data_4367 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of a Borrelia OspA mutant containing an extended single-layer beta-sheet ; _BMRB_accession_number 4367 _BMRB_flat_file_name bmr4367.str _Entry_type original _Submission_date 1999-07-14 _Accession_date 1999-07-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; This protein is a variant of OspA (wild-type accession number 4076) which contains a 23-residue insertion between residue 118 and 119. The insertion duplicates a beta-hairpin within the unique single-layer beta sheet of OspA. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Xiaolin . . 2 Link Karl . . 3 Koide Akiko . . 4 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" 277 "13C chemical shifts" 813 "15N chemical shifts" 277 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-23 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4076 'wild-type assignments' stop_ _Original_release_date 1999-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Design of single-layer beta-sheets without a hydrophobic core ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20129263 _PubMed_ID 10667801 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koide Shohei . . 2 Huang Xiaolin . . 3 Link Karl . . 4 Koide Akiko . . 5 Bu Zimei . . 6 Engelman Donald M. . stop_ _Journal_abbreviation Nature _Journal_volume 403 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 456 _Page_last 460 _Year 2000 _Details . loop_ _Keyword 'beta-sheet protein' design 'outer surface protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Pham, T. N. & Koide, S. (1998) NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer b-sheet. J. Biomol. NMR 11, 407-414. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pham T. . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_citation_2 _Saveframe_category citation _Citation_full ; Pham, T.-N., Koide, A. & Koide, S. (1998) A stable single-layer b-sheet without a hydrophobic core. Nat. Struct. Biol. 5, 115-119. ; _Citation_title ; A stable single-layer beta-sheet without a hydrophobic core. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9461076 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pham 'T N' N. . 2 Koide A . . 3 Koide S . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature structural biology' _Journal_volume 5 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 115 _Page_last 119 _Year 1998 _Details ; Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We show that the single-layer beta-sheet segment is surprisingly stable (deltaG for hydrogen exchange is approximately 8 kcal mol(-1) at 45 degrees C). Possible factors contributing to the stability of the single-layer beta-sheet are discussed based on an analysis of the crystal structure. ; save_ save_citation_3 _Saveframe_category citation _Citation_full ; Koide, S., Bu, Z., Risal,D., Pham, T.-N., Nakagawa, T., Tamura, A. & Engelman, D. M. (1999) Multi-step denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer b-sheet. Biochemistry 38, 4757-4767 ; _Citation_title ; Multistep denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer beta-sheet. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10200164 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koide S . . 2 Bu Z . . 3 Risal D . . 4 Pham 'T N' N. . 5 Nakagawa T . . 6 Tamura A . . 7 Engelman 'D M' M. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue 15 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 4757 _Page_last 4767 _Year 1999 _Details ; Outer surface protein A (OspA) from the Lyme disease spirochete, Borrelia burgdorferi, is a dumbbell-shaped protein in which two globular domains are connected by a three-stranded beta-sheet segment that is solvent-exposed on both faces. Previous studies showed that the whole protein, including the single-layer beta-sheet, is highly rigid. To elucidate the folding mechanism and the role of the central beta-sheet in the formation of the rigid molecule, we investigated the equilibrium thermal denaturation reaction of OspA. We applied differential scanning calorimetry, heteronuclear NMR spectroscopy, and solution small-angle X-ray scattering (SAXS) to characterize the reaction in detail. All three techniques revealed that OspA denatures in two separable cooperative transitions. NMR measurements on OspA specifically 15N-labeled at Lys residues identified the locations of the two folding units and revealed that the C-terminal segment is less stable than the remaining N-terminal segment. The boundary between the two folding units is located within the central beta-sheet. The interconversion among the three folding states (fully folded, C-terminus unfolded, and fully denatured) is slow relative to chemical shift differences (<24 Hz), indicating that there are significant kinetic barriers in the denaturation reactions. SAXS measurements determined the radius of gyration of the native protein to be 25.0 +/- 0.3 A, which increases to 34.4 +/- 1.0 A in the first transition, and then to 56.1 +/- 1.6 A in the second transition. Thus, the intermediate state, in which the C-terminal folding unit is already denatured, is still compact. These results provide a basis for elucidating the folding mechanism of OspA. ; save_ ################################## # Molecular system description # ################################## save_system_abbreviation _Saveframe_category molecular_system _Mol_system_name OspA+1bh _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OspA+1bh $OspA+1bh stop_ _System_molecular_weight 30260 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; Borrelia burgdorferi outer surface protein A mutant containing an extended single-layer beta-sheet. The monomeric state of the protein has been confirmed with solution by small angle X-ray scattering. ; save_ ######################## # Monomeric polymers # ######################## save_OspA+1bh _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'OspA mutant' _Abbreviation_common 'OspA mutant' _Molecular_mass 30260 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 280 _Mol_residue_sequence ; AKQNVSSLDEKNSVSVDLPG EMKVLVSKEKNKDGKYDLIA TVDKLELKGTSDKNNGSGVL EGVKADKSKVKLTISDDLGQ TTLEVFKEDGKTLVSKKVTS KDKSSTEEKFNEKGELSEKK ITRADKSSTEEKFNEKGEVS EKIITRADGTRLEYTGIKSD GSGKAKEVLKGYVLEGTLTA EKTTLVVKEGTVTLSKNISK SGEVSVELNDTDSSAATKKT AAWNSGTSTLTITVNSKKTK DLVFTKENTITVQQYDSNGT KLEGSAVEITKLDEIKNALK ; 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 LEU 117 133 SER 118 134 GLU 119 135 LYS 120 136 LYS 121 137 ILE 122 138 THR 123 139 ARG 124 140 ALA 125 141 ASP 126 119 LYS 127 120 SER 128 121 SER 129 122 THR 130 123 GLU 131 124 GLU 132 125 LYS 133 126 PHE 134 127 ASN 135 128 GLU 136 129 LYS 137 130 GLY 138 131 GLU 139 132 VAL 140 133 SER 141 134 GLU 142 135 LYS 143 136 ILE 144 137 ILE 145 138 THR 146 139 ARG 147 140 ALA 148 141 ASP 149 142 GLY 150 143 THR 151 144 ARG 152 145 LEU 153 146 GLU 154 147 TYR 155 148 THR 156 149 GLY 157 150 ILE 158 151 LYS 159 152 SER 160 153 ASP 161 154 GLY 162 155 SER 163 156 GLY 164 157 LYS 165 158 ALA 166 159 LYS 167 160 GLU 168 161 VAL 169 162 LEU 170 163 LYS 171 164 GLY 172 165 TYR 173 166 VAL 174 167 LEU 175 168 GLU 176 169 GLY 177 170 THR 178 171 LEU 179 172 THR 180 173 ALA 181 174 GLU 182 175 LYS 183 176 THR 184 177 THR 185 178 LEU 186 179 VAL 187 180 VAL 188 181 LYS 189 182 GLU 190 183 GLY 191 184 THR 192 185 VAL 193 186 THR 194 187 LEU 195 188 SER 196 189 LYS 197 190 ASN 198 191 ILE 199 192 SER 200 193 LYS 201 194 SER 202 195 GLY 203 196 GLU 204 197 VAL 205 198 SER 206 199 VAL 207 200 GLU 208 201 LEU 209 202 ASN 210 203 ASP 211 204 THR 212 205 ASP 213 206 SER 214 207 SER 215 208 ALA 216 209 ALA 217 210 THR 218 211 LYS 219 212 LYS 220 213 THR 221 214 ALA 222 215 ALA 223 216 TRP 224 217 ASN 225 218 SER 226 219 GLY 227 220 THR 228 221 SER 229 222 THR 230 223 LEU 231 224 THR 232 225 ILE 233 226 THR 234 227 VAL 235 228 ASN 236 229 SER 237 230 LYS 238 231 LYS 239 232 THR 240 233 LYS 241 234 ASP 242 235 LEU 243 236 VAL 244 237 PHE 245 238 THR 246 239 LYS 247 240 GLU 248 241 ASN 249 242 THR 250 243 ILE 251 244 THR 252 245 VAL 253 246 GLN 254 247 GLN 255 248 TYR 256 249 ASP 257 250 SER 258 251 ASN 259 252 GLY 260 253 THR 261 254 LYS 262 255 LEU 263 256 GLU 264 257 GLY 265 258 SER 266 259 ALA 267 260 VAL 268 261 GLU 269 262 ILE 270 263 THR 271 264 LYS 272 265 LEU 273 266 ASP 274 267 GLU 275 268 ILE 276 269 LYS 277 270 ASN 278 271 ALA 279 272 LEU 280 273 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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+1bh 'Lyme disease spirochete' 139 . . 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 _Vendor_name _Details $OspA+1bh 'recombinant technology' 'E. coli' . . BL21(DE3) plasmid pET24a Novagen 'natural gene containing a synthetic segment' 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+1bh 1.5 mM '[U-13C; U-15N]' 'sodium phosphate' 10 mM . 'sodium chloride' 50 mM . EDTA 0.05 mM . stop_ save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 na temperature 318 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_set_1 _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 protons' ppm 0 external indirect . . . 0.25144954 DSS H 1 'methyl protons' ppm 0 external direct . 'external to the sample' . . NH3 N 15 nitrogen ppm 0 external indirect . . . 0.101329 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_label _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_set_1 _Chem_shift_reference_set_label $chemical_shift_reference_set_1 _Mol_system_component_name OspA+1bh _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 CB C 33.2 0.5 1 3 . 2 LYS C C 176.11 0.09 1 4 . 3 GLN N N 122.9 0.1 1 5 . 3 GLN H H 8.40 0.010 1 6 . 3 GLN CA C 55.8 0.5 1 7 . 3 GLN CB C 29.9 0.5 1 8 . 3 GLN C C 175.44 0.09 1 9 . 4 ASN N N 121.6 0.1 1 10 . 4 ASN H H 8.48 0.010 1 11 . 4 ASN CA C 53.4 0.5 1 12 . 4 ASN CB C 39.0 0.5 1 13 . 4 ASN C C 174.93 0.09 1 14 . 5 VAL N N 120.9 0.1 1 15 . 5 VAL H H 8.04 0.010 1 16 . 5 VAL CA C 62.3 0.5 1 17 . 5 VAL CB C 33.0 0.5 1 18 . 5 VAL C C 175.91 0.09 1 19 . 6 SER N N 120.4 0.1 1 20 . 6 SER H H 8.34 0.010 1 21 . 6 SER CA C 58.2 0.5 1 22 . 6 SER CB C 64.1 0.5 1 23 . 6 SER C C 174.42 0.09 1 24 . 7 SER N N 119.1 0.1 1 25 . 7 SER H H 8.27 0.010 1 26 . 7 SER CA C 58.6 0.5 1 27 . 7 SER CB C 63.8 0.5 1 28 . 7 SER C C 174.21 0.09 1 29 . 8 LEU N N 124.1 0.1 1 30 . 8 LEU H H 7.91 0.010 1 31 . 8 LEU CA C 54.9 0.5 1 32 . 8 LEU CB C 42.5 0.5 1 33 . 8 LEU C C 176.20 0.09 1 34 . 9 ASP N N 123.2 0.1 1 35 . 9 ASP H H 8.71 0.010 1 36 . 9 ASP CA C 53.5 0.5 1 37 . 9 ASP CB C 41.8 0.5 1 38 . 9 ASP C C 176.81 0.09 1 39 . 10 GLU N N 120.9 0.1 1 40 . 10 GLU H H 8.63 0.010 1 41 . 10 GLU CA C 58.1 0.5 1 42 . 10 GLU CB C 29.5 0.5 1 43 . 10 GLU C C 177.14 0.09 1 44 . 11 LYS N N 119.8 0.1 1 45 . 11 LYS H H 8.34 0.010 1 46 . 11 LYS CA C 57.3 0.5 1 47 . 11 LYS CB C 32.5 0.5 1 48 . 11 LYS C C 177.62 0.09 1 49 . 12 ASN N N 118.5 0.1 1 50 . 12 ASN H H 8.06 0.010 1 51 . 12 ASN CA C 52.6 0.5 1 52 . 12 ASN CB C 39.3 0.5 1 53 . 12 ASN C C 175.02 0.09 1 54 . 13 SER N N 115.3 0.1 1 55 . 13 SER H H 7.76 0.010 1 56 . 13 SER CA C 58.0 0.5 1 57 . 13 SER CB C 67.3 0.5 1 58 . 13 SER C C 172.16 0.09 1 59 . 14 VAL N N 120.9 0.1 1 60 . 14 VAL H H 9.04 0.010 1 61 . 14 VAL CA C 61.0 0.5 1 62 . 14 VAL CB C 34.5 0.5 1 63 . 14 VAL C C 174.51 0.09 1 64 . 15 SER N N 120.0 0.1 1 65 . 15 SER H H 8.23 0.010 1 66 . 15 SER CA C 57.2 0.5 1 67 . 15 SER CB C 64.3 0.5 1 68 . 15 SER C C 174.44 0.09 1 69 . 16 VAL N N 130.3 0.1 1 70 . 16 VAL H H 9.30 0.010 1 71 . 16 VAL CA C 62.3 0.5 1 72 . 16 VAL CB C 34.4 0.5 1 73 . 16 VAL C C 174.95 0.09 1 74 . 17 ASP N N 127.4 0.1 1 75 . 17 ASP H H 8.20 0.010 1 76 . 17 ASP CA C 55.2 0.5 1 77 . 17 ASP CB C 42.1 0.5 1 78 . 17 ASP C C 175.40 0.09 1 79 . 18 LEU N N 123.1 0.1 1 80 . 18 LEU H H 8.32 0.010 1 81 . 18 LEU CA C 51.8 0.5 1 82 . 18 LEU CB C 44.2 0.5 1 83 . 19 PRO CA C 63.5 0.5 1 84 . 19 PRO CB C 32.0 0.5 1 85 . 19 PRO C C 176.13 0.09 1 86 . 20 GLY N N 111.4 0.1 1 87 . 20 GLY H H 8.70 0.010 1 88 . 20 GLY CA C 45.5 0.5 1 89 . 20 GLY C C 174.34 0.09 1 90 . 21 GLU N N 115.7 0.1 1 91 . 21 GLU H H 8.30 0.010 1 92 . 21 GLU CA C 57.2 0.5 1 93 . 21 GLU CB C 26.7 0.5 1 94 . 21 GLU C C 175.29 0.09 1 95 . 22 MET N N 117.5 0.1 1 96 . 22 MET H H 6.79 0.010 1 97 . 22 MET CA C 54.3 0.5 1 98 . 22 MET CB C 36.5 0.5 1 99 . 22 MET C C 174.18 0.09 1 100 . 23 LYS N N 122.1 0.1 1 101 . 23 LYS H H 8.11 0.010 1 102 . 23 LYS CA C 55.0 0.5 1 103 . 23 LYS CB C 36.1 0.5 1 104 . 23 LYS C C 174.84 0.09 1 105 . 24 VAL N N 123.0 0.1 1 106 . 24 VAL H H 8.72 0.010 1 107 . 24 VAL CA C 59.0 0.5 1 108 . 24 VAL CB C 35.7 0.5 1 109 . 24 VAL C C 171.97 0.09 1 110 . 25 LEU N N 128.5 0.1 1 111 . 25 LEU H H 9.12 0.010 1 112 . 25 LEU CA C 53.7 0.5 1 113 . 25 LEU CB C 42.8 0.5 1 114 . 25 LEU C C 175.81 0.09 1 115 . 26 VAL N N 123.2 0.1 1 116 . 26 VAL H H 8.87 0.010 1 117 . 26 VAL CA C 59.3 0.5 1 118 . 26 VAL CB C 34.3 0.5 1 119 . 26 VAL C C 176.35 0.09 1 120 . 27 SER N N 124.3 0.1 1 121 . 27 SER H H 9.06 0.010 1 122 . 27 SER CA C 59.6 0.5 1 123 . 27 SER CB C 64.2 0.5 1 124 . 27 SER C C 173.90 0.09 1 125 . 28 LYS N N 121.4 0.1 1 126 . 28 LYS H H 8.16 0.010 1 127 . 28 LYS CA C 59.0 0.5 1 128 . 28 LYS CB C 33.7 0.5 1 129 . 28 LYS C C 177.33 0.09 1 130 . 29 GLU N N 116.3 0.1 1 131 . 29 GLU H H 8.10 0.010 1 132 . 29 GLU CA C 53.8 0.5 1 133 . 29 GLU CB C 32.6 0.5 1 134 . 29 GLU C C 176.59 0.09 1 135 . 30 LYS N N 124.0 0.1 1 136 . 30 LYS H H 8.47 0.010 1 137 . 30 LYS CA C 56.4 0.5 1 138 . 30 LYS CB C 34.2 0.5 1 139 . 30 LYS C C 176.66 0.09 1 140 . 31 ASN N N 121.0 0.1 1 141 . 31 ASN H H 9.17 0.010 1 142 . 31 ASN CA C 51.1 0.5 1 143 . 31 ASN CB C 38.9 0.5 1 144 . 31 ASN C C 178.03 0.09 1 145 . 32 LYS N N 118.8 0.1 1 146 . 32 LYS H H 8.32 0.010 1 147 . 32 LYS CA C 58.8 0.5 1 148 . 32 LYS CB C 31.9 0.5 1 149 . 32 LYS C C 176.88 0.09 1 150 . 33 ASP N N 119.4 0.1 1 151 . 33 ASP H H 7.94 0.010 1 152 . 33 ASP CA C 54.2 0.5 1 153 . 33 ASP CB C 41.7 0.5 1 154 . 33 ASP C C 176.28 0.09 1 155 . 34 GLY N N 108.7 0.1 1 156 . 34 GLY H H 8.23 0.010 1 157 . 34 GLY CA C 45.8 0.5 1 158 . 34 GLY C C 173.22 0.09 1 159 . 35 LYS N N 119.5 0.1 1 160 . 35 LYS H H 7.33 0.010 1 161 . 35 LYS CA C 53.8 0.5 1 162 . 35 LYS CB C 35.9 0.5 1 163 . 35 LYS C C 173.82 0.09 1 164 . 36 TYR N N 119.7 0.1 1 165 . 36 TYR H H 9.13 0.010 1 166 . 36 TYR CA C 59.1 0.5 1 167 . 36 TYR CB C 38.6 0.5 1 168 . 36 TYR C C 175.71 0.09 1 169 . 37 ASP N N 123.2 0.1 1 170 . 37 ASP H H 8.48 0.010 1 171 . 37 ASP CA C 55.2 0.5 1 172 . 37 ASP CB C 43.9 0.5 1 173 . 37 ASP C C 174.54 0.09 1 174 . 38 LEU N N 121.3 0.1 1 175 . 38 LEU H H 8.40 0.010 1 176 . 38 LEU CA C 53.8 0.5 1 177 . 38 LEU CB C 46.4 0.5 1 178 . 38 LEU C C 177.26 0.09 1 179 . 39 ILE N N 121.9 0.1 1 180 . 39 ILE H H 8.69 0.010 1 181 . 39 ILE CA C 60.2 0.5 1 182 . 39 ILE CB C 42.6 0.5 1 183 . 39 ILE C C 173.66 0.09 1 184 . 40 ALA N N 127.2 0.1 1 185 . 40 ALA H H 8.56 0.010 1 186 . 40 ALA CA C 51.2 0.5 1 187 . 40 ALA CB C 23.6 0.5 1 188 . 40 ALA C C 175.52 0.09 1 189 . 41 THR N N 118.0 0.1 1 190 . 41 THR H H 8.80 0.010 1 191 . 41 THR CA C 61.3 0.5 1 192 . 41 THR CB C 69.9 0.5 1 193 . 41 THR C C 174.44 0.09 1 194 . 42 VAL N N 127.7 0.1 1 195 . 42 VAL H H 8.65 0.010 1 196 . 42 VAL CA C 61.0 0.5 1 197 . 42 VAL CB C 34.4 0.5 1 198 . 42 VAL C C 175.24 0.09 1 199 . 43 ASP N N 129.8 0.1 1 200 . 43 ASP H H 9.16 0.010 1 201 . 43 ASP CA C 55.9 0.5 1 202 . 43 ASP CB C 39.4 0.5 1 203 . 43 ASP C C 175.05 0.09 1 204 . 44 LYS N N 111.4 0.1 1 205 . 44 LYS H H 8.27 0.010 1 206 . 44 LYS CA C 57.8 0.5 1 207 . 44 LYS CB C 30.6 0.5 1 208 . 44 LYS C C 174.91 0.09 1 209 . 45 LEU N N 125.1 0.1 1 210 . 45 LEU H H 8.08 0.010 1 211 . 45 LEU CA C 54.0 0.5 1 212 . 45 LEU CB C 44.2 0.5 1 213 . 45 LEU C C 174.86 0.09 1 214 . 46 GLU N N 126.6 0.1 1 215 . 46 GLU H H 8.36 0.010 1 216 . 46 GLU CA C 56.3 0.5 1 217 . 46 GLU CB C 30.9 0.5 1 218 . 46 GLU C C 175.06 0.09 1 219 . 47 LEU N N 128.6 0.1 1 220 . 47 LEU H H 9.35 0.010 1 221 . 47 LEU CA C 53.5 0.5 1 222 . 47 LEU CB C 44.4 0.5 1 223 . 47 LEU C C 175.36 0.09 1 224 . 48 LYS N N 119.3 0.1 1 225 . 48 LYS H H 8.39 0.010 1 226 . 48 LYS CA C 55.1 0.5 1 227 . 48 LYS CB C 37.4 0.5 1 228 . 48 LYS C C 176.90 0.09 1 229 . 49 GLY N N 112.3 0.1 1 230 . 49 GLY H H 8.93 0.010 1 231 . 49 GLY CA C 45.6 0.5 1 232 . 49 GLY C C 172.13 0.09 1 233 . 50 THR N N 111.9 0.1 1 234 . 50 THR H H 8.49 0.010 1 235 . 50 THR CA C 59.6 0.5 1 236 . 50 THR CB C 73.6 0.5 1 237 . 50 THR C C 174.00 0.09 1 238 . 51 SER N N 113.6 0.1 1 239 . 51 SER H H 8.95 0.010 1 240 . 51 SER CA C 56.5 0.5 1 241 . 51 SER CB C 65.4 0.5 1 242 . 51 SER C C 173.60 0.09 1 243 . 52 ASP N N 125.2 0.1 1 244 . 52 ASP H H 8.86 0.010 1 245 . 52 ASP CA C 55.8 0.5 1 246 . 52 ASP CB C 41.1 0.5 1 247 . 52 ASP C C 176.09 0.09 1 248 . 53 LYS N N 120.4 0.1 1 249 . 53 LYS H H 8.67 0.010 1 250 . 53 LYS CA C 55.0 0.5 1 251 . 53 LYS CB C 35.5 0.5 1 252 . 53 LYS C C 176.02 0.09 1 253 . 54 ASN N N 117.2 0.1 1 254 . 54 ASN H H 7.77 0.010 1 255 . 54 ASN CA C 50.8 0.5 1 256 . 54 ASN CB C 36.3 0.5 1 257 . 54 ASN C C 174.46 0.09 1 258 . 55 ASN N N 116.1 0.1 1 259 . 55 ASN H H 7.57 0.010 1 260 . 55 ASN CA C 52.8 0.5 1 261 . 55 ASN CB C 38.2 0.5 1 262 . 55 ASN C C 173.82 0.09 1 263 . 56 GLY N N 110.4 0.1 1 264 . 56 GLY H H 9.06 0.010 1 265 . 56 GLY CA C 44.5 0.5 1 266 . 56 GLY C C 170.04 0.09 1 267 . 57 SER N N 110.4 0.1 1 268 . 57 SER H H 7.04 0.010 1 269 . 57 SER CA C 57.4 0.5 1 270 . 57 SER CB C 66.2 0.5 1 271 . 57 SER C C 174.15 0.09 1 272 . 58 GLY N N 107.1 0.1 1 273 . 58 GLY H H 7.71 0.010 1 274 . 58 GLY CA C 44.2 0.5 1 275 . 58 GLY C C 170.80 0.09 1 276 . 59 VAL N N 120.0 0.1 1 277 . 59 VAL H H 8.10 0.010 1 278 . 59 VAL CA C 61.1 0.5 1 279 . 59 VAL CB C 34.7 0.5 1 280 . 59 VAL C C 175.21 0.09 1 281 . 60 LEU N N 127.7 0.1 1 282 . 60 LEU H H 9.53 0.010 1 283 . 60 LEU CA C 54.9 0.5 1 284 . 60 LEU CB C 46.4 0.5 1 285 . 60 LEU C C 175.20 0.09 1 286 . 61 GLU N N 118.8 0.1 1 287 . 61 GLU H H 8.67 0.010 1 288 . 61 GLU CA C 54.9 0.5 1 289 . 61 GLU CB C 36.0 0.5 1 290 . 61 GLU C C 176.45 0.09 1 291 . 62 GLY N N 110.7 0.1 1 292 . 62 GLY H H 8.86 0.010 1 293 . 62 GLY CA C 45.3 0.5 1 294 . 62 GLY C C 171.04 0.09 1 295 . 63 VAL N N 121.2 0.1 1 296 . 63 VAL H H 8.56 0.010 1 297 . 63 VAL CA C 61.0 0.5 1 298 . 63 VAL CB C 35.1 0.5 1 299 . 63 VAL C C 175.45 0.09 1 300 . 64 LYS N N 125.2 0.1 1 301 . 64 LYS H H 8.71 0.010 1 302 . 64 LYS CA C 56.3 0.5 1 303 . 64 LYS CB C 34.7 0.5 1 304 . 64 LYS C C 178.76 0.09 1 305 . 65 ALA N N 125.6 0.1 1 306 . 65 ALA H H 8.75 0.010 1 307 . 65 ALA CA C 55.0 0.5 1 308 . 65 ALA CB C 18.3 0.5 1 309 . 65 ALA C C 178.00 0.09 1 310 . 66 ASP N N 115.8 0.1 1 311 . 66 ASP H H 7.48 0.010 1 312 . 66 ASP CA C 53.4 0.5 1 313 . 66 ASP CB C 39.6 0.5 1 314 . 66 ASP C C 176.41 0.09 1 315 . 67 LYS N N 111.9 0.1 1 316 . 67 LYS H H 8.00 0.010 1 317 . 67 LYS CA C 59.0 0.5 1 318 . 67 LYS CB C 29.6 0.5 1 319 . 67 LYS C C 175.63 0.09 1 320 . 68 SER N N 116.5 0.1 1 321 . 68 SER H H 8.14 0.010 1 322 . 68 SER CA C 60.8 0.5 1 323 . 68 SER CB C 63.1 0.5 1 324 . 68 SER C C 172.78 0.09 1 325 . 69 LYS N N 124.0 0.1 1 326 . 69 LYS H H 7.85 0.010 1 327 . 69 LYS CA C 55.5 0.5 1 328 . 69 LYS CB C 35.1 0.5 1 329 . 69 LYS C C 174.69 0.09 1 330 . 70 VAL N N 124.2 0.1 1 331 . 70 VAL H H 8.69 0.010 1 332 . 70 VAL CA C 61.0 0.5 1 333 . 70 VAL CB C 34.4 0.5 1 334 . 70 VAL C C 174.51 0.09 1 335 . 71 LYS N N 129.2 0.1 1 336 . 71 LYS H H 9.50 0.010 1 337 . 71 LYS CA C 55.3 0.5 1 338 . 71 LYS CB C 37.8 0.5 1 339 . 71 LYS C C 174.07 0.09 1 340 . 72 LEU N N 132.5 0.1 1 341 . 72 LEU H H 9.58 0.010 1 342 . 72 LEU CA C 52.8 0.5 1 343 . 72 LEU CB C 46.0 0.5 1 344 . 72 LEU C C 174.02 0.09 1 345 . 73 THR N N 124.2 0.1 1 346 . 73 THR H H 9.41 0.010 1 347 . 73 THR CA C 62.7 0.5 1 348 . 73 THR CB C 70.1 0.5 1 349 . 73 THR C C 174.24 0.09 1 350 . 74 ILE N N 132.4 0.1 1 351 . 74 ILE H H 9.48 0.010 1 352 . 74 ILE CA C 61.0 0.5 1 353 . 74 ILE CB C 40.5 0.5 1 354 . 74 ILE C C 176.54 0.09 1 355 . 75 SER N N 124.8 0.1 1 356 . 75 SER H H 8.41 0.010 1 357 . 75 SER CA C 59.5 0.5 1 358 . 75 SER CB C 64.3 0.5 1 359 . 75 SER C C 174.83 0.09 1 360 . 76 ASP N N 121.0 0.1 1 361 . 76 ASP H H 8.52 0.010 1 362 . 76 ASP CA C 57.6 0.5 1 363 . 76 ASP CB C 41.2 0.5 1 364 . 76 ASP C C 176.22 0.09 1 365 . 77 ASP N N 115.4 0.1 1 366 . 77 ASP H H 7.80 0.010 1 367 . 77 ASP CA C 52.3 0.5 1 368 . 77 ASP CB C 40.3 0.5 1 369 . 77 ASP C C 176.88 0.09 1 370 . 78 LEU N N 117.2 0.1 1 371 . 78 LEU H H 8.35 0.010 1 372 . 78 LEU CA C 56.5 0.5 1 373 . 78 LEU CB C 39.0 0.5 1 374 . 78 LEU C C 176.16 0.09 1 375 . 79 GLY N N 105.6 0.1 1 376 . 79 GLY H H 8.14 0.010 1 377 . 79 GLY CA C 46.2 0.5 1 378 . 79 GLY C C 173.64 0.09 1 379 . 80 GLN N N 118.8 0.1 1 380 . 80 GLN H H 7.84 0.010 1 381 . 80 GLN CA C 54.9 0.5 1 382 . 80 GLN CB C 33.7 0.5 1 383 . 80 GLN C C 174.68 0.09 1 384 . 81 THR N N 114.2 0.1 1 385 . 81 THR H H 8.84 0.010 1 386 . 81 THR CA C 59.1 0.5 1 387 . 81 THR CB C 71.4 0.5 1 388 . 81 THR C C 173.48 0.09 1 389 . 82 THR N N 119.8 0.1 1 390 . 82 THR H H 9.01 0.010 1 391 . 82 THR CA C 62.3 0.5 1 392 . 82 THR CB C 71.3 0.5 1 393 . 82 THR C C 172.41 0.09 1 394 . 83 LEU N N 132.7 0.1 1 395 . 83 LEU H H 9.56 0.010 1 396 . 83 LEU CA C 53.6 0.5 1 397 . 83 LEU CB C 44.7 0.5 1 398 . 83 LEU C C 175.82 0.09 1 399 . 84 GLU N N 130.6 0.1 1 400 . 84 GLU H H 9.64 0.010 1 401 . 84 GLU CA C 55.2 0.5 1 402 . 84 GLU CB C 35.2 0.5 1 403 . 84 GLU C C 173.49 0.09 1 404 . 85 VAL N N 122.7 0.1 1 405 . 85 VAL H H 8.28 0.010 1 406 . 85 VAL CA C 61.2 0.5 1 407 . 85 VAL CB C 33.3 0.5 1 408 . 85 VAL C C 174.41 0.09 1 409 . 86 PHE N N 126.7 0.1 1 410 . 86 PHE H H 9.67 0.010 1 411 . 86 PHE CA C 56.3 0.5 1 412 . 86 PHE CB C 43.8 0.5 1 413 . 86 PHE C C 176.82 0.09 1 414 . 87 LYS N N 117.6 0.1 1 415 . 87 LYS H H 8.39 0.010 1 416 . 87 LYS CA C 56.6 0.5 1 417 . 87 LYS CB C 33.8 0.5 1 418 . 87 LYS C C 176.66 0.09 1 419 . 88 GLU N N 119.9 0.1 1 420 . 88 GLU H H 8.78 0.010 1 421 . 88 GLU CA C 58.7 0.5 1 422 . 88 GLU CB C 29.6 0.5 1 423 . 88 GLU C C 176.12 0.09 1 424 . 89 ASP N N 117.4 0.1 1 425 . 89 ASP H H 7.32 0.010 1 426 . 89 ASP CA C 54.5 0.5 1 427 . 89 ASP CB C 39.9 0.5 1 428 . 89 ASP C C 177.60 0.09 1 429 . 90 GLY N N 110.5 0.1 1 430 . 90 GLY H H 8.71 0.010 1 431 . 90 GLY CA C 46.0 0.5 1 432 . 90 GLY C C 172.20 0.09 1 433 . 91 LYS N N 118.8 0.1 1 434 . 91 LYS H H 8.49 0.010 1 435 . 91 LYS CA C 56.9 0.5 1 436 . 91 LYS CB C 36.0 0.5 1 437 . 91 LYS C C 175.71 0.09 1 438 . 92 THR N N 123.1 0.1 1 439 . 92 THR H H 9.65 0.010 1 440 . 92 THR CA C 63.3 0.5 1 441 . 92 THR CB C 67.7 0.5 1 442 . 92 THR C C 173.73 0.09 1 443 . 93 LEU N N 132.5 0.1 1 444 . 93 LEU H H 8.38 0.010 1 445 . 93 LEU CA C 56.4 0.5 1 446 . 93 LEU CB C 43.2 0.5 1 447 . 93 LEU C C 176.03 0.09 1 448 . 94 VAL N N 121.6 0.1 1 449 . 94 VAL H H 9.13 0.010 1 450 . 94 VAL CA C 64.2 0.5 1 451 . 94 VAL C C 176.92 0.09 1 452 . 95 SER N N 113.4 0.1 1 453 . 95 SER H H 7.83 0.010 1 454 . 95 SER CA C 57.6 0.5 1 455 . 95 SER CB C 65.6 0.5 1 456 . 95 SER C C 171.67 0.09 1 457 . 96 LYS N N 123.0 0.1 1 458 . 96 LYS H H 8.96 0.010 1 459 . 96 LYS CA C 55.7 0.5 1 460 . 96 LYS CB C 37.5 0.5 1 461 . 96 LYS C C 174.24 0.09 1 462 . 97 LYS N N 130.1 0.1 1 463 . 97 LYS H H 9.24 0.010 1 464 . 97 LYS CA C 55.2 0.5 1 465 . 97 LYS CB C 36.1 0.5 1 466 . 97 LYS C C 175.28 0.09 1 467 . 98 VAL N N 132.7 0.1 1 468 . 98 VAL H H 9.32 0.010 1 469 . 98 VAL CA C 61.0 0.5 1 470 . 98 VAL CB C 34.3 0.5 1 471 . 98 VAL C C 175.99 0.09 1 472 . 99 THR N N 125.3 0.1 1 473 . 99 THR H H 9.05 0.010 1 474 . 99 THR CA C 62.2 0.5 1 475 . 99 THR CB C 70.1 0.5 1 476 . 99 THR C C 173.13 0.09 1 477 . 100 SER N N 120.4 0.1 1 478 . 100 SER H H 8.41 0.010 1 479 . 100 SER CA C 56.9 0.5 1 480 . 100 SER CB C 65.0 0.5 1 481 . 100 SER C C 176.68 0.09 1 482 . 101 LYS N N 125.5 0.1 1 483 . 101 LYS H H 8.37 0.010 1 484 . 101 LYS CA C 59.1 0.5 1 485 . 101 LYS CB C 32.8 0.5 1 486 . 101 LYS C C 175.81 0.09 1 487 . 102 ASP N N 120.1 0.1 1 488 . 102 ASP H H 7.98 0.010 1 489 . 102 ASP CA C 54.0 0.5 1 490 . 102 ASP CB C 39.5 0.5 1 491 . 102 ASP C C 175.75 0.09 1 492 . 103 LYS N N 112.0 0.1 1 493 . 103 LYS H H 8.09 0.010 1 494 . 103 LYS CA C 59.1 0.5 1 495 . 103 LYS CB C 29.6 0.5 1 496 . 103 LYS C C 175.88 0.09 1 497 . 104 SER N N 117.4 0.1 1 498 . 104 SER H H 8.20 0.010 1 499 . 104 SER CA C 58.5 0.5 1 500 . 104 SER CB C 64.7 0.5 1 501 . 104 SER C C 173.35 0.09 1 502 . 105 SER N N 115.4 0.1 1 503 . 105 SER H H 8.87 0.010 1 504 . 105 SER CA C 57.3 0.5 1 505 . 105 SER CB C 67.0 0.5 1 506 . 105 SER C C 174.06 0.09 1 507 . 106 THR N N 119.8 0.1 1 508 . 106 THR H H 9.08 0.010 1 509 . 106 THR CA C 61.9 0.5 1 510 . 106 THR CB C 71.5 0.5 1 511 . 106 THR C C 172.71 0.09 1 512 . 107 GLU N N 129.0 0.1 1 513 . 107 GLU H H 9.25 0.010 1 514 . 107 GLU CA C 54.8 0.5 1 515 . 107 GLU CB C 33.6 0.5 1 516 . 107 GLU C C 174.44 0.09 1 517 . 108 GLU N N 125.8 0.1 1 518 . 108 GLU H H 9.20 0.010 1 519 . 108 GLU CA C 55.0 0.5 1 520 . 108 GLU CB C 34.6 0.5 1 521 . 108 GLU C C 174.57 0.09 1 522 . 109 LYS N N 122.5 0.1 1 523 . 109 LYS H H 8.45 0.010 1 524 . 109 LYS CA C 55.1 0.5 1 525 . 109 LYS CB C 35.6 0.5 1 526 . 109 LYS C C 174.51 0.09 1 527 . 110 PHE N N 122.7 0.1 1 528 . 110 PHE H H 7.93 0.010 1 529 . 110 PHE CA C 56.8 0.5 1 530 . 110 PHE CB C 42.5 0.5 1 531 . 110 PHE C C 176.68 0.09 1 532 . 111 ASN N N 120.8 0.1 1 533 . 111 ASN H H 8.84 0.010 1 534 . 111 ASN CA C 50.6 0.5 1 535 . 111 ASN CB C 39.0 0.5 1 536 . 111 ASN C C 177.54 0.09 1 537 . 112 GLU N N 119.3 0.1 1 538 . 112 GLU H H 9.26 0.010 1 539 . 112 GLU CA C 59.0 0.5 1 540 . 112 GLU CB C 28.8 0.5 1 541 . 112 GLU C C 177.00 0.09 1 542 . 113 LYS N N 119.6 0.1 1 543 . 113 LYS H H 7.71 0.010 1 544 . 113 LYS CA C 55.5 0.5 1 545 . 113 LYS CB C 32.7 0.5 1 546 . 113 LYS C C 176.79 0.09 1 547 . 114 GLY N N 109.1 0.1 1 548 . 114 GLY H H 8.22 0.010 1 549 . 114 GLY CA C 45.9 0.5 1 550 . 114 GLY C C 174.12 0.09 1 551 . 115 GLU N N 120.4 0.1 1 552 . 115 GLU H H 7.75 0.010 1 553 . 115 GLU CA C 54.3 0.5 1 554 . 115 GLU CB C 30.5 0.5 1 555 . 115 GLU C C 176.31 0.09 1 556 . 116 LEU N N 125.6 0.1 1 557 . 116 LEU H H 8.52 0.010 1 558 . 116 LEU CA C 56.7 0.5 1 559 . 116 LEU CB C 42.1 0.5 1 560 . 116 LEU C C 176.03 0.09 1 561 . 117 SER N N 121.6 0.1 1 562 . 117 SER H H 9.13 0.010 1 563 . 117 SER CA C 59.1 0.5 1 564 . 117 SER CB C 65.2 0.5 1 565 . 117 SER C C 175.38 0.09 1 566 . 118 GLU N N 121.1 0.1 1 567 . 118 GLU H H 7.71 0.010 1 568 . 118 GLU CA C 55.7 0.5 1 569 . 118 GLU CB C 34.3 0.5 1 570 . 118 GLU C C 173.63 0.09 1 571 . 119 LYS N N 123.7 0.1 1 572 . 119 LYS H H 9.11 0.010 1 573 . 119 LYS CA C 55.4 0.5 1 574 . 119 LYS CB C 37.8 0.5 1 575 . 119 LYS C C 173.99 0.09 1 576 . 120 LYS N N 129.8 0.1 1 577 . 120 LYS H H 9.49 0.010 1 578 . 120 LYS CA C 55.2 0.5 1 579 . 120 LYS CB C 36.5 0.5 1 580 . 120 LYS C C 175.12 0.09 1 581 . 121 ILE N N 130.9 0.1 1 582 . 121 ILE H H 9.17 0.010 1 583 . 121 ILE CA C 60.5 0.5 1 584 . 121 ILE CB C 40.9 0.5 1 585 . 121 ILE C C 175.46 0.09 1 586 . 122 THR N N 125.2 0.1 1 587 . 122 THR H H 9.24 0.010 1 588 . 122 THR CA C 61.9 0.5 1 589 . 122 THR CB C 70.1 0.5 1 590 . 122 THR C C 174.26 0.09 1 591 . 123 ARG N N 125.3 0.1 1 592 . 123 ARG H H 8.66 0.010 1 593 . 123 ARG CA C 55.3 0.5 1 594 . 123 ARG CB C 32.3 0.5 1 595 . 123 ARG C C 178.09 0.09 1 596 . 124 ALA N N 124.8 0.1 1 597 . 124 ALA H H 8.79 0.010 1 598 . 124 ALA CA C 54.8 0.5 1 599 . 124 ALA CB C 18.8 0.5 1 600 . 124 ALA C C 177.48 0.09 1 601 . 125 ASP N N 116.0 0.1 1 602 . 125 ASP H H 7.56 0.010 1 603 . 125 ASP CA C 53.4 0.5 1 604 . 125 ASP CB C 39.6 0.5 1 605 . 125 ASP C C 175.71 0.09 1 606 . 126 LYS N N 110.7 0.1 1 607 . 126 LYS H H 7.92 0.010 1 608 . 126 LYS CA C 59.1 0.5 1 609 . 126 LYS CB C 29.6 0.5 1 610 . 126 LYS C C 176.52 0.09 1 611 . 127 SER N N 118.1 0.1 1 612 . 127 SER H H 8.31 0.010 1 613 . 127 SER CA C 59.1 0.5 1 614 . 127 SER CB C 64.5 0.5 1 615 . 127 SER C C 172.96 0.09 1 616 . 128 SER N N 113.7 0.1 1 617 . 128 SER H H 9.06 0.010 1 618 . 128 SER CA C 57.5 0.5 1 619 . 128 SER CB C 68.0 0.5 1 620 . 128 SER C C 174.35 0.09 1 621 . 129 THR N N 117.5 0.1 1 622 . 129 THR H H 8.98 0.010 1 623 . 129 THR CA C 61.8 0.5 1 624 . 129 THR CB C 71.3 0.5 1 625 . 129 THR C C 173.25 0.09 1 626 . 130 GLU N N 128.5 0.1 1 627 . 130 GLU H H 9.46 0.010 1 628 . 130 GLU CA C 55.2 0.5 1 629 . 130 GLU CB C 33.6 0.5 1 630 . 130 GLU C C 174.69 0.09 1 631 . 131 GLU N N 126.9 0.1 1 632 . 131 GLU H H 9.29 0.010 1 633 . 131 GLU CA C 54.8 0.5 1 634 . 131 GLU CB C 35.0 0.5 1 635 . 131 GLU C C 174.35 0.09 1 636 . 132 LYS N N 121.7 0.1 1 637 . 132 LYS H H 8.20 0.010 1 638 . 132 LYS CA C 54.9 0.5 1 639 . 132 LYS CB C 35.1 0.5 1 640 . 132 LYS C C 174.97 0.09 1 641 . 133 PHE N N 121.8 0.1 1 642 . 133 PHE H H 8.07 0.010 1 643 . 133 PHE CA C 56.9 0.5 1 644 . 133 PHE CB C 42.1 0.5 1 645 . 133 PHE C C 175.82 0.09 1 646 . 134 ASN N N 120.2 0.1 1 647 . 134 ASN H H 8.98 0.010 1 648 . 134 ASN CA C 51.0 0.5 1 649 . 134 ASN CB C 38.9 0.5 1 650 . 134 ASN C C 177.72 0.09 1 651 . 135 GLU N N 119.3 0.1 1 652 . 135 GLU H H 9.06 0.010 1 653 . 135 GLU CA C 59.2 0.5 1 654 . 135 GLU CB C 29.1 0.5 1 655 . 135 GLU C C 176.97 0.09 1 656 . 136 LYS N N 118.3 0.1 1 657 . 136 LYS H H 7.65 0.010 1 658 . 136 LYS CA C 55.7 0.5 1 659 . 136 LYS CB C 32.8 0.5 1 660 . 136 LYS C C 176.91 0.09 1 661 . 137 GLY N N 108.9 0.1 1 662 . 137 GLY H H 8.37 0.010 1 663 . 137 GLY CA C 45.7 0.5 1 664 . 137 GLY C C 174.12 0.09 1 665 . 138 GLU N N 120.4 0.1 1 666 . 138 GLU H H 7.75 0.010 1 667 . 138 GLU CA C 54.1 0.5 1 668 . 138 GLU CB C 30.7 0.5 1 669 . 138 GLU C C 176.14 0.09 1 670 . 139 VAL N N 124.0 0.1 1 671 . 139 VAL H H 8.36 0.010 1 672 . 139 VAL CA C 63.4 0.5 1 673 . 139 VAL CB C 31.9 0.5 1 674 . 139 VAL C C 175.43 0.09 1 675 . 140 SER N N 123.4 0.1 1 676 . 140 SER H H 8.97 0.010 1 677 . 140 SER CA C 58.5 0.5 1 678 . 140 SER CB C 65.6 0.5 1 679 . 140 SER C C 174.35 0.09 1 680 . 141 GLU N N 121.5 0.1 1 681 . 141 GLU H H 7.38 0.010 1 682 . 141 GLU CA C 55.4 0.5 1 683 . 141 GLU CB C 34.1 0.5 1 684 . 141 GLU C C 173.74 0.09 1 685 . 142 LYS N N 124.6 0.1 1 686 . 142 LYS H H 9.00 0.010 1 687 . 142 LYS CA C 55.3 0.5 1 688 . 142 LYS CB C 37.1 0.5 1 689 . 142 LYS C C 173.42 0.09 1 690 . 143 ILE N N 126.7 0.1 1 691 . 143 ILE H H 9.33 0.010 1 692 . 143 ILE CA C 60.2 0.5 1 693 . 143 ILE CB C 40.9 0.5 1 694 . 143 ILE C C 176.29 0.09 1 695 . 144 ILE N N 134.0 0.1 1 696 . 144 ILE H H 9.67 0.010 1 697 . 144 ILE CA C 60.9 0.5 1 698 . 144 ILE CB C 40.4 0.5 1 699 . 144 ILE C C 175.07 0.09 1 700 . 145 THR N N 125.6 0.1 1 701 . 145 THR H H 9.26 0.010 1 702 . 145 THR CA C 62.4 0.5 1 703 . 145 THR CB C 68.9 0.5 1 704 . 145 THR C C 175.00 0.09 1 705 . 146 ARG N N 126.7 0.1 1 706 . 146 ARG H H 8.98 0.010 1 707 . 146 ARG CA C 56.3 0.5 1 708 . 146 ARG CB C 30.9 0.5 1 709 . 146 ARG C C 178.06 0.09 1 710 . 147 ALA N N 125.0 0.1 1 711 . 147 ALA H H 8.95 0.010 1 712 . 147 ALA CA C 54.9 0.5 1 713 . 147 ALA CB C 18.4 0.5 1 714 . 147 ALA C C 177.52 0.09 1 715 . 148 ASP N N 113.8 0.1 1 716 . 148 ASP H H 7.26 0.010 1 717 . 148 ASP CA C 53.1 0.5 1 718 . 148 ASP CB C 40.5 0.5 1 719 . 148 ASP C C 177.29 0.09 1 720 . 149 GLY N N 109.3 0.1 1 721 . 149 GLY H H 7.98 0.010 1 722 . 149 GLY CA C 45.3 0.5 1 723 . 149 GLY C C 175.62 0.09 1 724 . 150 THR N N 115.1 0.1 1 725 . 150 THR H H 8.34 0.010 1 726 . 150 THR CA C 62.7 0.5 1 727 . 150 THR CB C 70.5 0.5 1 728 . 150 THR C C 173.46 0.09 1 729 . 151 ARG N N 116.1 0.1 1 730 . 151 ARG H H 8.21 0.010 1 731 . 151 ARG CA C 54.5 0.5 1 732 . 151 ARG CB C 36.1 0.5 1 733 . 151 ARG C C 174.79 0.09 1 734 . 152 LEU N N 123.7 0.1 1 735 . 152 LEU H H 9.12 0.010 1 736 . 152 LEU CA C 53.6 0.5 1 737 . 152 LEU CB C 45.4 0.5 1 738 . 152 LEU C C 174.71 0.09 1 739 . 153 GLU N N 121.8 0.1 1 740 . 153 GLU H H 9.08 0.010 1 741 . 153 GLU CA C 54.5 0.5 1 742 . 153 GLU CB C 32.3 0.5 1 743 . 153 GLU C C 175.22 0.09 1 744 . 154 TYR N N 126.2 0.1 1 745 . 154 TYR H H 9.38 0.010 1 746 . 154 TYR CA C 55.0 0.5 1 747 . 154 TYR CB C 40.2 0.5 1 748 . 154 TYR C C 175.66 0.09 1 749 . 155 THR N N 114.1 0.1 1 750 . 155 THR H H 8.74 0.010 1 751 . 155 THR CA C 59.5 0.5 1 752 . 155 THR CB C 72.3 0.5 1 753 . 155 THR C C 173.70 0.09 1 754 . 156 GLY N N 112.0 0.1 1 755 . 156 GLY H H 8.83 0.010 1 756 . 156 GLY CA C 47.3 0.5 1 757 . 156 GLY C C 175.22 0.09 1 758 . 157 ILE N N 118.8 0.1 1 759 . 157 ILE H H 7.75 0.010 1 760 . 157 ILE CA C 62.4 0.5 1 761 . 157 ILE CB C 37.5 0.5 1 762 . 157 ILE C C 177.63 0.09 1 763 . 158 LYS N N 129.5 0.1 1 764 . 158 LYS H H 8.88 0.010 1 765 . 158 LYS CA C 54.8 0.5 1 766 . 158 LYS CB C 35.1 0.5 1 767 . 158 LYS C C 179.60 0.09 1 768 . 159 SER N N 118.1 0.1 1 769 . 159 SER H H 8.62 0.010 1 770 . 159 SER CA C 61.4 0.5 1 771 . 159 SER CB C 62.9 0.5 1 772 . 159 SER C C 174.50 0.09 1 773 . 160 ASP N N 118.8 0.1 1 774 . 160 ASP H H 7.59 0.010 1 775 . 160 ASP CA C 53.3 0.5 1 776 . 160 ASP CB C 39.8 0.5 1 777 . 160 ASP C C 177.36 0.09 1 778 . 161 GLY N N 110.6 0.1 1 779 . 161 GLY H H 8.32 0.010 1 780 . 161 GLY CA C 45.0 0.5 1 781 . 161 GLY C C 172.64 0.09 1 782 . 162 SER N N 115.5 0.1 1 783 . 162 SER H H 7.86 0.010 1 784 . 162 SER CA C 57.2 0.5 1 785 . 162 SER CB C 65.3 0.5 1 786 . 162 SER C C 173.35 0.09 1 787 . 163 GLY N N 104.7 0.1 1 788 . 163 GLY H H 8.25 0.010 1 789 . 163 GLY CA C 46.2 0.5 1 790 . 163 GLY C C 172.72 0.09 1 791 . 164 LYS N N 124.7 0.1 1 792 . 164 LYS H H 8.95 0.010 1 793 . 164 LYS CA C 56.1 0.5 1 794 . 164 LYS CB C 33.6 0.5 1 795 . 164 LYS C C 174.87 0.09 1 796 . 165 ALA N N 123.5 0.1 1 797 . 165 ALA H H 7.92 0.010 1 798 . 165 ALA CA C 50.1 0.5 1 799 . 165 ALA CB C 25.5 0.5 1 800 . 165 ALA C C 175.81 0.09 1 801 . 166 LYS N N 122.2 0.1 1 802 . 166 LYS H H 8.54 0.010 1 803 . 166 LYS CA C 55.4 0.5 1 804 . 166 LYS CB C 36.7 0.5 1 805 . 166 LYS C C 173.62 0.09 1 806 . 167 GLU N N 128.1 0.1 1 807 . 167 GLU H H 9.54 0.010 1 808 . 167 GLU CA C 54.5 0.5 1 809 . 167 GLU CB C 32.7 0.5 1 810 . 167 GLU C C 174.35 0.09 1 811 . 168 VAL N N 130.6 0.1 1 812 . 168 VAL H H 9.49 0.010 1 813 . 168 VAL CA C 62.8 0.5 1 814 . 168 VAL CB C 31.9 0.5 1 815 . 168 VAL C C 174.90 0.09 1 816 . 169 LEU N N 129.3 0.1 1 817 . 169 LEU H H 7.76 0.010 1 818 . 169 LEU CA C 52.5 0.5 1 819 . 169 LEU CB C 40.7 0.5 1 820 . 169 LEU C C 175.95 0.09 1 821 . 170 LYS N N 120.8 0.1 1 822 . 170 LYS H H 7.87 0.010 1 823 . 170 LYS CA C 57.4 0.5 1 824 . 170 LYS CB C 30.4 0.5 1 825 . 170 LYS C C 176.32 0.09 1 826 . 171 GLY N N 114.1 0.1 1 827 . 171 GLY H H 7.96 0.010 1 828 . 171 GLY CA C 45.4 0.5 1 829 . 171 GLY C C 173.47 0.09 1 830 . 172 TYR N N 114.9 0.1 1 831 . 172 TYR H H 6.77 0.010 1 832 . 172 TYR CA C 55.8 0.5 1 833 . 172 TYR CB C 39.3 0.5 1 834 . 172 TYR C C 171.39 0.09 1 835 . 173 VAL N N 117.1 0.1 1 836 . 173 VAL H H 7.99 0.010 1 837 . 173 VAL CA C 59.6 0.5 1 838 . 173 VAL CB C 35.3 0.5 1 839 . 173 VAL C C 175.10 0.09 1 840 . 174 LEU N N 124.1 0.1 1 841 . 174 LEU H H 8.92 0.010 1 842 . 174 LEU CA C 52.6 0.5 1 843 . 174 LEU CB C 45.4 0.5 1 844 . 174 LEU C C 176.02 0.09 1 845 . 175 GLU N N 122.4 0.1 1 846 . 175 GLU H H 9.48 0.010 1 847 . 175 GLU CA C 55.5 0.5 1 848 . 175 GLU CB C 34.0 0.5 1 849 . 175 GLU C C 176.32 0.09 1 850 . 176 GLY N N 108.9 0.1 1 851 . 176 GLY H H 8.65 0.010 1 852 . 176 GLY CA C 46.5 0.5 1 853 . 176 GLY C C 174.19 0.09 1 854 . 177 THR N N 118.8 0.1 1 855 . 177 THR H H 9.14 0.010 1 856 . 177 THR CA C 60.9 0.5 1 857 . 177 THR CB C 73.2 0.5 1 858 . 177 THR C C 171.51 0.09 1 859 . 178 LEU N N 125.8 0.1 1 860 . 178 LEU H H 8.39 0.010 1 861 . 178 LEU CA C 54.0 0.5 1 862 . 178 LEU CB C 45.1 0.5 1 863 . 178 LEU C C 175.63 0.09 1 864 . 179 THR N N 118.2 0.1 1 865 . 179 THR H H 8.46 0.010 1 866 . 179 THR CA C 60.1 0.5 1 867 . 179 THR CB C 72.8 0.5 1 868 . 179 THR C C 173.68 0.09 1 869 . 180 ALA N N 122.2 0.1 1 870 . 180 ALA H H 8.78 0.010 1 871 . 180 ALA CA C 54.3 0.5 1 872 . 180 ALA CB C 18.2 0.5 1 873 . 180 ALA C C 178.26 0.09 1 874 . 181 GLU N N 113.2 0.1 1 875 . 181 GLU H H 7.92 0.010 1 876 . 181 GLU CA C 57.6 0.5 1 877 . 181 GLU CB C 31.4 0.5 1 878 . 181 GLU C C 176.06 0.09 1 879 . 182 LYS N N 116.7 0.1 1 880 . 182 LYS H H 7.59 0.010 1 881 . 182 LYS CA C 55.8 0.5 1 882 . 182 LYS CB C 34.7 0.5 1 883 . 182 LYS C C 174.38 0.09 1 884 . 183 THR N N 121.0 0.1 1 885 . 183 THR H H 8.65 0.010 1 886 . 183 THR CA C 62.4 0.5 1 887 . 183 THR CB C 70.5 0.5 1 888 . 183 THR C C 173.36 0.09 1 889 . 184 THR N N 125.1 0.1 1 890 . 184 THR H H 9.11 0.010 1 891 . 184 THR CA C 62.3 0.5 1 892 . 184 THR CB C 71.5 0.5 1 893 . 184 THR C C 172.63 0.09 1 894 . 185 LEU N N 131.8 0.1 1 895 . 185 LEU H H 9.30 0.010 1 896 . 185 LEU CA C 53.6 0.5 1 897 . 185 LEU CB C 42.3 0.5 1 898 . 185 LEU C C 175.62 0.09 1 899 . 186 VAL N N 120.9 0.1 1 900 . 186 VAL H H 8.41 0.010 1 901 . 186 VAL CA C 61.0 0.5 1 902 . 186 VAL CB C 36.1 0.5 1 903 . 186 VAL C C 175.61 0.09 1 904 . 187 VAL N N 126.9 0.1 1 905 . 187 VAL H H 9.10 0.010 1 906 . 187 VAL CA C 61.8 0.5 1 907 . 187 VAL CB C 34.9 0.5 1 908 . 187 VAL C C 173.32 0.09 1 909 . 188 LYS N N 127.9 0.1 1 910 . 188 LYS H H 8.41 0.010 1 911 . 188 LYS CA C 54.5 0.5 1 912 . 188 LYS CB C 35.9 0.5 1 913 . 188 LYS C C 175.47 0.09 1 914 . 189 GLU N N 125.3 0.1 1 915 . 189 GLU H H 8.57 0.010 1 916 . 189 GLU CA C 55.4 0.5 1 917 . 189 GLU CB C 32.1 0.5 1 918 . 189 GLU C C 175.88 0.09 1 919 . 190 GLY N N 121.2 0.1 1 920 . 190 GLY H H 9.00 0.010 1 921 . 190 GLY CA C 47.0 0.5 1 922 . 190 GLY C C 175.90 0.09 1 923 . 191 THR N N 119.8 0.1 1 924 . 191 THR H H 8.70 0.010 1 925 . 191 THR CA C 62.8 0.5 1 926 . 191 THR CB C 67.8 0.5 1 927 . 191 THR C C 174.48 0.09 1 928 . 192 VAL N N 126.1 0.1 1 929 . 192 VAL H H 8.33 0.010 1 930 . 192 VAL CA C 62.7 0.5 1 931 . 192 VAL CB C 33.1 0.5 1 932 . 192 VAL C C 175.44 0.09 1 933 . 193 THR N N 123.5 0.1 1 934 . 193 THR H H 9.04 0.010 1 935 . 193 THR CA C 62.5 0.5 1 936 . 193 THR CB C 70.8 0.5 1 937 . 193 THR C C 173.24 0.09 1 938 . 194 LEU N N 134.0 0.1 1 939 . 194 LEU H H 9.53 0.010 1 940 . 194 LEU CA C 54.0 0.5 1 941 . 194 LEU CB C 45.0 0.5 1 942 . 194 LEU C C 174.15 0.09 1 943 . 195 SER N N 122.8 0.1 1 944 . 195 SER H H 8.97 0.010 1 945 . 195 SER CA C 56.6 0.5 1 946 . 195 SER CB C 64.3 0.5 1 947 . 195 SER C C 171.69 0.09 1 948 . 196 LYS N N 128.0 0.1 1 949 . 196 LYS H H 9.50 0.010 1 950 . 196 LYS CA C 54.8 0.5 1 951 . 196 LYS CB C 34.6 0.5 1 952 . 196 LYS C C 173.47 0.09 1 953 . 197 ASN N N 126.9 0.1 1 954 . 197 ASN H H 9.00 0.010 1 955 . 197 ASN CA C 51.7 0.5 1 956 . 197 ASN CB C 41.2 0.5 1 957 . 197 ASN C C 174.41 0.09 1 958 . 198 ILE N N 122.4 0.1 1 959 . 198 ILE H H 9.18 0.010 1 960 . 198 ILE CA C 60.4 0.5 1 961 . 198 ILE CB C 40.8 0.5 1 962 . 198 ILE C C 177.42 0.09 1 963 . 199 SER N N 126.1 0.1 1 964 . 199 SER H H 9.19 0.010 1 965 . 199 SER CA C 58.1 0.5 1 966 . 199 SER CB C 65.0 0.5 1 967 . 199 SER C C 176.13 0.09 1 968 . 200 LYS N N 123.3 0.1 1 969 . 200 LYS H H 8.48 0.010 1 970 . 200 LYS CA C 59.2 0.5 1 971 . 200 LYS CB C 31.9 0.5 1 972 . 200 LYS C C 177.19 0.09 1 973 . 201 SER N N 113.1 0.1 1 974 . 201 SER H H 7.93 0.010 1 975 . 201 SER CA C 57.9 0.5 1 976 . 201 SER CB C 63.6 0.5 1 977 . 201 SER C C 174.99 0.09 1 978 . 202 GLY N N 111.9 0.1 1 979 . 202 GLY H H 8.03 0.010 1 980 . 202 GLY CA C 45.2 0.5 1 981 . 202 GLY C C 173.93 0.09 1 982 . 203 GLU N N 122.0 0.1 1 983 . 203 GLU H H 7.75 0.010 1 984 . 203 GLU CA C 56.9 0.5 1 985 . 203 GLU CB C 30.6 0.5 1 986 . 203 GLU C C 176.52 0.09 1 987 . 204 VAL N N 129.8 0.1 1 988 . 204 VAL H H 8.77 0.010 1 989 . 204 VAL CA C 61.3 0.5 1 990 . 204 VAL CB C 33.8 0.5 1 991 . 204 VAL C C 175.77 0.09 1 992 . 205 SER N N 121.8 0.1 1 993 . 205 SER H H 8.72 0.010 1 994 . 205 SER CA C 57.3 0.5 1 995 . 205 SER CB C 65.1 0.5 1 996 . 205 SER C C 171.16 0.09 1 997 . 206 VAL N N 120.6 0.1 1 998 . 206 VAL H H 3.98 0.010 1 999 . 206 VAL CA C 59.5 0.5 1 1000 . 206 VAL CB C 33.7 0.5 1 1001 . 206 VAL C C 173.07 0.09 1 1002 . 207 GLU N N 124.5 0.1 1 1003 . 207 GLU H H 8.51 0.010 1 1004 . 207 GLU CA C 53.9 0.5 1 1005 . 207 GLU CB C 34.2 0.5 1 1006 . 207 GLU C C 173.29 0.09 1 1007 . 208 LEU N N 124.5 0.1 1 1008 . 208 LEU H H 8.61 0.010 1 1009 . 208 LEU CA C 54.0 0.5 1 1010 . 208 LEU CB C 46.9 0.5 1 1011 . 208 LEU C C 174.77 0.09 1 1012 . 209 ASN N N 125.1 0.1 1 1013 . 209 ASN H H 8.88 0.010 1 1014 . 209 ASN CA C 52.9 0.5 1 1015 . 209 ASN CB C 43.1 0.5 1 1016 . 209 ASN C C 172.19 0.09 1 1017 . 210 ASP N N 126.8 0.1 1 1018 . 210 ASP H H 8.54 0.010 1 1019 . 210 ASP CA C 52.4 0.5 1 1020 . 210 ASP CB C 45.0 0.5 1 1021 . 210 ASP C C 177.37 0.09 1 1022 . 211 THR N N 117.5 0.1 1 1023 . 211 THR H H 8.49 0.010 1 1024 . 211 THR CA C 62.6 0.5 1 1025 . 211 THR CB C 68.5 0.5 1 1026 . 211 THR C C 175.53 0.09 1 1027 . 212 ASP N N 126.8 0.1 1 1028 . 212 ASP H H 8.37 0.010 1 1029 . 212 ASP CA C 55.4 0.5 1 1030 . 212 ASP CB C 41.3 0.5 1 1031 . 212 ASP C C 176.32 0.09 1 1032 . 213 SER N N 121.1 0.1 1 1033 . 213 SER H H 8.18 0.010 1 1034 . 213 SER CA C 58.7 0.5 1 1035 . 213 SER CB C 64.4 0.5 1 1036 . 213 SER C C 175.69 0.09 1 1037 . 214 SER N N 120.7 0.1 1 1038 . 214 SER H H 8.49 0.010 1 1039 . 214 SER CA C 57.3 0.5 1 1040 . 214 SER CB C 63.4 0.5 1 1041 . 214 SER C C 175.05 0.09 1 1042 . 215 ALA N N 131.8 0.1 1 1043 . 215 ALA H H 8.71 0.010 1 1044 . 215 ALA CA C 54.6 0.5 1 1045 . 215 ALA CB C 18.5 0.5 1 1046 . 215 ALA C C 178.99 0.09 1 1047 . 216 ALA N N 118.1 0.1 1 1048 . 216 ALA H H 7.97 0.010 1 1049 . 216 ALA CA C 54.0 0.5 1 1050 . 216 ALA CB C 19.4 0.5 1 1051 . 216 ALA C C 177.86 0.09 1 1052 . 217 THR N N 103.4 0.1 1 1053 . 217 THR H H 6.99 0.010 1 1054 . 217 THR CA C 61.0 0.5 1 1055 . 217 THR CB C 69.8 0.5 1 1056 . 217 THR C C 174.48 0.09 1 1057 . 218 LYS N N 124.3 0.1 1 1058 . 218 LYS H H 7.58 0.010 1 1059 . 218 LYS CA C 57.3 0.5 1 1060 . 218 LYS CB C 33.3 0.5 1 1061 . 218 LYS C C 176.26 0.09 1 1062 . 219 LYS N N 130.3 0.1 1 1063 . 219 LYS H H 10.29 0.010 1 1064 . 219 LYS CA C 56.9 0.5 1 1065 . 219 LYS CB C 33.9 0.5 1 1066 . 219 LYS C C 176.24 0.09 1 1067 . 220 THR N N 113.1 0.1 1 1068 . 220 THR H H 8.57 0.010 1 1069 . 220 THR CA C 60.1 0.5 1 1070 . 220 THR CB C 71.8 0.5 1 1071 . 220 THR C C 172.81 0.09 1 1072 . 221 ALA N N 122.5 0.1 1 1073 . 221 ALA H H 8.83 0.010 1 1074 . 221 ALA CA C 51.1 0.5 1 1075 . 221 ALA CB C 25.7 0.5 1 1076 . 221 ALA C C 175.44 0.09 1 1077 . 222 ALA N N 123.7 0.1 1 1078 . 222 ALA H H 8.25 0.010 1 1079 . 222 ALA CA C 50.7 0.5 1 1080 . 222 ALA CB C 22.4 0.5 1 1081 . 222 ALA C C 175.52 0.09 1 1082 . 223 TRP N N 125.6 0.1 1 1083 . 223 TRP H H 8.90 0.010 1 1084 . 223 TRP CA C 55.2 0.5 1 1085 . 223 TRP CB C 32.3 0.5 1 1086 . 223 TRP C C 174.52 0.09 1 1087 . 224 ASN N N 128.5 0.1 1 1088 . 224 ASN H H 8.13 0.010 1 1089 . 224 ASN CA C 50.9 0.5 1 1090 . 224 ASN CB C 39.4 0.5 1 1091 . 224 ASN C C 174.76 0.09 1 1092 . 225 SER N N 121.2 0.1 1 1093 . 225 SER H H 8.60 0.010 1 1094 . 225 SER CA C 60.9 0.5 1 1095 . 225 SER CB C 63.2 0.5 1 1096 . 225 SER C C 176.68 0.09 1 1097 . 226 GLY N N 110.9 0.1 1 1098 . 226 GLY H H 8.36 0.010 1 1099 . 226 GLY CA C 46.5 0.5 1 1100 . 226 GLY C C 175.44 0.09 1 1101 . 227 THR N N 108.4 0.1 1 1102 . 227 THR H H 7.00 0.010 1 1103 . 227 THR CA C 60.1 0.5 1 1104 . 227 THR CB C 69.4 0.5 1 1105 . 227 THR C C 175.61 0.09 1 1106 . 228 SER N N 122.0 0.1 1 1107 . 228 SER H H 7.57 0.010 1 1108 . 228 SER CA C 59.2 0.5 1 1109 . 228 SER CB C 62.7 0.5 1 1110 . 228 SER C C 172.20 0.09 1 1111 . 229 THR N N 111.4 0.1 1 1112 . 229 THR H H 6.64 0.010 1 1113 . 229 THR CA C 61.6 0.5 1 1114 . 229 THR CB C 71.6 0.5 1 1115 . 229 THR C C 172.69 0.09 1 1116 . 230 LEU N N 134.2 0.1 1 1117 . 230 LEU H H 10.21 0.010 1 1118 . 230 LEU CA C 53.1 0.5 1 1119 . 230 LEU CB C 45.9 0.5 1 1120 . 230 LEU C C 175.30 0.09 1 1121 . 231 THR N N 127.3 0.1 1 1122 . 231 THR H H 9.15 0.010 1 1123 . 231 THR CA C 62.3 0.5 1 1124 . 231 THR CB C 71.3 0.5 1 1125 . 231 THR C C 175.39 0.09 1 1126 . 232 ILE N N 132.8 0.1 1 1127 . 232 ILE H H 9.56 0.010 1 1128 . 232 ILE CA C 61.9 0.5 1 1129 . 232 ILE CB C 39.3 0.5 1 1130 . 232 ILE C C 174.19 0.09 1 1131 . 233 THR N N 125.4 0.1 1 1132 . 233 THR H H 9.15 0.010 1 1133 . 233 THR CA C 61.3 0.5 1 1134 . 233 THR CB C 71.7 0.5 1 1135 . 233 THR C C 173.07 0.09 1 1136 . 234 VAL N N 124.8 0.1 1 1137 . 234 VAL H H 8.61 0.010 1 1138 . 234 VAL CA C 61.9 0.5 1 1139 . 234 VAL CB C 35.7 0.5 1 1140 . 234 VAL C C 177.11 0.09 1 1141 . 235 ASN N N 132.2 0.1 1 1142 . 235 ASN H H 10.13 0.010 1 1143 . 235 ASN CA C 53.6 0.5 1 1144 . 235 ASN CB C 37.0 0.5 1 1145 . 235 ASN C C 175.07 0.09 1 1146 . 236 SER N N 107.1 0.1 1 1147 . 236 SER H H 8.65 0.010 1 1148 . 236 SER CA C 60.4 0.5 1 1149 . 236 SER CB C 62.4 0.5 1 1150 . 236 SER C C 172.77 0.09 1 1151 . 237 LYS N N 123.4 0.1 1 1152 . 237 LYS H H 7.83 0.010 1 1153 . 237 LYS CA C 54.6 0.5 1 1154 . 237 LYS CB C 35.0 0.5 1 1155 . 237 LYS C C 174.90 0.09 1 1156 . 238 LYS N N 126.8 0.1 1 1157 . 238 LYS H H 8.21 0.010 1 1158 . 238 LYS CA C 57.7 0.5 1 1159 . 238 LYS CB C 30.8 0.5 1 1160 . 238 LYS C C 176.69 0.09 1 1161 . 239 THR N N 113.1 0.1 1 1162 . 239 THR H H 9.18 0.010 1 1163 . 239 THR CA C 62.8 0.5 1 1164 . 239 THR CB C 69.5 0.5 1 1165 . 239 THR C C 176.86 0.09 1 1166 . 240 LYS N N 121.3 0.1 1 1167 . 240 LYS H H 7.57 0.010 1 1168 . 240 LYS CA C 56.0 0.5 1 1169 . 240 LYS CB C 36.6 0.5 1 1170 . 240 LYS C C 173.46 0.09 1 1171 . 241 ASP N N 121.9 0.1 1 1172 . 241 ASP H H 8.95 0.010 1 1173 . 241 ASP CA C 53.1 0.5 1 1174 . 241 ASP CB C 43.4 0.5 1 1175 . 241 ASP C C 176.39 0.09 1 1176 . 242 LEU N N 126.3 0.1 1 1177 . 242 LEU H H 9.62 0.010 1 1178 . 242 LEU CA C 53.9 0.5 1 1179 . 242 LEU CB C 44.6 0.5 1 1180 . 242 LEU C C 175.15 0.09 1 1181 . 243 VAL N N 126.3 0.1 1 1182 . 243 VAL H H 8.70 0.010 1 1183 . 243 VAL CA C 61.7 0.5 1 1184 . 243 VAL CB C 32.3 0.5 1 1185 . 243 VAL C C 174.74 0.09 1 1186 . 244 PHE N N 129.2 0.1 1 1187 . 244 PHE H H 8.72 0.010 1 1188 . 244 PHE CA C 56.7 0.5 1 1189 . 244 PHE CB C 38.0 0.5 1 1190 . 244 PHE C C 176.68 0.09 1 1191 . 245 THR N N 114.6 0.1 1 1192 . 245 THR H H 8.53 0.010 1 1193 . 245 THR CA C 61.9 0.5 1 1194 . 245 THR CB C 71.4 0.5 1 1195 . 245 THR C C 177.59 0.09 1 1196 . 246 LYS N N 121.7 0.1 1 1197 . 246 LYS H H 8.91 0.010 1 1198 . 246 LYS CA C 57.6 0.5 1 1199 . 246 LYS CB C 31.8 0.5 1 1200 . 246 LYS C C 176.90 0.09 1 1201 . 247 GLU N N 118.5 0.1 1 1202 . 247 GLU H H 7.60 0.010 1 1203 . 247 GLU CA C 56.3 0.5 1 1204 . 247 GLU CB C 28.5 0.5 1 1205 . 247 GLU C C 174.16 0.09 1 1206 . 248 ASN N N 112.3 0.1 1 1207 . 248 ASN H H 7.78 0.010 1 1208 . 248 ASN CA C 55.4 0.5 1 1209 . 248 ASN CB C 36.6 0.5 1 1210 . 248 ASN C C 174.17 0.09 1 1211 . 249 THR N N 108.3 0.1 1 1212 . 249 THR H H 7.33 0.010 1 1213 . 249 THR CA C 58.7 0.5 1 1214 . 249 THR CB C 72.2 0.5 1 1215 . 249 THR C C 173.22 0.09 1 1216 . 250 ILE N N 122.5 0.1 1 1217 . 250 ILE H H 8.41 0.010 1 1218 . 250 ILE CA C 59.7 0.5 1 1219 . 250 ILE CB C 41.3 0.5 1 1220 . 250 ILE C C 175.88 0.09 1 1221 . 251 THR N N 117.4 0.1 1 1222 . 251 THR H H 8.97 0.010 1 1223 . 251 THR CA C 59.0 0.5 1 1224 . 251 THR CB C 71.4 0.5 1 1225 . 251 THR C C 173.20 0.09 1 1226 . 252 VAL N N 120.9 0.1 1 1227 . 252 VAL H H 9.03 0.010 1 1228 . 252 VAL CA C 59.5 0.5 1 1229 . 252 VAL CB C 35.6 0.5 1 1230 . 252 VAL C C 173.83 0.09 1 1231 . 253 GLN N N 129.1 0.1 1 1232 . 253 GLN H H 8.47 0.010 1 1233 . 253 GLN CA C 55.7 0.5 1 1234 . 253 GLN CB C 31.6 0.5 1 1235 . 253 GLN C C 173.47 0.09 1 1236 . 254 GLN N N 125.9 0.1 1 1237 . 254 GLN H H 8.78 0.010 1 1238 . 254 GLN CA C 55.4 0.5 1 1239 . 254 GLN CB C 31.0 0.5 1 1240 . 254 GLN C C 175.23 0.09 1 1241 . 255 TYR N N 120.1 0.1 1 1242 . 255 TYR H H 7.58 0.010 1 1243 . 255 TYR CA C 58.2 0.5 1 1244 . 255 TYR CB C 41.5 0.5 1 1245 . 255 TYR C C 176.80 0.09 1 1246 . 256 ASP N N 119.3 0.1 1 1247 . 256 ASP H H 8.87 0.010 1 1248 . 256 ASP CA C 53.5 0.5 1 1249 . 256 ASP CB C 41.3 0.5 1 1250 . 256 ASP C C 177.41 0.09 1 1251 . 257 SER N N 116.7 0.1 1 1252 . 257 SER H H 8.73 0.010 1 1253 . 257 SER CA C 61.4 0.5 1 1254 . 257 SER CB C 63.0 0.5 1 1255 . 257 SER C C 175.08 0.09 1 1256 . 258 ASN N N 117.5 0.1 1 1257 . 258 ASN H H 7.91 0.010 1 1258 . 258 ASN CA C 53.4 0.5 1 1259 . 258 ASN CB C 39.5 0.5 1 1260 . 258 ASN C C 175.88 0.09 1 1261 . 259 GLY N N 111.3 0.1 1 1262 . 259 GLY H H 8.39 0.010 1 1263 . 259 GLY CA C 46.8 0.5 1 1264 . 259 GLY C C 174.80 0.09 1 1265 . 260 THR N N 114.6 0.1 1 1266 . 260 THR H H 9.34 0.010 1 1267 . 260 THR CA C 63.3 0.5 1 1268 . 260 THR CB C 70.3 0.5 1 1269 . 260 THR C C 174.62 0.09 1 1270 . 261 LYS N N 123.5 0.1 1 1271 . 261 LYS H H 8.39 0.010 1 1272 . 261 LYS CA C 54.9 0.5 1 1273 . 261 LYS CB C 35.2 0.5 1 1274 . 261 LYS C C 174.41 0.09 1 1275 . 262 LEU N N 124.2 0.1 1 1276 . 262 LEU H H 8.05 0.010 1 1277 . 262 LEU CA C 55.3 0.5 1 1278 . 262 LEU CB C 42.7 0.5 1 1279 . 262 LEU C C 177.03 0.09 1 1280 . 263 GLU N N 123.0 0.1 1 1281 . 263 GLU H H 8.62 0.010 1 1282 . 263 GLU CA C 54.7 0.5 1 1283 . 263 GLU CB C 33.1 0.5 1 1284 . 263 GLU C C 177.69 0.09 1 1285 . 264 GLY N N 113.0 0.1 1 1286 . 264 GLY H H 8.69 0.010 1 1287 . 264 GLY CA C 46.5 0.5 1 1288 . 264 GLY C C 173.58 0.09 1 1289 . 265 SER N N 118.5 0.1 1 1290 . 265 SER H H 8.12 0.010 1 1291 . 265 SER CA C 57.1 0.5 1 1292 . 265 SER CB C 65.6 0.5 1 1293 . 265 SER C C 173.12 0.09 1 1294 . 266 ALA N N 126.9 0.1 1 1295 . 266 ALA H H 8.44 0.010 1 1296 . 266 ALA CA C 52.2 0.5 1 1297 . 266 ALA CB C 18.7 0.5 1 1298 . 266 ALA C C 177.41 0.09 1 1299 . 267 VAL N N 123.6 0.1 1 1300 . 267 VAL H H 8.64 0.010 1 1301 . 267 VAL CA C 61.0 0.5 1 1302 . 267 VAL CB C 34.7 0.5 1 1303 . 267 VAL C C 175.08 0.09 1 1304 . 268 GLU N N 127.9 0.1 1 1305 . 268 GLU H H 8.55 0.010 1 1306 . 268 GLU CA C 56.7 0.5 1 1307 . 268 GLU CB C 31.0 0.5 1 1308 . 268 GLU C C 176.26 0.09 1 1309 . 269 ILE N N 129.2 0.1 1 1310 . 269 ILE H H 8.87 0.010 1 1311 . 269 ILE CA C 61.0 0.5 1 1312 . 269 ILE CB C 37.6 0.5 1 1313 . 269 ILE C C 177.10 0.09 1 1314 . 270 THR N N 118.3 0.1 1 1315 . 270 THR H H 9.38 0.010 1 1316 . 270 THR CA C 61.8 0.5 1 1317 . 270 THR CB C 71.4 0.5 1 1318 . 270 THR C C 173.23 0.09 1 1319 . 271 LYS N N 118.1 0.1 1 1320 . 271 LYS H H 7.28 0.010 1 1321 . 271 LYS CA C 54.6 0.5 1 1322 . 271 LYS CB C 36.0 0.5 1 1323 . 271 LYS C C 176.41 0.09 1 1324 . 272 LEU N N 126.0 0.1 1 1325 . 272 LEU H H 8.94 0.010 1 1326 . 272 LEU CA C 58.1 0.5 1 1327 . 272 LEU CB C 41.9 0.5 1 1328 . 272 LEU C C 179.42 0.09 1 1329 . 273 ASP N N 116.4 0.1 1 1330 . 273 ASP H H 8.81 0.010 1 1331 . 273 ASP CA C 57.2 0.5 1 1332 . 273 ASP CB C 40.4 0.5 1 1333 . 273 ASP C C 178.06 0.09 1 1334 . 274 GLU N N 117.0 0.1 1 1335 . 274 GLU H H 7.23 0.010 1 1336 . 274 GLU CA C 58.6 0.5 1 1337 . 274 GLU CB C 30.8 0.5 1 1338 . 274 GLU C C 179.60 0.09 1 1339 . 275 ILE N N 121.2 0.1 1 1340 . 275 ILE H H 7.33 0.010 1 1341 . 275 ILE CA C 64.7 0.5 1 1342 . 275 ILE CB C 37.6 0.5 1 1343 . 275 ILE C C 176.94 0.09 1 1344 . 276 LYS N N 118.9 0.1 1 1345 . 276 LYS H H 7.42 0.010 1 1346 . 276 LYS CA C 61.1 0.5 1 1347 . 276 LYS CB C 31.5 0.5 1 1348 . 276 LYS C C 178.92 0.09 1 1349 . 277 ASN N N 115.6 0.1 1 1350 . 277 ASN H H 8.03 0.010 1 1351 . 277 ASN CA C 55.8 0.5 1 1352 . 277 ASN CB C 38.3 0.5 1 1353 . 277 ASN C C 177.64 0.09 1 1354 . 278 ALA N N 122.2 0.1 1 1355 . 278 ALA H H 7.39 0.010 1 1356 . 278 ALA CA C 53.9 0.5 1 1357 . 278 ALA CB C 17.6 0.5 1 1358 . 278 ALA C C 177.17 0.09 1 1359 . 279 LEU N N 117.3 0.1 1 1360 . 279 LEU H H 7.31 0.010 1 1361 . 279 LEU CA C 54.1 0.5 1 1362 . 279 LEU CB C 41.6 0.5 1 1363 . 279 LEU C C 175.62 0.09 1 1364 . 280 LYS N N 124.6 0.1 1 1365 . 280 LYS H H 6.88 0.010 1 1366 . 280 LYS CA C 59.1 0.5 1 1367 . 280 LYS CB C 33.8 0.5 1 stop_ save_