data_19837 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471 ; _BMRB_accession_number 19837 _BMRB_flat_file_name bmr19837.str _Entry_type original _Submission_date 2014-03-05 _Accession_date 2014-03-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 882 "13C chemical shifts" 445 "15N chemical shifts" 345 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-20 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19835 'E. coli Trigger Factor in complex with unfolded PhoA220-310' 19836 'E. coli Trigger Factor in complex with unfolded PhoA1-150' stop_ _Original_release_date 2014-05-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for protein antiaggregation activity of the trigger factor chaperone' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24812405 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ _Journal_abbreviation Science _Journal_volume 344 _Journal_issue 6184 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1250494 _Page_last 1250494 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'E. coli Trigger Factor in complex with unfolded PhoA365-471' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 11880.312 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 114 _Mol_residue_sequence ; HMQIGETVDLDEAVQRALEF AKKEGNTLVIVTADHAHASQ IVAPDTKAPGLTQALNTKDG AVMVMSYGNSEEDSQEHTGS QLRIAAYGPHAANVVGLTDQ TDLFYTMKAALGLK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 HIS 2 2 MET 3 3 GLN 4 4 ILE 5 5 GLY 6 6 GLU 7 7 THR 8 8 VAL 9 9 ASP 10 10 LEU 11 11 ASP 12 12 GLU 13 13 ALA 14 14 VAL 15 15 GLN 16 16 ARG 17 17 ALA 18 18 LEU 19 19 GLU 20 20 PHE 21 21 ALA 22 22 LYS 23 23 LYS 24 24 GLU 25 25 GLY 26 26 ASN 27 27 THR 28 28 LEU 29 29 VAL 30 30 ILE 31 31 VAL 32 32 THR 33 33 ALA 34 34 ASP 35 35 HIS 36 36 ALA 37 37 HIS 38 38 ALA 39 39 SER 40 40 GLN 41 41 ILE 42 42 VAL 43 43 ALA 44 44 PRO 45 45 ASP 46 46 THR 47 47 LYS 48 48 ALA 49 49 PRO 50 50 GLY 51 51 LEU 52 52 THR 53 53 GLN 54 54 ALA 55 55 LEU 56 56 ASN 57 57 THR 58 58 LYS 59 59 ASP 60 60 GLY 61 61 ALA 62 62 VAL 63 63 MET 64 64 VAL 65 65 MET 66 66 SER 67 67 TYR 68 68 GLY 69 69 ASN 70 70 SER 71 71 GLU 72 72 GLU 73 73 ASP 74 74 SER 75 75 GLN 76 76 GLU 77 77 HIS 78 78 THR 79 79 GLY 80 80 SER 81 81 GLN 82 82 LEU 83 83 ARG 84 84 ILE 85 85 ALA 86 86 ALA 87 87 TYR 88 88 GLY 89 89 PRO 90 90 HIS 91 91 ALA 92 92 ALA 93 93 ASN 94 94 VAL 95 95 VAL 96 96 GLY 97 97 LEU 98 98 THR 99 99 ASP 100 100 GLN 101 101 THR 102 102 ASP 103 103 LEU 104 104 PHE 105 105 TYR 106 106 THR 107 107 MET 108 108 LYS 109 109 ALA 110 110 ALA 111 111 LEU 112 112 GLY 113 113 LEU 114 114 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 1AJA "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 98.25 449 100.00 100.00 2.68e-70 PDB 1AJB "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 98.25 449 100.00 100.00 2.68e-70 PDB 1AJC "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 98.25 449 100.00 100.00 2.68e-70 PDB 1AJD "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 98.25 449 100.00 100.00 2.68e-70 PDB 1ALH "Kinetics And Crystal Structure Of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->asn): A Mechanism Involving One Zinc Per Act" 98.25 446 99.11 100.00 1.24e-69 PDB 1ALI "Alkaline Phosphatase Mutant (H412n)" 98.25 449 99.11 100.00 2.79e-69 PDB 1ALJ "Alkaline Phosphatase Mutant (H412n)" 98.25 449 99.11 100.00 2.79e-69 PDB 1ALK "Reaction Mechanism Of Alkaline Phosphatase Based On Crystal Structures. Two Metal Ion Catalysis" 98.25 449 100.00 100.00 2.65e-70 PDB 1ANI "Alkaline Phosphatase (D153h, K328h)" 98.25 446 100.00 100.00 4.07e-70 PDB 1ANJ "Alkaline Phosphatase (K328h)" 98.25 446 100.00 100.00 3.50e-70 PDB 1B8J "Alkaline Phosphatase Complexed With Vanadate" 98.25 449 100.00 100.00 3.35e-70 PDB 1ED8 "Structure Of E. Coli Alkaline Phosphatase Inhibited By The Inorganic Phosphate At 1.75a Resolution" 98.25 449 100.00 100.00 3.28e-70 PDB 1ED9 "Structure Of E. Coli Alkaline Phosphatase Without The Inorganic Phosphate At 1.75a Resolution" 98.25 449 100.00 100.00 3.28e-70 PDB 1ELX "E. Coli Alkaline Phosphatase Mutant (S102a)" 98.25 449 100.00 100.00 3.14e-70 PDB 1ELY "E. Coli Alkaline Phosphatase Mutant (S102c)" 98.25 449 100.00 100.00 3.14e-70 PDB 1ELZ "E. Coli Alkaline Phosphatase Mutant (S102g)" 98.25 449 100.00 100.00 3.28e-70 PDB 1EW8 "Alkaline Phosphatase (e.c. 3.1.3.1) Complex With Phosphonoacetic Acid" 98.25 449 100.00 100.00 3.28e-70 PDB 1EW9 "Alkaline Phosphatase (E.C. 3.1.3.1) Complex With Mercaptomethyl Phosphonate" 98.25 449 100.00 100.00 3.28e-70 PDB 1HJK "Alkaline Phosphatase Mutant H331q" 98.25 449 100.00 100.00 3.24e-70 PDB 1HQA "Alkaline Phosphatase (H412q)" 98.25 449 99.11 99.11 3.57e-69 PDB 1KH4 "E. Coli Alkaline Phosphatase Mutant (d330n) In Complex With Phosphate" 98.25 449 100.00 100.00 2.18e-70 PDB 1KH5 "E. Coli Alkaline Phosphatase Mutant (d330n) Mimic Of The Transition States With Aluminium Fluoride" 98.25 449 100.00 100.00 2.18e-70 PDB 1KH7 "E. Coli Alkaline Phosphatase Mutant (d153gd330n)" 98.25 449 100.00 100.00 1.98e-70 PDB 1KH9 "E. Coli Alkaline Phosphatase Mutant (d153gd330n) Complex With Phosphate" 98.25 449 100.00 100.00 2.18e-70 PDB 1KHJ "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Mimic Of The Transition States With Aluminium Fluoride" 98.25 449 100.00 100.00 2.91e-70 PDB 1KHK "E. Coli Alkaline Phosphatase Mutant (d153hd330n)" 98.25 449 100.00 100.00 2.91e-70 PDB 1KHL "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Complex With Phosphate" 98.25 449 100.00 100.00 2.91e-70 PDB 1KHN "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Zinc Form" 98.25 449 100.00 100.00 2.91e-70 PDB 1URA "Alkaline Phosphatase (D51zn)" 98.25 446 100.00 100.00 2.54e-70 PDB 1URB "Alkaline Phosphatase (N51mg)" 98.25 446 100.00 100.00 2.54e-70 PDB 1Y6V "Structure Of E. Coli Alkaline Phosphatase In Presence Of Cobalt At 1.60 A Resolution" 98.25 449 100.00 100.00 3.28e-70 PDB 1Y7A "Structure Of D153hK328W E. COLI ALKALINE PHOSPHATASE IN Presence Of Cobalt At 1.77 A Resolution" 98.25 449 100.00 100.00 3.18e-70 PDB 2ANH "Alkaline Phosphatase (D153h)" 98.25 446 100.00 100.00 3.05e-70 PDB 2G9Y "Structure Of S102t E. Coli Alkaline Phosphatase In Presence Of Phosphate At 2.00 A Resolution" 98.25 449 100.00 100.00 3.14e-70 PDB 2GA3 "Structure Of S102t E. Coli Alkaline Phosphatase-Phosphate Intermediate At 2.20a Resolution" 98.25 449 100.00 100.00 3.35e-70 PDB 2MLZ "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa365-471" 100.00 114 100.00 100.00 3.60e-76 PDB 3BDF "Crystal Structure Of Metal-Free E. Coli Alkaline Phosphatase (T155v)" 98.25 458 100.00 100.00 7.90e-70 PDB 3BDG "Crystal Structure Of Wild-TypeT155V MIXED DIMER OF E. COLI ALKALINE Phosphatase" 98.25 458 100.00 100.00 3.50e-70 PDB 3BDH "Crystal Structure Of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase" 98.25 458 100.00 100.00 8.25e-70 PDB 3CMR "E. Coli Alkaline Phosphatase Mutant R166s In Complex With Phosphate" 98.25 449 100.00 100.00 3.24e-70 PDB 3DPC "Structure Of E.coli Alkaline Phosphatase Mutant In Complex With A Phosphorylated Peptide" 98.25 455 100.00 100.00 7.84e-70 PDB 3DYC "Structure Of E322y Alkaline Phosphatase In Complex With Inorganic Phosphate" 98.25 449 100.00 100.00 3.24e-70 PDB 3TG0 "E. Coli Alkaline Phosphatase With Bound Inorganic Phosphate" 98.25 449 100.00 100.00 3.28e-70 PDB 4KM4 "E. Coli Alkaline Phosphatase Mutant S102g/r166s In Complex With Inorganic Phosphate" 97.37 445 100.00 100.00 1.74e-69 PDB 4YR1 "Crystal Structure Of E. Coli Alkaline Phosphatase D101a/d153a In Complex With Inorganic Phosphate" 98.25 443 100.00 100.00 1.75e-70 DBJ BAB33856 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 98.25 494 99.11 100.00 3.23e-69 DBJ BAE76164 "alkaline phosphatase [Escherichia coli str. K12 substr. W3110]" 98.25 471 100.00 100.00 4.28e-70 DBJ BAG75928 "alkaline phosphatase [Escherichia coli SE11]" 98.25 494 99.11 100.00 1.60e-69 DBJ BAI23756 "bacterial alkaline phosphatase PhoA [Escherichia coli O26:H11 str. 11368]" 98.25 471 99.11 100.00 1.25e-69 DBJ BAI29227 "bacterial alkaline phosphatase PhoA [Escherichia coli O103:H2 str. 12009]" 98.25 471 99.11 100.00 1.10e-69 EMBL CAA28257 "alkaline phosphatase [Escherichia coli]" 98.25 471 100.00 100.00 4.28e-70 EMBL CAP74918 "alkaline phosphatase [Escherichia coli LF82]" 98.25 471 99.11 100.00 1.37e-69 EMBL CAQ30851 "alkaline phosphatase [Escherichia coli BL21(DE3)]" 98.25 471 99.11 100.00 1.65e-69 EMBL CAQ97255 "bacterial alkaline phosphatase [Escherichia coli IAI1]" 98.25 471 99.11 100.00 1.79e-69 EMBL CAR01727 "bacterial alkaline phosphatase [Escherichia coli S88]" 98.25 471 99.11 100.00 1.37e-69 GB AAA24363 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 98.25 471 99.11 100.00 2.22e-69 GB AAA24364 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 98.25 471 100.00 100.00 4.28e-70 GB AAA24365 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 98.25 471 100.00 100.00 4.28e-70 GB AAA24366 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 98.25 471 99.11 100.00 8.58e-70 GB AAA24367 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 98.25 471 99.11 100.00 1.97e-69 REF NP_308460 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 98.25 494 99.11 100.00 3.23e-69 REF NP_414917 "bacterial alkaline phosphatase [Escherichia coli str. K-12 substr. MG1655]" 98.25 471 100.00 100.00 4.28e-70 REF NP_706185 "alkaline phosphatase [Shigella flexneri 2a str. 301]" 98.25 494 99.11 100.00 1.96e-69 REF WP_000089619 "alkaline phosphatase [Escherichia coli]" 98.25 494 99.11 100.00 3.23e-69 REF WP_000089625 "alkaline phosphatase [Shigella flexneri]" 98.25 494 99.11 100.00 1.96e-69 SP P00634 "RecName: Full=Alkaline phosphatase; Short=APase; Flags: Precursor" 98.25 471 100.00 100.00 4.28e-70 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 48256.020 _Mol_thiol_state 'not present' _Details . _Residue_count 443 _Mol_residue_sequence ; MNHKVHHHHHHMQVSVETTQ GLGRRVTITIAADSIETAVK SELVNVAKKVRIDGFRKGKV PMNIVAQRYGASVRQDVLGD LMSRNFIDAIIKEKINPAGA PTYVPGEYKLGEDFTYSVEF EVYPEVELQGLEAIEVEKPI VEVTDADVDGMLDTLRKQQA TWKEKDGAVEAEDRVTIDFT GSVDGEEFEGGKASDFVLAM GQGRMIPGFEDGIKGHKAGE EFTIDVTFPEEYHAENLKGK AAKFAINLKKVEERELPELT AEFIKRFGVEDGSVEGLRAE VRKNMERELKSAIRNRVKSQ AIEGLVKANDIDVPAALIDS EIDVLRRQAAQRFGGNEKQA LELPRELFEEQAKRRVVVGL LLGEVIRTNELKADEERVKG LIEEMASAYEDPKEVIEFYS KNKELMDNMRNVALEEQAVE AVLAKAKVTEKETTFNELMN QQA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -10 MET 2 -9 ASN 3 -8 HIS 4 -7 LYS 5 -6 VAL 6 -5 HIS 7 -4 HIS 8 -3 HIS 9 -2 HIS 10 -1 HIS 11 0 HIS 12 1 MET 13 2 GLN 14 3 VAL 15 4 SER 16 5 VAL 17 6 GLU 18 7 THR 19 8 THR 20 9 GLN 21 10 GLY 22 11 LEU 23 12 GLY 24 13 ARG 25 14 ARG 26 15 VAL 27 16 THR 28 17 ILE 29 18 THR 30 19 ILE 31 20 ALA 32 21 ALA 33 22 ASP 34 23 SER 35 24 ILE 36 25 GLU 37 26 THR 38 27 ALA 39 28 VAL 40 29 LYS 41 30 SER 42 31 GLU 43 32 LEU 44 33 VAL 45 34 ASN 46 35 VAL 47 36 ALA 48 37 LYS 49 38 LYS 50 39 VAL 51 40 ARG 52 41 ILE 53 42 ASP 54 43 GLY 55 44 PHE 56 45 ARG 57 46 LYS 58 47 GLY 59 48 LYS 60 49 VAL 61 50 PRO 62 51 MET 63 52 ASN 64 53 ILE 65 54 VAL 66 55 ALA 67 56 GLN 68 57 ARG 69 58 TYR 70 59 GLY 71 60 ALA 72 61 SER 73 62 VAL 74 63 ARG 75 64 GLN 76 65 ASP 77 66 VAL 78 67 LEU 79 68 GLY 80 69 ASP 81 70 LEU 82 71 MET 83 72 SER 84 73 ARG 85 74 ASN 86 75 PHE 87 76 ILE 88 77 ASP 89 78 ALA 90 79 ILE 91 80 ILE 92 81 LYS 93 82 GLU 94 83 LYS 95 84 ILE 96 85 ASN 97 86 PRO 98 87 ALA 99 88 GLY 100 89 ALA 101 90 PRO 102 91 THR 103 92 TYR 104 93 VAL 105 94 PRO 106 95 GLY 107 96 GLU 108 97 TYR 109 98 LYS 110 99 LEU 111 100 GLY 112 101 GLU 113 102 ASP 114 103 PHE 115 104 THR 116 105 TYR 117 106 SER 118 107 VAL 119 108 GLU 120 109 PHE 121 110 GLU 122 111 VAL 123 112 TYR 124 113 PRO 125 114 GLU 126 115 VAL 127 116 GLU 128 117 LEU 129 118 GLN 130 119 GLY 131 120 LEU 132 121 GLU 133 122 ALA 134 123 ILE 135 124 GLU 136 125 VAL 137 126 GLU 138 127 LYS 139 128 PRO 140 129 ILE 141 130 VAL 142 131 GLU 143 132 VAL 144 133 THR 145 134 ASP 146 135 ALA 147 136 ASP 148 137 VAL 149 138 ASP 150 139 GLY 151 140 MET 152 141 LEU 153 142 ASP 154 143 THR 155 144 LEU 156 145 ARG 157 146 LYS 158 147 GLN 159 148 GLN 160 149 ALA 161 150 THR 162 151 TRP 163 152 LYS 164 153 GLU 165 154 LYS 166 155 ASP 167 156 GLY 168 157 ALA 169 158 VAL 170 159 GLU 171 160 ALA 172 161 GLU 173 162 ASP 174 163 ARG 175 164 VAL 176 165 THR 177 166 ILE 178 167 ASP 179 168 PHE 180 169 THR 181 170 GLY 182 171 SER 183 172 VAL 184 173 ASP 185 174 GLY 186 175 GLU 187 176 GLU 188 177 PHE 189 178 GLU 190 179 GLY 191 180 GLY 192 181 LYS 193 182 ALA 194 183 SER 195 184 ASP 196 185 PHE 197 186 VAL 198 187 LEU 199 188 ALA 200 189 MET 201 190 GLY 202 191 GLN 203 192 GLY 204 193 ARG 205 194 MET 206 195 ILE 207 196 PRO 208 197 GLY 209 198 PHE 210 199 GLU 211 200 ASP 212 201 GLY 213 202 ILE 214 203 LYS 215 204 GLY 216 205 HIS 217 206 LYS 218 207 ALA 219 208 GLY 220 209 GLU 221 210 GLU 222 211 PHE 223 212 THR 224 213 ILE 225 214 ASP 226 215 VAL 227 216 THR 228 217 PHE 229 218 PRO 230 219 GLU 231 220 GLU 232 221 TYR 233 222 HIS 234 223 ALA 235 224 GLU 236 225 ASN 237 226 LEU 238 227 LYS 239 228 GLY 240 229 LYS 241 230 ALA 242 231 ALA 243 232 LYS 244 233 PHE 245 234 ALA 246 235 ILE 247 236 ASN 248 237 LEU 249 238 LYS 250 239 LYS 251 240 VAL 252 241 GLU 253 242 GLU 254 243 ARG 255 244 GLU 256 245 LEU 257 246 PRO 258 247 GLU 259 248 LEU 260 249 THR 261 250 ALA 262 251 GLU 263 252 PHE 264 253 ILE 265 254 LYS 266 255 ARG 267 256 PHE 268 257 GLY 269 258 VAL 270 259 GLU 271 260 ASP 272 261 GLY 273 262 SER 274 263 VAL 275 264 GLU 276 265 GLY 277 266 LEU 278 267 ARG 279 268 ALA 280 269 GLU 281 270 VAL 282 271 ARG 283 272 LYS 284 273 ASN 285 274 MET 286 275 GLU 287 276 ARG 288 277 GLU 289 278 LEU 290 279 LYS 291 280 SER 292 281 ALA 293 282 ILE 294 283 ARG 295 284 ASN 296 285 ARG 297 286 VAL 298 287 LYS 299 288 SER 300 289 GLN 301 290 ALA 302 291 ILE 303 292 GLU 304 293 GLY 305 294 LEU 306 295 VAL 307 296 LYS 308 297 ALA 309 298 ASN 310 299 ASP 311 300 ILE 312 301 ASP 313 302 VAL 314 303 PRO 315 304 ALA 316 305 ALA 317 306 LEU 318 307 ILE 319 308 ASP 320 309 SER 321 310 GLU 322 311 ILE 323 312 ASP 324 313 VAL 325 314 LEU 326 315 ARG 327 316 ARG 328 317 GLN 329 318 ALA 330 319 ALA 331 320 GLN 332 321 ARG 333 322 PHE 334 323 GLY 335 324 GLY 336 325 ASN 337 326 GLU 338 327 LYS 339 328 GLN 340 329 ALA 341 330 LEU 342 331 GLU 343 332 LEU 344 333 PRO 345 334 ARG 346 335 GLU 347 336 LEU 348 337 PHE 349 338 GLU 350 339 GLU 351 340 GLN 352 341 ALA 353 342 LYS 354 343 ARG 355 344 ARG 356 345 VAL 357 346 VAL 358 347 VAL 359 348 GLY 360 349 LEU 361 350 LEU 362 351 LEU 363 352 GLY 364 353 GLU 365 354 VAL 366 355 ILE 367 356 ARG 368 357 THR 369 358 ASN 370 359 GLU 371 360 LEU 372 361 LYS 373 362 ALA 374 363 ASP 375 364 GLU 376 365 GLU 377 366 ARG 378 367 VAL 379 368 LYS 380 369 GLY 381 370 LEU 382 371 ILE 383 372 GLU 384 373 GLU 385 374 MET 386 375 ALA 387 376 SER 388 377 ALA 389 378 TYR 390 379 GLU 391 380 ASP 392 381 PRO 393 382 LYS 394 383 GLU 395 384 VAL 396 385 ILE 397 386 GLU 398 387 PHE 399 388 TYR 400 389 SER 401 390 LYS 402 391 ASN 403 392 LYS 404 393 GLU 405 394 LEU 406 395 MET 407 396 ASP 408 397 ASN 409 398 MET 410 399 ARG 411 400 ASN 412 401 VAL 413 402 ALA 414 403 LEU 415 404 GLU 416 405 GLU 417 406 GLN 418 407 ALA 419 408 VAL 420 409 GLU 421 410 ALA 422 411 VAL 423 412 LEU 424 413 ALA 425 414 LYS 426 415 ALA 427 416 LYS 428 417 VAL 429 418 THR 430 419 GLU 431 420 LYS 432 421 GLU 433 422 THR 434 423 THR 435 424 PHE 436 425 ASN 437 426 GLU 438 427 LEU 439 428 MET 440 429 ASN 441 430 GLN 442 431 GLN 443 432 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19835 entity_2 100.00 443 100.00 100.00 0.00e+00 BMRB 19836 entity_2 100.00 443 100.00 100.00 0.00e+00 PDB 1W26 "Trigger Factor In Complex With The Ribosome Forms A Molecular Cradle For Nascent Proteins" 97.29 432 97.68 97.68 0.00e+00 PDB 2MLX "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa220-310" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLY "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa1-150" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLZ "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa365-471" 100.00 443 100.00 100.00 0.00e+00 PDB 2VRH "Structure Of The E. Coli Trigger Factor Bound To A Translating Ribosome" 97.29 432 97.68 97.68 0.00e+00 DBJ BAB33913 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAD98926 "trigger factor tag [Expression vector pColdTF]" 100.00 489 100.00 100.00 0.00e+00 DBJ BAE76216 "peptidyl-prolyl cis/trans isomerase [Escherichia coli str. K-12 substr. W3110]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAG75986 "trigger factor [Escherichia coli SE11]" 97.52 432 99.77 100.00 0.00e+00 DBJ BAI23810 "peptidyl-prolyl cis/trans isomerase [Escherichia coli O26:H11 str. 11368]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAP74970 "Trigger factor [Escherichia coli LF82]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAQ30908 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli BL21(DE3)]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAQ97312 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli IAI1]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAR01780 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli S88]" 96.84 429 100.00 100.00 0.00e+00 EMBL CAR06670 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli ED1a]" 97.52 432 100.00 100.00 0.00e+00 GB AAA62791 "trigger factor [Escherichia coli]" 97.52 432 97.69 98.61 0.00e+00 GB AAB40192 "trigger factor [Escherichia coli]" 97.52 432 100.00 100.00 0.00e+00 GB AAC73539 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 GB AAG54786 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 GB AAN42037 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_286178 "trigger factor [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 REF NP_308517 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 REF NP_414970 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 REF NP_706330 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_752485 "trigger factor [Escherichia coli CFT073]" 97.52 432 99.77 99.77 0.00e+00 SP A1A8A5 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli APEC O1]" 96.84 429 100.00 100.00 0.00e+00 SP A7ZIJ4 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli E24377A]" 97.52 432 99.77 100.00 0.00e+00 SP A7ZX94 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli HS]" 97.52 432 100.00 100.00 0.00e+00 SP B1J012 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli ATCC 8739]" 97.52 432 100.00 100.00 0.00e+00 SP B1LJJ3 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli SMS-3-5]" 97.52 432 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'E. coli' 469008 Bacteria . Escherichia coli $entity_2 'E. coli' 469008 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) pET16b $entity_2 'recombinant technology' . Escherichia coli BL21(DE3) pCold stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.5 mM '[U-100% 13C; U-100% 15N]' $entity_2 0.5 mM '[U-100% 13C; U-100% 15N]' 'potassium chloride' 100 mM 'natural abundance' BME 3 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_OLIVIA _Saveframe_category software _Name OLIVIA _Version 1.16 loop_ _Vendor _Address _Electronic_address 'Olivia, Yokochi Masashi' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOSN _Saveframe_category software _Name TALOSN _Version . loop_ _Vendor _Address _Electronic_address 'Shen and Bax' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_PSVS _Saveframe_category software _Name PSVS _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Bhattacharya and Montelione' . . stop_ loop_ _Task validation stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-13C_HMQC-NOESY_HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C HMQC-NOESY_HMQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $OLIVIA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity_2 _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 12 MET HE H 2.108 0.02 1 2 1 12 MET CE C 17.403 0.20 1 3 3 14 VAL H H 8.321 0.02 1 4 3 14 VAL HG1 H 0.840 0.02 2 5 3 14 VAL HG2 H 0.858 0.02 2 6 3 14 VAL CG1 C 21.584 0.20 2 7 3 14 VAL CG2 C 17.303 0.20 2 8 3 14 VAL N N 122.686 0.20 1 9 4 15 SER H H 8.689 0.02 1 10 4 15 SER N N 121.236 0.20 1 11 5 16 VAL H H 8.806 0.02 1 12 5 16 VAL HG1 H 0.765 0.02 2 13 5 16 VAL HG2 H 1.056 0.02 2 14 5 16 VAL CG1 C 20.086 0.20 2 15 5 16 VAL CG2 C 21.484 0.20 2 16 5 16 VAL N N 125.511 0.20 1 17 6 17 GLU H H 8.922 0.02 1 18 6 17 GLU N N 126.142 0.20 1 19 7 18 THR H H 8.711 0.02 1 20 7 18 THR N N 118.421 0.20 1 21 8 19 THR H H 7.708 0.02 1 22 8 19 THR N N 117.503 0.20 1 23 9 20 GLN H H 8.239 0.02 1 24 9 20 GLN N N 119.524 0.20 1 25 11 22 LEU H H 8.990 0.02 1 26 11 22 LEU HD1 H 0.733 0.02 2 27 11 22 LEU HD2 H 0.934 0.02 2 28 11 22 LEU CD1 C 22.234 0.20 2 29 11 22 LEU CD2 C 25.718 0.20 2 30 11 22 LEU N N 129.153 0.20 1 31 12 23 GLY H H 8.537 0.02 1 32 12 23 GLY N N 106.953 0.20 1 33 13 24 ARG H H 8.919 0.02 1 34 13 24 ARG N N 124.485 0.20 1 35 14 25 ARG H H 8.684 0.02 1 36 14 25 ARG N N 120.539 0.20 1 37 15 26 VAL H H 9.312 0.02 1 38 15 26 VAL HG1 H 1.158 0.02 2 39 15 26 VAL HG2 H 1.054 0.02 2 40 15 26 VAL CG1 C 22.607 0.20 2 41 15 26 VAL CG2 C 21.443 0.20 2 42 15 26 VAL N N 126.770 0.20 1 43 16 27 THR H H 8.945 0.02 1 44 16 27 THR N N 125.094 0.20 1 45 17 28 ILE H H 8.563 0.02 1 46 17 28 ILE HD1 H 0.827 0.02 1 47 17 28 ILE CD1 C 13.908 0.20 1 48 17 28 ILE N N 129.070 0.20 1 49 18 29 THR H H 8.357 0.02 1 50 18 29 THR N N 121.479 0.20 1 51 19 30 ILE H H 9.912 0.02 1 52 19 30 ILE HD1 H 0.930 0.02 1 53 19 30 ILE CD1 C 14.412 0.20 1 54 19 30 ILE N N 127.534 0.20 1 55 20 31 ALA H H 8.690 0.02 1 56 20 31 ALA HB H 1.553 0.02 1 57 20 31 ALA CB C 19.542 0.20 1 58 20 31 ALA N N 129.247 0.20 1 59 21 32 ALA H H 9.376 0.02 1 60 21 32 ALA HB H 1.334 0.02 1 61 21 32 ALA CB C 18.742 0.20 1 62 21 32 ALA N N 126.228 0.20 1 63 22 33 ASP H H 8.927 0.02 1 64 22 33 ASP N N 115.111 0.20 1 65 23 34 SER H H 7.597 0.02 1 66 23 34 SER N N 116.495 0.20 1 67 24 35 ILE H H 7.390 0.02 1 68 24 35 ILE HD1 H 0.890 0.02 1 69 24 35 ILE CD1 C 14.923 0.20 1 70 24 35 ILE N N 122.361 0.20 1 71 25 36 GLU H H 8.233 0.02 1 72 25 36 GLU N N 117.692 0.20 1 73 26 37 THR H H 8.264 0.02 1 74 26 37 THR N N 115.095 0.20 1 75 27 38 ALA H H 7.328 0.02 1 76 27 38 ALA HB H 1.523 0.02 1 77 27 38 ALA CB C 18.985 0.20 1 78 27 38 ALA N N 125.189 0.20 1 79 28 39 VAL H H 8.607 0.02 1 80 28 39 VAL HG1 H 0.907 0.02 2 81 28 39 VAL HG2 H 0.823 0.02 2 82 28 39 VAL CG1 C 23.815 0.20 2 83 28 39 VAL CG2 C 20.965 0.20 2 84 28 39 VAL N N 119.922 0.20 1 85 29 40 LYS H H 8.102 0.02 1 86 29 40 LYS N N 118.843 0.20 1 87 30 41 SER H H 7.896 0.02 1 88 30 41 SER N N 112.454 0.20 1 89 31 42 GLU H H 7.871 0.02 1 90 31 42 GLU N N 121.930 0.20 1 91 32 43 LEU H H 8.664 0.02 1 92 32 43 LEU HD1 H 0.793 0.02 2 93 32 43 LEU HD2 H 0.679 0.02 2 94 32 43 LEU CD1 C 26.207 0.20 2 95 32 43 LEU CD2 C 23.471 0.20 2 96 32 43 LEU N N 121.004 0.20 1 97 33 44 VAL H H 7.683 0.02 1 98 33 44 VAL HG1 H 1.056 0.02 2 99 33 44 VAL HG2 H 0.655 0.02 2 100 33 44 VAL CG1 C 22.846 0.20 2 101 33 44 VAL CG2 C 21.438 0.20 2 102 33 44 VAL N N 118.838 0.20 1 103 34 45 ASN H H 7.241 0.02 1 104 34 45 ASN N N 118.030 0.20 1 105 35 46 VAL H H 8.445 0.02 1 106 35 46 VAL HG1 H 0.873 0.02 2 107 35 46 VAL HG2 H 0.872 0.02 2 108 35 46 VAL CG1 C 23.633 0.20 2 109 35 46 VAL CG2 C 22.866 0.20 2 110 35 46 VAL N N 121.777 0.20 1 111 36 47 ALA H H 8.311 0.02 1 112 36 47 ALA HB H 1.491 0.02 1 113 36 47 ALA CB C 18.907 0.20 1 114 36 47 ALA N N 120.267 0.20 1 115 37 48 LYS H H 7.351 0.02 1 116 37 48 LYS N N 114.141 0.20 1 117 38 49 LYS H H 7.606 0.02 1 118 38 49 LYS N N 115.473 0.20 1 119 39 50 VAL H H 7.419 0.02 1 120 39 50 VAL HG1 H 0.903 0.02 2 121 39 50 VAL HG2 H 0.718 0.02 2 122 39 50 VAL CG1 C 20.483 0.20 2 123 39 50 VAL CG2 C 21.327 0.20 2 124 39 50 VAL N N 116.433 0.20 1 125 40 51 ARG H H 8.368 0.02 1 126 40 51 ARG N N 124.277 0.20 1 127 41 52 ILE H H 8.073 0.02 1 128 41 52 ILE HD1 H 0.796 0.02 1 129 41 52 ILE CD1 C 13.971 0.20 1 130 41 52 ILE N N 124.148 0.20 1 131 42 53 ASP H H 8.573 0.02 1 132 42 53 ASP N N 124.954 0.20 1 133 43 54 GLY H H 8.475 0.02 1 134 43 54 GLY N N 110.101 0.20 1 135 44 55 PHE H H 8.085 0.02 1 136 44 55 PHE N N 118.593 0.20 1 137 45 56 ARG H H 8.721 0.02 1 138 45 56 ARG N N 122.232 0.20 1 139 46 57 LYS H H 8.634 0.02 1 140 46 57 LYS N N 122.694 0.20 1 141 47 58 GLY H H 8.924 0.02 1 142 47 58 GLY N N 113.989 0.20 1 143 48 59 LYS H H 8.093 0.02 1 144 48 59 LYS N N 119.432 0.20 1 145 49 60 VAL H H 8.061 0.02 1 146 49 60 VAL HG1 H 0.819 0.02 2 147 49 60 VAL HG2 H 0.654 0.02 2 148 49 60 VAL CG1 C 22.264 0.20 2 149 49 60 VAL CG2 C 21.368 0.20 2 150 49 60 VAL N N 123.619 0.20 1 151 51 62 MET HE H 1.939 0.02 1 152 51 62 MET CE C 16.268 0.20 1 153 52 63 ASN H H 8.833 0.02 1 154 52 63 ASN N N 123.474 0.20 1 155 53 64 ILE H H 7.208 0.02 1 156 53 64 ILE HD1 H 0.791 0.02 1 157 53 64 ILE CD1 C 11.563 0.20 1 158 53 64 ILE N N 121.514 0.20 1 159 54 65 VAL H H 7.494 0.02 1 160 54 65 VAL HG1 H 0.894 0.02 2 161 54 65 VAL HG2 H 0.893 0.02 2 162 54 65 VAL CG1 C 21.755 0.20 2 163 54 65 VAL CG2 C 21.202 0.20 2 164 54 65 VAL N N 120.799 0.20 1 165 55 66 ALA H H 8.869 0.02 1 166 55 66 ALA HB H 1.425 0.02 1 167 55 66 ALA CB C 17.841 0.20 1 168 55 66 ALA N N 120.856 0.20 1 169 56 67 GLN H H 7.666 0.02 1 170 56 67 GLN N N 118.538 0.20 1 171 57 68 ARG H H 8.020 0.02 1 172 57 68 ARG N N 116.667 0.20 1 173 58 69 TYR H H 8.619 0.02 1 174 58 69 TYR N N 114.284 0.20 1 175 59 70 GLY H H 8.158 0.02 1 176 59 70 GLY N N 109.105 0.20 1 177 60 71 ALA H H 8.507 0.02 1 178 60 71 ALA HB H 1.418 0.02 1 179 60 71 ALA CB C 17.878 0.20 1 180 60 71 ALA N N 122.730 0.20 1 181 61 72 SER H H 8.059 0.02 1 182 61 72 SER N N 115.187 0.20 1 183 62 73 VAL H H 8.399 0.02 1 184 62 73 VAL HG1 H 1.052 0.02 2 185 62 73 VAL HG2 H 0.902 0.02 2 186 62 73 VAL CG1 C 23.761 0.20 2 187 62 73 VAL CG2 C 22.741 0.20 2 188 62 73 VAL N N 122.495 0.20 1 189 63 74 ARG H H 8.300 0.02 1 190 63 74 ARG N N 118.635 0.20 1 191 64 75 GLN H H 7.481 0.02 1 192 64 75 GLN N N 116.268 0.20 1 193 65 76 ASP H H 7.847 0.02 1 194 65 76 ASP N N 121.702 0.20 1 195 66 77 VAL H H 8.728 0.02 1 196 66 77 VAL HG1 H 0.903 0.02 2 197 66 77 VAL CG1 C 23.133 0.20 2 198 66 77 VAL N N 121.548 0.20 1 199 67 78 LEU H H 8.284 0.02 1 200 67 78 LEU HD1 H 0.027 0.02 2 201 67 78 LEU HD2 H -0.120 0.02 2 202 67 78 LEU CD1 C 24.067 0.20 2 203 67 78 LEU CD2 C 22.218 0.20 2 204 67 78 LEU N N 119.779 0.20 1 205 68 79 GLY H H 7.660 0.02 1 206 68 79 GLY N N 104.928 0.20 1 207 69 80 ASP H H 7.723 0.02 1 208 69 80 ASP N N 123.146 0.20 1 209 70 81 LEU H H 8.948 0.02 1 210 70 81 LEU HD1 H 0.681 0.02 2 211 70 81 LEU HD2 H 0.738 0.02 2 212 70 81 LEU CD1 C 26.787 0.20 2 213 70 81 LEU CD2 C 22.399 0.20 2 214 70 81 LEU N N 118.632 0.20 1 215 71 82 MET H H 8.725 0.02 1 216 71 82 MET HE H 1.803 0.02 1 217 71 82 MET CE C 16.413 0.20 1 218 71 82 MET N N 120.051 0.20 1 219 72 83 SER H H 7.451 0.02 1 220 72 83 SER N N 115.745 0.20 1 221 73 84 ARG H H 8.634 0.02 1 222 73 84 ARG N N 121.209 0.20 1 223 74 85 ASN H H 8.347 0.02 1 224 74 85 ASN N N 114.087 0.20 1 225 75 86 PHE H H 7.738 0.02 1 226 75 86 PHE N N 121.314 0.20 1 227 76 87 ILE H H 8.218 0.02 1 228 76 87 ILE N N 119.891 0.20 1 229 77 88 ASP H H 7.666 0.02 1 230 77 88 ASP N N 116.921 0.20 1 231 78 89 ALA H H 7.513 0.02 1 232 78 89 ALA HB H 1.457 0.02 1 233 78 89 ALA CB C 18.752 0.20 1 234 78 89 ALA N N 120.884 0.20 1 235 79 90 ILE H H 8.030 0.02 1 236 79 90 ILE HD1 H 0.325 0.02 1 237 79 90 ILE CD1 C 13.436 0.20 1 238 79 90 ILE N N 113.413 0.20 1 239 80 91 ILE H H 7.892 0.02 1 240 80 91 ILE HD1 H 0.777 0.02 1 241 80 91 ILE CD1 C 13.166 0.20 1 242 80 91 ILE N N 122.547 0.20 1 243 81 92 LYS H H 7.821 0.02 1 244 81 92 LYS N N 121.440 0.20 1 245 82 93 GLU H H 8.011 0.02 1 246 82 93 GLU N N 114.760 0.20 1 247 83 94 LYS H H 7.737 0.02 1 248 83 94 LYS N N 117.012 0.20 1 249 84 95 ILE H H 7.948 0.02 1 250 84 95 ILE HD1 H 0.808 0.02 1 251 84 95 ILE CD1 C 13.491 0.20 1 252 84 95 ILE N N 119.229 0.20 1 253 85 96 ASN H H 8.653 0.02 1 254 85 96 ASN N N 124.286 0.20 1 255 87 98 ALA H H 9.209 0.02 1 256 87 98 ALA HB H 0.502 0.02 1 257 87 98 ALA CB C 18.741 0.20 1 258 87 98 ALA N N 125.524 0.20 1 259 88 99 GLY H H 7.554 0.02 1 260 88 99 GLY N N 107.014 0.20 1 261 89 100 ALA H H 8.411 0.02 1 262 89 100 ALA HB H 1.367 0.02 1 263 89 100 ALA CB C 18.461 0.20 1 264 89 100 ALA N N 124.058 0.20 1 265 91 102 THR H H 8.853 0.02 1 266 91 102 THR N N 117.682 0.20 1 267 92 103 TYR H H 9.054 0.02 1 268 92 103 TYR N N 126.639 0.20 1 269 93 104 VAL H H 9.523 0.02 1 270 93 104 VAL HG1 H 0.832 0.02 2 271 93 104 VAL HG2 H 0.729 0.02 2 272 93 104 VAL CG1 C 21.971 0.20 2 273 93 104 VAL CG2 C 19.213 0.20 2 274 93 104 VAL N N 124.611 0.20 1 275 95 106 GLY H H 6.857 0.02 1 276 95 106 GLY N N 109.037 0.20 1 277 96 107 GLU H H 8.389 0.02 1 278 96 107 GLU N N 119.656 0.20 1 279 97 108 TYR H H 8.911 0.02 1 280 97 108 TYR N N 126.986 0.20 1 281 98 109 LYS H H 8.380 0.02 1 282 98 109 LYS N N 131.055 0.20 1 283 99 110 LEU H H 7.947 0.02 1 284 99 110 LEU HD1 H 0.923 0.02 2 285 99 110 LEU HD2 H 0.849 0.02 2 286 99 110 LEU CD1 C 24.344 0.20 2 287 99 110 LEU CD2 C 24.891 0.20 2 288 99 110 LEU N N 124.566 0.20 1 289 100 111 GLY H H 8.274 0.02 1 290 100 111 GLY N N 113.138 0.20 1 291 101 112 GLU H H 7.884 0.02 1 292 101 112 GLU N N 119.234 0.20 1 293 102 113 ASP H H 8.627 0.02 1 294 102 113 ASP N N 121.919 0.20 1 295 103 114 PHE H H 8.923 0.02 1 296 103 114 PHE N N 123.333 0.20 1 297 104 115 THR H H 8.414 0.02 1 298 104 115 THR N N 126.257 0.20 1 299 105 116 TYR H H 8.945 0.02 1 300 105 116 TYR N N 122.193 0.20 1 301 106 117 SER H H 8.175 0.02 1 302 106 117 SER N N 112.325 0.20 1 303 107 118 VAL H H 9.037 0.02 1 304 107 118 VAL HG1 H 0.625 0.02 2 305 107 118 VAL HG2 H -0.553 0.02 2 306 107 118 VAL CG1 C 22.513 0.20 2 307 107 118 VAL CG2 C 21.989 0.20 2 308 107 118 VAL N N 121.772 0.20 1 309 108 119 GLU H H 8.971 0.02 1 310 108 119 GLU N N 125.633 0.20 1 311 109 120 PHE H H 7.865 0.02 1 312 109 120 PHE N N 117.269 0.20 1 313 110 121 GLU H H 8.612 0.02 1 314 110 121 GLU N N 118.490 0.20 1 315 111 122 VAL H H 8.113 0.02 1 316 111 122 VAL HG1 H 0.962 0.02 2 317 111 122 VAL HG2 H 0.866 0.02 2 318 111 122 VAL CG1 C 23.529 0.20 2 319 111 122 VAL CG2 C 17.936 0.20 2 320 111 122 VAL N N 113.925 0.20 1 321 112 123 TYR H H 8.124 0.02 1 322 112 123 TYR N N 118.544 0.20 1 323 114 125 GLU H H 8.361 0.02 1 324 114 125 GLU N N 121.276 0.20 1 325 115 126 VAL H H 8.272 0.02 1 326 115 126 VAL HG1 H 0.779 0.02 2 327 115 126 VAL HG2 H 0.833 0.02 2 328 115 126 VAL CG1 C 20.975 0.20 2 329 115 126 VAL CG2 C 20.707 0.20 2 330 115 126 VAL N N 123.799 0.20 1 331 116 127 GLU H H 8.281 0.02 1 332 116 127 GLU N N 126.552 0.20 1 333 117 128 LEU H H 8.599 0.02 1 334 117 128 LEU HD1 H 0.845 0.02 2 335 117 128 LEU HD2 H 0.767 0.02 2 336 117 128 LEU CD1 C 25.869 0.20 2 337 117 128 LEU CD2 C 23.878 0.20 2 338 117 128 LEU N N 125.293 0.20 1 339 118 129 GLN H H 9.384 0.02 1 340 118 129 GLN N N 123.141 0.20 1 341 119 130 GLY H H 8.450 0.02 1 342 119 130 GLY N N 105.407 0.20 1 343 120 131 LEU H H 8.117 0.02 1 344 120 131 LEU HD1 H 0.839 0.02 2 345 120 131 LEU CD1 C 25.241 0.20 2 346 120 131 LEU N N 121.908 0.20 1 347 121 132 GLU H H 8.631 0.02 1 348 121 132 GLU N N 113.478 0.20 1 349 122 133 ALA H H 7.249 0.02 1 350 122 133 ALA N N 120.430 0.20 1 351 123 134 ILE H H 7.056 0.02 1 352 123 134 ILE HD1 H 0.811 0.02 1 353 123 134 ILE CD1 C 13.825 0.20 1 354 123 134 ILE N N 122.953 0.20 1 355 124 135 GLU H H 8.256 0.02 1 356 124 135 GLU N N 127.507 0.20 1 357 125 136 VAL H H 8.392 0.02 1 358 125 136 VAL HG1 H 0.893 0.02 2 359 125 136 VAL CG1 C 21.140 0.20 2 360 125 136 VAL N N 123.511 0.20 1 361 126 137 GLU H H 9.093 0.02 1 362 126 137 GLU N N 128.242 0.20 1 363 127 138 LYS H H 9.219 0.02 1 364 127 138 LYS N N 131.560 0.20 1 365 129 140 ILE H H 8.060 0.02 1 366 129 140 ILE HD1 H 0.663 0.02 1 367 129 140 ILE CD1 C 10.841 0.20 1 368 129 140 ILE N N 125.191 0.20 1 369 130 141 VAL H H 8.024 0.02 1 370 130 141 VAL HG1 H 0.809 0.02 2 371 130 141 VAL HG2 H 0.790 0.02 2 372 130 141 VAL CG1 C 20.332 0.20 2 373 130 141 VAL CG2 C 21.493 0.20 2 374 130 141 VAL N N 126.342 0.20 1 375 132 143 VAL H H 8.621 0.02 1 376 132 143 VAL HG2 H 0.856 0.02 2 377 132 143 VAL CG2 C 23.257 0.20 2 378 132 143 VAL N N 122.074 0.20 1 379 133 144 THR H H 9.642 0.02 1 380 133 144 THR N N 123.521 0.20 1 381 134 145 ASP H H 8.780 0.02 1 382 134 145 ASP N N 121.214 0.20 1 383 135 146 ALA HB H 1.387 0.02 1 384 135 146 ALA CB C 17.829 0.20 1 385 137 148 VAL H H 7.571 0.02 1 386 137 148 VAL HG2 H 0.747 0.02 2 387 137 148 VAL CG2 C 22.333 0.20 2 388 137 148 VAL N N 123.149 0.20 1 389 138 149 ASP H H 8.626 0.02 1 390 138 149 ASP N N 120.802 0.20 1 391 139 150 GLY H H 8.110 0.02 1 392 139 150 GLY N N 107.883 0.20 1 393 140 151 MET HE H 1.176 0.02 1 394 140 151 MET CE C 16.999 0.20 1 395 141 152 LEU H H 8.489 0.02 1 396 141 152 LEU HD1 H 0.753 0.02 2 397 141 152 LEU HD2 H 0.716 0.02 2 398 141 152 LEU CD1 C 24.044 0.20 2 399 141 152 LEU CD2 C 25.523 0.20 2 400 141 152 LEU N N 121.796 0.20 1 401 142 153 ASP H H 7.946 0.02 1 402 142 153 ASP N N 119.511 0.20 1 403 143 154 THR H H 7.929 0.02 1 404 143 154 THR N N 118.267 0.20 1 405 144 155 LEU HD1 H 0.994 0.02 2 406 144 155 LEU HD2 H 0.748 0.02 2 407 144 155 LEU CD1 C 26.326 0.20 2 408 144 155 LEU CD2 C 22.488 0.20 2 409 145 156 ARG H H 8.212 0.02 1 410 145 156 ARG N N 119.364 0.20 1 411 146 157 LYS H H 7.829 0.02 1 412 146 157 LYS N N 119.353 0.20 1 413 147 158 GLN H H 7.809 0.02 1 414 147 158 GLN N N 118.555 0.20 1 415 148 159 GLN H H 8.478 0.02 1 416 148 159 GLN N N 120.893 0.20 1 417 149 160 ALA HB H 1.146 0.02 1 418 149 160 ALA CB C 19.647 0.20 1 419 150 161 THR H H 8.149 0.02 1 420 150 161 THR HA H 4.380 0.02 1 421 150 161 THR HB H 4.164 0.02 1 422 150 161 THR HG2 H 1.165 0.02 1 423 150 161 THR CA C 61.591 0.20 1 424 150 161 THR CB C 70.372 0.20 1 425 150 161 THR CG2 C 22.021 0.20 1 426 150 161 THR N N 114.995 0.20 1 427 151 162 TRP H H 8.437 0.02 1 428 151 162 TRP HA H 5.072 0.02 1 429 151 162 TRP HB2 H 2.732 0.02 2 430 151 162 TRP HB3 H 2.918 0.02 2 431 151 162 TRP HD1 H 7.027 0.02 1 432 151 162 TRP HE1 H 9.886 0.02 1 433 151 162 TRP HE3 H 7.180 0.02 1 434 151 162 TRP HH2 H 7.156 0.02 1 435 151 162 TRP CA C 56.347 0.20 1 436 151 162 TRP CB C 32.761 0.20 1 437 151 162 TRP CD1 C 127.409 0.20 1 438 151 162 TRP CE3 C 124.110 0.20 1 439 151 162 TRP CH2 C 123.267 0.20 1 440 151 162 TRP N N 122.869 0.20 1 441 151 162 TRP NE1 N 128.956 0.20 1 442 152 163 LYS H H 9.565 0.02 1 443 152 163 LYS HA H 4.968 0.02 1 444 152 163 LYS HB3 H 1.864 0.02 2 445 152 163 LYS HG2 H 1.416 0.02 1 446 152 163 LYS HG3 H 1.416 0.02 1 447 152 163 LYS HD2 H 1.706 0.02 1 448 152 163 LYS HD3 H 1.706 0.02 1 449 152 163 LYS HE2 H 2.965 0.02 1 450 152 163 LYS HE3 H 2.965 0.02 1 451 152 163 LYS CA C 54.265 0.20 1 452 152 163 LYS CB C 35.904 0.20 1 453 152 163 LYS CG C 23.842 0.20 1 454 152 163 LYS CD C 29.434 0.20 1 455 152 163 LYS CE C 42.131 0.20 1 456 152 163 LYS N N 121.621 0.20 1 457 153 164 GLU H H 8.903 0.02 1 458 153 164 GLU HA H 4.453 0.02 1 459 153 164 GLU HB2 H 1.845 0.02 1 460 153 164 GLU HB3 H 1.845 0.02 1 461 153 164 GLU HG2 H 2.242 0.02 2 462 153 164 GLU HG3 H 2.462 0.02 2 463 153 164 GLU CA C 58.230 0.20 1 464 153 164 GLU CB C 30.038 0.20 1 465 153 164 GLU CG C 37.276 0.20 1 466 153 164 GLU N N 124.069 0.20 1 467 154 165 LYS H H 8.843 0.02 1 468 154 165 LYS HA H 4.777 0.02 1 469 154 165 LYS HB2 H 1.706 0.02 2 470 154 165 LYS HD2 H 1.477 0.02 2 471 154 165 LYS HE2 H 2.554 0.02 2 472 154 165 LYS CA C 54.597 0.20 1 473 154 165 LYS CB C 36.180 0.20 1 474 154 165 LYS CD C 29.864 0.20 1 475 154 165 LYS CE C 42.193 0.20 1 476 154 165 LYS N N 123.826 0.20 1 477 155 166 ASP H H 8.731 0.02 1 478 155 166 ASP HA H 4.894 0.02 1 479 155 166 ASP HB2 H 2.687 0.02 2 480 155 166 ASP HB3 H 2.739 0.02 2 481 155 166 ASP CA C 53.309 0.20 1 482 155 166 ASP CB C 40.642 0.20 1 483 155 166 ASP N N 123.657 0.20 1 484 156 167 GLY H H 7.289 0.02 1 485 156 167 GLY HA2 H 3.903 0.02 2 486 156 167 GLY HA3 H 4.206 0.02 2 487 156 167 GLY CA C 44.064 0.20 1 488 156 167 GLY N N 106.418 0.20 1 489 157 168 ALA H H 8.260 0.02 1 490 157 168 ALA HA H 4.208 0.02 1 491 157 168 ALA HB H 1.119 0.02 1 492 157 168 ALA CA C 51.249 0.20 1 493 157 168 ALA CB C 20.194 0.20 1 494 157 168 ALA N N 119.989 0.20 1 495 158 169 VAL H H 8.766 0.02 1 496 158 169 VAL HA H 3.870 0.02 1 497 158 169 VAL HB H 2.119 0.02 1 498 158 169 VAL HG1 H 1.030 0.02 2 499 158 169 VAL HG2 H 1.223 0.02 2 500 158 169 VAL CA C 64.339 0.20 1 501 158 169 VAL CB C 32.825 0.20 1 502 158 169 VAL CG1 C 23.877 0.20 2 503 158 169 VAL CG2 C 25.871 0.20 2 504 158 169 VAL N N 119.228 0.20 1 505 159 170 GLU H H 9.654 0.02 1 506 159 170 GLU N N 132.162 0.20 1 507 160 171 ALA HA H 3.866 0.02 1 508 160 171 ALA HB H 1.499 0.02 1 509 160 171 ALA CA C 55.444 0.20 1 510 160 171 ALA CB C 20.017 0.20 1 511 161 172 GLU H H 8.107 0.02 1 512 161 172 GLU HA H 4.696 0.02 1 513 161 172 GLU HB2 H 2.087 0.02 1 514 161 172 GLU HB3 H 2.087 0.02 1 515 161 172 GLU HG2 H 2.206 0.02 1 516 161 172 GLU HG3 H 2.206 0.02 1 517 161 172 GLU CA C 55.147 0.20 1 518 161 172 GLU CB C 29.567 0.20 1 519 161 172 GLU CG C 37.263 0.20 1 520 161 172 GLU N N 111.837 0.20 1 521 162 173 ASP H H 7.270 0.02 1 522 162 173 ASP HA H 5.233 0.02 1 523 162 173 ASP CA C 55.279 0.20 1 524 162 173 ASP N N 122.895 0.20 1 525 163 174 ARG H H 8.899 0.02 1 526 163 174 ARG HA H 5.250 0.02 1 527 163 174 ARG HB2 H 0.165 0.02 2 528 163 174 ARG HB3 H 1.046 0.02 2 529 163 174 ARG HD2 H 2.375 0.02 1 530 163 174 ARG HD3 H 2.375 0.02 1 531 163 174 ARG CA C 54.744 0.20 1 532 163 174 ARG CB C 34.100 0.20 1 533 163 174 ARG CD C 43.726 0.20 1 534 163 174 ARG N N 118.483 0.20 1 535 164 175 VAL H H 9.034 0.02 1 536 164 175 VAL HA H 5.382 0.02 1 537 164 175 VAL HB H 2.170 0.02 1 538 164 175 VAL HG2 H 1.134 0.02 2 539 164 175 VAL CA C 58.187 0.20 1 540 164 175 VAL CB C 34.410 0.20 1 541 164 175 VAL CG2 C 24.232 0.20 2 542 164 175 VAL N N 119.528 0.20 1 543 165 176 THR H H 8.461 0.02 1 544 165 176 THR HA H 5.234 0.02 1 545 165 176 THR HB H 3.889 0.02 1 546 165 176 THR HG2 H 0.925 0.02 1 547 165 176 THR CA C 61.987 0.20 1 548 165 176 THR CB C 69.275 0.20 1 549 165 176 THR CG2 C 19.814 0.20 1 550 165 176 THR N N 119.090 0.20 1 551 166 177 ILE H H 9.590 0.02 1 552 166 177 ILE HA H 5.746 0.02 1 553 166 177 ILE HB H 2.087 0.02 1 554 166 177 ILE HG2 H 1.018 0.02 1 555 166 177 ILE HD1 H 1.032 0.02 1 556 166 177 ILE CA C 58.519 0.20 1 557 166 177 ILE CB C 42.860 0.20 1 558 166 177 ILE CG2 C 19.275 0.20 1 559 166 177 ILE CD1 C 14.568 0.20 1 560 166 177 ILE N N 119.703 0.20 1 561 167 178 ASP H H 8.555 0.02 1 562 167 178 ASP HA H 5.365 0.02 1 563 167 178 ASP HB2 H 2.627 0.02 2 564 167 178 ASP CA C 52.581 0.20 1 565 167 178 ASP CB C 42.466 0.20 1 566 167 178 ASP N N 119.158 0.20 1 567 168 179 PHE H H 8.584 0.02 1 568 168 179 PHE HA H 6.111 0.02 1 569 168 179 PHE HD1 H 6.964 0.02 1 570 168 179 PHE HD2 H 6.964 0.02 1 571 168 179 PHE HE1 H 6.377 0.02 1 572 168 179 PHE HE2 H 6.377 0.02 1 573 168 179 PHE HZ H 6.479 0.02 1 574 168 179 PHE CA C 55.812 0.20 1 575 168 179 PHE CD1 C 132.474 0.20 1 576 168 179 PHE CD2 C 132.474 0.20 1 577 168 179 PHE CE1 C 130.227 0.20 1 578 168 179 PHE CE2 C 130.227 0.20 1 579 168 179 PHE CZ C 130.149 0.20 1 580 168 179 PHE N N 114.570 0.20 1 581 169 180 THR H H 8.476 0.02 1 582 169 180 THR HA H 4.830 0.02 1 583 169 180 THR HB H 4.033 0.02 1 584 169 180 THR HG2 H 1.083 0.02 1 585 169 180 THR CA C 62.459 0.20 1 586 169 180 THR CB C 71.683 0.20 1 587 169 180 THR CG2 C 21.530 0.20 1 588 169 180 THR N N 114.609 0.20 1 589 170 181 GLY H H 9.241 0.02 1 590 170 181 GLY HA2 H 2.585 0.02 2 591 170 181 GLY HA3 H 4.615 0.02 2 592 170 181 GLY CA C 45.132 0.20 1 593 170 181 GLY N N 119.239 0.20 1 594 171 182 SER H H 9.033 0.02 1 595 171 182 SER HA H 5.051 0.02 1 596 171 182 SER HB2 H 3.297 0.02 2 597 171 182 SER HB3 H 3.544 0.02 2 598 171 182 SER CA C 57.440 0.20 1 599 171 182 SER CB C 66.230 0.20 1 600 171 182 SER N N 115.777 0.20 1 601 172 183 VAL H H 8.859 0.02 1 602 172 183 VAL HA H 4.476 0.02 1 603 172 183 VAL HB H 1.901 0.02 1 604 172 183 VAL HG1 H 0.804 0.02 2 605 172 183 VAL HG2 H 0.902 0.02 2 606 172 183 VAL CA C 61.465 0.20 1 607 172 183 VAL CB C 34.789 0.20 1 608 172 183 VAL CG1 C 21.426 0.20 2 609 172 183 VAL CG2 C 21.555 0.20 2 610 172 183 VAL N N 120.295 0.20 1 611 173 184 ASP H H 9.623 0.02 1 612 173 184 ASP HB2 H 2.724 0.02 2 613 173 184 ASP HB3 H 3.019 0.02 2 614 173 184 ASP CB C 39.631 0.20 1 615 173 184 ASP N N 129.087 0.20 1 616 174 185 GLY H H 8.671 0.02 1 617 174 185 GLY HA2 H 3.593 0.02 2 618 174 185 GLY HA3 H 4.218 0.02 2 619 174 185 GLY CA C 45.277 0.20 1 620 174 185 GLY N N 102.377 0.20 1 621 175 186 GLU H H 7.903 0.02 1 622 175 186 GLU HA H 4.729 0.02 1 623 175 186 GLU HB2 H 1.994 0.02 2 624 175 186 GLU HB3 H 2.146 0.02 2 625 175 186 GLU HG2 H 2.256 0.02 1 626 175 186 GLU HG3 H 2.256 0.02 1 627 175 186 GLU CA C 54.791 0.20 1 628 175 186 GLU CB C 32.024 0.20 1 629 175 186 GLU CG C 36.044 0.20 1 630 175 186 GLU N N 120.481 0.20 1 631 176 187 GLU H H 8.870 0.02 1 632 176 187 GLU HA H 4.472 0.02 1 633 176 187 GLU HB2 H 2.058 0.02 1 634 176 187 GLU HB3 H 2.058 0.02 1 635 176 187 GLU HG2 H 2.262 0.02 1 636 176 187 GLU HG3 H 2.262 0.02 1 637 176 187 GLU CA C 56.981 0.20 1 638 176 187 GLU CB C 30.165 0.20 1 639 176 187 GLU CG C 36.713 0.20 1 640 176 187 GLU N N 125.886 0.20 1 641 177 188 PHE H H 7.012 0.02 1 642 177 188 PHE HA H 5.103 0.02 1 643 177 188 PHE HB2 H 3.014 0.02 2 644 177 188 PHE HB3 H 3.125 0.02 2 645 177 188 PHE HD1 H 7.074 0.02 1 646 177 188 PHE HD2 H 7.074 0.02 1 647 177 188 PHE HE1 H 6.937 0.02 1 648 177 188 PHE HE2 H 6.937 0.02 1 649 177 188 PHE HZ H 7.133 0.02 1 650 177 188 PHE CA C 54.168 0.20 1 651 177 188 PHE CB C 41.288 0.20 1 652 177 188 PHE CD1 C 133.672 0.20 1 653 177 188 PHE CD2 C 133.672 0.20 1 654 177 188 PHE CE1 C 130.273 0.20 1 655 177 188 PHE CE2 C 130.273 0.20 1 656 177 188 PHE CZ C 128.437 0.20 1 657 177 188 PHE N N 116.904 0.20 1 658 178 189 GLU H H 9.047 0.02 1 659 178 189 GLU HA H 4.182 0.02 1 660 178 189 GLU HG2 H 2.368 0.02 1 661 178 189 GLU HG3 H 2.368 0.02 1 662 178 189 GLU CA C 57.948 0.20 1 663 178 189 GLU CG C 36.163 0.20 1 664 178 189 GLU N N 124.721 0.20 1 665 179 190 GLY H H 8.998 0.02 1 666 179 190 GLY HA2 H 4.073 0.02 2 667 179 190 GLY HA3 H 4.455 0.02 2 668 179 190 GLY CA C 45.811 0.20 1 669 179 190 GLY N N 113.437 0.20 1 670 180 191 GLY H H 7.769 0.02 1 671 180 191 GLY HA2 H 2.880 0.02 2 672 180 191 GLY HA3 H 4.291 0.02 2 673 180 191 GLY CA C 46.385 0.20 1 674 180 191 GLY N N 106.267 0.20 1 675 181 192 LYS H H 7.555 0.02 1 676 181 192 LYS HA H 5.285 0.02 1 677 181 192 LYS HB2 H 1.788 0.02 1 678 181 192 LYS HB3 H 1.788 0.02 1 679 181 192 LYS HG2 H 1.212 0.02 2 680 181 192 LYS HG3 H 1.544 0.02 2 681 181 192 LYS HD2 H 1.561 0.02 2 682 181 192 LYS HD3 H 1.629 0.02 2 683 181 192 LYS CA C 54.413 0.20 1 684 181 192 LYS CB C 36.337 0.20 1 685 181 192 LYS CG C 24.593 0.20 1 686 181 192 LYS CD C 29.264 0.20 1 687 181 192 LYS N N 119.134 0.20 1 688 182 193 ALA H H 8.031 0.02 1 689 182 193 ALA HB H 0.666 0.02 1 690 182 193 ALA CB C 23.224 0.20 1 691 182 193 ALA N N 125.121 0.20 1 692 183 194 SER H H 8.429 0.02 1 693 183 194 SER HA H 5.099 0.02 1 694 183 194 SER HB2 H 3.547 0.02 2 695 183 194 SER HB3 H 3.674 0.02 2 696 183 194 SER CA C 56.374 0.20 1 697 183 194 SER CB C 65.406 0.20 1 698 183 194 SER N N 115.504 0.20 1 699 184 195 ASP H H 9.644 0.02 1 700 184 195 ASP HA H 3.794 0.02 1 701 184 195 ASP HB2 H 2.563 0.02 2 702 184 195 ASP HB3 H 2.625 0.02 2 703 184 195 ASP CA C 56.186 0.20 1 704 184 195 ASP CB C 39.602 0.20 1 705 184 195 ASP N N 123.296 0.20 1 706 185 196 PHE H H 9.170 0.02 1 707 185 196 PHE HA H 4.407 0.02 1 708 185 196 PHE HB2 H 2.670 0.02 2 709 185 196 PHE HB3 H 3.277 0.02 2 710 185 196 PHE HE1 H 7.275 0.02 1 711 185 196 PHE HE2 H 7.275 0.02 1 712 185 196 PHE HZ H 7.167 0.02 1 713 185 196 PHE CA C 58.016 0.20 1 714 185 196 PHE CB C 40.318 0.20 1 715 185 196 PHE CE1 C 131.447 0.20 1 716 185 196 PHE CE2 C 131.447 0.20 1 717 185 196 PHE CZ C 129.578 0.20 1 718 185 196 PHE N N 121.401 0.20 1 719 186 197 VAL H H 7.884 0.02 1 720 186 197 VAL HA H 4.512 0.02 1 721 186 197 VAL HB H 1.639 0.02 1 722 186 197 VAL HG1 H 0.427 0.02 2 723 186 197 VAL HG2 H 0.809 0.02 2 724 186 197 VAL CA C 62.000 0.20 1 725 186 197 VAL CB C 31.452 0.20 1 726 186 197 VAL CG1 C 20.681 0.20 2 727 186 197 VAL CG2 C 20.992 0.20 2 728 186 197 VAL N N 129.373 0.20 1 729 187 198 LEU H H 9.313 0.02 1 730 187 198 LEU HA H 4.414 0.02 1 731 187 198 LEU HB2 H 1.228 0.02 2 732 187 198 LEU HB3 H 1.935 0.02 2 733 187 198 LEU HG H 1.331 0.02 1 734 187 198 LEU HD1 H 0.948 0.02 2 735 187 198 LEU HD2 H 0.991 0.02 2 736 187 198 LEU CA C 52.970 0.20 1 737 187 198 LEU CB C 44.756 0.20 1 738 187 198 LEU CG C 27.657 0.20 1 739 187 198 LEU CD1 C 26.005 0.20 2 740 187 198 LEU CD2 C 23.099 0.20 2 741 187 198 LEU N N 130.998 0.20 1 742 188 199 ALA H H 8.648 0.02 1 743 188 199 ALA HA H 4.277 0.02 1 744 188 199 ALA HB H 1.261 0.02 1 745 188 199 ALA CA C 51.869 0.20 1 746 188 199 ALA CB C 16.869 0.20 1 747 188 199 ALA N N 132.436 0.20 1 748 189 200 MET H H 8.636 0.02 1 749 189 200 MET HA H 4.207 0.02 1 750 189 200 MET HB2 H 2.111 0.02 1 751 189 200 MET HB3 H 2.111 0.02 1 752 189 200 MET HG2 H 2.276 0.02 2 753 189 200 MET HG3 H 2.633 0.02 2 754 189 200 MET HE H 2.002 0.02 1 755 189 200 MET CA C 56.925 0.20 1 756 189 200 MET CB C 33.417 0.20 1 757 189 200 MET CG C 32.435 0.20 1 758 189 200 MET CE C 16.998 0.20 1 759 189 200 MET N N 125.261 0.20 1 760 190 201 GLY H H 10.201 0.02 1 761 190 201 GLY HA2 H 3.931 0.02 2 762 190 201 GLY HA3 H 4.269 0.02 2 763 190 201 GLY CA C 46.440 0.20 1 764 190 201 GLY N N 109.632 0.20 1 765 191 202 GLN H H 9.071 0.02 1 766 191 202 GLN HA H 4.636 0.02 1 767 191 202 GLN HG2 H 2.238 0.02 2 768 191 202 GLN HG3 H 2.299 0.02 2 769 191 202 GLN CA C 54.247 0.20 1 770 191 202 GLN CG C 33.388 0.20 1 771 191 202 GLN N N 118.562 0.20 1 772 192 203 GLY H H 9.148 0.02 1 773 192 203 GLY HA2 H 4.027 0.02 1 774 192 203 GLY HA3 H 4.027 0.02 1 775 192 203 GLY CA C 46.447 0.20 1 776 192 203 GLY N N 110.966 0.20 1 777 194 205 MET HA H 5.086 0.02 1 778 194 205 MET HB2 H 2.083 0.02 1 779 194 205 MET HB3 H 2.083 0.02 1 780 194 205 MET HE H 0.749 0.02 1 781 194 205 MET CA C 51.937 0.20 1 782 194 205 MET CB C 33.716 0.20 1 783 194 205 MET CE C 16.256 0.20 1 784 195 206 ILE H H 7.550 0.02 1 785 195 206 ILE HA H 4.341 0.02 1 786 195 206 ILE HB H 1.902 0.02 1 787 195 206 ILE HG12 H 1.309 0.02 1 788 195 206 ILE HG13 H 1.309 0.02 1 789 195 206 ILE HG2 H 0.969 0.02 1 790 195 206 ILE HD1 H 0.310 0.02 1 791 195 206 ILE CA C 60.162 0.20 1 792 195 206 ILE CB C 37.256 0.20 1 793 195 206 ILE CG1 C 25.257 0.20 1 794 195 206 ILE CG2 C 18.624 0.20 1 795 195 206 ILE CD1 C 14.014 0.20 1 796 195 206 ILE N N 115.418 0.20 1 797 197 208 GLY H H 8.479 0.02 1 798 197 208 GLY HA2 H 3.763 0.02 2 799 197 208 GLY HA3 H 4.407 0.02 2 800 197 208 GLY CA C 45.741 0.20 1 801 197 208 GLY N N 111.764 0.20 1 802 198 209 PHE H H 7.729 0.02 1 803 198 209 PHE HB2 H 2.492 0.02 2 804 198 209 PHE HB3 H 3.069 0.02 2 805 198 209 PHE HD1 H 6.221 0.02 1 806 198 209 PHE HD2 H 6.221 0.02 1 807 198 209 PHE HE1 H 5.795 0.02 1 808 198 209 PHE HE2 H 5.795 0.02 1 809 198 209 PHE HZ H 5.732 0.02 1 810 198 209 PHE CB C 40.843 0.20 1 811 198 209 PHE CD1 C 130.736 0.20 1 812 198 209 PHE CD2 C 130.736 0.20 1 813 198 209 PHE CE1 C 130.408 0.20 1 814 198 209 PHE CE2 C 130.408 0.20 1 815 198 209 PHE CZ C 128.557 0.20 1 816 198 209 PHE N N 122.737 0.20 1 817 200 211 ASP HA H 4.210 0.02 1 818 200 211 ASP HB2 H 2.517 0.02 2 819 200 211 ASP HB3 H 2.653 0.02 2 820 200 211 ASP CA C 57.192 0.20 1 821 200 211 ASP CB C 40.295 0.20 1 822 201 212 GLY H H 7.408 0.02 1 823 201 212 GLY HA2 H 3.613 0.02 2 824 201 212 GLY HA3 H 4.147 0.02 2 825 201 212 GLY CA C 46.135 0.20 1 826 201 212 GLY N N 103.102 0.20 1 827 202 213 ILE H H 7.347 0.02 1 828 202 213 ILE HA H 3.868 0.02 1 829 202 213 ILE HB H 1.948 0.02 1 830 202 213 ILE HG12 H 0.934 0.02 1 831 202 213 ILE HG13 H 0.934 0.02 1 832 202 213 ILE HG2 H 1.169 0.02 1 833 202 213 ILE HD1 H 0.756 0.02 1 834 202 213 ILE CA C 63.159 0.20 1 835 202 213 ILE CB C 38.796 0.20 1 836 202 213 ILE CG1 C 29.153 0.20 1 837 202 213 ILE CG2 C 18.882 0.20 1 838 202 213 ILE CD1 C 14.042 0.20 1 839 202 213 ILE N N 119.068 0.20 1 840 203 214 LYS H H 7.027 0.02 1 841 203 214 LYS HA H 3.576 0.02 1 842 203 214 LYS HB2 H 1.728 0.02 1 843 203 214 LYS HB3 H 1.728 0.02 1 844 203 214 LYS HG2 H 1.121 0.02 1 845 203 214 LYS HG3 H 1.121 0.02 1 846 203 214 LYS HD2 H 1.761 0.02 1 847 203 214 LYS HD3 H 1.761 0.02 1 848 203 214 LYS CA C 58.595 0.20 1 849 203 214 LYS CB C 32.477 0.20 1 850 203 214 LYS CG C 26.011 0.20 1 851 203 214 LYS CD C 29.626 0.20 1 852 203 214 LYS N N 117.552 0.20 1 853 204 215 GLY H H 8.920 0.02 1 854 204 215 GLY HA2 H 3.494 0.02 2 855 204 215 GLY HA3 H 4.185 0.02 2 856 204 215 GLY CA C 45.136 0.20 1 857 204 215 GLY N N 109.266 0.20 1 858 205 216 HIS H H 7.492 0.02 1 859 205 216 HIS HB2 H 2.828 0.02 2 860 205 216 HIS HB3 H 2.875 0.02 2 861 205 216 HIS HD2 H 6.577 0.02 1 862 205 216 HIS CB C 30.469 0.20 1 863 205 216 HIS CD2 C 120.738 0.20 1 864 205 216 HIS N N 117.812 0.20 1 865 206 217 LYS H H 8.632 0.02 1 866 206 217 LYS HA H 4.686 0.02 1 867 206 217 LYS HB2 H 1.652 0.02 2 868 206 217 LYS HB3 H 1.763 0.02 2 869 206 217 LYS HG2 H 1.145 0.02 1 870 206 217 LYS HG3 H 1.145 0.02 1 871 206 217 LYS HD2 H 1.688 0.02 1 872 206 217 LYS HD3 H 1.688 0.02 1 873 206 217 LYS CA C 54.675 0.20 1 874 206 217 LYS CB C 36.235 0.20 1 875 206 217 LYS CG C 24.824 0.20 1 876 206 217 LYS CD C 29.387 0.20 1 877 206 217 LYS N N 117.905 0.20 1 878 207 218 ALA H H 8.777 0.02 1 879 207 218 ALA HA H 3.884 0.02 1 880 207 218 ALA HB H 1.402 0.02 1 881 207 218 ALA CA C 53.758 0.20 1 882 207 218 ALA CB C 18.040 0.20 1 883 207 218 ALA N N 121.088 0.20 1 884 208 219 GLY H H 9.204 0.02 1 885 208 219 GLY HA2 H 3.846 0.02 2 886 208 219 GLY HA3 H 4.476 0.02 2 887 208 219 GLY CA C 44.774 0.20 1 888 208 219 GLY N N 110.710 0.20 1 889 209 220 GLU H H 7.938 0.02 1 890 209 220 GLU HA H 4.621 0.02 1 891 209 220 GLU HB2 H 2.361 0.02 1 892 209 220 GLU HB3 H 2.361 0.02 1 893 209 220 GLU HG2 H 2.383 0.02 2 894 209 220 GLU HG3 H 2.610 0.02 2 895 209 220 GLU CA C 57.225 0.20 1 896 209 220 GLU CB C 32.332 0.20 1 897 209 220 GLU CG C 38.266 0.20 1 898 209 220 GLU N N 119.805 0.20 1 899 210 221 GLU H H 8.301 0.02 1 900 210 221 GLU HA H 5.397 0.02 1 901 210 221 GLU HG2 H 2.129 0.02 2 902 210 221 GLU HG3 H 2.203 0.02 2 903 210 221 GLU CA C 54.720 0.20 1 904 210 221 GLU CG C 36.821 0.20 1 905 210 221 GLU N N 119.721 0.20 1 906 211 222 PHE H H 8.296 0.02 1 907 211 222 PHE HA H 5.006 0.02 1 908 211 222 PHE HB2 H 2.976 0.02 2 909 211 222 PHE HB3 H 3.197 0.02 2 910 211 222 PHE HD1 H 6.513 0.02 1 911 211 222 PHE HD2 H 6.513 0.02 1 912 211 222 PHE HE1 H 6.798 0.02 1 913 211 222 PHE HE2 H 6.798 0.02 1 914 211 222 PHE HZ H 6.737 0.02 1 915 211 222 PHE CA C 55.790 0.20 1 916 211 222 PHE CB C 39.000 0.20 1 917 211 222 PHE CD1 C 132.450 0.20 1 918 211 222 PHE CD2 C 132.450 0.20 1 919 211 222 PHE CE1 C 130.140 0.20 1 920 211 222 PHE CE2 C 130.140 0.20 1 921 211 222 PHE CZ C 127.431 0.20 1 922 211 222 PHE N N 120.340 0.20 1 923 212 223 THR H H 8.751 0.02 1 924 212 223 THR HA H 5.541 0.02 1 925 212 223 THR HB H 3.953 0.02 1 926 212 223 THR HG2 H 1.116 0.02 1 927 212 223 THR CA C 60.756 0.20 1 928 212 223 THR CB C 71.091 0.20 1 929 212 223 THR CG2 C 21.979 0.20 1 930 212 223 THR N N 115.323 0.20 1 931 213 224 ILE H H 8.956 0.02 1 932 213 224 ILE HA H 4.850 0.02 1 933 213 224 ILE HB H 1.898 0.02 1 934 213 224 ILE HG2 H 0.882 0.02 1 935 213 224 ILE HD1 H 0.234 0.02 1 936 213 224 ILE CA C 59.398 0.20 1 937 213 224 ILE CB C 41.303 0.20 1 938 213 224 ILE CG2 C 18.311 0.20 1 939 213 224 ILE CD1 C 14.512 0.20 1 940 213 224 ILE N N 119.607 0.20 1 941 214 225 ASP H H 8.506 0.02 1 942 214 225 ASP HA H 5.459 0.02 1 943 214 225 ASP HB2 H 2.514 0.02 2 944 214 225 ASP HB3 H 2.638 0.02 2 945 214 225 ASP CA C 53.857 0.20 1 946 214 225 ASP CB C 43.038 0.20 1 947 214 225 ASP N N 123.134 0.20 1 948 215 226 VAL H H 8.611 0.02 1 949 215 226 VAL HA H 4.494 0.02 1 950 215 226 VAL HB H 1.886 0.02 1 951 215 226 VAL HG1 H 0.602 0.02 2 952 215 226 VAL HG2 H 0.662 0.02 2 953 215 226 VAL CA C 60.042 0.20 1 954 215 226 VAL CB C 36.502 0.20 1 955 215 226 VAL CG1 C 21.656 0.20 2 956 215 226 VAL CG2 C 21.082 0.20 2 957 215 226 VAL N N 119.114 0.20 1 958 216 227 THR H H 8.634 0.02 1 959 216 227 THR HA H 4.983 0.02 1 960 216 227 THR HB H 3.819 0.02 1 961 216 227 THR HG2 H 1.030 0.02 1 962 216 227 THR CA C 61.187 0.20 1 963 216 227 THR CB C 70.095 0.20 1 964 216 227 THR CG2 C 21.389 0.20 1 965 216 227 THR N N 120.641 0.20 1 966 217 228 PHE H H 8.931 0.02 1 967 217 228 PHE HB2 H 2.238 0.02 2 968 217 228 PHE HB3 H 3.274 0.02 2 969 217 228 PHE HD1 H 6.496 0.02 1 970 217 228 PHE HD2 H 6.496 0.02 1 971 217 228 PHE HE1 H 6.824 0.02 1 972 217 228 PHE HE2 H 6.824 0.02 1 973 217 228 PHE HZ H 7.004 0.02 1 974 217 228 PHE CB C 39.430 0.20 1 975 217 228 PHE CD1 C 131.697 0.20 1 976 217 228 PHE CD2 C 131.697 0.20 1 977 217 228 PHE CE1 C 130.545 0.20 1 978 217 228 PHE CE2 C 130.545 0.20 1 979 217 228 PHE CZ C 128.413 0.20 1 980 217 228 PHE N N 127.602 0.20 1 981 218 229 PRO HA H 4.511 0.02 1 982 218 229 PRO HB2 H 2.605 0.02 2 983 218 229 PRO HG2 H 2.208 0.02 2 984 218 229 PRO HG3 H 2.300 0.02 2 985 218 229 PRO HD2 H 3.315 0.02 2 986 218 229 PRO HD3 H 3.913 0.02 2 987 218 229 PRO CA C 62.625 0.20 1 988 218 229 PRO CB C 32.673 0.20 1 989 218 229 PRO CG C 27.713 0.20 1 990 218 229 PRO CD C 50.597 0.20 1 991 219 230 GLU H H 8.900 0.02 1 992 219 230 GLU HA H 3.873 0.02 1 993 219 230 GLU HG2 H 2.349 0.02 2 994 219 230 GLU CA C 59.441 0.20 1 995 219 230 GLU CG C 36.565 0.20 1 996 219 230 GLU N N 122.935 0.20 1 997 220 231 GLU H H 8.180 0.02 1 998 220 231 GLU HA H 4.533 0.02 1 999 220 231 GLU HB2 H 1.942 0.02 2 1000 220 231 GLU HB3 H 2.165 0.02 2 1001 220 231 GLU HG2 H 2.257 0.02 1 1002 220 231 GLU HG3 H 2.257 0.02 1 1003 220 231 GLU CA C 55.275 0.20 1 1004 220 231 GLU CB C 28.684 0.20 1 1005 220 231 GLU CG C 36.117 0.20 1 1006 220 231 GLU N N 115.074 0.20 1 1007 221 232 TYR H H 7.477 0.02 1 1008 221 232 TYR HB2 H 2.384 0.02 2 1009 221 232 TYR HB3 H 3.396 0.02 2 1010 221 232 TYR HD1 H 7.107 0.02 1 1011 221 232 TYR HD2 H 7.107 0.02 1 1012 221 232 TYR HE1 H 6.732 0.02 1 1013 221 232 TYR HE2 H 6.732 0.02 1 1014 221 232 TYR CB C 40.632 0.20 1 1015 221 232 TYR CD1 C 132.078 0.20 1 1016 221 232 TYR CD2 C 132.078 0.20 1 1017 221 232 TYR CE1 C 119.729 0.20 1 1018 221 232 TYR CE2 C 119.729 0.20 1 1019 221 232 TYR N N 122.128 0.20 1 1020 222 233 HIS H H 6.855 0.02 1 1021 222 233 HIS HA H 4.149 0.02 1 1022 222 233 HIS HB2 H 2.881 0.02 2 1023 222 233 HIS HB3 H 3.031 0.02 2 1024 222 233 HIS HD2 H 6.678 0.02 1 1025 222 233 HIS CA C 58.246 0.20 1 1026 222 233 HIS CB C 29.861 0.20 1 1027 222 233 HIS CD2 C 118.885 0.20 1 1028 222 233 HIS N N 120.583 0.20 1 1029 223 234 ALA H H 5.566 0.02 1 1030 223 234 ALA HA H 4.550 0.02 1 1031 223 234 ALA HB H 1.148 0.02 1 1032 223 234 ALA CA C 50.809 0.20 1 1033 223 234 ALA CB C 18.383 0.20 1 1034 223 234 ALA N N 122.633 0.20 1 1035 224 235 GLU H H 8.923 0.02 1 1036 224 235 GLU HA H 3.785 0.02 1 1037 224 235 GLU HB2 H 2.071 0.02 1 1038 224 235 GLU HB3 H 2.071 0.02 1 1039 224 235 GLU HG2 H 2.330 0.02 1 1040 224 235 GLU HG3 H 2.330 0.02 1 1041 224 235 GLU CA C 59.739 0.20 1 1042 224 235 GLU CB C 30.289 0.20 1 1043 224 235 GLU CG C 35.875 0.20 1 1044 224 235 GLU N N 126.791 0.20 1 1045 225 236 ASN H H 8.772 0.02 1 1046 225 236 ASN HA H 4.442 0.02 1 1047 225 236 ASN HB2 H 2.730 0.02 2 1048 225 236 ASN HB3 H 2.766 0.02 2 1049 225 236 ASN CA C 54.486 0.20 1 1050 225 236 ASN CB C 36.848 0.20 1 1051 225 236 ASN N N 112.844 0.20 1 1052 226 237 LEU H H 7.071 0.02 1 1053 226 237 LEU HA H 4.041 0.02 1 1054 226 237 LEU HB2 H 0.115 0.02 2 1055 226 237 LEU HB3 H 0.852 0.02 2 1056 226 237 LEU HD1 H 0.074 0.02 2 1057 226 237 LEU HD2 H -0.265 0.02 2 1058 226 237 LEU CA C 54.013 0.20 1 1059 226 237 LEU CB C 43.321 0.20 1 1060 226 237 LEU CD1 C 25.232 0.20 2 1061 226 237 LEU CD2 C 21.199 0.20 2 1062 226 237 LEU N N 117.327 0.20 1 1063 227 238 LYS H H 7.015 0.02 1 1064 227 238 LYS HA H 3.828 0.02 1 1065 227 238 LYS HB2 H 1.822 0.02 2 1066 227 238 LYS HG2 H 1.489 0.02 2 1067 227 238 LYS HG3 H 1.571 0.02 2 1068 227 238 LYS CA C 58.165 0.20 1 1069 227 238 LYS CB C 32.491 0.20 1 1070 227 238 LYS CG C 23.980 0.20 1 1071 227 238 LYS N N 117.407 0.20 1 1072 228 239 GLY H H 7.214 0.02 1 1073 228 239 GLY HA2 H 3.693 0.02 2 1074 228 239 GLY HA3 H 4.026 0.02 2 1075 228 239 GLY CA C 46.053 0.20 1 1076 228 239 GLY N N 111.321 0.20 1 1077 229 240 LYS H H 7.871 0.02 1 1078 229 240 LYS HB2 H 1.625 0.02 2 1079 229 240 LYS HB3 H 1.886 0.02 2 1080 229 240 LYS HD2 H 1.560 0.02 2 1081 229 240 LYS HD3 H 1.633 0.02 2 1082 229 240 LYS CB C 33.211 0.20 1 1083 229 240 LYS CD C 28.632 0.20 1 1084 229 240 LYS N N 119.219 0.20 1 1085 230 241 ALA H H 8.366 0.02 1 1086 230 241 ALA HB H 1.426 0.02 1 1087 230 241 ALA CB C 18.895 0.20 1 1088 230 241 ALA N N 123.883 0.20 1 1089 231 242 ALA H H 9.314 0.02 1 1090 231 242 ALA HA H 5.235 0.02 1 1091 231 242 ALA HB H 1.305 0.02 1 1092 231 242 ALA CA C 50.376 0.20 1 1093 231 242 ALA CB C 24.262 0.20 1 1094 231 242 ALA N N 126.753 0.20 1 1095 232 243 LYS H H 8.687 0.02 1 1096 232 243 LYS HA H 5.450 0.02 1 1097 232 243 LYS HB2 H 1.554 0.02 2 1098 232 243 LYS HB3 H 1.592 0.02 2 1099 232 243 LYS CA C 54.416 0.20 1 1100 232 243 LYS CB C 36.086 0.20 1 1101 232 243 LYS N N 120.561 0.20 1 1102 233 244 PHE H H 9.143 0.02 1 1103 233 244 PHE HA H 5.243 0.02 1 1104 233 244 PHE HB2 H 2.463 0.02 2 1105 233 244 PHE HB3 H 2.679 0.02 2 1106 233 244 PHE HD1 H 6.998 0.02 1 1107 233 244 PHE HD2 H 6.998 0.02 1 1108 233 244 PHE HE1 H 7.137 0.02 1 1109 233 244 PHE HE2 H 7.137 0.02 1 1110 233 244 PHE HZ H 7.417 0.02 1 1111 233 244 PHE CA C 56.802 0.20 1 1112 233 244 PHE CB C 42.231 0.20 1 1113 233 244 PHE CD1 C 131.511 0.20 1 1114 233 244 PHE CD2 C 131.511 0.20 1 1115 233 244 PHE CE1 C 131.598 0.20 1 1116 233 244 PHE CE2 C 131.598 0.20 1 1117 233 244 PHE CZ C 129.203 0.20 1 1118 233 244 PHE N N 118.831 0.20 1 1119 234 245 ALA H H 8.544 0.02 1 1120 234 245 ALA HA H 4.649 0.02 1 1121 234 245 ALA HB H 1.354 0.02 1 1122 234 245 ALA CA C 51.763 0.20 1 1123 234 245 ALA CB C 18.765 0.20 1 1124 234 245 ALA N N 127.993 0.20 1 1125 235 246 ILE H H 9.151 0.02 1 1126 235 246 ILE HA H 4.777 0.02 1 1127 235 246 ILE HB H 0.552 0.02 1 1128 235 246 ILE HG2 H 0.498 0.02 1 1129 235 246 ILE HD1 H 0.306 0.02 1 1130 235 246 ILE CA C 58.815 0.20 1 1131 235 246 ILE CB C 38.346 0.20 1 1132 235 246 ILE CG2 C 17.924 0.20 1 1133 235 246 ILE CD1 C 12.328 0.20 1 1134 235 246 ILE N N 126.269 0.20 1 1135 236 247 ASN H H 8.593 0.02 1 1136 236 247 ASN HA H 5.009 0.02 1 1137 236 247 ASN HB2 H 2.706 0.02 2 1138 236 247 ASN HB3 H 2.868 0.02 2 1139 236 247 ASN CA C 52.091 0.20 1 1140 236 247 ASN CB C 40.209 0.20 1 1141 236 247 ASN N N 124.152 0.20 1 1142 237 248 LEU H H 8.601 0.02 1 1143 237 248 LEU HA H 4.709 0.02 1 1144 237 248 LEU HB2 H 1.294 0.02 1 1145 237 248 LEU HB3 H 1.294 0.02 1 1146 237 248 LEU HG H 1.367 0.02 1 1147 237 248 LEU HD1 H 0.847 0.02 2 1148 237 248 LEU HD2 H 0.950 0.02 2 1149 237 248 LEU CA C 54.675 0.20 1 1150 237 248 LEU CB C 42.860 0.20 1 1151 237 248 LEU CG C 28.091 0.20 1 1152 237 248 LEU CD1 C 27.155 0.20 2 1153 237 248 LEU CD2 C 25.043 0.20 2 1154 237 248 LEU N N 127.425 0.20 1 1155 238 249 LYS H H 8.677 0.02 1 1156 238 249 LYS HA H 4.368 0.02 1 1157 238 249 LYS HB2 H 1.455 0.02 2 1158 238 249 LYS HB3 H 1.852 0.02 2 1159 238 249 LYS HG2 H 1.218 0.02 1 1160 238 249 LYS HG3 H 1.218 0.02 1 1161 238 249 LYS HD2 H 1.531 0.02 2 1162 238 249 LYS HD3 H 1.600 0.02 2 1163 238 249 LYS CA C 58.268 0.20 1 1164 238 249 LYS CB C 33.513 0.20 1 1165 238 249 LYS CG C 25.288 0.20 1 1166 238 249 LYS CD C 28.927 0.20 1 1167 238 249 LYS N N 127.371 0.20 1 1168 239 250 LYS H H 7.610 0.02 1 1169 239 250 LYS HA H 4.481 0.02 1 1170 239 250 LYS HD2 H 1.547 0.02 1 1171 239 250 LYS HD3 H 1.547 0.02 1 1172 239 250 LYS HE2 H 2.794 0.02 1 1173 239 250 LYS HE3 H 2.794 0.02 1 1174 239 250 LYS CA C 56.642 0.20 1 1175 239 250 LYS CD C 29.321 0.20 1 1176 239 250 LYS CE C 41.644 0.20 1 1177 239 250 LYS N N 117.739 0.20 1 1178 240 251 VAL H H 9.169 0.02 1 1179 240 251 VAL HA H 4.622 0.02 1 1180 240 251 VAL HB H 2.297 0.02 1 1181 240 251 VAL HG1 H 1.032 0.02 2 1182 240 251 VAL HG2 H 1.064 0.02 2 1183 240 251 VAL CA C 62.159 0.20 1 1184 240 251 VAL CB C 34.582 0.20 1 1185 240 251 VAL CG1 C 22.993 0.20 2 1186 240 251 VAL CG2 C 22.877 0.20 2 1187 240 251 VAL N N 126.249 0.20 1 1188 241 252 GLU H H 9.360 0.02 1 1189 241 252 GLU HA H 5.348 0.02 1 1190 241 252 GLU CA C 54.173 0.20 1 1191 241 252 GLU N N 124.946 0.20 1 1192 242 253 GLU H H 9.519 0.02 1 1193 242 253 GLU HA H 5.510 0.02 1 1194 242 253 GLU HG2 H 2.128 0.02 1 1195 242 253 GLU HG3 H 2.128 0.02 1 1196 242 253 GLU CA C 52.894 0.20 1 1197 242 253 GLU CG C 34.824 0.20 1 1198 242 253 GLU N N 117.529 0.20 1 1199 243 254 ARG H H 8.490 0.02 1 1200 243 254 ARG HB2 H 1.041 0.02 2 1201 243 254 ARG HB3 H 1.175 0.02 2 1202 243 254 ARG HG2 H 0.599 0.02 2 1203 243 254 ARG HG3 H 0.767 0.02 2 1204 243 254 ARG HD2 H 2.600 0.02 1 1205 243 254 ARG HD3 H 2.600 0.02 1 1206 243 254 ARG CB C 30.339 0.20 1 1207 243 254 ARG CG C 26.901 0.20 1 1208 243 254 ARG CD C 43.050 0.20 1 1209 243 254 ARG N N 123.665 0.20 1 1210 244 255 GLU H H 8.279 0.02 1 1211 244 255 GLU HA H 4.251 0.02 1 1212 244 255 GLU HB2 H 1.973 0.02 2 1213 244 255 GLU HG3 H 2.096 0.02 2 1214 244 255 GLU CA C 56.002 0.20 1 1215 244 255 GLU CG C 36.722 0.20 1 1216 244 255 GLU N N 124.181 0.20 1 1217 245 256 LEU H H 8.509 0.02 1 1218 245 256 LEU HA H 4.602 0.02 1 1219 245 256 LEU HB2 H 1.514 0.02 2 1220 245 256 LEU HB3 H 1.560 0.02 2 1221 245 256 LEU HG H 1.568 0.02 1 1222 245 256 LEU HD1 H 0.888 0.02 2 1223 245 256 LEU HD2 H 0.830 0.02 2 1224 245 256 LEU CA C 52.615 0.20 1 1225 245 256 LEU CB C 41.749 0.20 1 1226 245 256 LEU CG C 27.031 0.20 1 1227 245 256 LEU CD1 C 25.173 0.20 2 1228 245 256 LEU CD2 C 23.310 0.20 2 1229 245 256 LEU N N 126.963 0.20 1 1230 246 257 PRO HA H 4.441 0.02 1 1231 246 257 PRO HB2 H 2.241 0.02 2 1232 246 257 PRO HB3 H 1.852 0.02 2 1233 246 257 PRO HG2 H 1.970 0.02 1 1234 246 257 PRO HG3 H 1.970 0.02 1 1235 246 257 PRO HD2 H 3.637 0.02 2 1236 246 257 PRO HD3 H 3.804 0.02 2 1237 246 257 PRO CA C 63.161 0.20 1 1238 246 257 PRO CB C 32.117 0.20 1 1239 246 257 PRO CG C 27.269 0.20 1 1240 246 257 PRO CD C 50.515 0.20 1 1241 247 258 GLU H H 8.504 0.02 1 1242 247 258 GLU HA H 4.238 0.02 1 1243 247 258 GLU HG2 H 2.286 0.02 1 1244 247 258 GLU HG3 H 2.286 0.02 1 1245 247 258 GLU CA C 56.524 0.20 1 1246 247 258 GLU CG C 36.265 0.20 1 1247 247 258 GLU N N 120.736 0.20 1 1248 248 259 LEU HD1 H 0.538 0.02 2 1249 248 259 LEU HD2 H 0.793 0.02 2 1250 248 259 LEU CD1 C 23.001 0.20 2 1251 248 259 LEU CD2 C 25.391 0.20 2 1252 249 260 THR H H 7.913 0.02 1 1253 249 260 THR N N 114.501 0.20 1 1254 250 261 ALA H H 8.630 0.02 1 1255 250 261 ALA HB H 1.485 0.02 1 1256 250 261 ALA CB C 18.328 0.20 1 1257 250 261 ALA N N 124.158 0.20 1 1258 251 262 GLU H H 8.298 0.02 1 1259 251 262 GLU N N 116.864 0.20 1 1260 252 263 PHE H H 7.860 0.02 1 1261 252 263 PHE N N 121.906 0.20 1 1262 253 264 ILE HD1 H 0.666 0.02 1 1263 253 264 ILE CD1 C 13.104 0.20 1 1264 257 268 GLY H H 7.678 0.02 1 1265 257 268 GLY N N 105.707 0.20 1 1266 258 269 VAL H H 7.231 0.02 1 1267 258 269 VAL HG1 H 0.927 0.02 2 1268 258 269 VAL HG2 H 0.774 0.02 2 1269 258 269 VAL CG1 C 21.073 0.20 2 1270 258 269 VAL CG2 C 20.143 0.20 2 1271 258 269 VAL N N 120.829 0.20 1 1272 259 270 GLU H H 8.516 0.02 1 1273 259 270 GLU N N 127.545 0.20 1 1274 260 271 ASP H H 8.166 0.02 1 1275 260 271 ASP N N 116.883 0.20 1 1276 261 272 GLY H H 8.052 0.02 1 1277 261 272 GLY N N 108.155 0.20 1 1278 262 273 SER H H 8.159 0.02 1 1279 262 273 SER N N 116.084 0.20 1 1280 263 274 VAL H H 8.623 0.02 1 1281 263 274 VAL HG2 H 1.023 0.02 2 1282 263 274 VAL CG2 C 22.290 0.20 2 1283 263 274 VAL N N 124.106 0.20 1 1284 264 275 GLU H H 8.733 0.02 1 1285 264 275 GLU N N 121.409 0.20 1 1286 265 276 GLY H H 8.316 0.02 1 1287 265 276 GLY N N 110.551 0.20 1 1288 266 277 LEU HD1 H 0.508 0.02 2 1289 266 277 LEU HD2 H 0.758 0.02 2 1290 266 277 LEU CD1 C 23.167 0.20 2 1291 266 277 LEU CD2 C 26.172 0.20 2 1292 267 278 ARG H H 8.553 0.02 1 1293 267 278 ARG N N 119.154 0.20 1 1294 268 279 ALA HB H 1.524 0.02 1 1295 268 279 ALA CB C 18.031 0.20 1 1296 269 280 GLU H H 7.826 0.02 1 1297 269 280 GLU N N 121.125 0.20 1 1298 270 281 VAL H H 8.300 0.02 1 1299 270 281 VAL HG1 H 0.846 0.02 2 1300 270 281 VAL HG2 H 1.021 0.02 2 1301 270 281 VAL CG1 C 22.844 0.20 2 1302 270 281 VAL CG2 C 22.259 0.20 2 1303 270 281 VAL N N 120.014 0.20 1 1304 271 282 ARG H H 7.587 0.02 1 1305 271 282 ARG N N 123.530 0.20 1 1306 274 285 MET HE H 2.071 0.02 1 1307 274 285 MET CE C 17.215 0.20 1 1308 278 289 LEU H H 8.832 0.02 1 1309 278 289 LEU HD1 H 0.708 0.02 2 1310 278 289 LEU HD2 H 0.775 0.02 2 1311 278 289 LEU CD1 C 26.597 0.20 2 1312 278 289 LEU CD2 C 24.036 0.20 2 1313 278 289 LEU N N 122.558 0.20 1 1314 279 290 LYS H H 7.945 0.02 1 1315 279 290 LYS N N 119.149 0.20 1 1316 280 291 SER H H 7.554 0.02 1 1317 280 291 SER N N 114.462 0.20 1 1318 281 292 ALA HB H 1.456 0.02 1 1319 281 292 ALA CB C 18.800 0.20 1 1320 282 293 ILE H H 8.728 0.02 1 1321 282 293 ILE HD1 H 0.843 0.02 1 1322 282 293 ILE CD1 C 14.085 0.20 1 1323 282 293 ILE N N 120.893 0.20 1 1324 283 294 ARG H H 7.618 0.02 1 1325 283 294 ARG N N 119.316 0.20 1 1326 284 295 ASN H H 8.334 0.02 1 1327 284 295 ASN N N 117.696 0.20 1 1328 285 296 ARG H H 8.211 0.02 1 1329 285 296 ARG N N 123.511 0.20 1 1330 286 297 VAL H H 8.295 0.02 1 1331 286 297 VAL HG1 H 1.106 0.02 2 1332 286 297 VAL CG1 C 22.222 0.20 2 1333 286 297 VAL N N 120.224 0.20 1 1334 288 299 SER H H 8.326 0.02 1 1335 288 299 SER N N 112.838 0.20 1 1336 289 300 GLN H H 7.364 0.02 1 1337 289 300 GLN N N 119.576 0.20 1 1338 290 301 ALA H H 8.177 0.02 1 1339 290 301 ALA HB H 1.399 0.02 1 1340 290 301 ALA CB C 17.683 0.20 1 1341 290 301 ALA N N 124.384 0.20 1 1342 291 302 ILE H H 8.341 0.02 1 1343 291 302 ILE HD1 H 0.760 0.02 1 1344 291 302 ILE CD1 C 12.313 0.20 1 1345 291 302 ILE N N 116.474 0.20 1 1346 292 303 GLU H H 8.222 0.02 1 1347 292 303 GLU N N 119.754 0.20 1 1348 293 304 GLY H H 8.011 0.02 1 1349 293 304 GLY N N 105.283 0.20 1 1350 294 305 LEU HD1 H 0.776 0.02 2 1351 294 305 LEU HD2 H 0.793 0.02 2 1352 294 305 LEU CD1 C 23.773 0.20 2 1353 294 305 LEU CD2 C 24.233 0.20 2 1354 295 306 VAL H H 8.337 0.02 1 1355 295 306 VAL N N 119.566 0.20 1 1356 296 307 LYS H H 8.157 0.02 1 1357 296 307 LYS N N 119.089 0.20 1 1358 297 308 ALA H H 7.152 0.02 1 1359 297 308 ALA HB H 1.439 0.02 1 1360 297 308 ALA CB C 20.426 0.20 1 1361 297 308 ALA N N 117.142 0.20 1 1362 298 309 ASN H H 7.259 0.02 1 1363 298 309 ASN N N 118.396 0.20 1 1364 299 310 ASP H H 8.319 0.02 1 1365 299 310 ASP N N 123.131 0.20 1 1366 300 311 ILE HD1 H 0.838 0.02 1 1367 300 311 ILE CD1 C 14.329 0.20 1 1368 301 312 ASP H H 8.374 0.02 1 1369 301 312 ASP N N 124.008 0.20 1 1370 302 313 VAL H H 8.083 0.02 1 1371 302 313 VAL HG1 H 1.104 0.02 2 1372 302 313 VAL CG1 C 23.847 0.20 2 1373 302 313 VAL N N 122.342 0.20 1 1374 304 315 ALA H H 8.689 0.02 1 1375 304 315 ALA HB H 1.474 0.02 1 1376 304 315 ALA CB C 18.321 0.20 1 1377 304 315 ALA N N 129.036 0.20 1 1378 305 316 ALA H H 8.760 0.02 1 1379 305 316 ALA HB H 1.416 0.02 1 1380 305 316 ALA CB C 18.431 0.20 1 1381 305 316 ALA N N 117.697 0.20 1 1382 306 317 LEU H H 7.145 0.02 1 1383 306 317 LEU HD1 H 0.940 0.02 2 1384 306 317 LEU HD2 H 0.882 0.02 2 1385 306 317 LEU CD1 C 25.017 0.20 2 1386 306 317 LEU CD2 C 22.679 0.20 2 1387 306 317 LEU N N 115.580 0.20 1 1388 307 318 ILE H H 7.114 0.02 1 1389 307 318 ILE HD1 H 0.838 0.02 1 1390 307 318 ILE CD1 C 13.052 0.20 1 1391 307 318 ILE N N 121.044 0.20 1 1392 308 319 ASP H H 8.531 0.02 1 1393 308 319 ASP N N 120.256 0.20 1 1394 310 321 GLU H H 7.545 0.02 1 1395 310 321 GLU N N 123.920 0.20 1 1396 311 322 ILE HD1 H 0.898 0.02 1 1397 311 322 ILE CD1 C 14.162 0.20 1 1398 312 323 ASP H H 7.280 0.02 1 1399 312 323 ASP N N 119.259 0.20 1 1400 313 324 VAL H H 7.324 0.02 1 1401 313 324 VAL N N 121.453 0.20 1 1402 314 325 LEU H H 8.013 0.02 1 1403 314 325 LEU HD1 H 0.827 0.02 2 1404 314 325 LEU HD2 H 0.966 0.02 2 1405 314 325 LEU CD1 C 21.787 0.20 2 1406 314 325 LEU CD2 C 26.450 0.20 2 1407 314 325 LEU N N 125.070 0.20 1 1408 318 329 ALA H H 7.961 0.02 1 1409 318 329 ALA HB H 1.654 0.02 1 1410 318 329 ALA CB C 18.114 0.20 1 1411 318 329 ALA N N 123.112 0.20 1 1412 319 330 ALA H H 8.017 0.02 1 1413 319 330 ALA HB H 1.280 0.02 1 1414 319 330 ALA CB C 17.980 0.20 1 1415 319 330 ALA N N 120.142 0.20 1 1416 320 331 GLN H H 7.673 0.02 1 1417 320 331 GLN N N 117.616 0.20 1 1418 321 332 ARG H H 7.525 0.02 1 1419 321 332 ARG N N 118.982 0.20 1 1420 322 333 PHE H H 7.563 0.02 1 1421 322 333 PHE N N 116.736 0.20 1 1422 324 335 GLY H H 8.073 0.02 1 1423 324 335 GLY N N 108.774 0.20 1 1424 326 337 GLU H H 8.525 0.02 1 1425 326 337 GLU N N 121.773 0.20 1 1426 327 338 LYS H H 8.003 0.02 1 1427 327 338 LYS N N 120.105 0.20 1 1428 328 339 GLN H H 7.874 0.02 1 1429 328 339 GLN N N 118.481 0.20 1 1430 329 340 ALA H H 7.967 0.02 1 1431 329 340 ALA HB H 1.337 0.02 1 1432 329 340 ALA CB C 18.501 0.20 1 1433 329 340 ALA N N 122.676 0.20 1 1434 330 341 LEU H H 7.678 0.02 1 1435 330 341 LEU HD1 H 0.852 0.02 2 1436 330 341 LEU HD2 H 0.772 0.02 2 1437 330 341 LEU CD1 C 24.791 0.20 2 1438 330 341 LEU CD2 C 22.616 0.20 2 1439 330 341 LEU N N 116.818 0.20 1 1440 332 343 LEU HD1 H 1.122 0.02 2 1441 332 343 LEU HD2 H 0.968 0.02 2 1442 332 343 LEU CD1 C 26.360 0.20 2 1443 332 343 LEU CD2 C 22.648 0.20 2 1444 334 345 ARG H H 8.689 0.02 1 1445 334 345 ARG N N 123.299 0.20 1 1446 335 346 GLU H H 9.458 0.02 1 1447 335 346 GLU N N 117.922 0.20 1 1448 336 347 LEU H H 7.421 0.02 1 1449 336 347 LEU HD1 H 0.706 0.02 2 1450 336 347 LEU HD2 H 0.821 0.02 2 1451 336 347 LEU CD1 C 22.560 0.20 2 1452 336 347 LEU CD2 C 24.976 0.20 2 1453 336 347 LEU N N 119.446 0.20 1 1454 338 349 GLU H H 7.314 0.02 1 1455 338 349 GLU N N 120.133 0.20 1 1456 339 350 GLU H H 8.623 0.02 1 1457 339 350 GLU N N 120.224 0.20 1 1458 341 352 ALA HB H 1.498 0.02 1 1459 341 352 ALA CB C 20.435 0.20 1 1460 342 353 LYS H H 8.223 0.02 1 1461 342 353 LYS N N 117.631 0.20 1 1462 344 355 ARG H H 7.974 0.02 1 1463 344 355 ARG N N 117.636 0.20 1 1464 345 356 VAL HG1 H 0.956 0.02 2 1465 345 356 VAL HG2 H 0.895 0.02 2 1466 345 356 VAL CG1 C 22.918 0.20 2 1467 345 356 VAL CG2 C 22.999 0.20 2 1468 347 358 VAL H H 8.427 0.02 1 1469 347 358 VAL HG1 H 0.777 0.02 2 1470 347 358 VAL HG2 H 0.742 0.02 2 1471 347 358 VAL CG1 C 26.181 0.20 2 1472 347 358 VAL CG2 C 21.957 0.20 2 1473 347 358 VAL N N 120.180 0.20 1 1474 348 359 GLY H H 8.000 0.02 1 1475 348 359 GLY N N 106.156 0.20 1 1476 349 360 LEU HD1 H 0.807 0.02 2 1477 349 360 LEU HD2 H 0.854 0.02 2 1478 349 360 LEU CD1 C 26.386 0.20 2 1479 349 360 LEU CD2 C 22.856 0.20 2 1480 351 362 LEU H H 9.045 0.02 1 1481 351 362 LEU HD1 H 1.071 0.02 2 1482 351 362 LEU HD2 H 0.617 0.02 2 1483 351 362 LEU CD1 C 23.616 0.20 2 1484 351 362 LEU CD2 C 21.153 0.20 2 1485 351 362 LEU N N 118.150 0.20 1 1486 352 363 GLY H H 8.213 0.02 1 1487 352 363 GLY N N 107.366 0.20 1 1488 353 364 GLU H H 7.671 0.02 1 1489 353 364 GLU N N 124.022 0.20 1 1490 354 365 VAL H H 8.034 0.02 1 1491 354 365 VAL HG1 H 0.938 0.02 2 1492 354 365 VAL CG1 C 21.979 0.20 2 1493 354 365 VAL N N 125.052 0.20 1 1494 355 366 ILE HD1 H 0.684 0.02 1 1495 355 366 ILE CD1 C 14.446 0.20 1 1496 357 368 THR H H 8.619 0.02 1 1497 357 368 THR N N 112.480 0.20 1 1498 358 369 ASN H H 7.350 0.02 1 1499 358 369 ASN N N 116.654 0.20 1 1500 360 371 LEU H H 7.955 0.02 1 1501 360 371 LEU HD1 H 0.679 0.02 2 1502 360 371 LEU HD2 H 0.811 0.02 2 1503 360 371 LEU CD1 C 25.092 0.20 2 1504 360 371 LEU CD2 C 22.295 0.20 2 1505 360 371 LEU N N 116.451 0.20 1 1506 362 373 ALA H H 8.894 0.02 1 1507 362 373 ALA HB H 1.275 0.02 1 1508 362 373 ALA CB C 18.332 0.20 1 1509 362 373 ALA N N 126.837 0.20 1 1510 363 374 ASP H H 8.872 0.02 1 1511 363 374 ASP N N 125.349 0.20 1 1512 364 375 GLU H H 8.970 0.02 1 1513 364 375 GLU N N 127.959 0.20 1 1514 367 378 VAL H H 7.945 0.02 1 1515 367 378 VAL HG1 H 0.915 0.02 2 1516 367 378 VAL HG2 H 0.837 0.02 2 1517 367 378 VAL CG1 C 23.866 0.20 2 1518 367 378 VAL CG2 C 21.571 0.20 2 1519 367 378 VAL N N 120.736 0.20 1 1520 368 379 LYS H H 7.681 0.02 1 1521 368 379 LYS N N 118.703 0.20 1 1522 369 380 GLY H H 7.843 0.02 1 1523 369 380 GLY N N 107.006 0.20 1 1524 370 381 LEU H H 8.212 0.02 1 1525 370 381 LEU HD1 H 0.808 0.02 2 1526 370 381 LEU HD2 H 0.847 0.02 2 1527 370 381 LEU CD1 C 25.798 0.20 2 1528 370 381 LEU CD2 C 22.804 0.20 2 1529 370 381 LEU N N 124.690 0.20 1 1530 371 382 ILE H H 7.929 0.02 1 1531 371 382 ILE HD1 H 0.784 0.02 1 1532 371 382 ILE CD1 C 14.288 0.20 1 1533 371 382 ILE N N 121.284 0.20 1 1534 374 385 MET HE H 1.729 0.02 1 1535 374 385 MET CE C 16.775 0.20 1 1536 375 386 ALA HB H 1.545 0.02 1 1537 375 386 ALA CB C 19.145 0.20 1 1538 377 388 ALA H H 7.297 0.02 1 1539 377 388 ALA HB H 1.203 0.02 1 1540 377 388 ALA CB C 19.214 0.20 1 1541 377 388 ALA N N 122.982 0.20 1 1542 382 393 LYS H H 7.810 0.02 1 1543 382 393 LYS N N 115.702 0.20 1 1544 383 394 GLU H H 7.433 0.02 1 1545 383 394 GLU N N 119.613 0.20 1 1546 384 395 VAL H H 7.154 0.02 1 1547 384 395 VAL HG1 H 0.637 0.02 2 1548 384 395 VAL HG2 H 0.537 0.02 2 1549 384 395 VAL CG1 C 20.977 0.20 2 1550 384 395 VAL CG2 C 21.734 0.20 2 1551 384 395 VAL N N 121.077 0.20 1 1552 385 396 ILE HD1 H 0.801 0.02 1 1553 385 396 ILE CD1 C 13.594 0.20 1 1554 386 397 GLU H H 8.093 0.02 1 1555 386 397 GLU N N 120.627 0.20 1 1556 387 398 PHE H H 7.902 0.02 1 1557 387 398 PHE N N 121.081 0.20 1 1558 388 399 TYR H H 8.497 0.02 1 1559 388 399 TYR N N 119.320 0.20 1 1560 390 401 LYS H H 7.151 0.02 1 1561 390 401 LYS N N 118.492 0.20 1 1562 391 402 ASN H H 7.386 0.02 1 1563 391 402 ASN N N 121.692 0.20 1 1564 392 403 LYS H H 8.509 0.02 1 1565 392 403 LYS N N 127.486 0.20 1 1566 393 404 GLU H H 8.271 0.02 1 1567 393 404 GLU N N 118.749 0.20 1 1568 394 405 LEU H H 7.670 0.02 1 1569 394 405 LEU HD1 H 0.380 0.02 2 1570 394 405 LEU HD2 H 0.585 0.02 2 1571 394 405 LEU CD1 C 25.119 0.20 2 1572 394 405 LEU CD2 C 22.733 0.20 2 1573 394 405 LEU N N 120.652 0.20 1 1574 395 406 MET HE H 1.923 0.02 1 1575 395 406 MET CE C 15.860 0.20 1 1576 397 408 ASN H H 7.873 0.02 1 1577 397 408 ASN N N 119.483 0.20 1 1578 398 409 MET HE H 1.914 0.02 1 1579 398 409 MET CE C 17.347 0.20 1 1580 401 412 VAL H H 7.933 0.02 1 1581 401 412 VAL HG1 H 1.075 0.02 2 1582 401 412 VAL HG2 H 0.926 0.02 2 1583 401 412 VAL CG1 C 22.561 0.20 2 1584 401 412 VAL CG2 C 21.744 0.20 2 1585 401 412 VAL N N 123.710 0.20 1 1586 402 413 ALA HB H 1.444 0.02 1 1587 402 413 ALA CB C 18.073 0.20 1 1588 403 414 LEU HD1 H 0.785 0.02 2 1589 403 414 LEU HD2 H 0.738 0.02 2 1590 403 414 LEU CD1 C 24.275 0.20 2 1591 403 414 LEU CD2 C 24.271 0.20 2 1592 404 415 GLU H H 8.086 0.02 1 1593 404 415 GLU N N 120.226 0.20 1 1594 406 417 GLN H H 8.632 0.02 1 1595 406 417 GLN HE21 H 7.067 0.02 2 1596 406 417 GLN HE22 H 7.260 0.02 2 1597 406 417 GLN N N 119.739 0.20 1 1598 406 417 GLN NE2 N 106.878 0.20 1 1599 407 418 ALA H H 8.784 0.02 1 1600 407 418 ALA HB H 1.460 0.02 1 1601 407 418 ALA CB C 18.373 0.20 1 1602 407 418 ALA N N 125.441 0.20 1 1603 408 419 VAL HG1 H 0.948 0.02 2 1604 408 419 VAL HG2 H 0.874 0.02 2 1605 408 419 VAL CG1 C 23.127 0.20 2 1606 408 419 VAL CG2 C 21.107 0.20 2 1607 410 421 ALA H H 7.784 0.02 1 1608 410 421 ALA HB H 1.395 0.02 1 1609 410 421 ALA CB C 17.276 0.20 1 1610 410 421 ALA N N 123.354 0.20 1 1611 411 422 VAL HG1 H 0.760 0.02 2 1612 411 422 VAL HG2 H 1.010 0.02 2 1613 411 422 VAL CG1 C 25.626 0.20 2 1614 411 422 VAL CG2 C 23.186 0.20 2 1615 412 423 LEU H H 8.419 0.02 1 1616 412 423 LEU HD1 H 0.749 0.02 2 1617 412 423 LEU HD2 H 0.711 0.02 2 1618 412 423 LEU CD1 C 25.655 0.20 2 1619 412 423 LEU CD2 C 23.887 0.20 2 1620 412 423 LEU N N 120.168 0.20 1 1621 413 424 ALA H H 7.568 0.02 1 1622 413 424 ALA N N 118.380 0.20 1 1623 414 425 LYS H H 7.071 0.02 1 1624 414 425 LYS N N 115.374 0.20 1 1625 415 426 ALA H H 7.100 0.02 1 1626 415 426 ALA HB H 1.246 0.02 1 1627 415 426 ALA CB C 19.768 0.20 1 1628 415 426 ALA N N 121.839 0.20 1 1629 417 428 VAL H H 8.365 0.02 1 1630 417 428 VAL HG1 H 0.782 0.02 2 1631 417 428 VAL HG2 H 0.799 0.02 2 1632 417 428 VAL CG1 C 20.937 0.20 2 1633 417 428 VAL CG2 C 21.616 0.20 2 1634 417 428 VAL N N 129.614 0.20 1 1635 418 429 THR H H 8.882 0.02 1 1636 418 429 THR N N 124.190 0.20 1 1637 419 430 GLU H H 8.703 0.02 1 1638 419 430 GLU N N 124.456 0.20 1 1639 420 431 LYS H H 8.228 0.02 1 1640 420 431 LYS N N 124.755 0.20 1 1641 421 432 GLU H H 9.092 0.02 1 1642 421 432 GLU N N 130.970 0.20 1 1643 422 433 THR H H 8.367 0.02 1 1644 422 433 THR N N 120.672 0.20 1 1645 423 434 THR H H 8.442 0.02 1 1646 423 434 THR N N 112.844 0.20 1 1647 424 435 PHE H H 9.786 0.02 1 1648 424 435 PHE N N 124.858 0.20 1 1649 425 436 ASN H H 9.337 0.02 1 1650 425 436 ASN N N 116.191 0.20 1 1651 426 437 GLU H H 7.610 0.02 1 1652 426 437 GLU N N 119.000 0.20 1 1653 427 438 LEU H H 7.872 0.02 1 1654 427 438 LEU HD1 H 0.997 0.02 2 1655 427 438 LEU HD2 H 0.890 0.02 2 1656 427 438 LEU CD1 C 26.331 0.20 2 1657 427 438 LEU CD2 C 24.169 0.20 2 1658 427 438 LEU N N 120.236 0.20 1 1659 428 439 MET H H 8.086 0.02 1 1660 428 439 MET HE H 1.723 0.02 1 1661 428 439 MET CE C 16.796 0.20 1 1662 428 439 MET N N 114.044 0.20 1 1663 429 440 ASN H H 7.507 0.02 1 1664 429 440 ASN N N 117.627 0.20 1 1665 430 441 GLN H H 7.736 0.02 1 1666 430 441 GLN N N 119.854 0.20 1 1667 431 442 GLN H H 8.072 0.02 1 1668 431 442 GLN N N 121.469 0.20 1 1669 432 443 ALA H H 7.858 0.02 1 1670 432 443 ALA HB H 1.311 0.02 1 1671 432 443 ALA CB C 19.987 0.20 1 1672 432 443 ALA N N 131.612 0.20 1 stop_ save_