data_4111 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Assignment of the Triple Labelled 30 kDa Cell-adhesion Domain from Enteropathogenic E.coli ; _BMRB_accession_number 4111 _BMRB_flat_file_name bmr4111.str _Entry_type original _Submission_date 1998-02-24 _Accession_date 1998-02-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represent the cell adhesion domain (residues 660-939) of intact Intimin. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kelly Geoff . . 2 Prasannan Sunil . . 3 Daniel Sarah . . 4 Frankel Gad . . 5 Dougan Gordon . . 6 Connerton Iain . . 7 Matthews Stephen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 247 "13C chemical shifts" 478 "15N chemical shifts" 247 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-01-21 original author . stop_ _Original_release_date 1999-01-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kelly, G., Prasannan, S., Daniel, S., Frankel, G., Dougan, G., Connerton, I., and Matthews, S., "Sequential Assignment of the Triple Labelled 30.1 kDa Cell-adhesion Domain of Intimin from Enteropathogenic E. coli," J. Biomol. NMR 12, 189-191 (1998). ; _Citation_title ; Sequential Assignment of the Triple Labelled 30.1 kDa Cell-adhesion Domain of Intimin from Enteropathogenic E. coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98399496 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kelly Geoff . . 2 Prasannan Sunil . . 3 Daniel Sarah . . 4 Frankel Gad . . 5 Dougan Gordon . . 6 Connerton Iain . . 7 Matthews Stephen . . stop_ _Journal_abbreviation 'J Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 189 _Page_last 191 _Year 1998 _Details . loop_ _Keyword deuteration intimin NMR 'nuclear magnetic resonance' protein 'resonance assignments' stop_ save_ ################################## # Molecular system description # ################################## save_system_Int-CAD _Saveframe_category molecular_system _Mol_system_name 'Intimin cell adhesion domain' _Abbreviation_common Int-CAD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Int-CAD $Int-CAD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'cell adhesion' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Int-CAD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Intimin cell adhesion domain' _Abbreviation_common Int-CAD _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 280 _Mol_residue_sequence ; ITEIKADKTTAVANGQDAIT YTVKVMKGDKPVSNQEVTFT TTLGKLSNSTEKTDTNGYAK VTLTSTTPGKSLVSARVSDV AVDVKAPEVEFFTTLTIDDG NIEIVGTGVKGKLPTVWLQY GQVNLKASGGNGKYTWRSAN PAIASVDASSGQVTLKEKGT TTISVISSDNQTATYTIATP NSLIVPNMSKRVTYNDAVNT CKNFGGKLPSSQNELENVFK AWGAANKYEYYKSSQTIISW VQQTAQDAKSGVASTYDLVK QNPLNNIKASESNAYATCVK ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 THR 3 GLU 4 ILE 5 LYS 6 ALA 7 ASP 8 LYS 9 THR 10 THR 11 ALA 12 VAL 13 ALA 14 ASN 15 GLY 16 GLN 17 ASP 18 ALA 19 ILE 20 THR 21 TYR 22 THR 23 VAL 24 LYS 25 VAL 26 MET 27 LYS 28 GLY 29 ASP 30 LYS 31 PRO 32 VAL 33 SER 34 ASN 35 GLN 36 GLU 37 VAL 38 THR 39 PHE 40 THR 41 THR 42 THR 43 LEU 44 GLY 45 LYS 46 LEU 47 SER 48 ASN 49 SER 50 THR 51 GLU 52 LYS 53 THR 54 ASP 55 THR 56 ASN 57 GLY 58 TYR 59 ALA 60 LYS 61 VAL 62 THR 63 LEU 64 THR 65 SER 66 THR 67 THR 68 PRO 69 GLY 70 LYS 71 SER 72 LEU 73 VAL 74 SER 75 ALA 76 ARG 77 VAL 78 SER 79 ASP 80 VAL 81 ALA 82 VAL 83 ASP 84 VAL 85 LYS 86 ALA 87 PRO 88 GLU 89 VAL 90 GLU 91 PHE 92 PHE 93 THR 94 THR 95 LEU 96 THR 97 ILE 98 ASP 99 ASP 100 GLY 101 ASN 102 ILE 103 GLU 104 ILE 105 VAL 106 GLY 107 THR 108 GLY 109 VAL 110 LYS 111 GLY 112 LYS 113 LEU 114 PRO 115 THR 116 VAL 117 TRP 118 LEU 119 GLN 120 TYR 121 GLY 122 GLN 123 VAL 124 ASN 125 LEU 126 LYS 127 ALA 128 SER 129 GLY 130 GLY 131 ASN 132 GLY 133 LYS 134 TYR 135 THR 136 TRP 137 ARG 138 SER 139 ALA 140 ASN 141 PRO 142 ALA 143 ILE 144 ALA 145 SER 146 VAL 147 ASP 148 ALA 149 SER 150 SER 151 GLY 152 GLN 153 VAL 154 THR 155 LEU 156 LYS 157 GLU 158 LYS 159 GLY 160 THR 161 THR 162 THR 163 ILE 164 SER 165 VAL 166 ILE 167 SER 168 SER 169 ASP 170 ASN 171 GLN 172 THR 173 ALA 174 THR 175 TYR 176 THR 177 ILE 178 ALA 179 THR 180 PRO 181 ASN 182 SER 183 LEU 184 ILE 185 VAL 186 PRO 187 ASN 188 MET 189 SER 190 LYS 191 ARG 192 VAL 193 THR 194 TYR 195 ASN 196 ASP 197 ALA 198 VAL 199 ASN 200 THR 201 CYS 202 LYS 203 ASN 204 PHE 205 GLY 206 GLY 207 LYS 208 LEU 209 PRO 210 SER 211 SER 212 GLN 213 ASN 214 GLU 215 LEU 216 GLU 217 ASN 218 VAL 219 PHE 220 LYS 221 ALA 222 TRP 223 GLY 224 ALA 225 ALA 226 ASN 227 LYS 228 TYR 229 GLU 230 TYR 231 TYR 232 LYS 233 SER 234 SER 235 GLN 236 THR 237 ILE 238 ILE 239 SER 240 TRP 241 VAL 242 GLN 243 GLN 244 THR 245 ALA 246 GLN 247 ASP 248 ALA 249 LYS 250 SER 251 GLY 252 VAL 253 ALA 254 SER 255 THR 256 TYR 257 ASP 258 LEU 259 VAL 260 LYS 261 GLN 262 ASN 263 PRO 264 LEU 265 ASN 266 ASN 267 ILE 268 LYS 269 ALA 270 SER 271 GLU 272 SER 273 ASN 274 ALA 275 TYR 276 ALA 277 THR 278 CYS 279 VAL 280 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1E5U "Nmr Representative Structure Of Intimin-190 (Int190) From Enteropathogenic E. Coli" 66.79 187 100.00 100.00 2.94e-130 PDB 1F00 "Crystal Structure Of C-Terminal 282-Residue Fragment Of Enteropathogenic E. Coli Intimin" 100.00 282 100.00 100.00 0.00e+00 PDB 1F02 "Crystal Structure Of C-Terminal 282-Residue Fragment Of Intimin In Complex With Translocated Intimin Receptor (Tir) Intimin-Bin" 100.00 282 100.00 100.00 0.00e+00 EMBL CAG29634 "intimin alpha-1 [Escherichia coli]" 71.07 199 100.00 100.00 2.61e-135 EMBL CAG29721 "intimin alpha-1, partial [Escherichia coli]" 71.07 199 100.00 100.00 2.61e-135 EMBL CAG29722 "intimin alpha-1 [Escherichia coli]" 71.07 202 100.00 100.00 2.04e-135 EMBL CAG29769 "intimin alpha-1, partial [Escherichia coli]" 71.07 199 100.00 100.00 2.61e-135 EMBL CAG29783 "intimin alpha-1, partial [Escherichia coli]" 71.07 202 100.00 100.00 2.04e-135 GB AAL83295 "intimin [Escherichia coli]" 95.00 266 99.25 99.25 0.00e+00 GB ACB11562 "intimin [Escherichia coli]" 87.14 260 99.59 99.59 1.23e-171 GB ACX48507 "intimin [Escherichia coli]" 91.79 257 99.61 99.61 0.00e+00 GB ACX48508 "intimin [Escherichia coli]" 91.79 257 98.83 99.22 2.97e-180 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 _Variant $Int-CAD 'E. coli' 562 Eubacteria . Escherichia coli 'EPEC O127:H6' E2348/69 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 $Int-CAD 'recombinant technology' 'E. coli' Escherichia 'Escherichia coli' 'EPEC o127:H6' plasmid pET 'pET contains the eae gene' 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 $Int-CAD 1.0 mM '[U-100% 15N; U-100% 13C, U-80% 2H]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX-500 _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . na temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449519 DSS H 1 'methyl protons' ppm 0.0 external direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329122 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name Int-CAD _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ILE H H 8.1 0.01 1 2 . 1 ILE N N 121.7 0.2 1 3 . 1 ILE CA C 62.9 0.2 1 4 . 1 ILE C C 176.2 0.2 1 5 . 2 THR H H 8.11 0.01 1 6 . 2 THR N N 116.6 0.2 1 7 . 2 THR CA C 60.4 0.2 1 8 . 2 THR C C 175.3 0.2 1 9 . 3 GLU H H 9.04 0.01 1 10 . 3 GLU N N 122.6 0.2 1 11 . 3 GLU CA C 55.00 0.2 1 12 . 3 GLU C C 175.00 0.2 1 13 . 4 ILE H H 8.43 0.01 1 14 . 4 ILE N N 119.8 0.2 1 15 . 4 ILE CA C 56.9 0.2 1 16 . 4 ILE C C 172.8 0.2 1 17 . 5 LYS H H 8.69 0.01 1 18 . 5 LYS N N 125.1 0.2 1 19 . 5 LYS CA C 54.00 0.2 1 20 . 5 LYS C C 174.00 0.2 1 21 . 6 ALA H H 8.27 0.01 1 22 . 6 ALA N N 123.3 0.2 1 23 . 6 ALA CA C 49.2 0.2 1 24 . 6 ALA C C 175.2 0.2 1 25 . 7 ASP H H 8.85 0.01 1 26 . 7 ASP N N 121.3 0.2 1 27 . 7 ASP CA C 55.1 0.2 1 28 . 7 ASP C C 175.3 0.2 1 29 . 8 LYS H H 7.63 0.01 1 30 . 8 LYS N N 118.7 0.2 1 31 . 8 LYS CA C 54.3 0.2 1 32 . 8 LYS C C 173.9 0.2 1 33 . 9 THR H H 8.14 0.01 1 34 . 9 THR N N 102.1 0.2 1 35 . 9 THR CA C 60.5 0.2 1 36 . 9 THR C C 175.3 0.2 1 37 . 10 THR H H 7.36 0.01 1 38 . 10 THR N N 112.7 0.2 1 39 . 10 THR CA C 58.7 0.2 1 40 . 10 THR C C 172.2 0.2 1 41 . 11 ALA H H 8.12 0.01 1 42 . 11 ALA N N 121.1 0.2 1 43 . 11 ALA CA C 50.3 0.2 1 44 . 11 ALA C C 176.1 0.2 1 45 . 12 VAL H H 10.1 0.01 1 46 . 12 VAL N N 123.5 0.2 1 47 . 12 VAL CA C 61.8 0.2 1 48 . 12 VAL C C 177.6 0.2 1 49 . 13 ALA H H 9.18 0.01 1 50 . 13 ALA N N 131.5 0.2 1 51 . 13 ALA CA C 48.9 0.2 1 52 . 13 ALA C C 176.5 0.2 1 53 . 14 ASN H H 8.46 0.01 1 54 . 14 ASN N N 117.1 0.2 1 55 . 14 ASN CA C 50.4 0.2 1 56 . 14 ASN C C 176.9 0.2 1 57 . 15 GLY H H 8.31 0.01 1 58 . 15 GLY N N 109.2 0.2 1 59 . 15 GLY CA C 45.4 0.2 1 60 . 15 GLY C C 172.00 0.2 1 61 . 16 GLN H H 8.17 0.01 1 62 . 16 GLN N N 117.8 0.2 1 63 . 16 GLN CA C 55.6 0.2 1 64 . 16 GLN C C 175.3 0.2 1 65 . 17 ASP H H 8.65 0.01 1 66 . 17 ASP N N 122.4 0.2 1 67 . 17 ASP CA C 54.9 0.2 1 68 . 17 ASP C C 174.9 0.2 1 69 . 18 ALA H H 7.94 0.01 1 70 . 18 ALA N N 127.00 0.2 1 71 . 18 ALA CA C 49.9 0.2 1 72 . 18 ALA C C 177.9 0.2 1 73 . 19 ILE H H 8.96 0.01 1 74 . 19 ILE N N 124.2 0.2 1 75 . 19 ILE CA C 60.4 0.2 1 76 . 19 ILE C C 175.5 0.2 1 77 . 20 THR H H 9.47 0.01 1 78 . 20 THR N N 125.1 0.2 1 79 . 20 THR CA C 61.9 0.2 1 80 . 20 THR C C 174.4 0.2 1 81 . 21 TYR H H 9.43 0.01 1 82 . 21 TYR N N 128.6 0.2 1 83 . 21 TYR CA C 56.3 0.2 1 84 . 21 TYR C C 175.00 0.2 1 85 . 22 THR H H 8.88 0.01 1 86 . 22 THR N N 115.2 0.2 1 87 . 22 THR CA C 60.9 0.2 1 88 . 22 THR C C 174.7 0.2 1 89 . 23 VAL H H 9.42 0.01 1 90 . 23 VAL N N 124.2 0.2 1 91 . 23 VAL CA C 58.6 0.2 1 92 . 23 VAL C C 173.1 0.2 1 93 . 24 LYS H H 8.08 0.01 1 94 . 24 LYS N N 124.8 0.2 1 95 . 24 LYS CA C 53.9 0.2 1 96 . 24 LYS C C 175.00 0.2 1 97 . 25 VAL H H 9.11 0.01 1 98 . 25 VAL N N 127.00 0.2 1 99 . 25 VAL CA C 60.4 0.2 1 100 . 25 VAL C C 174.8 0.2 1 101 . 26 MET H H 8.51 0.01 1 102 . 26 MET N N 121.8 0.2 1 103 . 26 MET CA C 53.3 0.2 1 104 . 26 MET C C 175.5 0.2 1 105 . 27 LYS H H 8.95 0.01 1 106 . 27 LYS N N 123.1 0.2 1 107 . 27 LYS CA C 55.00 0.2 1 108 . 27 LYS C C 176.7 0.2 1 109 . 28 GLY H H 8.87 0.01 1 110 . 28 GLY N N 118.2 0.2 1 111 . 28 GLY CA C 46.8 0.2 1 112 . 28 GLY C C 174.00 0.2 1 113 . 29 ASP H H 8.52 0.01 1 114 . 29 ASP N N 123.3 0.2 1 115 . 29 ASP CA C 53.4 0.2 1 116 . 29 ASP C C 175.3 0.2 1 117 . 30 LYS H H 7.73 0.01 1 118 . 30 LYS N N 119.6 0.2 1 119 . 30 LYS CA C 52.1 0.2 1 120 . 30 LYS C C 173.3 0.2 1 121 . 32 VAL H H 7.62 0.01 1 122 . 32 VAL N N 119.1 0.2 1 123 . 32 VAL CA C 62.00 0.2 1 124 . 32 VAL C C 175.3 0.2 1 125 . 33 SER H H 8.44 0.01 1 126 . 33 SER N N 122.8 0.2 1 127 . 33 SER CA C 56.2 0.2 1 128 . 33 SER C C 174.3 0.2 1 129 . 34 ASN H H 8.3 0.01 1 130 . 34 ASN N N 119.1 0.2 1 131 . 34 ASN CA C 54.2 0.2 1 132 . 35 GLN H H 8.39 0.01 1 133 . 35 GLN N N 117.8 0.2 1 134 . 35 GLN CA C 53.4 0.2 1 135 . 35 GLN C C 175.8 0.2 1 136 . 36 GLU H H 8.83 0.01 1 137 . 36 GLU N N 126.6 0.2 1 138 . 36 GLU CA C 57.1 0.2 1 139 . 36 GLU C C 175.3 0.2 1 140 . 37 VAL H H 9.15 0.01 1 141 . 37 VAL N N 128.4 0.2 1 142 . 37 VAL CA C 60.1 0.2 1 143 . 37 VAL C C 174.3 0.2 1 144 . 38 THR H H 8.65 0.01 1 145 . 38 THR N N 119.1 0.2 1 146 . 38 THR CA C 60.1 0.2 1 147 . 38 THR C C 173.8 0.2 1 148 . 39 PHE H H 9.16 0.01 1 149 . 39 PHE N N 123.7 0.2 1 150 . 39 PHE CA C 56.2 0.2 1 151 . 39 PHE C C 175.2 0.2 1 152 . 40 THR H H 8.73 0.01 1 153 . 40 THR N N 112.3 0.2 1 154 . 40 THR CA C 59.9 0.2 1 155 . 40 THR C C 172.6 0.2 1 156 . 41 THR H H 8.5 0.01 1 157 . 41 THR N N 113.8 0.2 1 158 . 41 THR CA C 57.8 0.2 1 159 . 41 THR C C 173.2 0.2 1 160 . 42 THR H H 7.62 0.01 1 161 . 42 THR N N 116.00 0.2 1 162 . 42 THR CA C 62.00 0.2 1 163 . 42 THR C C 174.9 0.2 1 164 . 43 LEU H H 7.79 0.01 1 165 . 43 LEU N N 124.6 0.2 1 166 . 43 LEU CA C 56.00 0.2 1 167 . 43 LEU C C 175.1 0.2 1 168 . 44 GLY H H 8.38 0.01 1 169 . 44 GLY N N 114.9 0.2 1 170 . 44 GLY CA C 43.1 0.2 1 171 . 44 GLY C C 172.2 0.2 1 172 . 45 LYS H H 8.96 0.01 1 173 . 45 LYS N N 119.8 0.2 1 174 . 45 LYS CA C 54.2 0.2 1 175 . 45 LYS C C 176.3 0.2 1 176 . 46 LEU H H 8.69 0.01 1 177 . 46 LEU N N 129.5 0.2 1 178 . 46 LEU CA C 53.00 0.2 1 179 . 46 LEU C C 179.00 0.2 1 180 . 47 SER H H 9.3 0.01 1 181 . 47 SER N N 118.00 0.2 1 182 . 47 SER CA C 60.3 0.2 1 183 . 47 SER C C 174.8 0.2 1 184 . 48 ASN H H 7.08 0.01 1 185 . 48 ASN N N 116.00 0.2 1 186 . 48 ASN CA C 52.4 0.2 1 187 . 48 ASN C C 173.00 0.2 1 188 . 49 SER H H 8.42 0.01 1 189 . 49 SER N N 112.5 0.2 1 190 . 49 SER CA C 59.4 0.2 1 191 . 49 SER C C 172.9 0.2 1 192 . 50 THR H H 7.6 0.01 1 193 . 50 THR N N 113.4 0.2 1 194 . 50 THR CA C 59.8 0.2 1 195 . 50 THR C C 173.7 0.2 1 196 . 51 GLU H H 8.91 0.01 1 197 . 51 GLU N N 122.9 0.2 1 198 . 51 GLU CA C 53.9 0.2 1 199 . 51 GLU C C 174.4 0.2 1 200 . 53 THR H H 8.55 0.01 1 201 . 53 THR N N 112.1 0.2 1 202 . 53 THR CA C 60.5 0.2 1 203 . 53 THR C C 176.4 0.2 1 204 . 54 ASP H H 8.95 0.01 1 205 . 54 ASP N N 123.5 0.2 1 206 . 54 ASP CA C 51.9 0.2 1 207 . 54 ASP C C 177.8 0.2 1 208 . 55 THR H H 7.77 0.01 1 209 . 55 THR N N 108.1 0.2 1 210 . 55 THR CA C 64.2 0.2 1 211 . 55 THR C C 174.8 0.2 1 212 . 56 ASN H H 8.31 0.01 1 213 . 56 ASN N N 117.1 0.2 1 214 . 56 ASN CA C 52.4 0.2 1 215 . 56 ASN C C 173.9 0.2 1 216 . 57 GLY H H 8.1 0.01 1 217 . 57 GLY N N 106.3 0.2 1 218 . 57 GLY CA C 44.6 0.2 1 219 . 57 GLY C C 173.1 0.2 1 220 . 58 TYR H H 8.29 0.01 1 221 . 58 TYR N N 116.7 0.2 1 222 . 58 TYR CA C 56.9 0.2 1 223 . 58 TYR C C 177.5 0.2 1 224 . 59 ALA H H 9.08 0.01 1 225 . 59 ALA N N 122.6 0.2 1 226 . 59 ALA CA C 50.5 0.2 1 227 . 59 ALA C C 175.00 0.2 1 228 . 60 LYS H H 8.44 0.01 1 229 . 60 LYS N N 120.2 0.2 1 230 . 60 LYS CA C 54.1 0.2 1 231 . 60 LYS C C 175.2 0.2 1 232 . 62 THR H H 8.24 0.01 1 233 . 62 THR N N 111.9 0.2 1 234 . 62 THR CA C 58.9 0.2 1 235 . 62 THR C C 173.1 0.2 1 236 . 63 LEU H H 9.34 0.01 1 237 . 63 LEU N N 124.4 0.2 1 238 . 63 LEU CA C 53.4 0.2 1 239 . 63 LEU C C 175.6 0.2 1 240 . 64 THR H H 8.08 0.01 1 241 . 64 THR N N 114.1 0.2 1 242 . 64 THR CA C 58.9 0.2 1 243 . 64 THR C C 172.9 0.2 1 244 . 65 SER H H 9.07 0.01 1 245 . 65 SER N N 111.2 0.2 1 246 . 65 SER CA C 57.1 0.2 1 247 . 65 SER C C 175.4 0.2 1 248 . 66 THR H H 7.88 0.01 1 249 . 66 THR N N 114.5 0.2 1 250 . 66 THR CA C 60.8 0.2 1 251 . 69 GLY H H 8.18 0.01 1 252 . 69 GLY N N 106.8 0.2 1 253 . 69 GLY CA C 43.4 0.2 1 254 . 69 GLY C C 172.6 0.2 1 255 . 70 LYS H H 8.19 0.01 1 256 . 70 LYS N N 118.5 0.2 1 257 . 70 LYS CA C 54.9 0.2 1 258 . 70 LYS C C 176.4 0.2 1 259 . 71 SER H H 8.68 0.01 1 260 . 71 SER N N 113.8 0.2 1 261 . 71 SER CA C 56.9 0.2 1 262 . 71 SER C C 174.00 0.2 1 263 . 72 LEU H H 8.43 0.01 1 264 . 72 LEU N N 131.9 0.2 1 265 . 72 LEU CA C 53.6 0.2 1 266 . 72 LEU C C 175.5 0.2 1 267 . 73 VAL H H 7.66 0.01 1 268 . 73 VAL N N 130.1 0.2 1 269 . 73 VAL CA C 60.3 0.2 1 270 . 73 VAL C C 174.1 0.2 1 271 . 74 SER H H 8.52 0.01 1 272 . 74 SER N N 119.8 0.2 1 273 . 74 SER CA C 55.6 0.2 1 274 . 74 SER C C 175.00 0.2 1 275 . 75 ALA H H 8.8 0.01 1 276 . 75 ALA N N 123.1 0.2 1 277 . 75 ALA CA C 49.2 0.2 1 278 . 75 ALA C C 175.00 0.2 1 279 . 76 ARG H H 8.33 0.01 1 280 . 76 ARG N N 117.4 0.2 1 281 . 76 ARG CA C 54.4 0.2 1 282 . 76 ARG C C 175.5 0.2 1 283 . 78 SER H H 8.81 0.01 1 284 . 78 SER N N 123.3 0.2 1 285 . 78 SER CA C 60.8 0.2 1 286 . 79 ASP H H 8.09 0.01 1 287 . 79 ASP N N 116.9 0.2 1 288 . 79 ASP CA C 55.2 0.2 1 289 . 79 ASP C C 175.7 0.2 1 290 . 80 VAL H H 7.44 0.01 1 291 . 80 VAL N N 116.7 0.2 1 292 . 80 VAL CA C 60.9 0.2 1 293 . 80 VAL C C 175.6 0.2 1 294 . 81 ALA H H 8.55 0.01 1 295 . 81 ALA N N 129.2 0.2 1 296 . 81 ALA CA C 52.1 0.2 1 297 . 81 ALA C C 176.6 0.2 1 298 . 82 VAL H H 7.51 0.01 1 299 . 82 VAL N N 118.2 0.2 1 300 . 82 VAL CA C 60.8 0.2 1 301 . 82 VAL C C 174.1 0.2 1 302 . 83 ASP H H 8.31 0.01 1 303 . 83 ASP N N 124.6 0.2 1 304 . 83 ASP CA C 53.1 0.2 1 305 . 83 ASP C C 175.3 0.2 1 306 . 84 VAL H H 9.04 0.01 1 307 . 84 VAL N N 122.6 0.2 1 308 . 84 VAL CA C 61.5 0.2 1 309 . 84 VAL C C 175.00 0.2 1 310 . 85 LYS H H 8.33 0.01 1 311 . 85 LYS N N 124.6 0.2 1 312 . 85 LYS CA C 55.7 0.2 1 313 . 85 LYS C C 176.3 0.2 1 314 . 86 ALA H H 8.64 0.01 1 315 . 86 ALA N N 125.7 0.2 1 316 . 86 ALA CA C 49.4 0.2 1 317 . 86 ALA C C 173.9 0.2 1 318 . 88 GLU H H 8.41 0.01 1 319 . 88 GLU N N 122.6 0.2 1 320 . 88 GLU CA C 57.3 0.2 1 321 . 88 GLU C C 175.6 0.2 1 322 . 89 VAL H H 7.79 0.01 1 323 . 89 VAL N N 115.8 0.2 1 324 . 89 VAL CA C 58.4 0.2 1 325 . 89 VAL C C 174.2 0.2 1 326 . 90 GLU H H 7.81 0.01 1 327 . 90 GLU N N 119.1 0.2 1 328 . 90 GLU CA C 54.9 0.2 1 329 . 90 GLU C C 172.9 0.2 1 330 . 91 PHE H H 8.53 0.01 1 331 . 91 PHE N N 119.7 0.2 1 332 . 91 PHE CA C 55.3 0.2 1 333 . 91 PHE C C 173.5 0.2 1 334 . 92 PHE H H 8.91 0.01 1 335 . 92 PHE N N 119.9 0.2 1 336 . 92 PHE CA C 56.4 0.2 1 337 . 92 PHE C C 170.00 0.2 1 338 . 93 THR H H 9.19 0.01 1 339 . 93 THR N N 116.9 0.2 1 340 . 93 THR CA C 62.7 0.2 1 341 . 93 THR C C 175.4 0.2 1 342 . 94 THR H H 8.48 0.01 1 343 . 94 THR N N 122.9 0.2 1 344 . 94 THR CA C 63.7 0.2 1 345 . 94 THR C C 173.6 0.2 1 346 . 95 LEU H H 8.35 0.01 1 347 . 95 LEU N N 130.4 0.2 1 348 . 95 LEU CA C 53.9 0.2 1 349 . 95 LEU C C 175.5 0.2 1 350 . 96 THR H H 8.95 0.01 1 351 . 96 THR N N 118.9 0.2 1 352 . 96 THR CA C 60.9 0.2 1 353 . 96 THR C C 172.7 0.2 1 354 . 97 ILE H H 8.31 0.01 1 355 . 97 ILE N N 120.9 0.2 1 356 . 97 ILE CA C 60.3 0.2 1 357 . 97 ILE C C 175.4 0.2 1 358 . 98 ASP H H 8.16 0.01 1 359 . 98 ASP N N 125.9 0.2 1 360 . 98 ASP CA C 52.7 0.2 1 361 . 98 ASP C C 176.6 0.2 1 362 . 99 ASP H H 8.6 0.01 1 363 . 99 ASP N N 125.5 0.2 1 364 . 99 ASP CA C 54.8 0.2 1 365 . 99 ASP C C 175.3 0.2 1 366 . 100 GLY H H 8.3 0.01 1 367 . 100 GLY N N 104.8 0.2 1 368 . 100 GLY CA C 43.9 0.2 1 369 . 100 GLY C C 173.3 0.2 1 370 . 101 ASN H H 7.01 0.01 1 371 . 101 ASN N N 119.6 0.2 1 372 . 101 ASN CA C 51.5 0.2 1 373 . 101 ASN C C 173.9 0.2 1 374 . 102 ILE H H 8.59 0.01 1 375 . 102 ILE N N 124.6 0.2 1 376 . 102 ILE CA C 61.7 0.2 1 377 . 102 ILE C C 175.7 0.2 1 378 . 103 GLU H H 8.15 0.01 1 379 . 103 GLU N N 128.6 0.2 1 380 . 103 GLU CA C 54.00 0.2 1 381 . 103 GLU C C 175.7 0.2 1 382 . 104 ILE H H 8.68 0.01 1 383 . 104 ILE N N 129.00 0.2 1 384 . 104 ILE CA C 60.2 0.2 1 385 . 104 ILE C C 178.6 0.2 1 386 . 105 VAL H H 8.19 0.01 1 387 . 105 VAL N N 128.1 0.2 1 388 . 105 VAL CA C 66.5 0.2 1 389 . 105 VAL C C 177.8 0.2 1 390 . 106 GLY H H 8.17 0.01 1 391 . 106 GLY N N 129.7 0.2 1 392 . 106 GLY CA C 45.5 0.2 1 393 . 106 GLY C C 173.5 0.2 1 394 . 107 THR H H 6.74 0.01 1 395 . 107 THR N N 103.3 0.2 1 396 . 107 THR CA C 60.2 0.2 1 397 . 107 THR C C 176.1 0.2 1 398 . 108 GLY H H 8.47 0.01 1 399 . 108 GLY N N 111.2 0.2 1 400 . 108 GLY CA C 45.00 0.2 1 401 . 108 GLY C C 173.6 0.2 1 402 . 109 VAL H H 7.66 0.01 1 403 . 109 VAL N N 122.2 0.2 1 404 . 109 VAL CA C 62.8 0.2 1 405 . 109 VAL C C 175.00 0.2 1 406 . 110 LYS H H 8.16 0.01 1 407 . 110 LYS N N 124.8 0.2 1 408 . 110 LYS CA C 53.7 0.2 1 409 . 110 LYS C C 176.9 0.2 1 410 . 111 GLY H H 8.27 0.01 1 411 . 111 GLY N N 110.5 0.2 1 412 . 111 GLY CA C 45.4 0.2 1 413 . 111 GLY C C 172.8 0.2 1 414 . 112 LYS H H 8.1 0.01 1 415 . 112 LYS N N 119.6 0.2 1 416 . 112 LYS CA C 55.4 0.2 1 417 . 112 LYS C C 177.7 0.2 1 418 . 113 LEU H H 8.27 0.01 1 419 . 113 LEU N N 124.6 0.2 1 420 . 113 LEU CA C 53.2 0.2 1 421 . 113 LEU C C 175.6 0.2 1 422 . 115 THR H H 8.21 0.01 1 423 . 115 THR N N 122.8 0.2 1 424 . 115 THR CA C 60.7 0.2 1 425 . 115 THR C C 170.6 0.2 1 426 . 116 VAL H H 8.67 0.01 1 427 . 116 VAL N N 119.7 0.2 1 428 . 116 VAL CA C 61.8 0.2 1 429 . 116 VAL C C 175.5 0.2 1 430 . 120 TYR H H 8.63 0.01 1 431 . 120 TYR N N 120.4 0.2 1 432 . 121 GLY H H 8.05 0.01 1 433 . 121 GLY N N 104.6 0.2 1 434 . 121 GLY CA C 44.2 0.2 1 435 . 121 GLY C C 170.9 0.2 1 436 . 122 GLN H H 6.45 0.01 1 437 . 122 GLN N N 118.00 0.2 1 438 . 122 GLN CA C 53.7 0.2 1 439 . 122 GLN C C 175.1 0.2 1 440 . 123 VAL H H 8.81 0.01 1 441 . 123 VAL N N 111.6 0.2 1 442 . 123 VAL CA C 57.2 0.2 1 443 . 123 VAL C C 173.5 0.2 1 444 . 124 ASN H H 9.47 0.01 1 445 . 124 ASN N N 120.00 0.2 1 446 . 124 ASN CA C 51.6 0.2 1 447 . 124 ASN C C 174.9 0.2 1 448 . 125 LEU H H 7.25 0.01 1 449 . 125 LEU N N 124.00 0.2 1 450 . 125 LEU CA C 53.3 0.2 1 451 . 125 LEU C C 175.5 0.2 1 452 . 126 LYS H H 9.02 0.01 1 453 . 126 LYS N N 121.1 0.2 1 454 . 126 LYS CA C 53.9 0.2 1 455 . 126 LYS C C 174.8 0.2 1 456 . 127 ALA H H 8.77 0.01 1 457 . 127 ALA N N 127.3 0.2 1 458 . 127 ALA CA C 49.2 0.2 1 459 . 127 ALA C C 175.9 0.2 1 460 . 128 SER H H 8.49 0.01 1 461 . 128 SER N N 112.7 0.2 1 462 . 128 SER CA C 56.8 0.2 1 463 . 128 SER C C 173.2 0.2 1 464 . 129 GLY H H 8.48 0.01 1 465 . 129 GLY N N 106.6 0.2 1 466 . 129 GLY CA C 43.4 0.2 1 467 . 129 GLY C C 176.6 0.2 1 468 . 130 GLY H H 8.27 0.01 1 469 . 130 GLY N N 104.6 0.2 1 470 . 130 GLY CA C 45.9 0.2 1 471 . 130 GLY C C 172.9 0.2 1 472 . 131 ASN H H 7.92 0.01 1 473 . 131 ASN N N 120.2 0.2 1 474 . 131 ASN CA C 51.2 0.2 1 475 . 131 ASN C C 176.00 0.2 1 476 . 132 GLY H H 6.91 0.01 1 477 . 132 GLY N N 103.00 0.2 1 478 . 132 GLY CA C 44.5 0.2 1 479 . 132 GLY C C 171.1 0.2 1 480 . 133 LYS H H 7.38 0.01 1 481 . 133 LYS N N 121.1 0.2 1 482 . 133 LYS CA C 54.4 0.2 1 483 . 133 LYS C C 175.2 0.2 1 484 . 134 TYR H H 7.86 0.01 1 485 . 134 TYR N N 122.9 0.2 1 486 . 134 TYR CA C 54.00 0.2 1 487 . 134 TYR C C 176.5 0.2 1 488 . 135 THR H H 8.47 0.01 1 489 . 135 THR N N 116.9 0.2 1 490 . 135 THR CA C 61.3 0.2 1 491 . 135 THR C C 172.8 0.2 1 492 . 136 TRP H H 9.29 0.01 1 493 . 136 TRP N N 127.3 0.2 1 494 . 136 TRP CA C 56.1 0.2 1 495 . 136 TRP C C 176.9 0.2 1 496 . 137 ARG H H 9.4 0.01 1 497 . 137 ARG N N 120.2 0.2 1 498 . 137 ARG CA C 54.8 0.2 1 499 . 137 ARG C C 174.00 0.2 1 500 . 138 SER H H 8.87 0.01 1 501 . 138 SER N N 115.8 0.2 1 502 . 138 SER CA C 54.2 0.2 1 503 . 138 SER C C 175.3 0.2 1 504 . 139 ALA H H 8.47 0.01 1 505 . 139 ALA N N 127.9 0.2 1 506 . 139 ALA CA C 53.5 0.2 1 507 . 139 ALA C C 177.5 0.2 1 508 . 140 ASN H H 7.74 0.01 1 509 . 140 ASN N N 111.9 0.2 1 510 . 140 ASN CA C 50.4 0.2 1 511 . 144 ALA H H 7.24 0.01 1 512 . 144 ALA N N 117.6 0.2 1 513 . 144 ALA CA C 51.1 0.2 1 514 . 144 ALA C C 174.6 0.2 1 515 . 145 SER H H 8.66 0.01 1 516 . 145 SER N N 118.2 0.2 1 517 . 145 SER CA C 55.4 0.2 1 518 . 145 SER C C 172.7 0.2 1 519 . 146 VAL H H 9.14 0.01 1 520 . 146 VAL N N 119.6 0.2 1 521 . 146 VAL CA C 57.2 0.2 1 522 . 146 VAL C C 173.1 0.2 1 523 . 147 ASP H H 8.17 0.01 1 524 . 147 ASP N N 129.2 0.2 1 525 . 147 ASP CA C 54.2 0.2 1 526 . 147 ASP C C 176.9 0.2 1 527 . 148 ALA H H 8.75 0.01 1 528 . 148 ALA N N 128.8 0.2 1 529 . 148 ALA CA C 54.5 0.2 1 530 . 148 ALA C C 178.6 0.2 1 531 . 149 SER H H 8.39 0.01 1 532 . 149 SER N N 107.4 0.2 1 533 . 149 SER CA C 58.8 0.2 1 534 . 149 SER C C 176.6 0.2 1 535 . 150 SER H H 8.82 0.01 1 536 . 150 SER N N 116.5 0.2 1 537 . 150 SER CA C 58.5 0.2 1 538 . 150 SER C C 176.1 0.2 1 539 . 151 GLY H H 7.37 0.01 1 540 . 151 GLY N N 112.1 0.2 1 541 . 151 GLY CA C 54.00 0.2 1 542 . 151 GLY C C 171.4 0.2 1 543 . 152 GLN H H 7.21 0.01 1 544 . 152 GLN N N 116.7 0.2 1 545 . 152 GLN CA C 55.6 0.2 1 546 . 152 GLN C C 175.9 0.2 1 547 . 153 VAL H H 9.85 0.01 1 548 . 153 VAL N N 134.5 0.2 1 549 . 153 VAL CA C 59.9 0.2 1 550 . 154 THR H H 8.49 0.01 1 551 . 154 THR N N 112.7 0.2 1 552 . 154 THR CA C 57.8 0.2 1 553 . 154 THR C C 171.00 0.2 1 554 . 156 LYS H H 8.53 0.01 1 555 . 156 LYS N N 120.2 0.2 1 556 . 156 LYS C C 171.6 0.2 1 557 . 157 GLU H H 8.08 0.01 1 558 . 157 GLU N N 116.6 0.2 1 559 . 157 GLU C C 171.2 0.2 1 560 . 158 LYS H H 8.87 0.01 1 561 . 158 LYS N N 119.1 0.2 1 562 . 158 LYS CA C 56.4 0.2 1 563 . 158 LYS C C 175.1 0.2 1 564 . 159 GLY H H 7.15 0.01 1 565 . 159 GLY N N 114.3 0.2 1 566 . 159 GLY CA C 44.6 0.2 1 567 . 159 GLY C C 168.2 0.2 1 568 . 160 THR H H 7.84 0.01 1 569 . 160 THR N N 109.6 0.2 1 570 . 160 THR CA C 56.8 0.2 1 571 . 160 THR C C 173.5 0.2 1 572 . 161 THR H H 7.82 0.01 1 573 . 161 THR N N 117.6 0.2 1 574 . 161 THR CA C 60.00 0.2 1 575 . 161 THR C C 171.7 0.2 1 576 . 162 THR H H 8.15 0.01 1 577 . 162 THR N N 115.6 0.2 1 578 . 162 THR CA C 60.6 0.2 1 579 . 162 THR C C 173.4 0.2 1 580 . 163 ILE H H 9.55 0.01 1 581 . 163 ILE N N 128.1 0.2 1 582 . 163 ILE CA C 56.8 0.2 1 583 . 163 ILE C C 174.9 0.2 1 584 . 164 SER H H 9.44 0.01 1 585 . 164 SER N N 120.7 0.2 1 586 . 164 SER CA C 56.1 0.2 1 587 . 169 ASP H H 9.13 0.01 1 588 . 169 ASP N N 118.00 0.2 1 589 . 169 ASP CA C 53.6 0.2 1 590 . 169 ASP C C 173.7 0.2 1 591 . 170 ASN H H 8.32 0.01 1 592 . 170 ASN N N 113.4 0.2 1 593 . 170 ASN CA C 53.8 0.2 1 594 . 170 ASN C C 174.6 0.2 1 595 . 171 GLN H H 6.95 0.01 1 596 . 171 GLN N N 116.00 0.2 1 597 . 171 GLN CA C 55.3 0.2 1 598 . 171 GLN C C 174.2 0.2 1 599 . 172 THR H H 8.31 0.01 1 600 . 172 THR N N 113.4 0.2 1 601 . 172 THR CA C 60.6 0.2 1 602 . 172 THR C C 173.3 0.2 1 603 . 173 ALA H H 8.91 0.01 1 604 . 173 ALA N N 128.4 0.2 1 605 . 173 ALA CA C 50.4 0.2 1 606 . 173 ALA C C 175.6 0.2 1 607 . 174 THR H H 8.32 0.01 1 608 . 174 THR N N 109.00 0.2 1 609 . 174 THR CA C 59.9 0.2 1 610 . 174 THR C C 173.7 0.2 1 611 . 175 TYR H H 9.34 0.01 1 612 . 175 TYR N N 123.2 0.2 1 613 . 175 TYR CA C 56.6 0.2 1 614 . 175 TYR C C 173.4 0.2 1 615 . 176 THR H H 8.31 0.01 1 616 . 176 THR N N 126.4 0.2 1 617 . 176 THR CA C 62.4 0.2 1 618 . 176 THR C C 172.4 0.2 1 619 . 177 ILE H H 8.51 0.01 1 620 . 177 ILE N N 127.5 0.2 1 621 . 177 ILE CA C 60.4 0.2 1 622 . 177 ILE C C 174.5 0.2 1 623 . 178 ALA H H 8.5 0.01 1 624 . 178 ALA N N 133.2 0.2 1 625 . 178 ALA CA C 51.00 0.2 1 626 . 178 ALA C C 176.00 0.2 1 627 . 179 THR H H 7.78 0.01 1 628 . 179 THR N N 117.8 0.2 1 629 . 179 THR CA C 60.00 0.2 1 630 . 179 THR C C 173.3 0.2 1 631 . 181 ASN H H 8.94 0.01 1 632 . 181 ASN N N 116.9 0.2 1 633 . 181 ASN CA C 55.4 0.2 1 634 . 181 ASN C C 176.9 0.2 1 635 . 182 SER H H 7.09 0.01 1 636 . 182 SER N N 107.4 0.2 1 637 . 182 SER CA C 56.5 0.2 1 638 . 182 SER C C 170.5 0.2 1 639 . 183 LEU H H 9.14 0.01 1 640 . 183 LEU N N 125.3 0.2 1 641 . 183 LEU CA C 52.6 0.2 1 642 . 183 LEU C C 173.5 0.2 1 643 . 184 ILE H H 8.81 0.01 1 644 . 184 ILE N N 126.5 0.2 1 645 . 184 ILE CA C 58.3 0.2 1 646 . 187 ASN H H 8.2 0.01 1 647 . 187 ASN N N 123.5 0.2 1 648 . 187 ASN CA C 53.1 0.2 1 649 . 187 ASN C C 175.5 0.2 1 650 . 188 MET H H 8.38 0.01 1 651 . 188 MET N N 120.9 0.2 1 652 . 188 MET CA C 54.1 0.2 1 653 . 188 MET C C 177.00 0.2 1 654 . 189 SER H H 8.3 0.01 1 655 . 189 SER N N 115.4 0.2 1 656 . 189 SER CA C 61.4 0.2 1 657 . 189 SER C C 179.2 0.2 1 658 . 190 LYS H H 7.25 0.01 1 659 . 190 LYS N N 112.7 0.2 1 660 . 190 LYS CA C 59.4 0.2 1 661 . 190 LYS C C 174.5 0.2 1 662 . 191 ARG H H 8.4 0.01 1 663 . 191 ARG N N 121.1 0.2 1 664 . 191 ARG CA C 56.3 0.2 1 665 . 191 ARG C C 175.9 0.2 1 666 . 192 VAL H H 9.01 0.01 1 667 . 192 VAL N N 112.1 0.2 1 668 . 192 VAL CA C 58.7 0.2 1 669 . 192 VAL C C 177.3 0.2 1 670 . 193 THR H H 8.56 0.01 1 671 . 193 THR N N 112.3 0.2 1 672 . 193 THR CA C 60.9 0.2 1 673 . 193 THR C C 174.5 0.2 1 674 . 194 TYR H H 7.58 0.01 1 675 . 194 TYR N N 121.5 0.2 1 676 . 194 TYR CA C 61.8 0.2 1 677 . 194 TYR C C 176.6 0.2 1 678 . 195 ASN H H 8.56 0.01 1 679 . 195 ASN N N 114.9 0.2 1 680 . 195 ASN CA C 55.5 0.2 1 681 . 195 ASN C C 178.2 0.2 1 682 . 196 ASP H H 7.49 0.01 1 683 . 196 ASP N N 119.1 0.2 1 684 . 196 ASP CA C 56.5 0.2 1 685 . 196 ASP C C 179.1 0.2 1 686 . 197 ALA H H 8.3 0.01 1 687 . 197 ALA N N 126.6 0.2 1 688 . 197 ALA CA C 55.00 0.2 1 689 . 197 ALA C C 178.1 0.2 1 690 . 198 VAL H H 7.88 0.01 1 691 . 198 VAL N N 118.2 0.2 1 692 . 198 VAL CA C 66.1 0.2 1 693 . 198 VAL C C 179.5 0.2 1 694 . 199 ASN H H 7.49 0.01 1 695 . 199 ASN N N 117.1 0.2 1 696 . 199 ASN CA C 55.9 0.2 1 697 . 199 ASN C C 177.2 0.2 1 698 . 200 THR H H 8.6 0.01 1 699 . 200 THR N N 118.9 0.2 1 700 . 200 THR CA C 66.6 0.2 1 701 . 200 THR C C 176.7 0.2 1 702 . 201 CYS H H 8.31 0.01 1 703 . 201 CYS N N 116.9 0.2 1 704 . 201 CYS CA C 55.2 0.2 1 705 . 201 CYS C C 177.2 0.2 1 706 . 202 LYS H H 8.3 0.01 1 707 . 202 LYS N N 123.1 0.2 1 708 . 202 LYS CA C 59.3 0.2 1 709 . 202 LYS C C 180.4 0.2 1 710 . 203 ASN H H 8.14 0.01 1 711 . 203 ASN N N 118.9 0.2 1 712 . 203 ASN CA C 55.2 0.2 1 713 . 203 ASN C C 176.3 0.2 1 714 . 204 PHE H H 7.58 0.01 1 715 . 204 PHE N N 117.1 0.2 1 716 . 204 PHE CA C 56.3 0.2 1 717 . 204 PHE C C 175.2 0.2 1 718 . 205 GLY H H 7.89 0.01 1 719 . 205 GLY N N 106.8 0.2 1 720 . 205 GLY CA C 45.1 0.2 1 721 . 205 GLY C C 174.7 0.2 1 722 . 206 GLY H H 8.21 0.01 1 723 . 206 GLY N N 107.00 0.2 1 724 . 206 GLY CA C 43.8 0.2 1 725 . 206 GLY C C 171.8 0.2 1 726 . 207 LYS H H 8.49 0.01 1 727 . 207 LYS N N 117.4 0.2 1 728 . 207 LYS C C 175.4 0.2 1 729 . 210 SER H H 9.55 0.01 1 730 . 210 SER N N 119.1 0.2 1 731 . 210 SER CA C 60.4 0.2 1 732 . 210 SER C C 173.9 0.2 1 733 . 211 SER H H 7.5 0.01 1 734 . 211 SER N N 109.9 0.2 1 735 . 211 SER CA C 56.9 0.2 1 736 . 211 SER C C 174.6 0.2 1 737 . 212 GLN H H 9.64 0.01 1 738 . 212 GLN N N 119.8 0.2 1 739 . 212 GLN CA C 58.9 0.2 1 740 . 212 GLN C C 177.5 0.2 1 741 . 213 ASN H H 8.25 0.01 1 742 . 213 ASN N N 116.3 0.2 1 743 . 213 ASN CA C 55.7 0.2 1 744 . 213 ASN C C 176.2 0.2 1 745 . 214 GLU H H 7.68 0.01 1 746 . 214 GLU N N 119.6 0.2 1 747 . 214 GLU CA C 59.4 0.2 1 748 . 214 GLU C C 179.3 0.2 1 749 . 215 LEU H H 6.59 0.01 1 750 . 215 LEU N N 114.1 0.2 1 751 . 215 LEU CA C 55.9 0.2 1 752 . 215 LEU C C 178.2 0.2 1 753 . 216 GLU H H 8.36 0.01 1 754 . 216 GLU N N 123.9 0.2 1 755 . 216 GLU CA C 58.5 0.2 1 756 . 216 GLU C C 176.7 0.2 1 757 . 217 ASN H H 8.00 0.01 1 758 . 217 ASN N N 116.00 0.2 1 759 . 217 ASN CA C 55.6 0.2 1 760 . 217 ASN C C 176.1 0.2 1 761 . 218 VAL H H 7.26 0.01 1 762 . 218 VAL N N 121.00 0.2 1 763 . 218 VAL CA C 66.00 0.2 1 764 . 218 VAL C C 174.8 0.2 1 765 . 219 PHE H H 8.14 0.01 1 766 . 219 PHE N N 122.8 0.2 1 767 . 219 PHE CA C 60.8 0.2 1 768 . 219 PHE C C 170.6 0.2 1 769 . 220 LYS H H 9.08 0.01 1 770 . 220 LYS N N 119.3 0.2 1 771 . 220 LYS CA C 58.9 0.2 1 772 . 220 LYS C C 177.2 0.2 1 773 . 221 ALA H H 7.24 0.01 1 774 . 221 ALA N N 118.00 0.2 1 775 . 221 ALA C C 178.6 0.2 1 776 . 222 TRP H H 8.4 0.01 1 777 . 222 TRP N N 112.7 0.2 1 778 . 222 TRP CA C 57.4 0.2 1 779 . 222 TRP C C 175.7 0.2 1 780 . 223 GLY H H 8.61 0.01 1 781 . 223 GLY N N 111.6 0.2 1 782 . 223 GLY CA C 42.8 0.2 1 783 . 223 GLY C C 169.9 0.2 1 784 . 224 ALA H H 7.71 0.01 1 785 . 224 ALA N N 118.2 0.2 1 786 . 224 ALA CA C 52.00 0.2 1 787 . 224 ALA C C 181.00 0.2 1 788 . 225 ALA H H 7.94 0.01 1 789 . 225 ALA N N 121.3 0.2 1 790 . 225 ALA CA C 54.3 0.2 1 791 . 225 ALA C C 177.00 0.2 1 792 . 226 ASN H H 7.37 0.01 1 793 . 226 ASN N N 107.7 0.2 1 794 . 226 ASN CA C 53.1 0.2 1 795 . 226 ASN C C 175.5 0.2 1 796 . 227 LYS H H 7.47 0.01 1 797 . 227 LYS N N 116.6 0.2 1 798 . 227 LYS CA C 61.00 0.2 1 799 . 227 LYS C C 173.4 0.2 1 800 . 229 GLU H H 8.00 0.01 1 801 . 229 GLU N N 123.1 0.2 1 802 . 229 GLU CA C 59.3 0.2 1 803 . 229 GLU C C 178.6 0.2 1 804 . 230 TYR H H 9.02 0.01 1 805 . 230 TYR N N 117.6 0.2 1 806 . 230 TYR CA C 60.9 0.2 1 807 . 230 TYR C C 176.00 0.2 1 808 . 231 TYR H H 7.16 0.01 1 809 . 231 TYR N N 111.2 0.2 1 810 . 231 TYR CA C 55.2 0.2 1 811 . 231 TYR C C 177.6 0.2 1 812 . 232 LYS H H 7.17 0.01 1 813 . 232 LYS N N 120.2 0.2 1 814 . 232 LYS CA C 58.9 0.2 1 815 . 232 LYS C C 177.4 0.2 1 816 . 233 SER H H 8.24 0.01 1 817 . 233 SER N N 112.3 0.2 1 818 . 233 SER CA C 58.00 0.2 1 819 . 235 GLN H H 8.83 0.01 1 820 . 235 GLN N N 120.7 0.2 1 821 . 235 GLN CA C 55.1 0.2 1 822 . 235 GLN C C 175.2 0.2 1 823 . 236 THR H H 7.45 0.01 1 824 . 236 THR N N 111.4 0.2 1 825 . 236 THR CA C 59.1 0.2 1 826 . 236 THR C C 172.5 0.2 1 827 . 237 ILE H H 9.22 0.01 1 828 . 237 ILE N N 128.4 0.2 1 829 . 237 ILE CA C 60.00 0.2 1 830 . 237 ILE C C 175.9 0.2 1 831 . 238 ILE H H 7.22 0.01 1 832 . 238 ILE N N 127.3 0.2 1 833 . 238 ILE CA C 61.7 0.2 1 834 . 238 ILE C C 174.00 0.2 1 835 . 239 SER H H 8.99 0.01 1 836 . 239 SER N N 124.8 0.2 1 837 . 239 SER CA C 58.2 0.2 1 838 . 239 SER C C 172.8 0.2 1 839 . 240 TRP H H 7.26 0.01 1 840 . 240 TRP N N 121.5 0.2 1 841 . 240 TRP CA C 57.4 0.2 1 842 . 240 TRP C C 176.1 0.2 1 843 . 243 GLN H H 8.48 0.01 1 844 . 243 GLN N N 122.9 0.2 1 845 . 243 GLN CA C 56.5 0.2 1 846 . 243 GLN C C 178.9 0.2 1 847 . 244 THR H H 9.5 0.01 1 848 . 244 THR N N 114.9 0.2 1 849 . 244 THR CA C 60.3 0.2 1 850 . 244 THR C C 175.3 0.2 1 851 . 245 ALA H H 8.8 0.01 1 852 . 245 ALA N N 121.8 0.2 1 853 . 245 ALA CA C 55.1 0.2 1 854 . 245 ALA C C 180.8 0.2 1 855 . 246 GLN H H 8.09 0.01 1 856 . 246 GLN N N 116.9 0.2 1 857 . 246 GLN CA C 57.9 0.2 1 858 . 246 GLN C C 178.3 0.2 1 859 . 247 ASP H H 7.63 0.01 1 860 . 247 ASP N N 122.2 0.2 1 861 . 247 ASP CA C 56.8 0.2 1 862 . 249 LYS H H 7.27 0.01 1 863 . 249 LYS N N 118.00 0.2 1 864 . 249 LYS CA C 58.4 0.2 1 865 . 249 LYS C C 178.2 0.2 1 866 . 250 SER H H 7.57 0.01 1 867 . 250 SER N N 111.2 0.2 1 868 . 250 SER CA C 58.4 0.2 1 869 . 250 SER C C 174.1 0.2 1 870 . 251 GLY H H 7.98 0.01 1 871 . 251 GLY N N 111.00 0.2 1 872 . 251 GLY CA C 46.00 0.2 1 873 . 251 GLY C C 175.4 0.2 1 874 . 252 VAL H H 7.83 0.01 1 875 . 252 VAL N N 111.4 0.2 1 876 . 252 VAL CA C 58.3 0.2 1 877 . 252 VAL C C 173.7 0.2 1 878 . 253 ALA H H 9.45 0.01 1 879 . 253 ALA N N 121.3 0.2 1 880 . 253 ALA CA C 51.4 0.2 1 881 . 253 ALA C C 175.3 0.2 1 882 . 254 SER H H 9.42 0.01 1 883 . 254 SER N N 114.7 0.2 1 884 . 254 SER CA C 57.8 0.2 1 885 . 254 SER C C 172.6 0.2 1 886 . 255 THR H H 8.86 0.01 1 887 . 255 THR N N 107.00 0.2 1 888 . 255 THR CA C 59.6 0.2 1 889 . 255 THR C C 175.8 0.2 1 890 . 256 TYR H H 8.75 0.01 1 891 . 256 TYR N N 120.00 0.2 1 892 . 256 TYR C C 174.9 0.2 1 893 . 260 LYS H H 6.68 0.01 1 894 . 260 LYS N N 113.6 0.2 1 895 . 260 LYS CA C 56.1 0.2 1 896 . 260 LYS C C 175.9 0.2 1 897 . 261 GLN H H 8.17 0.01 1 898 . 261 GLN N N 111.4 0.2 1 899 . 261 GLN CA C 59.1 0.2 1 900 . 261 GLN C C 172.1 0.2 1 901 . 262 ASN H H 7.98 0.01 1 902 . 262 ASN N N 118.9 0.2 1 903 . 262 ASN CA C 52.4 0.2 1 904 . 262 ASN C C 170.00 0.2 1 905 . 264 LEU H H 7.65 0.01 1 906 . 264 LEU N N 124.4 0.2 1 907 . 264 LEU CA C 53.4 0.2 1 908 . 264 LEU C C 175.8 0.2 1 909 . 265 ASN H H 8.41 0.01 1 910 . 265 ASN N N 116.5 0.2 1 911 . 265 ASN CA C 50.6 0.2 1 912 . 265 ASN C C 173.6 0.2 1 913 . 266 ASN H H 9.11 0.01 1 914 . 266 ASN N N 112.5 0.2 1 915 . 266 ASN CA C 54.00 0.2 1 916 . 266 ASN C C 173.9 0.2 1 917 . 267 ILE H H 8.51 0.01 1 918 . 267 ILE N N 120.7 0.2 1 919 . 267 ILE CA C 57.8 0.2 1 920 . 267 ILE C C 177.00 0.2 1 921 . 268 LYS H H 8.69 0.01 1 922 . 268 LYS N N 127.00 0.2 1 923 . 268 LYS CA C 58.7 0.2 1 924 . 268 LYS C C 178.1 0.2 1 925 . 269 ALA H H 8.22 0.01 1 926 . 269 ALA N N 126.6 0.2 1 927 . 269 ALA CA C 53.3 0.2 1 928 . 269 ALA C C 178.6 0.2 1 929 . 270 SER H H 7.89 0.01 1 930 . 270 SER N N 110.8 0.2 1 931 . 270 SER CA C 57.6 0.2 1 932 . 270 SER C C 172.8 0.2 1 933 . 271 GLU H H 7.11 0.01 1 934 . 271 GLU N N 119.1 0.2 1 935 . 271 GLU CA C 53.3 0.2 1 936 . 271 GLU C C 177.00 0.2 1 937 . 272 SER H H 8.72 0.01 1 938 . 272 SER N N 118.00 0.2 1 939 . 272 SER CA C 56.1 0.2 1 940 . 272 SER C C 175.00 0.2 1 941 . 273 ASN H H 8.02 0.01 1 942 . 273 ASN N N 120.4 0.2 1 943 . 273 ASN CA C 52.4 0.2 1 944 . 273 ASN C C 174.00 0.2 1 945 . 274 ALA H H 7.43 0.01 1 946 . 274 ALA N N 118.00 0.2 1 947 . 274 ALA CA C 50.1 0.2 1 948 . 274 ALA C C 173.7 0.2 1 949 . 275 TYR H H 9.03 0.01 1 950 . 275 TYR N N 117.4 0.2 1 951 . 275 TYR CA C 58.3 0.2 1 952 . 275 TYR C C 174.8 0.2 1 953 . 276 ALA H H 9.11 0.01 1 954 . 276 ALA N N 121.3 0.2 1 955 . 276 ALA CA C 50.6 0.2 1 956 . 276 ALA C C 175.2 0.2 1 957 . 277 THR H H 9.27 0.01 1 958 . 277 THR N N 127.00 0.2 1 959 . 277 THR CA C 61.4 0.2 1 960 . 277 THR C C 174.4 0.2 1 961 . 278 CYS H H 8.16 0.01 1 962 . 278 CYS N N 123.1 0.2 1 963 . 278 CYS CA C 50.9 0.2 1 964 . 278 CYS C C 172.8 0.2 1 965 . 279 VAL H H 9.51 0.01 1 966 . 279 VAL N N 122.4 0.2 1 967 . 279 VAL CA C 61.2 0.2 1 968 . 279 VAL C C 175.5 0.2 1 969 . 280 LYS H H 9.22 0.01 1 970 . 280 LYS N N 132.6 0.2 1 971 . 280 LYS CA C 56.4 0.2 1 972 . 280 LYS C C 180.2 0.2 1 stop_ save_