30.7 0.5 1 376 . 44 LYS HB2 H 2.05 0.06 2 377 . 44 LYS HB3 H 2.05 0.06 2 378 . 44 LYS CG C 25.4 0.5 1 379 . 44 LYS CD C 28.9 0.5 1 380 . 44 LYS CE C 42.4 0.5 1 381 . 44 LYS C C 174.96 0.09 1 382 . 45 LEU N N 125.0 0.1 1 383 . 45 LEU H H 8.09 0.007 1 384 . 45 LEU CA C 54.1 0.5 1 385 . 45 LEU HA H 4.53 0.06 1 386 . 45 LEU CB C 44.2 0.5 1 387 . 45 LEU HB2 H 1.49 0.06 2 388 . 45 LEU HB3 H 1.88 0.06 2 389 . 45 LEU CG C 26.2 0.5 1 390 . 45 LEU CD1 C 24.3 0.5 2 391 . 45 LEU CD2 C 24.3 0.5 2 392 . 45 LEU C C 174.87 0.09 1 393 . 46 GLU N N 126.6 0.1 1 394 . 46 GLU H H 8.35 0.007 1 395 . 46 GLU CA C 56.2 0.5 1 396 . 46 GLU HA H 4.66 0.06 1 397 . 46 GLU CB C 30.9 0.5 1 398 . 46 GLU HB2 H 1.97 0.06 2 399 . 46 GLU HB3 H 1.97 0.06 2 400 . 46 GLU CG C 37.4 0.5 1 401 . 46 GLU HG2 H 2.15 0.06 2 402 . 46 GLU HG3 H 2.15 0.06 2 403 . 46 GLU C C 175.08 0.09 1 404 . 47 LEU N N 128.5 0.1 1 405 . 47 LEU H H 9.34 0.007 1 406 . 47 LEU CA C 53.6 0.5 1 407 . 47 LEU HA H 4.65 0.06 1 408 . 47 LEU CB C 44.4 0.5 1 409 . 47 LEU HB2 H 1.16 0.06 2 410 . 47 LEU HB3 H 1.62 0.06 2 411 . 47 LEU CG C 27.3 0.5 1 412 . 47 LEU CD1 C 23.7 0.5 2 413 . 47 LEU CD2 C 23.7 0.5 2 414 . 47 LEU C C 175.38 0.09 1 415 . 48 LYS N N 119.2 0.1 1 416 . 48 LYS H H 8.40 0.007 1 417 . 48 LYS CA C 55.1 0.5 1 418 . 48 LYS HA H 5.57 0.06 1 419 . 48 LYS CB C 37.3 0.5 1 420 . 48 LYS HB2 H 1.93 0.06 2 421 . 48 LYS HB3 H 2.01 0.06 2 422 . 48 LYS CG C 25.2 0.5 1 423 . 48 LYS CD C 29.4 0.5 1 424 . 48 LYS CE C 42.4 0.5 1 425 . 48 LYS C C 176.91 0.09 1 426 . 49 GLY N N 112.3 0.1 1 427 . 49 GLY H H 8.92 0.007 1 428 . 49 GLY CA C 45.6 0.5 1 429 . 49 GLY HA2 H 4.76 0.06 2 430 . 49 GLY HA3 H 4.76 0.06 2 431 . 49 GLY C C 172.16 0.09 1 432 . 50 THR N N 112.0 0.1 1 433 . 50 THR H H 8.49 0.007 1 434 . 50 THR CA C 59.8 0.5 1 435 . 50 THR HA H 5.77 0.06 1 436 . 50 THR CB C 73.1 0.5 1 437 . 50 THR HB H 4.05 0.06 1 438 . 50 THR C C 174.02 0.09 1 439 . 51 SER N N 113.6 0.1 1 440 . 51 SER H H 8.94 0.007 1 441 . 51 SER CA C 56.6 0.5 1 442 . 51 SER HA H 4.98 0.06 1 443 . 51 SER CB C 65.4 0.5 1 444 . 51 SER HB2 H 4.23 0.06 2 445 . 51 SER HB3 H 4.23 0.06 2 446 . 51 SER C C 173.62 0.09 1 447 . 52 ASP N N 125.3 0.1 1 448 . 52 ASP H H 8.86 0.007 1 449 . 52 ASP CA C 55.7 0.5 1 450 . 52 ASP HA H 4.89 0.06 1 451 . 52 ASP CB C 41.1 0.5 1 452 . 52 ASP HB2 H 2.80 0.06 2 453 . 52 ASP HB3 H 2.80 0.06 2 454 . 52 ASP C C 176.11 0.09 1 455 . 53 LYS N N 120.3 0.1 1 456 . 53 LYS H H 8.66 0.007 1 457 . 53 LYS CA C 55.1 0.5 1 458 . 53 LYS HA H 4.65 0.06 1 459 . 53 LYS CB C 35.4 0.5 1 460 . 53 LYS HB2 H 1.69 0.06 2 461 . 53 LYS HB3 H 1.86 0.06 2 462 . 53 LYS CG C 24.8 0.5 1 463 . 53 LYS CD C 28.8 0.5 1 464 . 53 LYS CE C 42.1 0.5 1 465 . 53 LYS C C 176.04 0.09 1 466 . 54 ASN N N 117.3 0.1 1 467 . 54 ASN H H 7.77 0.007 1 468 . 54 ASN CA C 50.9 0.5 1 469 . 54 ASN HA H 4.12 0.06 1 470 . 54 ASN CB C 36.4 0.5 1 471 . 54 ASN HB2 H 2.50 0.06 2 472 . 54 ASN HB3 H 2.50 0.06 2 473 . 54 ASN C C 174.47 0.09 1 474 . 55 ASN N N 116.0 0.1 1 475 . 55 ASN H H 7.57 0.007 1 476 . 55 ASN CA C 52.9 0.5 1 477 . 55 ASN HA H 4.48 0.06 1 478 . 55 ASN CB C 38.1 0.5 1 479 . 55 ASN HB2 H 2.83 0.06 2 480 . 55 ASN HB3 H 3.13 0.06 2 481 . 55 ASN C C 173.84 0.09 1 482 . 56 GLY N N 110.4 0.1 1 483 . 56 GLY H H 9.06 0.007 1 484 . 56 GLY CA C 44.5 0.5 1 485 . 56 GLY HA2 H 2.98 0.06 2 486 . 56 GLY HA3 H 4.22 0.06 2 487 . 56 GLY C C 170.07 0.09 1 488 . 57 SER N N 110.4 0.1 1 489 . 57 SER H H 7.04 0.007 1 490 . 57 SER CA C 57.4 0.5 1 491 . 57 SER HA H 3.97 0.06 1 492 . 57 SER CB C 66.0 0.5 1 493 . 57 SER HB2 H 3.78 0.06 2 494 . 57 SER HB3 H 3.78 0.06 2 495 . 57 SER C C 174.17 0.09 1 496 . 58 GLY N N 107.0 0.1 1 497 . 58 GLY H H 7.68 0.007 1 498 . 58 GLY CA C 44.2 0.5 1 499 . 58 GLY HA2 H 3.94 0.06 2 500 . 58 GLY HA3 H 4.49 0.06 2 501 . 58 GLY C C 170.82 0.09 1 502 . 59 VAL N N 120.0 0.1 1 503 . 59 VAL H H 8.10 0.007 1 504 . 59 VAL CA C 61.3 0.5 1 505 . 59 VAL HA H 5.15 0.06 1 506 . 59 VAL CB C 34.6 0.5 1 507 . 59 VAL HB H 1.98 0.06 1 508 . 59 VAL CG1 C 21.4 0.5 2 509 . 59 VAL CG2 C 21.4 0.5 2 510 . 59 VAL C C 175.23 0.09 1 511 . 60 LEU N N 127.7 0.1 1 512 . 60 LEU H H 9.52 0.007 1 513 . 60 LEU CA C 54.9 0.5 1 514 . 60 LEU HA H 4.88 0.06 1 515 . 60 LEU CB C 46.5 0.5 1 516 . 60 LEU HB2 H 1.49 0.06 2 517 . 60 LEU HB3 H 1.49 0.06 2 518 . 60 LEU CG C 29.4 0.5 1 519 . 60 LEU CD1 C 26.3 0.5 2 520 . 60 LEU CD2 C 26.3 0.5 2 521 . 60 LEU C C 175.22 0.09 1 522 . 61 GLU N N 118.9 0.1 1 523 . 61 GLU H H 8.67 0.007 1 524 . 61 GLU CA C 55.0 0.5 1 525 . 61 GLU HA H 5.75 0.06 1 526 . 61 GLU CB C 35.9 0.5 1 527 . 61 GLU HB2 H 2.08 0.06 2 528 . 61 GLU HB3 H 2.26 0.06 2 529 . 61 GLU CG C 37.4 0.5 1 530 . 61 GLU C C 176.46 0.09 1 531 . 62 GLY N N 110.7 0.1 1 532 . 62 GLY H H 8.85 0.007 1 533 . 62 GLY CA C 45.3 0.5 1 534 . 62 GLY HA2 H 3.89 0.06 2 535 . 62 GLY HA3 H 4.64 0.06 2 536 . 62 GLY C C 171.05 0.09 1 537 . 63 VAL N N 121.3 0.1 1 538 . 63 VAL H H 8.56 0.007 1 539 . 63 VAL CA C 61.1 0.5 1 540 . 63 VAL HA H 5.00 0.06 1 541 . 63 VAL CB C 35.0 0.5 1 542 . 63 VAL HB H 1.97 0.06 1 543 . 63 VAL CG1 C 20.8 0.5 2 544 . 63 VAL CG2 C 20.8 0.5 2 545 . 63 VAL C C 175.47 0.09 1 546 . 64 LYS N N 125.3 0.1 1 547 . 64 LYS H H 8.72 0.007 1 548 . 64 LYS CA C 56.4 0.5 1 549 . 64 LYS HA H 4.41 0.06 1 550 . 64 LYS CB C 34.7 0.5 1 551 . 64 LYS CG C 26.4 0.5 1 552 . 64 LYS CD C 29.3 0.5 1 553 . 64 LYS CE C 41.5 0.5 1 554 . 64 LYS C C 178.77 0.09 1 555 . 65 ALA N N 125.6 0.1 1 556 . 65 ALA H H 8.75 0.007 1 557 . 65 ALA CA C 55.1 0.5 1 558 . 65 ALA HA H 4.16 0.06 1 559 . 65 ALA CB C 18.1 0.5 1 560 . 65 ALA HB H 1.49 0.06 2 561 . 65 ALA C C 178.03 0.09 1 562 . 66 ASP N N 115.7 0.1 1 563 . 66 ASP H H 7.47 0.007 1 564 . 66 ASP CA C 53.3 0.5 1 565 . 66 ASP HA H 4.50 0.06 1 566 . 66 ASP CB C 39.6 0.5 1 567 . 66 ASP HB2 H 2.55 0.06 2 568 . 66 ASP HB3 H 3.12 0.06 2 569 . 66 ASP C C 176.44 0.09 1 570 . 67 LYS N N 112.0 0.1 1 571 . 67 LYS H H 7.99 0.007 1 572 . 67 LYS CA C 59.2 0.5 1 573 . 67 LYS HA H 3.67 0.06 1 574 . 67 LYS CB C 29.6 0.5 1 575 . 67 LYS HB2 H 2.02 0.06 2 576 . 67 LYS HB3 H 2.44 0.06 2 577 . 67 LYS CD C 25.5 0.5 1 578 . 67 LYS CE C 42.4 0.5 1 579 . 67 LYS C C 175.66 0.09 1 580 . 68 SER N N 116.5 0.1 1 581 . 68 SER H H 8.14 0.007 1 582 . 68 SER CA C 60.8 0.5 1 583 . 68 SER HA H 4.22 0.06 1 584 . 68 SER CB C 63.1 0.5 1 585 . 68 SER HB2 H 4.03 0.06 2 586 . 68 SER HB3 H 4.03 0.06 2 587 . 68 SER C C 172.79 0.09 1 588 . 69 LYS N N 124.0 0.1 1 589 . 69 LYS H H 7.81 0.007 1 590 . 69 LYS CA C 55.6 0.5 1 591 . 69 LYS HA H 4.95 0.06 1 592 . 69 LYS CB C 35.1 0.5 1 593 . 69 LYS HB2 H 1.76 0.06 2 594 . 69 LYS HB3 H 1.99 0.06 2 595 . 69 LYS CG C 25.6 0.5 1 596 . 69 LYS CD C 28.9 0.5 1 597 . 69 LYS CE C 42.4 0.5 1 598 . 69 LYS C C 174.70 0.09 1 599 . 70 VAL N N 124.2 0.1 1 600 . 70 VAL H H 8.69 0.007 1 601 . 70 VAL CA C 61.2 0.5 1 602 . 70 VAL HA H 5.10 0.06 1 603 . 70 VAL CB C 34.5 0.5 1 604 . 70 VAL HB H 1.64 0.06 1 605 . 70 VAL CG1 C 21.8 0.5 2 606 . 70 VAL CG2 C 21.8 0.5 2 607 . 70 VAL C C 174.48 0.09 1 608 . 71 LYS N N 129.1 0.1 1 609 . 71 LYS H H 9.48 0.007 1 610 . 71 LYS CA C 55.3 0.5 1 611 . 71 LYS HA H 5.33 0.06 1 612 . 71 LYS CB C 37.8 0.5 1 613 . 71 LYS HB2 H 1.83 0.06 2 614 . 71 LYS HB3 H 2.05 0.06 2 615 . 71 LYS CG C 25.6 0.5 1 616 . 71 LYS CD C 29.8 0.5 1 617 . 71 LYS CE C 42.2 0.5 1 618 . 71 LYS C C 174.06 0.09 1 619 . 72 LEU N N 132.5 0.1 1 620 . 72 LEU H H 9.57 0.007 1 621 . 72 LEU CA C 53.0 0.5 1 622 . 72 LEU HA H 5.51 0.06 1 623 . 72 LEU CB C 46.1 0.5 1 624 . 72 LEU HB2 H 1.08 0.06 2 625 . 72 LEU HB3 H 1.80 0.06 2 626 . 72 LEU CG C 26.5 0.5 1 627 . 72 LEU C C 174.04 0.09 1 628 . 73 THR N N 124.2 0.1 1 629 . 73 THR H H 9.40 0.007 1 630 . 73 THR CA C 62.6 0.5 1 631 . 73 THR HA H 4.96 0.06 1 632 . 73 THR CB C 69.9 0.5 1 633 . 73 THR CG2 C 20.4 0.5 1 634 . 73 THR C C 174.24 0.09 1 635 . 74 ILE N N 132.2 0.1 1 636 . 74 ILE H H 9.47 0.007 1 637 . 74 ILE CA C 61.2 0.5 1 638 . 74 ILE HA H 4.56 0.06 1 639 . 74 ILE CB C 40.4 0.5 1 640 . 74 ILE HB H 1.92 0.06 1 641 . 74 ILE CG1 C 28.5 0.5 2 642 . 74 ILE CD1 C 16.1 0.5 1 643 . 74 ILE CG2 C 19.8 0.5 2 644 . 74 ILE C C 176.53 0.09 1 645 . 75 SER N N 124.8 0.1 1 646 . 75 SER H H 8.40 0.007 1 647 . 75 SER CA C 59.7 0.5 1 648 . 75 SER HA H 4.42 0.06 1 649 . 75 SER CB C 64.3 0.5 1 650 . 75 SER HB2 H 3.89 0.06 2 651 . 75 SER HB3 H 4.06 0.06 2 652 . 75 SER C C 174.83 0.09 1 653 . 76 ASP N N 121.0 0.1 1 654 . 76 ASP H H 8.51 0.007 1 655 . 76 ASP CA C 57.7 0.5 1 656 . 76 ASP HA H 4.38 0.06 1 657 . 76 ASP CB C 41.2 0.5 1 658 . 76 ASP HB2 H 2.63 0.06 2 659 . 76 ASP HB3 H 2.63 0.06 2 660 . 76 ASP C C 176.25 0.09 1 661 . 77 ASP N N 115.4 0.1 1 662 . 77 ASP H H 7.79 0.007 1 663 . 77 ASP CA C 52.3 0.5 1 664 . 77 ASP HA H 4.49 0.06 1 665 . 77 ASP CB C 40.3 0.5 1 666 . 77 ASP HB2 H 2.52 0.06 2 667 . 77 ASP HB3 H 2.99 0.06 2 668 . 77 ASP C C 176.90 0.09 1 669 . 78 LEU N N 117.3 0.1 1 670 . 78 LEU H H 8.33 0.007 1 671 . 78 LEU CA C 56.5 0.5 1 672 . 78 LEU HA H 3.54 0.06 1 673 . 78 LEU CB C 39.1 0.5 1 674 . 78 LEU HB2 H 1.51 0.06 2 675 . 78 LEU HB3 H 2.08 0.06 2 676 . 78 LEU CG C 27.5 0.5 1 677 . 78 LEU CD1 C 22.9 0.5 2 678 . 78 LEU CD2 C 25.4 0.5 2 679 . 78 LEU C C 176.17 0.09 1 680 . 79 GLY N N 105.6 0.1 1 681 . 79 GLY H H 8.13 0.007 1 682 . 79 GLY CA C 46.2 0.5 1 683 . 79 GLY HA2 H 3.63 0.06 2 684 . 79 GLY HA3 H 3.90 0.06 2 685 . 79 GLY C C 173.68 0.09 1 686 . 80 GLN N N 118.7 0.1 1 687 . 80 GLN H H 7.83 0.007 1 688 . 80 GLN CA C 54.9 0.5 1 689 . 80 GLN HA H 5.37 0.06 1 690 . 80 GLN CB C 33.9 0.5 1 691 . 80 GLN HB2 H 1.95 0.06 2 692 . 80 GLN HB3 H 1.95 0.06 2 693 . 80 GLN C C 174.74 0.09 1 694 . 81 THR N N 114.1 0.1 1 695 . 81 THR H H 8.86 0.007 1 696 . 81 THR CA C 59.0 0.5 1 697 . 81 THR HA H 5.17 0.06 1 698 . 81 THR CB C 71.2 0.5 1 699 . 81 THR HB H 4.00 0.06 1 700 . 81 THR CG2 C 20.3 0.5 1 701 . 81 THR C C 173.56 0.09 1 702 . 82 THR N N 119.7 0.1 1 703 . 82 THR H H 9.04 0.007 1 704 . 82 THR CA C 62.1 0.5 1 705 . 82 THR HA H 5.09 0.06 1 706 . 82 THR CB C 71.1 0.5 1 707 . 82 THR HB H 4.09 0.06 1 708 . 82 THR CG2 C 20.9 0.5 1 709 . 82 THR C C 172.46 0.09 1 710 . 83 LEU N N 132.7 0.1 1 711 . 83 LEU H H 9.53 0.007 1 712 . 83 LEU CA C 53.6 0.5 1 713 . 83 LEU HA H 5.34 0.06 1 714 . 83 LEU CB C 44.8 0.5 1 715 . 83 LEU HB2 H 1.31 0.06 2 716 . 83 LEU HB3 H 1.95 0.06 2 717 . 83 LEU CG C 25.9 0.5 1 718 . 83 LEU CD1 C 24.6 0.5 2 719 . 83 LEU CD2 C 24.6 0.5 2 720 . 83 LEU C C 175.85 0.09 1 721 . 84 GLU N N 130.6 0.1 1 722 . 84 GLU H H 9.63 0.007 1 723 . 84 GLU CA C 55.1 0.5 1 724 . 84 GLU HA H 4.26 0.06 1 725 . 84 GLU CB C 35.2 0.5 1 726 . 84 GLU HB2 H 1.80 0.06 2 727 . 84 GLU HB3 H 1.80 0.06 2 728 . 84 GLU CG C 38.8 0.5 1 729 . 84 GLU C C 173.50 0.09 1 730 . 85 VAL N N 122.6 0.1 1 731 . 85 VAL H H 8.24 0.007 1 732 . 85 VAL CA C 61.3 0.5 1 733 . 85 VAL HA H 4.82 0.06 1 734 . 85 VAL CB C 33.4 0.5 1 735 . 85 VAL HB H 2.00 0.06 1 736 . 85 VAL CG1 C 21.0 0.5 2 737 . 85 VAL CG2 C 21.0 0.5 2 738 . 85 VAL C C 174.43 0.09 1 739 . 86 PHE N N 126.9 0.1 1 740 . 86 PHE H H 9.67 0.007 1 741 . 86 PHE CA C 56.4 0.5 1 742 . 86 PHE HA H 5.34 0.06 1 743 . 86 PHE CB C 43.8 0.5 1 744 . 86 PHE HB2 H 2.90 0.06 2 745 . 86 PHE HB3 H 3.12 0.06 2 746 . 86 PHE C C 176.81 0.09 1 747 . 87 LYS N N 117.6 0.1 1 748 . 87 LYS H H 8.37 0.007 1 749 . 87 LYS CA C 56.5 0.5 1 750 . 87 LYS HA H 4.47 0.06 1 751 . 87 LYS CB C 33.8 0.5 1 752 . 87 LYS HB2 H 2.03 0.06 2 753 . 87 LYS HB3 H 2.19 0.06 2 754 . 87 LYS CG C 26.1 0.5 1 755 . 87 LYS CD C 29.1 0.5 1 756 . 87 LYS C C 176.65 0.09 1 757 . 88 GLU N N 120.0 0.1 1 758 . 88 GLU H H 8.80 0.007 1 759 . 88 GLU CA C 58.7 0.5 1 760 . 88 GLU HA H 4.18 0.06 1 761 . 88 GLU CB C 29.6 0.5 1 762 . 88 GLU HB2 H 2.06 0.06 2 763 . 88 GLU HB3 H 2.06 0.06 2 764 . 88 GLU CG C 35.6 0.5 1 765 . 88 GLU C C 176.13 0.09 1 766 . 89 ASP N N 117.4 0.1 1 767 . 89 ASP H H 7.32 0.007 1 768 . 89 ASP CA C 54.6 0.5 1 769 . 89 ASP HA H 4.28 0.06 1 770 . 89 ASP CB C 40.0 0.5 1 771 . 89 ASP HB2 H 2.81 0.06 2 772 . 89 ASP HB3 H 2.91 0.06 2 773 . 89 ASP C C 177.61 0.09 1 774 . 90 GLY N N 110.4 0.1 1 775 . 90 GLY H H 8.70 0.007 1 776 . 90 GLY CA C 46.1 0.5 1 777 . 90 GLY HA2 H 3.22 0.06 2 778 . 90 GLY HA3 H 3.91 0.06 2 779 . 90 GLY C C 172.22 0.09 1 780 . 91 LYS N N 118.7 0.1 1 781 . 91 LYS H H 8.48 0.007 1 782 . 91 LYS CA C 56.9 0.5 1 783 . 91 LYS HA H 4.28 0.06 1 784 . 91 LYS CB C 35.9 0.5 1 785 . 91 LYS HB2 H 1.49 0.06 2 786 . 91 LYS HB3 H 1.65 0.06 2 787 . 91 LYS CG C 24.0 0.5 1 788 . 91 LYS CD C 28.8 0.5 1 789 . 91 LYS CE C 42.1 0.5 1 790 . 91 LYS C C 175.81 0.09 1 791 . 92 THR N N 123.1 0.1 1 792 . 92 THR H H 9.65 0.007 1 793 . 92 THR CA C 63.5 0.5 1 794 . 92 THR HA H 4.20 0.06 1 795 . 92 THR CB C 67.7 0.5 1 796 . 92 THR CG2 C 21.1 0.5 1 797 . 92 THR C C 173.77 0.09 1 798 . 93 LEU N N 132.5 0.1 1 799 . 93 LEU H H 8.32 0.007 1 800 . 93 LEU CA C 56.2 0.5 1 801 . 93 LEU HA H 3.83 0.06 1 802 . 93 LEU CB C 43.0 0.5 1 803 . 93 LEU HB2 H 4.66 0.06 2 804 . 93 LEU HB3 H 4.83 0.06 2 805 . 93 LEU CG C 25.1 0.5 1 806 . 93 LEU C C 176.23 0.09 1 807 . 94 VAL N N 122.1 0.1 1 808 . 94 VAL H H 9.20 0.007 1 809 . 94 VAL CA C 64.0 0.5 1 810 . 94 VAL HA H 4.23 0.06 1 811 . 94 VAL CB C 33.7 0.5 1 812 . 94 VAL HB H 1.80 0.06 1 813 . 94 VAL CG1 C 21.1 0.5 2 814 . 94 VAL CG2 C 21.1 0.5 2 815 . 94 VAL C C 176.97 0.09 1 816 . 95 SER N N 113.9 0.1 1 817 . 95 SER H H 7.82 0.007 1 818 . 95 SER CA C 57.5 0.5 1 819 . 95 SER HA H 5.42 0.06 1 820 . 95 SER CB C 67.5 0.5 1 821 . 95 SER HB2 H 3.82 0.06 2 822 . 95 SER HB3 H 3.99 0.06 2 823 . 95 SER C C 174.21 0.09 1 824 . 96 LYS N N 117.6 0.1 1 825 . 96 LYS H H 8.93 0.007 1 826 . 96 LYS CA C 55.8 0.5 1 827 . 96 LYS HA H 5.25 0.06 1 828 . 96 LYS CB C 37.5 0.5 1 829 . 96 LYS HB2 H 1.98 0.06 2 830 . 96 LYS HB3 H 1.81 0.06 2 831 . 96 LYS CD C 29.8 0.5 1 832 . 96 LYS CE C 42.1 0.5 1 833 . 96 LYS C C 174.22 0.09 1 834 . 97 LYS N N 130.6 0.1 1 835 . 97 LYS H H 9.30 0.007 1 836 . 97 LYS CA C 55.2 0.5 1 837 . 97 LYS HA H 5.60 0.06 1 838 . 97 LYS CB C 36.4 0.5 1 839 . 97 LYS HB2 H 1.74 0.06 2 840 . 97 LYS HB3 H 1.93 0.06 2 841 . 97 LYS CG C 25.6 0.5 1 842 . 97 LYS CD C 29.8 0.5 1 843 . 97 LYS CE C 42.0 0.5 1 844 . 97 LYS C C 175.23 0.09 1 845 . 98 VAL N N 133.2 0.1 1 846 . 98 VAL H H 9.22 0.007 1 847 . 98 VAL CA C 61.2 0.5 1 848 . 98 VAL HA H 5.22 0.06 1 849 . 98 VAL CB C 34.1 0.5 1 850 . 98 VAL HB H 2.03 0.06 1 851 . 98 VAL CG1 C 20.9 0.5 2 852 . 98 VAL CG2 C 20.9 0.5 2 853 . 98 VAL C C 175.86 0.09 1 854 . 99 THR N N 125.5 0.1 1 855 . 99 THR H H 9.07 0.007 1 856 . 99 THR CA C 62.1 0.5 1 857 . 99 THR HA H 4.85 0.06 1 858 . 99 THR CB C 70.0 0.5 1 859 . 99 THR HB H 3.71 0.06 1 860 . 99 THR CG2 C 21.0 0.5 1 861 . 99 THR C C 173.19 0.09 1 862 . 100 SER N N 120.8 0.1 1 863 . 100 SER H H 8.54 0.007 1 864 . 100 SER CA C 57.2 0.5 1 865 . 100 SER HA H 5.37 0.06 1 866 . 100 SER CB C 64.8 0.5 1 867 . 100 SER HB2 H 3.96 0.06 2 868 . 100 SER HB3 H 4.06 0.06 2 869 . 100 SER C C 176.59 0.09 1 870 . 101 LYS N N 125.3 0.1 1 871 . 101 LYS H H 8.25 0.007 1 872 . 101 LYS CA C 58.9 0.5 1 873 . 101 LYS HA H 4.05 0.06 1 874 . 101 LYS CB C 32.8 0.5 1 875 . 101 LYS HB2 H 2.03 0.06 2 876 . 101 LYS HB3 H 2.03 0.06 2 877 . 101 LYS CG C 24.2 0.5 1 878 . 101 LYS CD C 29.5 0.5 1 879 . 101 LYS CE C 24.2 0.5 1 880 . 101 LYS C C 175.76 0.09 1 881 . 102 ASP N N 120.0 0.1 1 882 . 102 ASP H H 7.90 0.007 1 883 . 102 ASP CA C 54.0 0.5 1 884 . 102 ASP HA H 4.44 0.06 1 885 . 102 ASP CB C 39.6 0.5 1 886 . 102 ASP HB2 H 2.57 0.06 2 887 . 102 ASP HB3 H 3.07 0.06 2 888 . 102 ASP C C 175.34 0.09 1 889 . 103 LYS N N 110.7 0.1 1 890 . 103 LYS H H 7.94 0.007 1 891 . 103 LYS CA C 59.5 0.5 1 892 . 103 LYS HA H 3.77 0.06 1 893 . 103 LYS CB C 29.8 0.5 1 894 . 103 LYS HB2 H 2.05 0.06 2 895 . 103 LYS HB3 H 2.53 0.06 2 896 . 103 LYS CD C 26.0 0.5 1 897 . 103 LYS CE C 42.4 0.5 1 898 . 103 LYS C C 176.28 0.09 1 899 . 104 SER N N 118.2 0.1 1 900 . 104 SER H H 8.34 0.007 1 901 . 104 SER CA C 58.7 0.5 1 902 . 104 SER HA H 4.39 0.06 1 903 . 104 SER CB C 67.5 0.5 1 904 . 104 SER HB2 H 3.79 0.06 2 905 . 104 SER HB3 H 4.22 0.06 2 906 . 104 SER C C 173.23 0.09 1 907 . 105 SER N N 114.1 0.1 1 908 . 105 SER H H 8.97 0.007 1 909 . 105 SER CA C 57.5 0.5 1 910 . 105 SER HA H 5.61 0.06 1 911 . 105 SER CB C 67.5 0.5 1 912 . 105 SER HB2 H 3.85 0.06 2 913 . 105 SER HB3 H 3.85 0.06 2 914 . 105 SER C C 174.21 0.09 1 915 . 106 THR N N 117.6 0.1 1 916 . 106 THR H H 8.93 0.007 1 917 . 106 THR CA C 61.8 0.5 1 918 . 106 THR HA H 5.19 0.06 1 919 . 106 THR CB C 71.4 0.5 1 920 . 106 THR HB H 3.98 0.06 1 921 . 106 THR C C 172.97 0.09 1 922 . 107 GLU N N 129.3 0.1 1 923 . 107 GLU H H 9.26 0.007 1 924 . 107 GLU CA C 54.8 0.5 1 925 . 107 GLU HA H 5.38 0.06 1 926 . 107 GLU CB C 33.5 0.5 1 927 . 107 GLU HB2 H 1.78 0.06 2 928 . 107 GLU HB3 H 2.10 0.06 2 929 . 107 GLU CG C 36.7 0.5 1 930 . 107 GLU C C 174.47 0.09 1 931 . 108 GLU N N 126.9 0.1 1 932 . 108 GLU H H 9.23 0.007 1 933 . 108 GLU CA C 54.8 0.5 1 934 . 108 GLU HA H 4.96 0.06 1 935 . 108 GLU CB C 35.1 0.5 1 936 . 108 GLU HB2 H 1.55 0.06 2 937 . 108 GLU HB3 H 1.97 0.06 2 938 . 108 GLU CG C 37.7 0.5 1 939 . 108 GLU C C 174.57 0.09 1 940 . 109 LYS N N 121.8 0.1 1 941 . 109 LYS H H 8.28 0.007 1 942 . 109 LYS CA C 54.9 0.5 1 943 . 109 LYS HA H 4.85 0.06 1 944 . 109 LYS CB C 35.0 0.5 1 945 . 109 LYS HB2 H 1.60 0.06 2 946 . 109 LYS HB3 H 1.95 0.06 2 947 . 109 LYS CG C 25.1 0.5 1 948 . 109 LYS CD C 28.9 0.5 1 949 . 109 LYS CE C 42.3 0.5 1 950 . 109 LYS C C 175.03 0.09 1 951 . 110 PHE N N 121.6 0.1 1 952 . 110 PHE H H 7.80 0.007 1 953 . 110 PHE CA C 57.1 0.5 1 954 . 110 PHE HA H 5.14 0.06 1 955 . 110 PHE CB C 42.5 0.5 1 956 . 110 PHE HB2 H 2.81 0.06 2 957 . 110 PHE HB3 H 2.81 0.06 2 958 . 110 PHE C C 176.53 0.09 1 959 . 111 ASN N N 120.5 0.1 1 960 . 111 ASN H H 8.89 0.007 1 961 . 111 ASN CA C 50.8 0.5 1 962 . 111 ASN HA H 4.97 0.06 1 963 . 111 ASN CB C 38.9 0.5 1 964 . 111 ASN HB2 H 2.98 0.06 2 965 . 111 ASN HB3 H 3.62 0.06 2 966 . 111 ASN C C 177.76 0.09 1 967 . 112 GLU N N 119.4 0.1 1 968 . 112 GLU H H 9.21 0.007 1 969 . 112 GLU CA C 59.3 0.5 1 970 . 112 GLU HA H 4.18 0.06 1 971 . 112 GLU CB C 28.9 0.5 1 972 . 112 GLU HB2 H 2.14 0.06 2 973 . 112 GLU HB3 H 2.14 0.06 2 974 . 112 GLU CG C 36.3 0.5 1 975 . 112 GLU C C 176.93 0.09 1 976 . 113 LYS N N 118.7 0.1 1 977 . 113 LYS H H 7.63 0.007 1 978 . 113 LYS CA C 55.7 0.5 1 979 . 113 LYS HA H 4.45 0.06 1 980 . 113 LYS CB C 32.7 0.5 1 981 . 113 LYS HB2 H 1.75 0.06 2 982 . 113 LYS HB3 H 2.04 0.06 2 983 . 113 LYS CG C 25.1 0.5 1 984 . 113 LYS CD C 28.9 0.5 1 985 . 113 LYS C C 176.90 0.09 1 986 . 114 GLY N N 108.8 0.1 1 987 . 114 GLY H H 8.26 0.007 1 988 . 114 GLY CA C 45.8 0.5 1 989 . 114 GLY HA2 H 3.88 0.06 2 990 . 114 GLY HA3 H 4.23 0.06 2 991 . 114 GLY C C 174.14 0.09 1 992 . 115 GLU N N 120.7 0.1 1 993 . 115 GLU H H 7.78 0.007 1 994 . 115 GLU CA C 54.2 0.5 1 995 . 115 GLU HA H 4.56 0.06 1 996 . 115 GLU CB C 30.7 0.5 1 997 . 115 GLU HB2 H 1.95 0.06 2 998 . 115 GLU HB3 H 1.95 0.06 2 999 . 115 GLU CG C 36.1 0.5 1 1000 . 115 GLU HG2 H 2.18 0.06 2 1001 . 115 GLU HG3 H 2.18 0.06 2 1002 . 115 GLU C C 176.29 0.09 1 1003 . 116 VAL N N 124.7 0.1 1 1004 . 116 VAL H H 8.44 0.007 1 1005 . 116 VAL CA C 63.6 0.5 1 1006 . 116 VAL HA H 3.51 0.06 1 1007 . 116 VAL CB C 31.7 0.5 1 1008 . 116 VAL HB H 1.78 0.06 1 1009 . 116 VAL C C 174.99 0.09 1 1010 . 117 SER N N 122.7 0.1 1 1011 . 117 SER H H 8.94 0.007 1 1012 . 117 SER CA C 58.4 0.5 1 1013 . 117 SER HA H 4.71 0.06 1 1014 . 117 SER CB C 65.5 0.5 1 1015 . 117 SER HB2 H 3.58 0.06 2 1016 . 117 SER HB3 H 3.90 0.06 2 1017 . 117 SER C C 174.28 0.09 1 1018 . 118 GLU N N 121.3 0.1 1 1019 . 118 GLU H H 7.41 0.007 1 1020 . 118 GLU CA C 55.4 0.5 1 1021 . 118 GLU HA H 4.92 0.06 1 1022 . 118 GLU CB C 34.2 0.5 1 1023 . 118 GLU HB2 H 1.97 0.06 2 1024 . 118 GLU HB3 H 1.97 0.06 2 1025 . 118 GLU CG C 36.9 0.5 1 1026 . 118 GLU HG2 H 2.15 0.06 2 1027 . 118 GLU HG3 H 2.15 0.06 2 1028 . 118 GLU C C 173.83 0.09 1 1029 . 119 LYS N N 124.5 0.1 1 1030 . 119 LYS H H 9.03 0.007 1 1031 . 119 LYS CA C 55.5 0.5 1 1032 . 119 LYS HA H 5.37 0.06 1 1033 . 119 LYS CB C 36.9 0.5 1 1034 . 119 LYS HB2 H 1.59 0.06 2 1035 . 119 LYS HB3 H 1.76 0.06 2 1036 . 119 LYS CD C 29.8 0.5 1 1037 . 119 LYS CE C 42.0 0.5 1 1038 . 119 LYS C C 173.34 0.09 1 1039 . 120 ILE N N 127.1 0.1 1 1040 . 120 ILE H H 9.39 0.007 1 1041 . 120 ILE CA C 60.2 0.5 1 1042 . 120 ILE HA H 4.94 0.06 1 1043 . 120 ILE CB C 40.6 0.5 1 1044 . 120 ILE HB H 1.90 0.06 1 1045 . 120 ILE CG1 C 27.9 0.5 2 1046 . 120 ILE CD1 C 13.4 0.5 1 1047 . 120 ILE CG2 C 18.2 0.5 2 1048 . 120 ILE C C 176.27 0.09 1 1049 . 121 ILE N N 134.1 0.1 1 1050 . 121 ILE H H 9.66 0.007 1 1051 . 121 ILE CA C 60.9 0.5 1 1052 . 121 ILE HA H 4.78 0.06 1 1053 . 121 ILE CB C 40.3 0.5 1 1054 . 121 ILE HB H 1.99 0.06 1 1055 . 121 ILE CG1 C 27.7 0.5 2 1056 . 121 ILE CD1 C 14.7 0.5 1 1057 . 121 ILE CG2 C 17.1 0.5 2 1058 . 121 ILE C C 175.14 0.09 1 1059 . 122 THR N N 125.6 0.1 1 1060 . 122 THR H H 9.35 0.007 1 1061 . 122 THR CA C 62.4 0.5 1 1062 . 122 THR HA H 4.73 0.06 1 1063 . 122 THR CB C 69.1 0.5 1 1064 . 122 THR HB H 4.24 0.06 1 1065 . 122 THR CG2 C 20.5 0.5 1 1066 . 122 THR C C 174.88 0.09 1 1067 . 123 ARG N N 126.6 0.1 1 1068 . 123 ARG H H 8.93 0.007 1 1069 . 123 ARG CA C 56.1 0.5 1 1070 . 123 ARG HA H 4.42 0.06 1 1071 . 123 ARG CB C 30.8 0.5 1 1072 . 123 ARG C C 178.05 0.09 1 1073 . 124 ALA N N 124.8 0.1 1 1074 . 124 ALA H H 8.88 0.007 1 1075 . 124 ALA CA C 54.9 0.5 1 1076 . 124 ALA HA H 3.90 0.06 1 1077 . 124 ALA CB C 18.6 0.5 1 1078 . 124 ALA HB H 1.43 0.06 2 1079 . 124 ALA C C 177.58 0.09 1 1080 . 125 ASP N N 113.6 0.1 1 1081 . 125 ASP H H 7.24 0.007 1 1082 . 125 ASP CA C 53.2 0.5 1 1083 . 125 ASP HA H 4.47 0.06 1 1084 . 125 ASP CB C 40.5 0.5 1 1085 . 125 ASP HB2 H 2.55 0.06 2 1086 . 125 ASP HB3 H 3.09 0.06 2 1087 . 125 ASP C C 177.37 0.09 1 1088 . 126 GLY N N 109.5 0.1 1 1089 . 126 GLY H H 8.03 0.007 1 1090 . 126 GLY CA C 45.3 0.5 1 1091 . 126 GLY HA2 H 3.54 0.06 2 1092 . 126 GLY HA3 H 4.35 0.06 2 1093 . 126 GLY C C 175.67 0.09 1 1094 . 127 THR N N 115.2 0.1 1 1095 . 127 THR H H 8.33 0.007 1 1096 . 127 THR CA C 62.9 0.5 1 1097 . 127 THR HA H 4.42 0.06 1 1098 . 127 THR CB C 70.6 0.5 1 1099 . 127 THR CG2 C 22.3 0.5 1 1100 . 127 THR C C 173.40 0.09 1 1101 . 128 ARG N N 116.0 0.1 1 1102 . 128 ARG H H 8.20 0.007 1 1103 . 128 ARG CA C 54.6 0.5 1 1104 . 128 ARG HA H 5.76 0.06 1 1105 . 128 ARG CB C 36.2 0.5 1 1106 . 128 ARG HB2 H 1.54 0.06 2 1107 . 128 ARG HB3 H 1.70 0.06 2 1108 . 128 ARG CG C 27.3 0.5 1 1109 . 128 ARG CD C 44.2 0.5 1 1110 . 128 ARG C C 174.83 0.09 1 1111 . 129 LEU N N 123.7 0.1 1 1112 . 129 LEU H H 9.11 0.007 1 1113 . 129 LEU CA C 53.8 0.5 1 1114 . 129 LEU HA H 4.93 0.06 1 1115 . 129 LEU CB C 45.3 0.5 1 1116 . 129 LEU HB2 H 1.13 0.06 2 1117 . 129 LEU HB3 H 1.43 0.06 2 1118 . 129 LEU CG C 24.5 0.5 1 1119 . 129 LEU C C 174.73 0.09 1 1120 . 130 GLU N N 121.8 0.1 1 1121 . 130 GLU H H 9.07 0.007 1 1122 . 130 GLU CA C 54.6 0.5 1 1123 . 130 GLU HA H 4.80 0.06 1 1124 . 130 GLU CB C 32.1 0.5 1 1125 . 130 GLU HB2 H 1.76 0.06 2 1126 . 130 GLU HB3 H 1.76 0.06 2 1127 . 130 GLU CG C 36.3 0.5 1 1128 . 130 GLU C C 175.25 0.09 1 1129 . 131 TYR N N 126.3 0.1 1 1130 . 131 TYR H H 9.39 0.007 1 1131 . 131 TYR CA C 54.9 0.5 1 1132 . 131 TYR HA H 6.00 0.06 1 1133 . 131 TYR CB C 40.1 0.5 1 1134 . 131 TYR C C 175.74 0.09 1 1135 . 132 THR N N 114.1 0.1 1 1136 . 132 THR H H 8.76 0.007 1 1137 . 132 THR CA C 59.6 0.5 1 1138 . 132 THR HA H 5.01 0.06 1 1139 . 132 THR CB C 72.3 0.5 1 1140 . 132 THR HB H 4.25 0.06 1 1141 . 132 THR C C 173.68 0.09 1 1142 . 133 GLY N N 112.0 0.1 1 1143 . 133 GLY H H 8.80 0.007 1 1144 . 133 GLY CA C 47.3 0.5 1 1145 . 133 GLY HA2 H 3.78 0.06 2 1146 . 133 GLY HA3 H 3.92 0.06 2 1147 . 133 GLY C C 175.25 0.09 1 1148 . 134 ILE N N 118.9 0.1 1 1149 . 134 ILE H H 7.77 0.007 1 1150 . 134 ILE CA C 62.6 0.5 1 1151 . 134 ILE HA H 4.40 0.06 1 1152 . 134 ILE CB C 37.6 0.5 1 1153 . 134 ILE HB H 1.94 0.06 1 1154 . 134 ILE CD1 C 17.3 0.5 1 1155 . 134 ILE C C 177.57 0.09 1 1156 . 135 LYS N N 129.3 0.1 1 1157 . 135 LYS H H 8.86 0.007 1 1158 . 135 LYS CA C 55.0 0.5 1 1159 . 135 LYS CB C 35.1 0.5 1 1160 . 135 LYS CG C 25.0 0.5 1 1161 . 135 LYS CD C 28.8 0.5 1 1162 . 135 LYS C C 179.61 0.09 1 1163 . 136 SER N N 118.1 0.1 1 1164 . 136 SER H H 8.62 0.007 1 1165 . 136 SER CA C 61.6 0.5 1 1166 . 136 SER HA H 4.13 0.06 1 1167 . 136 SER CB C 63.0 0.5 1 1168 . 136 SER HB2 H 3.96 0.06 2 1169 . 136 SER HB3 H 3.96 0.06 2 1170 . 136 SER C C 174.52 0.09 1 1171 . 137 ASP N N 118.9 0.1 1 1172 . 137 ASP H H 7.59 0.007 1 1173 . 137 ASP CA C 53.3 0.5 1 1174 . 137 ASP HA H 4.28 0.06 1 1175 . 137 ASP CB C 39.7 0.5 1 1176 . 137 ASP HB2 H 2.04 0.06 2 1177 . 137 ASP HB3 H 2.04 0.06 2 1178 . 137 ASP C C 177.38 0.09 1 1179 . 138 GLY N N 110.6 0.1 1 1180 . 138 GLY H H 8.31 0.007 1 1181 . 138 GLY CA C 45.1 0.5 1 1182 . 138 GLY HA2 H 3.47 0.06 2 1183 . 138 GLY HA3 H 4.03 0.06 2 1184 . 138 GLY C C 172.64 0.09 1 1185 . 139 SER N N 115.5 0.1 1 1186 . 139 SER H H 7.85 0.007 1 1187 . 139 SER CA C 57.0 0.5 1 1188 . 139 SER HA H 4.88 0.06 1 1189 . 139 SER CB C 65.4 0.5 1 1190 . 139 SER HB2 H 4.12 0.06 2 1191 . 139 SER HB3 H 4.12 0.06 2 1192 . 139 SER C C 173.36 0.09 1 1193 . 140 GLY N N 104.6 0.1 1 1194 . 140 GLY H H 8.23 0.007 1 1195 . 140 GLY CA C 46.2 0.5 1 1196 . 140 GLY HA2 H 3.77 0.06 2 1197 . 140 GLY HA3 H 4.39 0.06 2 1198 . 140 GLY C C 172.74 0.09 1 1199 . 141 LYS N N 124.7 0.1 1 1200 . 141 LYS H H 8.96 0.007 1 1201 . 141 LYS CA C 56.1 0.5 1 1202 . 141 LYS HA H 4.75 0.06 1 1203 . 141 LYS CB C 33.6 0.5 1 1204 . 141 LYS HB2 H 1.93 0.06 2 1205 . 141 LYS HB3 H 1.93 0.06 2 1206 . 141 LYS CG C 25.1 0.5 1 1207 . 141 LYS CD C 28.8 0.5 1 1208 . 141 LYS CE C 42.1 0.5 1 1209 . 141 LYS C C 174.89 0.09 1 1210 . 142 ALA N N 123.4 0.1 1 1211 . 142 ALA H H 7.92 0.007 1 1212 . 142 ALA CA C 50.0 0.5 1 1213 . 142 ALA HA H 5.59 0.06 1 1214 . 142 ALA CB C 25.6 0.5 1 1215 . 142 ALA HB H 1.09 0.06 1 1216 . 142 ALA C C 175.82 0.09 1 1217 . 143 LYS N N 122.3 0.1 1 1218 . 143 LYS H H 8.54 0.007 1 1219 . 143 LYS CA C 55.4 0.5 1 1220 . 143 LYS HA H 5.07 0.06 1 1221 . 143 LYS CB C 36.7 0.5 1 1222 . 143 LYS HB2 H 1.66 0.06 2 1223 . 143 LYS HB3 H 1.66 0.06 2 1224 . 143 LYS CG C 25.0 0.5 1 1225 . 143 LYS CD C 29.4 0.5 1 1226 . 143 LYS CE C 42.0 0.5 1 1227 . 143 LYS C C 173.59 0.09 1 1228 . 144 GLU N N 128.2 0.1 1 1229 . 144 GLU H H 9.53 0.007 1 1230 . 144 GLU CA C 54.6 0.5 1 1231 . 144 GLU HA H 5.17 0.06 1 1232 . 144 GLU CB C 32.7 0.5 1 1233 . 144 GLU HB2 H 1.47 0.06 2 1234 . 144 GLU HB3 H 2.15 0.06 2 1235 . 144 GLU CG C 37.3 0.5 1 1236 . 144 GLU C C 174.37 0.09 1 1237 . 145 VAL N N 130.6 0.1 1 1238 . 145 VAL H H 9.48 0.007 1 1239 . 145 VAL CA C 63.1 0.5 1 1240 . 145 VAL HA H 3.98 0.06 1 1241 . 145 VAL CB C 31.7 0.5 1 1242 . 145 VAL HB H 1.98 0.06 1 1243 . 145 VAL CG1 C 19.5 0.5 2 1244 . 145 VAL CG2 C 20.7 0.5 2 1245 . 145 VAL C C 174.91 0.09 1 1246 . 146 LEU N N 129.3 0.1 1 1247 . 146 LEU H H 7.75 0.007 1 1248 . 146 LEU CA C 52.7 0.5 1 1249 . 146 LEU HA H 4.54 0.06 1 1250 . 146 LEU CB C 40.7 0.5 1 1251 . 146 LEU HB2 H 4.68 0.06 2 1252 . 146 LEU HB3 H 1.25 0.06 2 1253 . 146 LEU CG C 27.6 0.5 1 1254 . 146 LEU CD1 C 22.8 0.5 2 1255 . 146 LEU CD2 C 24.2 0.5 2 1256 . 146 LEU C C 175.97 0.09 1 1257 . 147 LYS N N 120.8 0.1 1 1258 . 147 LYS H H 7.86 0.007 1 1259 . 147 LYS CA C 57.5 0.5 1 1260 . 147 LYS HA H 4.19 0.06 1 1261 . 147 LYS CB C 30.4 0.5 1 1262 . 147 LYS HB2 H 1.74 0.06 2 1263 . 147 LYS HB3 H 1.74 0.06 2 1264 . 147 LYS CG C 24.7 0.5 1 1265 . 147 LYS CD C 29.0 0.5 1 1266 . 147 LYS CE C 42.4 0.5 1 1267 . 147 LYS C C 176.34 0.09 1 1268 . 148 GLY N N 114.1 0.1 1 1269 . 148 GLY H H 7.96 0.007 1 1270 . 148 GLY CA C 45.3 0.5 1 1271 . 148 GLY HA2 H 3.73 0.06 2 1272 . 148 GLY HA3 H 4.78 0.06 2 1273 . 148 GLY C C 173.48 0.09 1 1274 . 149 TYR N N 114.9 0.1 1 1275 . 149 TYR H H 6.76 0.007 1 1276 . 149 TYR CA C 55.9 0.5 1 1277 . 149 TYR HA H 4.86 0.06 1 1278 . 149 TYR CB C 39.3 0.5 1 1279 . 149 TYR HB2 H 3.32 0.06 2 1280 . 149 TYR HB3 H 3.32 0.06 2 1281 . 149 TYR C C 171.42 0.09 1 1282 . 150 VAL N N 117.1 0.1 1 1283 . 150 VAL H H 7.98 0.007 1 1284 . 150 VAL CA C 59.7 0.5 1 1285 . 150 VAL HA H 5.03 0.06 1 1286 . 150 VAL CB C 35.3 0.5 1 1287 . 150 VAL HB H 1.98 0.06 1 1288 . 150 VAL CG1 C 21.1 0.5 2 1289 . 150 VAL CG2 C 21.1 0.5 2 1290 . 150 VAL C C 175.12 0.09 1 1291 . 151 LEU N N 124.2 0.1 1 1292 . 151 LEU H H 8.91 0.007 1 1293 . 151 LEU CA C 52.7 0.5 1 1294 . 151 LEU HA H 5.05 0.06 1 1295 . 151 LEU CB C 45.4 0.5 1 1296 . 151 LEU HB2 H 1.33 0.06 2 1297 . 151 LEU HB3 H 1.33 0.06 2 1298 . 151 LEU CG C 25.5 0.5 1 1299 . 151 LEU CD1 C 23.1 0.5 2 1300 . 151 LEU CD2 C 23.1 0.5 2 1301 . 151 LEU C C 176.04 0.09 1 1302 . 152 GLU N N 122.4 0.1 1 1303 . 152 GLU H H 9.48 0.007 1 1304 . 152 GLU CA C 55.5 0.5 1 1305 . 152 GLU HA H 5.11 0.06 1 1306 . 152 GLU CB C 34.2 0.5 1 1307 . 152 GLU HB2 H 2.14 0.06 2 1308 . 152 GLU HB3 H 2.25 0.06 2 1309 . 152 GLU CG C 37.7 0.5 1 1310 . 152 GLU C C 176.34 0.09 1 1311 . 153 GLY N N 109.0 0.1 1 1312 . 153 GLY H H 8.65 0.007 1 1313 . 153 GLY CA C 46.5 0.5 1 1314 . 153 GLY HA2 H 4.29 0.06 2 1315 . 153 GLY HA3 H 5.20 0.06 2 1316 . 153 GLY C C 174.22 0.09 1 1317 . 154 THR N N 118.9 0.1 1 1318 . 154 THR H H 9.15 0.007 1 1319 . 154 THR CA C 61.0 0.5 1 1320 . 154 THR HA H 4.97 0.06 1 1321 . 154 THR CB C 72.8 0.5 1 1322 . 154 THR HB H 4.30 0.06 1 1323 . 154 THR C C 171.53 0.09 1 1324 . 155 LEU N N 125.8 0.1 1 1325 . 155 LEU H H 8.38 0.007 1 1326 . 155 LEU CA C 54.1 0.5 1 1327 . 155 LEU HA H 4.94 0.06 1 1328 . 155 LEU CB C 45.2 0.5 1 1329 . 155 LEU HB2 H 1.26 0.06 2 1330 . 155 LEU HB3 H 1.26 0.06 2 1331 . 155 LEU CG C 25.2 0.5 1 1332 . 155 LEU CD1 C 22.3 0.5 2 1333 . 155 LEU CD2 C 22.3 0.5 2 1334 . 155 LEU C C 175.65 0.09 1 1335 . 156 THR N N 118.1 0.1 1 1336 . 156 THR H H 8.45 0.007 1 1337 . 156 THR CA C 60.2 0.5 1 1338 . 156 THR HA H 4.46 0.06 1 1339 . 156 THR CB C 72.8 0.5 1 1340 . 156 THR C C 173.69 0.09 1 1341 . 157 ALA N N 122.1 0.1 1 1342 . 157 ALA H H 8.76 0.007 1 1343 . 157 ALA CA C 54.3 0.5 1 1344 . 157 ALA HA H 4.01 0.06 1 1345 . 157 ALA CB C 18.1 0.5 1 1346 . 157 ALA HB H 1.43 0.06 1 1347 . 157 ALA C C 178.29 0.09 1 1348 . 158 GLU N N 113.3 0.1 1 1349 . 158 GLU H H 7.91 0.007 1 1350 . 158 GLU CA C 57.7 0.5 1 1351 . 158 GLU HA H 4.21 0.06 1 1352 . 158 GLU CB C 31.4 0.5 1 1353 . 158 GLU HB2 H 1.95 0.06 2 1354 . 158 GLU HB3 H 1.95 0.06 2 1355 . 158 GLU CG C 36.4 0.5 1 1356 . 158 GLU HG2 H 2.17 0.06 2 1357 . 158 GLU HG3 H 2.17 0.06 2 1358 . 158 GLU C C 176.10 0.09 1 1359 . 159 LYS N N 116.5 0.1 1 1360 . 159 LYS H H 7.57 0.007 1 1361 . 159 LYS CA C 56.0 0.5 1 1362 . 159 LYS HA H 4.71 0.06 1 1363 . 159 LYS CB C 34.6 0.5 1 1364 . 159 LYS HB2 H 1.45 0.06 2 1365 . 159 LYS HB3 H 1.93 0.06 2 1366 . 159 LYS CG C 22.7 0.5 1 1367 . 159 LYS CD C 29.8 0.5 1 1368 . 159 LYS C C 174.36 0.09 1 1369 . 160 THR N N 121.0 0.1 1 1370 . 160 THR H H 8.64 0.007 1 1371 . 160 THR CA C 62.3 0.5 1 1372 . 160 THR HA H 4.97 0.06 1 1373 . 160 THR CB C 70.5 0.5 1 1374 . 160 THR HB H 4.12 0.06 1 1375 . 160 THR CG2 C 20.9 0.5 1 1376 . 160 THR C C 173.38 0.09 1 1377 . 161 THR N N 125.0 0.1 1 1378 . 161 THR H H 9.10 0.007 1 1379 . 161 THR CA C 62.2 0.5 1 1380 . 161 THR HA H 5.06 0.06 1 1381 . 161 THR CB C 71.3 0.5 1 1382 . 161 THR HB H 3.72 0.06 1 1383 . 161 THR CG2 C 19.5 0.5 1 1384 . 161 THR C C 172.65 0.09 1 1385 . 162 LEU N N 131.9 0.1 1 1386 . 162 LEU H H 9.30 0.007 1 1387 . 162 LEU CA C 53.6 0.5 1 1388 . 162 LEU HA H 4.69 0.06 1 1389 . 162 LEU CB C 42.3 0.5 1 1390 . 162 LEU HB2 H 1.76 0.06 2 1391 . 162 LEU HB3 H 2.03 0.06 2 1392 . 162 LEU CG C 25.5 0.5 1 1393 . 162 LEU CD1 C 24.2 0.5 2 1394 . 162 LEU CD2 C 27.3 0.5 2 1395 . 162 LEU C C 175.63 0.09 1 1396 . 163 VAL N N 120.8 0.1 1 1397 . 163 VAL H H 8.41 0.007 1 1398 . 163 VAL CA C 61.2 0.5 1 1399 . 163 VAL HA H 5.32 0.06 1 1400 . 163 VAL CB C 36.2 0.5 1 1401 . 163 VAL HB H 1.90 0.06 1 1402 . 163 VAL CG1 C 20.9 0.5 2 1403 . 163 VAL CG2 C 20.9 0.5 2 1404 . 163 VAL C C 175.63 0.09 1 1405 . 164 VAL N N 126.9 0.1 1 1406 . 164 VAL H H 9.09 0.007 1 1407 . 164 VAL CA C 61.7 0.5 1 1408 . 164 VAL HA H 4.33 0.06 1 1409 . 164 VAL CB C 35.0 0.5 1 1410 . 164 VAL HB H 1.91 0.06 1 1411 . 164 VAL CG1 C 21.5 0.5 2 1412 . 164 VAL CG2 C 21.5 0.5 2 1413 . 164 VAL C C 173.35 0.09 1 1414 . 165 LYS N N 127.9 0.1 1 1415 . 165 LYS H H 8.40 0.007 1 1416 . 165 LYS CA C 54.6 0.5 1 1417 . 165 LYS HA H 5.26 0.06 1 1418 . 165 LYS CB C 35.9 0.5 1 1419 . 165 LYS HB2 H 1.54 0.06 2 1420 . 165 LYS HB3 H 1.80 0.06 2 1421 . 165 LYS CG C 25.1 0.5 1 1422 . 165 LYS CD C 29.4 0.5 1 1423 . 165 LYS CE C 42.1 0.5 1 1424 . 165 LYS C C 175.50 0.09 1 1425 . 166 GLU N N 125.3 0.1 1 1426 . 166 GLU H H 8.56 0.007 1 1427 . 166 GLU CA C 55.5 0.5 1 1428 . 166 GLU HA H 4.59 0.06 1 1429 . 166 GLU CB C 32.1 0.5 1 1430 . 166 GLU CG C 35.1 0.5 1 1431 . 166 GLU C C 175.90 0.09 1 1432 . 167 GLY N N 121.3 0.1 1 1433 . 167 GLY H H 8.99 0.007 1 1434 . 167 GLY CA C 47.1 0.5 1 1435 . 167 GLY HA2 H 3.71 0.06 2 1436 . 167 GLY HA3 H 4.16 0.06 2 1437 . 167 GLY C C 175.93 0.09 1 1438 . 168 THR N N 119.7 0.1 1 1439 . 168 THR H H 8.70 0.007 1 1440 . 168 THR CA C 63.0 0.5 1 1441 . 168 THR HA H 4.96 0.06 1 1442 . 168 THR CB C 67.7 0.5 1 1443 . 168 THR HB H 4.22 0.06 1 1444 . 168 THR CG2 C 21.7 0.5 1 1445 . 168 THR C C 174.49 0.09 1 1446 . 169 VAL N N 126.1 0.1 1 1447 . 169 VAL H H 8.33 0.007 1 1448 . 169 VAL CA C 62.6 0.5 1 1449 . 169 VAL HA H 4.70 0.06 1 1450 . 169 VAL CB C 33.1 0.5 1 1451 . 169 VAL HB H 2.35 0.06 1 1452 . 169 VAL CG1 C 23.2 0.5 2 1453 . 169 VAL CG2 C 23.2 0.5 2 1454 . 169 VAL C C 175.45 0.09 1 1455 . 170 THR N N 123.4 0.1 1 1456 . 170 THR H H 9.04 0.007 1 1457 . 170 THR CA C 62.2 0.5 1 1458 . 170 THR HA H 4.80 0.06 1 1459 . 170 THR CB C 70.9 0.5 1 1460 . 170 THR HB H 3.93 0.06 1 1461 . 170 THR CG2 C 21.3 0.5 1 1462 . 170 THR C C 173.26 0.09 1 1463 . 171 LEU N N 134.0 0.1 1 1464 . 171 LEU H H 9.52 0.007 1 1465 . 171 LEU CA C 54.0 0.5 1 1466 . 171 LEU HA H 4.93 0.06 1 1467 . 171 LEU CB C 45.0 0.5 1 1468 . 171 LEU HB2 H 1.32 0.06 2 1469 . 171 LEU HB3 H 1.32 0.06 2 1470 . 171 LEU CG C 26.1 0.5 1 1471 . 171 LEU CD1 C 25.1 0.5 2 1472 . 171 LEU CD2 C 25.1 0.5 2 1473 . 171 LEU C C 174.16 0.09 1 1474 . 172 SER N N 122.9 0.1 1 1475 . 172 SER H H 8.96 0.007 1 1476 . 172 SER CA C 56.7 0.5 1 1477 . 172 SER HA H 5.36 0.06 1 1478 . 172 SER CB C 64.2 0.5 1 1479 . 172 SER HB2 H 3.50 0.06 2 1480 . 172 SER HB3 H 3.50 0.06 2 1481 . 172 SER C C 171.71 0.09 1 1482 . 173 LYS N N 127.9 0.1 1 1483 . 173 LYS H H 9.49 0.007 1 1484 . 173 LYS CA C 54.8 0.5 1 1485 . 173 LYS HA H 4.30 0.06 1 1486 . 173 LYS CB C 34.7 0.5 1 1487 . 173 LYS CG C 25.9 0.5 1 1488 . 173 LYS CD C 31.0 0.5 1 1489 . 173 LYS CE C 41.9 0.5 1 1490 . 173 LYS C C 173.48 0.09 1 1491 . 174 ASN N N 126.9 0.1 1 1492 . 174 ASN H H 8.99 0.007 1 1493 . 174 ASN CA C 51.7 0.5 1 1494 . 174 ASN HA H 5.69 0.06 1 1495 . 174 ASN CB C 41.1 0.5 1 1496 . 174 ASN HB2 H 2.14 0.06 2 1497 . 174 ASN HB3 H 2.69 0.06 2 1498 . 174 ASN C C 174.40 0.09 1 1499 . 175 ILE N N 122.4 0.1 1 1500 . 175 ILE H H 9.17 0.007 1 1501 . 175 ILE CA C 60.3 0.5 1 1502 . 175 ILE HA H 4.68 0.06 1 1503 . 175 ILE CB C 40.9 0.5 1 1504 . 175 ILE HB H 1.55 0.06 1 1505 . 175 ILE CG1 C 27.0 0.5 2 1506 . 175 ILE CD1 C 14.6 0.5 1 1507 . 175 ILE CG2 C 17.2 0.5 2 1508 . 175 ILE C C 177.43 0.09 1 1509 . 176 SER N N 126.1 0.1 1 1510 . 176 SER H H 9.17 0.007 1 1511 . 176 SER CA C 58.1 0.5 1 1512 . 176 SER HA H 4.60 0.06 1 1513 . 176 SER CB C 65.0 0.5 1 1514 . 176 SER HB2 H 4.07 0.06 2 1515 . 176 SER HB3 H 4.07 0.06 2 1516 . 176 SER C C 176.12 0.09 1 1517 . 177 LYS N N 123.4 0.1 1 1518 . 177 LYS H H 8.46 0.007 1 1519 . 177 LYS CA C 59.3 0.5 1 1520 . 177 LYS HA H 4.09 0.06 1 1521 . 177 LYS CB C 31.8 0.5 1 1522 . 177 LYS HB2 H 1.92 0.06 2 1523 . 177 LYS HB3 H 1.92 0.06 2 1524 . 177 LYS CG C 24.5 0.5 1 1525 . 177 LYS CD C 29.2 0.5 1 1526 . 177 LYS CE C 42.0 0.5 1 1527 . 177 LYS C C 177.20 0.09 1 1528 . 178 SER N N 112.8 0.1 1 1529 . 178 SER H H 7.92 0.007 1 1530 . 178 SER CA C 57.9 0.5 1 1531 . 178 SER HA H 4.50 0.06 1 1532 . 178 SER CB C 63.6 0.5 1 1533 . 178 SER HB2 H 3.83 0.06 2 1534 . 178 SER HB3 H 3.83 0.06 2 1535 . 178 SER C C 174.99 0.09 1 1536 . 179 GLY N N 111.9 0.1 1 1537 . 179 GLY H H 8.02 0.007 1 1538 . 179 GLY CA C 45.2 0.5 1 1539 . 179 GLY HA2 H 3.46 0.06 2 1540 . 179 GLY HA3 H 4.31 0.06 2 1541 . 179 GLY C C 173.96 0.09 1 1542 . 180 GLU N N 122.1 0.1 1 1543 . 180 GLU H H 7.73 0.007 1 1544 . 180 GLU CA C 56.9 0.5 1 1545 . 180 GLU HA H 4.29 0.06 1 1546 . 180 GLU CB C 30.6 0.5 1 1547 . 180 GLU HB2 H 1.95 0.06 2 1548 . 180 GLU HB3 H 1.95 0.06 2 1549 . 180 GLU CG C 36.4 0.5 1 1550 . 180 GLU HG2 H 2.19 0.06 2 1551 . 180 GLU HG3 H 2.19 0.06 2 1552 . 180 GLU C C 176.54 0.09 1 1553 . 181 VAL N N 129.8 0.1 1 1554 . 181 VAL H H 8.77 0.007 1 1555 . 181 VAL CA C 61.5 0.5 1 1556 . 181 VAL HA H 5.03 0.06 1 1557 . 181 VAL CB C 33.6 0.5 1 1558 . 181 VAL HB H 2.06 0.06 1 1559 . 181 VAL CG1 C 22.4 0.5 2 1560 . 181 VAL CG2 C 21.0 0.5 2 1561 . 181 VAL C C 175.80 0.09 1 1562 . 182 SER N N 121.8 0.1 1 1563 . 182 SER H H 8.71 0.007 1 1564 . 182 SER CA C 57.2 0.5 1 1565 . 182 SER CB C 65.1 0.5 1 1566 . 182 SER C C 171.16 0.09 1 1567 . 183 VAL N N 120.8 0.1 1 1568 . 183 VAL H H 3.98 0.007 1 1569 . 183 VAL CA C 59.7 0.5 1 1570 . 183 VAL HA H 4.59 0.06 1 1571 . 183 VAL CB C 33.7 0.5 1 1572 . 183 VAL HB H 4.78 0.06 1 1573 . 183 VAL CG1 C 19.6 0.5 2 1574 . 183 VAL CG2 C 17.6 0.5 2 1575 . 183 VAL C C 173.09 0.09 1 1576 . 184 GLU N N 124.5 0.1 1 1577 . 184 GLU H H 8.51 0.007 1 1578 . 184 GLU CA C 53.8 0.5 1 1579 . 184 GLU HA H 4.55 0.06 1 1580 . 184 GLU CB C 34.3 0.5 1 1581 . 184 GLU HB2 H 1.78 0.06 2 1582 . 184 GLU HB3 H 1.78 0.06 2 1583 . 184 GLU CG C 35.9 0.5 1 1584 . 184 GLU HG2 H 1.90 0.06 2 1585 . 184 GLU HG3 H 1.90 0.06 2 1586 . 184 GLU C C 173.31 0.09 1 1587 . 185 LEU N N 124.5 0.1 1 1588 . 185 LEU H H 8.61 0.007 1 1589 . 185 LEU CA C 54.1 0.5 1 1590 . 185 LEU HA H 5.25 0.06 1 1591 . 185 LEU CB C 47.0 0.5 1 1592 . 185 LEU HB2 H 1.34 0.06 2 1593 . 185 LEU HB3 H 1.59 0.06 2 1594 . 185 LEU CG C 27.4 0.5 1 1595 . 185 LEU CD1 C 26.0 0.5 2 1596 . 185 LEU CD2 C 26.0 0.5 2 1597 . 185 LEU C C 174.79 0.09 1 1598 . 186 ASN N N 125.1 0.1 1 1599 . 186 ASN H H 8.87 0.007 1 1600 . 186 ASN CA C 53.0 0.5 1 1601 . 186 ASN HA H 5.11 0.06 1 1602 . 186 ASN CB C 43.1 0.5 1 1603 . 186 ASN HB2 H 2.64 0.06 2 1604 . 186 ASN HB3 H 2.64 0.06 2 1605 . 186 ASN C C 172.21 0.09 1 1606 . 187 ASP N N 126.9 0.1 1 1607 . 187 ASP H H 8.54 0.007 1 1608 . 187 ASP CA C 52.4 0.5 1 1609 . 187 ASP HA H 5.60 0.06 1 1610 . 187 ASP CB C 45.0 0.5 1 1611 . 187 ASP HB2 H 2.53 0.06 2 1612 . 187 ASP HB3 H 3.21 0.06 2 1613 . 187 ASP C C 177.39 0.09 1 1614 . 188 THR N N 117.5 0.1 1 1615 . 188 THR H H 8.48 0.007 1 1616 . 188 THR CA C 62.6 0.5 1 1617 . 188 THR HA H 4.59 0.06 1 1618 . 188 THR CB C 68.6 0.5 1 1619 . 188 THR HB H 4.26 0.06 1 1620 . 188 THR CG2 C 21.3 0.5 1 1621 . 188 THR C C 175.54 0.09 1 1622 . 189 ASP N N 126.9 0.1 1 1623 . 189 ASP H H 8.37 0.007 1 1624 . 189 ASP CA C 55.2 0.5 1 1625 . 189 ASP HA H 4.29 0.06 1 1626 . 189 ASP CB C 41.2 0.5 1 1627 . 189 ASP HB2 H 2.51 0.06 2 1628 . 189 ASP HB3 H 2.98 0.06 2 1629 . 189 ASP C C 176.34 0.09 1 1630 . 190 SER N N 121.1 0.1 1 1631 . 190 SER H H 8.17 0.007 1 1632 . 190 SER CA C 58.6 0.5 1 1633 . 190 SER HA H 4.42 0.06 1 1634 . 190 SER CB C 64.4 0.5 1 1635 . 190 SER HB2 H 3.89 0.06 2 1636 . 190 SER HB3 H 4.06 0.06 2 1637 . 190 SER C C 175.71 0.09 1 1638 . 191 SER N N 120.8 0.1 1 1639 . 191 SER H H 8.49 0.007 1 1640 . 191 SER CA C 57.4 0.5 1 1641 . 191 SER HA H 4.50 0.06 1 1642 . 191 SER CB C 63.5 0.5 1 1643 . 191 SER HB2 H 3.89 0.06 2 1644 . 191 SER HB3 H 4.12 0.06 2 1645 . 191 SER C C 175.07 0.09 1 1646 . 192 ALA N N 131.9 0.1 1 1647 . 192 ALA H H 8.71 0.007 1 1648 . 192 ALA CA C 54.7 0.5 1 1649 . 192 ALA HA H 4.00 0.06 1 1650 . 192 ALA CB C 18.5 0.5 1 1651 . 192 ALA HB H 1.44 0.06 2 1652 . 192 ALA C C 179.01 0.09 1 1653 . 193 ALA N N 118.1 0.1 1 1654 . 193 ALA H H 7.97 0.007 1 1655 . 193 ALA CA C 54.1 0.5 1 1656 . 193 ALA HA H 4.07 0.06 1 1657 . 193 ALA CB C 19.4 0.5 1 1658 . 193 ALA HB H 1.37 0.06 2 1659 . 193 ALA C C 177.87 0.09 1 1660 . 194 THR N N 103.3 0.1 1 1661 . 194 THR H H 6.99 0.007 1 1662 . 194 THR CA C 61.2 0.5 1 1663 . 194 THR HA H 4.30 0.06 1 1664 . 194 THR CB C 69.6 0.5 1 1665 . 194 THR CG2 C 21.6 0.5 1 1666 . 194 THR C C 174.50 0.09 1 1667 . 195 LYS N N 124.4 0.1 1 1668 . 195 LYS H H 7.58 0.007 1 1669 . 195 LYS CA C 57.4 0.5 1 1670 . 195 LYS HA H 4.15 0.06 1 1671 . 195 LYS CB C 33.3 0.5 1 1672 . 195 LYS HB2 H 1.49 0.06 2 1673 . 195 LYS HB3 H 1.75 0.06 2 1674 . 195 LYS CG C 27.0 0.5 1 1675 . 195 LYS CD C 29.8 0.5 1 1676 . 195 LYS CE C 39.3 0.5 1 1677 . 195 LYS C C 176.28 0.09 1 1678 . 196 LYS N N 130.3 0.1 1 1679 . 196 LYS H H 10.28 0.007 1 1680 . 196 LYS CA C 57.0 0.5 1 1681 . 196 LYS HA H 4.83 0.06 1 1682 . 196 LYS CB C 33.9 0.5 1 1683 . 196 LYS HB2 H 1.64 0.06 2 1684 . 196 LYS HB3 H 1.87 0.06 2 1685 . 196 LYS CG C 27.1 0.5 1 1686 . 196 LYS CD C 29.0 0.5 1 1687 . 196 LYS C C 176.27 0.09 1 1688 . 197 THR N N 113.1 0.1 1 1689 . 197 THR H H 8.56 0.007 1 1690 . 197 THR CA C 60.2 0.5 1 1691 . 197 THR HA H 4.57 0.06 1 1692 . 197 THR CB C 71.9 0.5 1 1693 . 197 THR HB H 4.22 0.06 1 1694 . 197 THR CG2 C 14.8 0.5 1 1695 . 197 THR C C 172.84 0.09 1 1696 . 198 ALA N N 122.6 0.1 1 1697 . 198 ALA H H 8.83 0.007 1 1698 . 198 ALA CA C 51.2 0.5 1 1699 . 198 ALA HA H 5.62 0.06 1 1700 . 198 ALA CB C 25.7 0.5 1 1701 . 198 ALA HB H 1.38 0.06 2 1702 . 198 ALA C C 175.46 0.09 1 1703 . 199 ALA N N 123.7 0.1 1 1704 . 199 ALA H H 8.25 0.007 1 1705 . 199 ALA CA C 50.8 0.5 1 1706 . 199 ALA HA H 4.89 0.06 1 1707 . 199 ALA CB C 22.3 0.5 1 1708 . 199 ALA HB H 1.43 0.06 2 1709 . 199 ALA C C 175.53 0.09 1 1710 . 200 TRP N N 125.6 0.1 1 1711 . 200 TRP H H 8.89 0.007 1 1712 . 200 TRP CA C 55.2 0.5 1 1713 . 200 TRP HA H 5.44 0.06 1 1714 . 200 TRP CB C 32.3 0.5 1 1715 . 200 TRP HB2 H 3.23 0.06 2 1716 . 200 TRP HB3 H 3.45 0.06 2 1717 . 200 TRP C C 174.54 0.09 1 1718 . 201 ASN N N 128.5 0.1 1 1719 . 201 ASN H H 8.13 0.007 1 1720 . 201 ASN CA C 51.0 0.5 1 1721 . 201 ASN HA H 4.76 0.06 1 1722 . 201 ASN CB C 39.5 0.5 1 1723 . 201 ASN HB2 H 2.41 0.06 2 1724 . 201 ASN HB3 H 2.41 0.06 2 1725 . 201 ASN C C 174.77 0.09 1 1726 . 202 SER N N 121.3 0.1 1 1727 . 202 SER H H 8.60 0.007 1 1728 . 202 SER CA C 60.8 0.5 1 1729 . 202 SER HA H 4.06 0.06 1 1730 . 202 SER CB C 63.3 0.5 1 1731 . 202 SER HB2 H 3.78 0.06 2 1732 . 202 SER HB3 H 3.78 0.06 2 1733 . 202 SER C C 176.69 0.09 1 1734 . 203 GLY N N 110.9 0.1 1 1735 . 203 GLY H H 8.35 0.007 1 1736 . 203 GLY CA C 46.6 0.5 1 1737 . 203 GLY HA2 H 3.96 0.06 2 1738 . 203 GLY HA3 H 3.96 0.06 2 1739 . 203 GLY C C 175.45 0.09 1 1740 . 204 THR N N 108.3 0.1 1 1741 . 204 THR H H 6.99 0.007 1 1742 . 204 THR CA C 60.2 0.5 1 1743 . 204 THR HA H 4.39 0.06 1 1744 . 204 THR CB C 69.5 0.5 1 1745 . 204 THR CG2 C 20.8 0.5 1 1746 . 204 THR C C 175.63 0.09 1 1747 . 205 SER N N 122.1 0.1 1 1748 . 205 SER H H 7.56 0.007 1 1749 . 205 SER CA C 59.2 0.5 1 1750 . 205 SER HA H 4.55 0.06 1 1751 . 205 SER CB C 62.6 0.5 1 1752 . 205 SER HB2 H 3.40 0.06 2 1753 . 205 SER HB3 H 3.96 0.06 2 1754 . 205 SER C C 172.23 0.09 1 1755 . 206 THR N N 111.4 0.1 1 1756 . 206 THR H H 6.64 0.007 1 1757 . 206 THR CA C 61.7 0.5 1 1758 . 206 THR HA H 5.13 0.06 1 1759 . 206 THR CB C 71.8 0.5 1 1760 . 206 THR HB H 3.62 0.06 1 1761 . 206 THR CG2 C 18.6 0.5 1 1762 . 206 THR C C 172.72 0.09 1 1763 . 207 LEU N N 134.3 0.1 1 1764 . 207 LEU H H 10.21 0.007 1 1765 . 207 LEU CA C 53.2 0.5 1 1766 . 207 LEU HA H 5.53 0.06 1 1767 . 207 LEU CB C 45.8 0.5 1 1768 . 207 LEU CG C 27.0 0.5 1 1769 . 207 LEU CD1 C 24.5 0.5 2 1770 . 207 LEU CD2 C 24.5 0.5 2 1771 . 207 LEU C C 175.31 0.09 1 1772 . 208 THR N N 127.2 0.1 1 1773 . 208 THR H H 9.15 0.007 1 1774 . 208 THR CA C 62.6 0.5 1 1775 . 208 THR HA H 5.60 0.06 1 1776 . 208 THR CB C 71.4 0.5 1 1777 . 208 THR HB H 3.82 0.06 1 1778 . 208 THR CG2 C 20.9 0.5 1 1779 . 208 THR C C 175.40 0.09 1 1780 . 209 ILE N N 132.8 0.1 1 1781 . 209 ILE H H 9.55 0.007 1 1782 . 209 ILE CA C 61.9 0.5 1 1783 . 209 ILE HA H 4.67 0.06 1 1784 . 209 ILE CB C 39.2 0.5 1 1785 . 209 ILE HB H 1.95 0.06 1 1786 . 209 ILE CG1 C 17.2 0.5 2 1787 . 209 ILE CD1 C 13.5 0.5 1 1788 . 209 ILE CG2 C 17.2 0.5 2 1789 . 209 ILE C C 174.21 0.09 1 1790 . 210 THR N N 125.5 0.1 1 1791 . 210 THR H H 9.15 0.007 1 1792 . 210 THR CA C 61.5 0.5 1 1793 . 210 THR HA H 5.00 0.06 1 1794 . 210 THR CB C 71.5 0.5 1 1795 . 210 THR HB H 3.62 0.06 1 1796 . 210 THR CG2 C 20.3 0.5 1 1797 . 210 THR C C 173.09 0.09 1 1798 . 211 VAL N N 124.8 0.1 1 1799 . 211 VAL H H 8.61 0.007 1 1800 . 211 VAL CA C 61.8 0.5 1 1801 . 211 VAL HA H 4.29 0.06 1 1802 . 211 VAL CB C 35.4 0.5 1 1803 . 211 VAL HB H 1.81 0.06 1 1804 . 211 VAL CG1 C 20.9 0.5 2 1805 . 211 VAL CG2 C 20.9 0.5 2 1806 . 211 VAL C C 177.12 0.09 1 1807 . 212 ASN N N 132.2 0.1 1 1808 . 212 ASN H H 10.13 0.007 1 1809 . 212 ASN CA C 53.6 0.5 1 1810 . 212 ASN HA H 4.33 0.06 1 1811 . 212 ASN CB C 36.9 0.5 1 1812 . 212 ASN HB2 H 2.77 0.06 2 1813 . 212 ASN HB3 H 3.24 0.06 2 1814 . 212 ASN C C 175.08 0.09 1 1815 . 213 SER N N 107.0 0.1 1 1816 . 213 SER H H 8.65 0.007 1 1817 . 213 SER CA C 60.7 0.5 1 1818 . 213 SER HA H 4.21 0.06 1 1819 . 213 SER CB C 62.6 0.5 1 1820 . 213 SER HB2 H 3.73 0.06 2 1821 . 213 SER HB3 H 4.00 0.06 2 1822 . 213 SER C C 172.78 0.09 1 1823 . 214 LYS N N 123.5 0.1 1 1824 . 214 LYS H H 7.82 0.007 1 1825 . 214 LYS CA C 54.7 0.5 1 1826 . 214 LYS HA H 4.62 0.06 1 1827 . 214 LYS CB C 34.9 0.5 1 1828 . 214 LYS HB2 H 1.64 0.06 2 1829 . 214 LYS HB3 H 1.64 0.06 2 1830 . 214 LYS CG C 24.5 0.5 1 1831 . 214 LYS CD C 29.2 0.5 1 1832 . 214 LYS CE C 42.4 0.5 1 1833 . 214 LYS C C 174.92 0.09 1 1834 . 215 LYS N N 126.8 0.1 1 1835 . 215 LYS H H 8.20 0.007 1 1836 . 215 LYS CA C 57.8 0.5 1 1837 . 215 LYS HA H 4.17 0.06 1 1838 . 215 LYS CB C 30.7 0.5 1 1839 . 215 LYS CD C 29.3 0.5 1 1840 . 215 LYS CE C 42.0 0.5 1 1841 . 215 LYS C C 176.71 0.09 1 1842 . 216 THR N N 113.1 0.1 1 1843 . 216 THR H H 9.17 0.007 1 1844 . 216 THR CA C 62.8 0.5 1 1845 . 216 THR HA H 4.71 0.06 1 1846 . 216 THR CB C 69.3 0.5 1 1847 . 216 THR HB H 4.17 0.06 1 1848 . 216 THR CG2 C 22.3 0.5 1 1849 . 216 THR C C 176.88 0.09 1 1850 . 217 LYS N N 121.3 0.1 1 1851 . 217 LYS H H 7.57 0.007 1 1852 . 217 LYS CA C 56.0 0.5 1 1853 . 217 LYS HA H 5.46 0.06 1 1854 . 217 LYS CB C 36.7 0.5 1 1855 . 217 LYS HB2 H 1.65 0.06 2 1856 . 217 LYS HB3 H 2.03 0.06 2 1857 . 217 LYS CG C 24.3 0.5 1 1858 . 217 LYS CD C 29.2 0.5 1 1859 . 217 LYS CE C 42.3 0.5 1 1860 . 217 LYS C C 173.47 0.09 1 1861 . 218 ASP N N 121.8 0.1 1 1862 . 218 ASP H H 8.95 0.007 1 1863 . 218 ASP CA C 53.2 0.5 1 1864 . 218 ASP HA H 5.85 0.06 1 1865 . 218 ASP CB C 43.4 0.5 1 1866 . 218 ASP HB2 H 2.21 0.06 2 1867 . 218 ASP HB3 H 2.38 0.06 2 1868 . 218 ASP C C 176.42 0.09 1 1869 . 219 LEU N N 126.3 0.1 1 1870 . 219 LEU H H 9.61 0.007 1 1871 . 219 LEU CA C 54.0 0.5 1 1872 . 219 LEU HA H 5.63 0.06 1 1873 . 219 LEU CB C 44.6 0.5 1 1874 . 219 LEU HB2 H 1.53 0.06 2 1875 . 219 LEU HB3 H 2.03 0.06 2 1876 . 219 LEU CG C 28.9 0.5 1 1877 . 219 LEU CD1 C 25.3 0.5 2 1878 . 219 LEU CD2 C 25.3 0.5 2 1879 . 219 LEU C C 175.16 0.09 1 1880 . 220 VAL N N 126.3 0.1 1 1881 . 220 VAL H H 8.69 0.007 1 1882 . 220 VAL CA C 61.7 0.5 1 1883 . 220 VAL HA H 4.72 0.06 1 1884 . 220 VAL CB C 32.1 0.5 1 1885 . 220 VAL HB H 2.23 0.06 1 1886 . 220 VAL CG1 C 20.9 0.5 2 1887 . 220 VAL CG2 C 20.9 0.5 2 1888 . 220 VAL C C 174.75 0.09 1 1889 . 221 PHE N N 129.2 0.1 1 1890 . 221 PHE H H 8.71 0.007 1 1891 . 221 PHE CA C 56.8 0.5 1 1892 . 221 PHE HA H 4.91 0.06 1 1893 . 221 PHE CB C 38.1 0.5 1 1894 . 221 PHE HB2 H 3.29 0.06 2 1895 . 221 PHE HB3 H 3.18 0.06 2 1896 . 221 PHE C C 176.69 0.09 1 1897 . 222 THR N N 114.7 0.1 1 1898 . 222 THR H H 8.53 0.007 1 1899 . 222 THR CA C 62.0 0.5 1 1900 . 222 THR HA H 4.66 0.06 1 1901 . 222 THR CB C 71.4 0.5 1 1902 . 222 THR HB H 4.36 0.06 1 1903 . 222 THR CG2 C 18.5 0.5 1 1904 . 222 THR C C 177.57 0.09 1 1905 . 223 LYS N N 121.8 0.1 1 1906 . 223 LYS H H 8.90 0.007 1 1907 . 223 LYS CA C 57.7 0.5 1 1908 . 223 LYS HA H 4.29 0.06 1 1909 . 223 LYS CB C 31.7 0.5 1 1910 . 223 LYS HB2 H 1.93 0.06 2 1911 . 223 LYS HB3 H 1.93 0.06 2 1912 . 223 LYS CG C 24.8 0.5 1 1913 . 223 LYS CD C 28.9 0.5 1 1914 . 223 LYS CE C 42.4 0.5 1 1915 . 223 LYS C C 176.91 0.09 1 1916 . 224 GLU N N 118.4 0.1 1 1917 . 224 GLU H H 7.58 0.007 1 1918 . 224 GLU CA C 56.3 0.5 1 1919 . 224 GLU HA H 4.48 0.06 1 1920 . 224 GLU CB C 28.4 0.5 1 1921 . 224 GLU HB2 H 1.91 0.06 2 1922 . 224 GLU HB3 H 2.24 0.06 2 1923 . 224 GLU CG C 36.8 0.5 1 1924 . 224 GLU C C 174.15 0.09 1 1925 . 225 ASN N N 112.3 0.1 1 1926 . 225 ASN H H 7.78 0.007 1 1927 . 225 ASN CA C 55.7 0.5 1 1928 . 225 ASN HA H 4.43 0.06 1 1929 . 225 ASN CB C 36.6 0.5 1 1930 . 225 ASN HB2 H 2.62 0.06 2 1931 . 225 ASN HB3 H 3.11 0.06 2 1932 . 225 ASN C C 174.20 0.09 1 1933 . 226 THR N N 108.3 0.1 1 1934 . 226 THR H H 7.33 0.007 1 1935 . 226 THR CA C 58.9 0.5 1 1936 . 226 THR HA H 4.65 0.06 1 1937 . 226 THR CB C 72.4 0.5 1 1938 . 226 THR HB H 4.32 0.06 1 1939 . 226 THR C C 173.24 0.09 1 1940 . 227 ILE N N 122.4 0.1 1 1941 . 227 ILE H H 8.40 0.007 1 1942 . 227 ILE CA C 59.8 0.5 1 1943 . 227 ILE HA H 5.26 0.06 1 1944 . 227 ILE CB C 41.3 0.5 1 1945 . 227 ILE HB H 1.19 0.06 1 1946 . 227 ILE CG1 C 27.1 0.5 2 1947 . 227 ILE CD1 C 17.1 0.5 1 1948 . 227 ILE C C 175.91 0.09 1 1949 . 228 THR N N 117.3 0.1 1 1950 . 228 THR H H 8.97 0.007 1 1951 . 228 THR CA C 58.9 0.5 1 1952 . 228 THR HA H 5.42 0.06 1 1953 . 228 THR CB C 71.5 0.5 1 1954 . 228 THR HB H 5.21 0.06 1 1955 . 228 THR CG2 C 18.0 0.5 1 1956 . 228 THR C C 173.22 0.09 1 1957 . 229 VAL N N 120.9 0.1 1 1958 . 229 VAL H H 9.03 0.007 1 1959 . 229 VAL CA C 59.5 0.5 1 1960 . 229 VAL HA H 5.31 0.06 1 1961 . 229 VAL CB C 35.6 0.5 1 1962 . 229 VAL HB H 1.81 0.06 1 1963 . 229 VAL CG1 C 19.5 0.5 2 1964 . 229 VAL CG2 C 19.5 0.5 2 1965 . 229 VAL C C 173.84 0.09 1 1966 . 230 GLN N N 129.0 0.1 1 1967 . 230 GLN H H 8.47 0.007 1 1968 . 230 GLN CA C 55.6 0.5 1 1969 . 230 GLN HA H 4.61 0.06 1 1970 . 230 GLN CB C 31.6 0.5 1 1971 . 230 GLN HB2 H 1.77 0.06 2 1972 . 230 GLN HB3 H 1.77 0.06 2 1973 . 230 GLN CG C 33.5 0.5 1 1974 . 230 GLN C C 173.49 0.09 1 1975 . 231 GLN N N 125.8 0.1 1 1976 . 231 GLN H H 8.78 0.007 1 1977 . 231 GLN CA C 55.4 0.5 1 1978 . 231 GLN HA H 4.94 0.06 1 1979 . 231 GLN CB C 31.1 0.5 1 1980 . 231 GLN HB2 H 2.14 0.06 2 1981 . 231 GLN HB3 H 2.40 0.06 2 1982 . 231 GLN CG C 34.6 0.5 1 1983 . 231 GLN C C 175.25 0.09 1 1984 . 232 TYR N N 120.0 0.1 1 1985 . 232 TYR H H 7.57 0.007 1 1986 . 232 TYR CA C 58.3 0.5 1 1987 . 232 TYR HA H 4.88 0.06 1 1988 . 232 TYR CB C 41.5 0.5 1 1989 . 232 TYR HB2 H 2.81 0.06 2 1990 . 232 TYR HB3 H 2.81 0.06 2 1991 . 233 ASP N N 119.2 0.1 1 1992 . 233 ASP H H 8.86 0.007 1 1993 . 233 ASP CA C 53.6 0.5 1 1994 . 233 ASP HA H 4.60 0.06 1 1995 . 233 ASP CB C 41.4 0.5 1 1996 . 233 ASP C C 177.41 0.09 1 1997 . 234 SER N N 116.8 0.1 1 1998 . 234 SER H H 8.73 0.007 1 1999 . 234 SER CA C 61.6 0.5 1 2000 . 234 SER HA H 4.16 0.06 1 2001 . 234 SER CB C 63.1 0.5 1 2002 . 234 SER HB2 H 3.96 0.06 2 2003 . 234 SER HB3 H 3.96 0.06 2 2004 . 234 SER C C 175.09 0.09 1 2005 . 235 ASN N N 117.6 0.1 1 2006 . 235 ASN H H 7.91 0.007 1 2007 . 235 ASN CA C 53.4 0.5 1 2008 . 235 ASN HA H 4.83 0.06 1 2009 . 235 ASN CB C 39.5 0.5 1 2010 . 235 ASN HB2 H 2.90 0.06 2 2011 . 235 ASN HB3 H 2.90 0.06 2 2012 . 235 ASN C C 175.89 0.09 1 2013 . 236 GLY N N 111.3 0.1 1 2014 . 236 GLY H H 8.39 0.007 1 2015 . 236 GLY CA C 46.8 0.5 1 2016 . 236 GLY HA2 H 4.03 0.06 2 2017 . 236 GLY HA3 H 4.03 0.06 2 2018 . 236 GLY C C 174.82 0.09 1 2019 . 237 THR N N 114.7 0.1 1 2020 . 237 THR H H 9.34 0.007 1 2021 . 237 THR CA C 63.4 0.5 1 2022 . 237 THR HA H 4.48 0.06 1 2023 . 237 THR CB C 70.2 0.5 1 2024 . 237 THR HB H 4.33 0.06 1 2025 . 237 THR CG2 C 21.3 0.5 1 2026 . 237 THR C C 174.64 0.09 1 2027 . 238 LYS N N 123.4 0.1 1 2028 . 238 LYS H H 8.39 0.007 1 2029 . 238 LYS CA C 55.0 0.5 1 2030 . 238 LYS HA H 4.66 0.06 1 2031 . 238 LYS CB C 35.2 0.5 1 2032 . 238 LYS HB2 H 1.77 0.06 2 2033 . 238 LYS HB3 H 1.77 0.06 2 2034 . 238 LYS CG C 23.6 0.5 1 2035 . 238 LYS CD C 29.2 0.5 1 2036 . 238 LYS CE C 42.2 0.5 1 2037 . 238 LYS C C 174.44 0.09 1 2038 . 239 LEU N N 124.2 0.1 1 2039 . 239 LEU H H 8.05 0.007 1 2040 . 239 LEU CA C 55.2 0.5 1 2041 . 239 LEU HA H 3.90 0.06 1 2042 . 239 LEU CB C 42.7 0.5 1 2043 . 239 LEU HB2 H 1.35 0.06 2 2044 . 239 LEU HB3 H 1.35 0.06 2 2045 . 239 LEU CG C 27.0 0.5 1 2046 . 239 LEU CD1 C 25.5 0.5 2 2047 . 239 LEU CD2 C 25.5 0.5 2 2048 . 239 LEU C C 177.05 0.09 1 2049 . 240 GLU N N 122.9 0.1 1 2050 . 240 GLU H H 8.62 0.007 1 2051 . 240 GLU CA C 54.7 0.5 1 2052 . 240 GLU HA H 4.61 0.06 1 2053 . 240 GLU CB C 33.1 0.5 1 2054 . 240 GLU HB2 H 1.76 0.06 2 2055 . 240 GLU HB3 H 1.87 0.06 2 2056 . 240 GLU CG C 35.9 0.5 1 2057 . 240 GLU HG2 H 2.09 0.06 2 2058 . 240 GLU HG3 H 2.09 0.06 2 2059 . 240 GLU C C 177.71 0.09 1 2060 . 241 GLY N N 113.0 0.1 1 2061 . 241 GLY H H 8.69 0.007 1 2062 . 241 GLY CA C 46.5 0.5 1 2063 . 241 GLY HA2 H 3.79 0.06 2 2064 . 241 GLY HA3 H 3.96 0.06 2 2065 . 241 GLY C C 173.60 0.09 1 2066 . 242 SER N N 118.6 0.1 1 2067 . 242 SER H H 8.12 0.007 1 2068 . 242 SER CA C 57.0 0.5 1 2069 . 242 SER HA H 4.70 0.06 1 2070 . 242 SER CB C 65.5 0.5 1 2071 . 242 SER HB2 H 3.66 0.06 2 2072 . 242 SER HB3 H 3.81 0.06 2 2073 . 242 SER C C 173.14 0.09 1 2074 . 243 ALA N N 126.9 0.1 1 2075 . 243 ALA H H 8.44 0.007 1 2076 . 243 ALA CA C 52.3 0.5 1 2077 . 243 ALA HA H 4.43 0.06 1 2078 . 243 ALA CB C 18.7 0.5 1 2079 . 243 ALA HB H 1.21 0.06 1 2080 . 243 ALA C C 177.42 0.09 1 2081 . 244 VAL N N 123.7 0.1 1 2082 . 244 VAL H H 8.64 0.007 1 2083 . 244 VAL CA C 61.1 0.5 1 2084 . 244 VAL HA H 4.32 0.06 1 2085 . 244 VAL CB C 34.9 0.5 1 2086 . 244 VAL HB H 2.00 0.06 1 2087 . 244 VAL CG1 C 20.7 0.5 2 2088 . 244 VAL CG2 C 20.7 0.5 2 2089 . 244 VAL C C 175.10 0.09 1 2090 . 245 GLU N N 127.9 0.1 1 2091 . 245 GLU H H 8.54 0.007 1 2092 . 245 GLU CA C 56.8 0.5 1 2093 . 245 GLU HA H 4.40 0.06 1 2094 . 245 GLU CB C 31.0 0.5 1 2095 . 245 GLU HB2 H 1.51 0.06 2 2096 . 245 GLU HB3 H 1.94 0.06 2 2097 . 245 GLU CG C 36.7 0.5 1 2098 . 245 GLU C C 176.29 0.09 1 2099 . 246 ILE N N 129.3 0.1 1 2100 . 246 ILE H H 8.86 0.007 1 2101 . 246 ILE CA C 61.2 0.5 1 2102 . 246 ILE HA H 4.06 0.06 1 2103 . 246 ILE CB C 37.5 0.5 1 2104 . 246 ILE HB H 1.86 0.06 1 2105 . 246 ILE CG2 C 18.0 0.5 2 2106 . 246 ILE C C 177.12 0.09 1 2107 . 247 THR N N 118.4 0.1 1 2108 . 247 THR H H 9.37 0.007 1 2109 . 247 THR CA C 61.7 0.5 1 2110 . 247 THR HA H 4.86 0.06 1 2111 . 247 THR CB C 71.2 0.5 1 2112 . 247 THR HB H 4.50 0.06 1 2113 . 247 THR CG2 C 21.0 0.5 1 2114 . 247 THR C C 173.25 0.09 1 2115 . 248 LYS N N 118.1 0.1 1 2116 . 248 LYS H H 7.27 0.007 1 2117 . 248 LYS CA C 54.6 0.5 1 2118 . 248 LYS HA H 4.74 0.06 1 2119 . 248 LYS CB C 36.1 0.5 1 2120 . 248 LYS HB2 H 1.69 0.06 2 2121 . 248 LYS HB3 H 2.12 0.06 2 2122 . 248 LYS CG C 23.8 0.5 1 2123 . 248 LYS CD C 29.2 0.5 1 2124 . 248 LYS CE C 42.0 0.5 1 2125 . 248 LYS C C 176.43 0.09 1 2126 . 249 LEU N N 126.0 0.1 1 2127 . 249 LEU H H 8.93 0.007 1 2128 . 249 LEU CA C 58.0 0.5 1 2129 . 249 LEU HA H 3.61 0.06 1 2130 . 249 LEU CB C 42.0 0.5 1 2131 . 249 LEU HB2 H 1.75 0.06 2 2132 . 249 LEU HB3 H 1.90 0.06 2 2133 . 249 LEU CG C 25.7 0.5 1 2134 . 249 LEU CD1 C 27.5 0.5 2 2135 . 249 LEU CD2 C 23.7 0.5 2 2136 . 249 LEU C C 179.43 0.09 1 2137 . 250 ASP N N 116.3 0.1 1 2138 . 250 ASP H H 8.80 0.007 1 2139 . 250 ASP CA C 57.2 0.5 1 2140 . 250 ASP HA H 4.21 0.06 1 2141 . 250 ASP CB C 40.5 0.5 1 2142 . 250 ASP HB2 H 2.40 0.06 2 2143 . 250 ASP HB3 H 2.69 0.06 2 2144 . 250 ASP C C 178.07 0.09 1 2145 . 251 GLU N N 117.0 0.1 1 2146 . 251 GLU H H 7.22 0.007 1 2147 . 251 GLU CA C 58.5 0.5 1 2148 . 251 GLU HA H 4.11 0.06 1 2149 . 251 GLU CB C 30.8 0.5 1 2150 . 251 GLU HB2 H 1.99 0.06 2 2151 . 251 GLU HB3 H 1.99 0.06 2 2152 . 251 GLU CG C 37.2 0.5 1 2153 . 251 GLU C C 179.62 0.09 1 2154 . 252 ILE N N 121.2 0.1 1 2155 . 252 ILE H H 7.32 0.007 1 2156 . 252 ILE CA C 64.8 0.5 1 2157 . 252 ILE HA H 3.67 0.06 1 2158 . 252 ILE CB C 37.7 0.5 1 2159 . 252 ILE HB H 1.86 0.06 1 2160 . 252 ILE CG1 C 29.7 0.5 2 2161 . 252 ILE CD1 C 17.3 0.5 1 2162 . 252 ILE C C 176.96 0.09 1 2163 . 253 LYS N N 118.9 0.1 1 2164 . 253 LYS H H 7.42 0.007 1 2165 . 253 LYS CA C 61.2 0.5 1 2166 . 253 LYS HA H 3.57 0.06 1 2167 . 253 LYS CB C 31.6 0.5 1 2168 . 253 LYS HB2 H 1.91 0.06 2 2169 . 253 LYS HB3 H 1.91 0.06 2 2170 . 253 LYS CG C 27.0 0.5 1 2171 . 253 LYS CD C 29.5 0.5 1 2172 . 253 LYS CE C 45.7 0.5 1 2173 . 253 LYS C C 178.94 0.09 1 2174 . 254 ASN N N 115.6 0.1 1 2175 . 254 ASN H H 8.02 0.007 1 2176 . 254 ASN CA C 55.8 0.5 1 2177 . 254 ASN HA H 4.27 0.06 1 2178 . 254 ASN CB C 38.3 0.5 1 2179 . 254 ASN HB2 H 2.77 0.06 2 2180 . 254 ASN HB3 H 2.77 0.06 2 2181 . 254 ASN C C 177.65 0.09 1 2182 . 255 ALA N N 122.1 0.1 1 2183 . 255 ALA H H 7.38 0.007 1 2184 . 255 ALA CA C 53.8 0.5 1 2185 . 255 ALA HA H 4.18 0.06 1 2186 . 255 ALA CB C 17.6 0.5 1 2187 . 255 ALA HB H 2.06 0.06 1 2188 . 255 ALA C C 177.19 0.09 1 2189 . 256 LEU N N 117.3 0.1 1 2190 . 256 LEU H H 7.30 0.007 1 2191 . 256 LEU CA C 54.2 0.5 1 2192 . 256 LEU HA H 4.17 0.06 1 2193 . 256 LEU CB C 41.6 0.5 1 2194 . 256 LEU HB2 H 1.64 0.06 2 2195 . 256 LEU HB3 H 1.86 0.06 2 2196 . 256 LEU CG C 25.6 0.5 1 2197 . 256 LEU CD1 C 21.4 0.5 2 2198 . 256 LEU CD2 C 21.4 0.5 2 2199 . 256 LEU C C 175.65 0.09 1 2200 . 257 LYS N N 124.5 0.1 1 2201 . 257 LYS H H 6.88 0.007 1 2202 . 257 LYS CA C 59.1 0.5 1 2203 . 257 LYS CB C 33.8 0.5 1 stop_ save_