data_18266 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of Dengue Virus NS2B/NS3 in complex with Aprotinin ; _BMRB_accession_number 18266 _BMRB_flat_file_name bmr18266.str _Entry_type original _Submission_date 2012-02-15 _Accession_date 2012-02-15 _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 Bi Yunchen . . 2 Zhu Lei . . 3 Wang Junfeng . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 172 "13C chemical shifts" 530 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-24 update BMRB 'update entry citation' 2012-06-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 13C and 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22623057 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bi Yunchen . . 2 Zhu Lei . . 3 Li Hua . . 4 Wu Bo . . 5 Liu Jinsong . . 6 Wang Junfeng . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 7 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 137 _Page_last 139 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Dengue Virus NS2B/NS3 in complex with Aprotinin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Dengue Virus NS2B/NS3' $entity Aprotinin $Aprotinin 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 247 _Mol_residue_sequence ; GSHMLEADLELERAADVRWE EQAEISGSSPILSITISEDG SMSIKNEEEEQTLGGGGSGG GGAGVLWDVPSPPPVGKAEL EDGAYRIKQKGILGYSQIGA GVYKEGTFHTMWHVTRGAVL MHKGKRIEPSWADVKKDLIS YGGGWKLEGEWKEGEEVQVL ALEPGKNPRAVQTKPGLFKT NTGTIGAVSLDFSPGTSGSP IVDKKGKVVGLYGNGVVTRS GAYVSAIAQTEKSIEDNPEI EDDIFRK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 LEU 6 GLU 7 ALA 8 ASP 9 LEU 10 GLU 11 LEU 12 GLU 13 ARG 14 ALA 15 ALA 16 ASP 17 VAL 18 ARG 19 TRP 20 GLU 21 GLU 22 GLN 23 ALA 24 GLU 25 ILE 26 SER 27 GLY 28 SER 29 SER 30 PRO 31 ILE 32 LEU 33 SER 34 ILE 35 THR 36 ILE 37 SER 38 GLU 39 ASP 40 GLY 41 SER 42 MET 43 SER 44 ILE 45 LYS 46 ASN 47 GLU 48 GLU 49 GLU 50 GLU 51 GLN 52 THR 53 LEU 54 GLY 55 GLY 56 GLY 57 GLY 58 SER 59 GLY 60 GLY 61 GLY 62 GLY 63 ALA 64 GLY 65 VAL 66 LEU 67 TRP 68 ASP 69 VAL 70 PRO 71 SER 72 PRO 73 PRO 74 PRO 75 VAL 76 GLY 77 LYS 78 ALA 79 GLU 80 LEU 81 GLU 82 ASP 83 GLY 84 ALA 85 TYR 86 ARG 87 ILE 88 LYS 89 GLN 90 LYS 91 GLY 92 ILE 93 LEU 94 GLY 95 TYR 96 SER 97 GLN 98 ILE 99 GLY 100 ALA 101 GLY 102 VAL 103 TYR 104 LYS 105 GLU 106 GLY 107 THR 108 PHE 109 HIS 110 THR 111 MET 112 TRP 113 HIS 114 VAL 115 THR 116 ARG 117 GLY 118 ALA 119 VAL 120 LEU 121 MET 122 HIS 123 LYS 124 GLY 125 LYS 126 ARG 127 ILE 128 GLU 129 PRO 130 SER 131 TRP 132 ALA 133 ASP 134 VAL 135 LYS 136 LYS 137 ASP 138 LEU 139 ILE 140 SER 141 TYR 142 GLY 143 GLY 144 GLY 145 TRP 146 LYS 147 LEU 148 GLU 149 GLY 150 GLU 151 TRP 152 LYS 153 GLU 154 GLY 155 GLU 156 GLU 157 VAL 158 GLN 159 VAL 160 LEU 161 ALA 162 LEU 163 GLU 164 PRO 165 GLY 166 LYS 167 ASN 168 PRO 169 ARG 170 ALA 171 VAL 172 GLN 173 THR 174 LYS 175 PRO 176 GLY 177 LEU 178 PHE 179 LYS 180 THR 181 ASN 182 THR 183 GLY 184 THR 185 ILE 186 GLY 187 ALA 188 VAL 189 SER 190 LEU 191 ASP 192 PHE 193 SER 194 PRO 195 GLY 196 THR 197 SER 198 GLY 199 SER 200 PRO 201 ILE 202 VAL 203 ASP 204 LYS 205 LYS 206 GLY 207 LYS 208 VAL 209 VAL 210 GLY 211 LEU 212 TYR 213 GLY 214 ASN 215 GLY 216 VAL 217 VAL 218 THR 219 ARG 220 SER 221 GLY 222 ALA 223 TYR 224 VAL 225 SER 226 ALA 227 ILE 228 ALA 229 GLN 230 THR 231 GLU 232 LYS 233 SER 234 ILE 235 GLU 236 ASP 237 ASN 238 PRO 239 GLU 240 ILE 241 GLU 242 ASP 243 ASP 244 ILE 245 PHE 246 ARG 247 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-03 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 19080 NS3pro 69.64 186 98.84 99.42 6.24e-117 BMRB 19305 entity_1 95.95 240 97.47 98.73 1.03e-159 BMRB 19306 entity_1 95.95 244 97.47 98.73 6.32e-160 PDB 2FOM "Dengue Virus Ns2bNS3 PROTEASE" 74.90 185 99.46 99.46 1.81e-127 PDB 2M9P "Nmr Structure Of An Inhibitor Bound Dengue Ns3 Protease" 95.95 240 97.47 98.73 1.03e-159 PDB 2M9Q "Nmr Structure Of An Inhibitor Bound Dengue Ns3 Protease" 95.95 240 97.47 98.73 1.03e-159 PDB 4M9F "Dengue Virus Ns2b-ns3 Protease A125c Variant At Ph 8.5" 100.00 247 99.19 99.19 1.17e-172 PDB 4M9I "A125c Ns2b-ns3 Protease From Dengue Virus At Ph 5.5" 100.00 247 99.19 99.19 1.17e-172 PDB 4M9K "Ns2b-ns3 Protease From Dengue Virus At Ph 5.5" 100.00 247 99.60 99.60 3.64e-173 PDB 4M9M "Ns2b-ns3 Protease From Dengue Virus At Ph 8.5" 100.00 247 99.60 99.60 3.64e-173 PDB 4M9T "Ns2b-ns3 Protease From Dengue Virus In The Presence Of Dtnb, A Covalent Allosteric Inhibitor" 100.00 247 99.19 99.19 1.17e-172 EMBL CAA40704 "non-structural protein 3, partial [Dengue virus 2]" 74.90 618 99.46 100.00 7.65e-124 GB AHG23115 "polyprotein, partial [Dengue virus 2]" 74.90 3378 97.84 100.00 1.28e-115 GB AIC36825 "nonstructural protein NS3, partial [Dengue virus 2]" 74.90 618 98.92 99.46 4.49e-123 GB AIE47697 "non-structural protein 3, partial [Dengue virus 2]" 74.90 618 98.92 99.46 4.49e-123 GB AIE47698 "non-structural protein 3, partial [Dengue virus 2]" 74.90 618 98.92 99.46 3.01e-123 GB AIE47699 "non-structural protein 3, partial [Dengue virus 2]" 74.90 618 98.92 99.46 4.49e-123 REF NP_739587 "Nonstructural protein NS3 [Dengue virus 2]" 74.90 618 98.38 99.46 1.22e-122 SP P27914 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Envelope protein E; Contains: RecName: Full=Non-structural protein 1;" 74.90 1683 99.46 100.00 5.59e-118 stop_ save_ save_Aprotinin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Aprotinin _Molecular_mass . _Mol_thiol_state . _Details ; The aprotinin is the bovine version of the small protein basic pancreatic trypsin inhibitor, or BPTI, which inhibits trypsin and related proteolytic enzymes. ; _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCMRTCGGA ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 PRO 3 ASP 4 PHE 5 CYS 6 LEU 7 GLU 8 PRO 9 PRO 10 TYR 11 THR 12 GLY 13 PRO 14 CYS 15 LYS 16 ALA 17 ARG 18 ILE 19 ILE 20 ARG 21 TYR 22 PHE 23 TYR 24 ASN 25 ALA 26 LYS 27 ALA 28 GLY 29 LEU 30 CYS 31 GLN 32 THR 33 PHE 34 VAL 35 TYR 36 GLY 37 GLY 38 CYS 39 ARG 40 ALA 41 LYS 42 ARG 43 ASN 44 ASN 45 PHE 46 LYS 47 SER 48 ALA 49 GLU 50 ASP 51 CYS 52 MET 53 ARG 54 THR 55 CYS 56 GLY 57 GLY 58 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 1039 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 1156 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 1179 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 236 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 237 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 262 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 263 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 264 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 338 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 411 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 412 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 413 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 414 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 415 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 416 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 419 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 45 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 46 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 48 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 485 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 4868 BPTI-R52 100.00 58 98.28 98.28 1.28e-32 BMRB 49 "basic pancreatic trypsin inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 4968 BPTI_monomer 100.00 58 100.00 100.00 9.45e-34 BMRB 5171 BPTI_G37A 100.00 58 98.28 98.28 3.84e-33 BMRB 5307 "Basic Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 BMRB 5358 BPTI 100.00 58 100.00 100.00 9.45e-34 BMRB 5359 BPTI 100.00 58 100.00 100.00 9.45e-34 PDB 1B0C "Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallized From Thiocyanate, Chloride Or Sulfate" 100.00 58 100.00 100.00 9.45e-34 PDB 1BHC "Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate" 100.00 58 100.00 100.00 9.45e-34 PDB 1BPI "The Structure Of Bovine Pancreatic Trypsin Inhibitor At 125k: Definition Of Carboxyl-Terminal Residues Glycine-57 And Alanine-5" 100.00 58 100.00 100.00 9.45e-34 PDB 1BPT "Crevice-Forming Mutants Of Bpti: Crystal Structures Of F22a, Y23a, N43g, And F45a" 100.00 58 98.28 98.28 9.77e-33 PDB 1BTH "Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 1BTI "Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" 100.00 58 98.28 98.28 9.87e-33 PDB 1BZ5 "Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallize From Thiocyanate, Chloride Or Sulfate" 100.00 58 100.00 100.00 9.45e-34 PDB 1BZX "The Crystal Structure Of Anionic Salmon Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 1CBW "Bovine Chymotrypsin Complexed To Bpti" 100.00 58 100.00 100.00 9.45e-34 PDB 1CO7 "R117h Mutant Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" 100.00 99 100.00 100.00 1.53e-34 PDB 1D0D "Crystal Structure Of Tick Anticoagulant Protein Complexed With Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 1EAW "Crystal Structure Of The Mtsp1 (Matriptase)-Bpti (Aprotinin) Complex" 100.00 58 100.00 100.00 9.45e-34 PDB 1F5R "Rat Trypsinogen Mutant Complexed With Bovine Pancreatic Trypsin Inhibitor" 100.00 65 100.00 100.00 9.12e-34 PDB 1F7Z "Rat Trypsinogen K15a Complexed With Bovine Pancreatic Trypsin Inhibitor" 100.00 65 100.00 100.00 9.12e-34 PDB 1FAN "Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" 100.00 58 98.28 98.28 9.87e-33 PDB 1FY8 "Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex" 100.00 58 100.00 100.00 9.45e-34 PDB 1JV8 "Nmr Structure Of Bpti Mutant G37a" 100.00 58 98.28 98.28 3.84e-33 PDB 1JV9 "Nmr Structure Of Bpti Mutant G37a" 100.00 58 98.28 98.28 3.84e-33 PDB 1MTN "Bovine Alpha-Chymotrypsin:bpti Crystallization" 100.00 58 100.00 100.00 9.45e-34 PDB 1NAG "Crevice-forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F" 100.00 58 98.28 98.28 7.69e-33 PDB 1OA5 "The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure" 100.00 58 100.00 100.00 9.45e-34 PDB 1OA6 "The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure" 100.00 58 100.00 100.00 9.45e-34 PDB 1PIT "Determination Of A High-Quality Nuclear Magnetic Resonance Solution Structure Of The Bovine Pancreatic Trypsin Inhibitor And Co" 98.28 58 100.00 100.00 4.62e-33 PDB 1TPA "The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors" 100.00 58 100.00 100.00 9.45e-34 PDB 1UUA "Solution Structure Of A Truncated Bovine Pancreatic Trypsin Inhibitor, 3-58 Bpti" 96.55 56 100.00 100.00 3.58e-32 PDB 1YKT "TrypsinBPTI COMPLEX MUTANT" 96.55 56 100.00 100.00 2.17e-32 PDB 2FI4 "Crystal Structure Of A Bpti Variant (Cys14->ser) In Complex With Trypsin" 100.00 58 98.28 98.28 6.97e-33 PDB 2FI5 "Crystal Structure Of A Bpti Variant (Cys38->ser) In Complex With Trypsin" 100.00 58 98.28 98.28 6.97e-33 PDB 2FTL "Crystal Structure Of Trypsin Complexed With Bpti At 100k" 100.00 58 100.00 100.00 9.45e-34 PDB 2FTM "Crystal Structure Of Trypsin Complexed With The Bpti Variant (Tyr35- >gly)" 100.00 58 98.28 98.28 1.87e-32 PDB 2HEX "Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 2IJO "Crystal Structure Of The West Nile Virus Ns2b-Ns3 Protease Complexed With Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 2KAI "Refined 2.5 Angstroms X-Ray Crystal Structure Of The Complex Formed By Porcine Kallikrein A And The Bovine Pancreatic Trypsin I" 100.00 58 100.00 100.00 9.45e-34 PDB 2PTC "The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors" 100.00 58 100.00 100.00 9.45e-34 PDB 2R9P "Human Mesotrypsin Complexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)" 100.00 58 100.00 100.00 9.45e-34 PDB 2RA3 "Human Cationic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (bpti)" 100.00 58 100.00 100.00 9.45e-34 PDB 2TGP "The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors" 100.00 58 100.00 100.00 9.45e-34 PDB 2TPI "On The Disordered Activation Domain In Trypsinogen. Chemical Labelling And Low-Temperature Crystallography" 100.00 58 100.00 100.00 9.45e-34 PDB 3BTK "The Crystal Structures Of The Complexes Between Bovine Beta- Trypsin And Ten P1 Variants Of Bpti" 100.00 58 100.00 100.00 9.45e-34 PDB 3FP6 "Anionic Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined To The 1.49 A Resolution Limit" 100.00 58 100.00 100.00 9.45e-34 PDB 3FP7 "Anionic Trypsin Variant S195a In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Cleaved At The Scissile Bond (Lys15-Al" 74.14 43 100.00 100.00 1.76e-21 PDB 3FP8 "Anionic Trypsin Variant S195a In Complex With Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined To The 1.46 A Resolution Li" 100.00 58 100.00 100.00 9.45e-34 PDB 3GYM "Structure Of Prostasin In Complex With Aprotinin" 100.00 58 100.00 100.00 9.45e-34 PDB 3LDI "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" 100.00 58 100.00 100.00 9.45e-34 PDB 3LDJ "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" 100.00 58 100.00 100.00 9.45e-34 PDB 3LDM "Crystal Structure Of Aprotinin In Complex With Sucrose Octasulfate: Unusual Interactions And Implication For Heparin Binding" 100.00 58 100.00 100.00 9.45e-34 PDB 3OTJ "A Crystal Structure Of Trypsin Complexed With Bpti (Bovine Pancreatic Trypsin Inhibitor) By X-RayNEUTRON JOINT REFINEMENT" 98.28 58 100.00 100.00 4.62e-33 PDB 3TGI "Wild-Type Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" 100.00 65 100.00 100.00 9.12e-34 PDB 3TGJ "S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" 100.00 65 100.00 100.00 9.12e-34 PDB 3TGK "Trypsinogen Mutant D194n And Deletion Of Ile 16-Val 17 Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" 100.00 65 100.00 100.00 9.12e-34 PDB 3TPI "The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors" 100.00 58 100.00 100.00 9.45e-34 PDB 3U1J "Aprotinin Bound To Dengue Virus Protease" 100.00 58 100.00 100.00 9.45e-34 PDB 4BNR "Extremely Stable Complex Of Crayfish Trypsin With Bovine Trypsin Inhibitor" 100.00 100 100.00 100.00 1.36e-34 PDB 4DG4 "Human Mesotrypsin-s39y Complexed With Bovine Pancreatic Trypsin Inhibitor (bpti)" 100.00 58 100.00 100.00 9.45e-34 PDB 4PTI "The Geometry Of The Reactive Site And Of The Peptide Groups In Trypsin, Trypsinogen And Its Complexes With Inhibitors" 100.00 58 100.00 100.00 9.45e-34 PDB 4TPI "The Refined 2.2-angstroms (0.22-nm) X-ray Crystal Structure Of The Ternary Complex Formed By Bovine Trypsinogen, Valine-valine " 100.00 58 98.28 100.00 2.77e-33 PDB 5PTI "Structure Of Bovine Pancreatic Trypsin Inhibitor. Results Of Joint Neutron And X-Ray Refinement Of Crystal Form Ii" 98.28 58 100.00 100.00 4.62e-33 PDB 6PTI "Structure Of Form Iii Crystals Of Bovine Pancreatic Trypsin Inhibitor" 100.00 58 100.00 100.00 9.45e-34 PDB 8PTI "Crystal Structure Of A Y35g Mutant Of Bovine Pancreatic Trypsin Inhibitor" 100.00 58 98.28 98.28 1.87e-32 PDB 9PTI "Basic Pancreatic Trypsin Inhibitor (met 52 Oxidized)" 100.00 58 98.28 98.28 1.05e-32 EMBL CAA27062 "unnamed protein product [Bos taurus]" 100.00 89 100.00 100.00 1.02e-33 EMBL CAA27063 "unnamed protein product [Bos taurus]" 100.00 58 100.00 100.00 9.45e-34 EMBL CAA28371 "unnamed protein product [synthetic construct]" 100.00 59 100.00 100.00 7.71e-34 EMBL CAA28886 "trypsin ihibitor precursor [Bos taurus]" 100.00 92 100.00 100.00 1.69e-34 EMBL CAA37967 "aprotinin [synthetic construct]" 100.00 59 100.00 100.00 9.89e-34 GB AAA72535 "alkaline phosphatase/pancreatic trypsin inhibitor precursor [synthetic construct]" 100.00 79 98.28 100.00 4.10e-34 GB AAB25189 "major cationic kallikrein inhibitor [cattle, posterior pituitary gland, Peptide, 58 aa]" 100.00 58 100.00 100.00 9.45e-34 GB AAD13685 "trypsin inhibitor [Bos taurus]" 100.00 100 100.00 100.00 1.36e-34 GB ABX57797 "aprotinin precursor [Plastid transformation vector pAPR20]" 100.00 104 100.00 100.00 4.63e-35 GB ABX57799 "aprotinin precursor [Plastid transformation vector pAPR21]" 100.00 100 100.00 100.00 6.39e-35 PRF 1405218A "aprotinin analog" 98.28 57 100.00 100.00 3.87e-33 PRF 1405218D "aprotinin analog" 100.00 59 100.00 100.00 7.96e-34 PRF 1510193A BPTI 100.00 100 98.28 100.00 5.65e-34 PRF 681071A "inhibitor,basic pancreatic trypsin" 100.00 58 100.00 100.00 9.45e-34 SP P00974 "RecName: Full=Pancreatic trypsin inhibitor; AltName: Full=Aprotinin; AltName: Full=Basic protease inhibitor; Short=BPI; Short=B" 100.00 100 100.00 100.00 1.36e-34 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 'Dengue virus' 12637 Viruses . Flavivirus 'Dengue virus' 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 'recombinant technology' . Escherichia coli . pET15b 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 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' $entity 0.6 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' $Aprotinin 1.2 mM '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 . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 120 . mM pH 7.0 . pH pressure 1 . atm temperature 303 . 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_ _Experiment_label '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '2D 1H-15N HSQC' '3D HN(CA)CO' 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 'Dengue Virus NS2B/NS3' _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 6 6 GLU C C 175.678 0.002 1 2 6 6 GLU CA C 55.706 0.005 1 3 6 6 GLU CB C 29.531 0.000 1 4 7 7 ALA H H 8.180 0.005 1 5 7 7 ALA C C 177.044 0.017 1 6 7 7 ALA CA C 51.474 0.036 1 7 7 7 ALA CB C 19.154 0.028 1 8 7 7 ALA N N 125.534 0.025 1 9 8 8 ASP H H 8.204 0.004 1 10 8 8 ASP C C 175.322 0.022 1 11 8 8 ASP CA C 54.363 0.018 1 12 8 8 ASP CB C 41.078 0.000 1 13 8 8 ASP N N 120.616 0.022 1 14 9 9 LEU H H 8.044 0.005 1 15 9 9 LEU C C 175.531 0.023 1 16 9 9 LEU CA C 53.484 0.045 1 17 9 9 LEU CB C 42.464 0.030 1 18 9 9 LEU N N 120.904 0.030 1 19 10 10 GLU H H 9.089 0.005 1 20 10 10 GLU C C 175.714 0.012 1 21 10 10 GLU CA C 53.829 0.072 1 22 10 10 GLU CB C 32.907 0.000 1 23 10 10 GLU N N 122.177 0.024 1 24 11 11 LEU H H 8.268 0.005 1 25 11 11 LEU C C 177.404 0.009 1 26 11 11 LEU CA C 53.135 0.065 1 27 11 11 LEU CB C 43.499 0.006 1 28 11 11 LEU N N 121.472 0.026 1 29 12 12 GLU H H 8.592 0.005 1 30 12 12 GLU C C 174.507 0.011 1 31 12 12 GLU CA C 54.603 0.057 1 32 12 12 GLU CB C 33.570 0.000 1 33 12 12 GLU N N 121.395 0.021 1 34 13 13 ARG H H 9.308 0.004 1 35 13 13 ARG C C 175.147 0.004 1 36 13 13 ARG CA C 58.592 0.083 1 37 13 13 ARG N N 132.496 0.058 1 38 14 14 ALA H H 8.937 0.006 1 39 14 14 ALA C C 176.316 0.009 1 40 14 14 ALA CA C 51.823 0.010 1 41 14 14 ALA CB C 22.647 0.000 1 42 14 14 ALA N N 127.317 0.028 1 43 15 15 ALA H H 7.540 0.004 1 44 15 15 ALA C C 175.353 0.006 1 45 15 15 ALA CA C 51.380 0.071 1 46 15 15 ALA CB C 21.909 0.006 1 47 15 15 ALA N N 116.628 0.013 1 48 16 16 ASP H H 8.386 0.005 1 49 16 16 ASP C C 175.361 0.010 1 50 16 16 ASP CA C 53.589 0.095 1 51 16 16 ASP CB C 40.756 0.013 1 52 16 16 ASP N N 120.307 0.021 1 53 17 17 VAL H H 8.770 0.004 1 54 17 17 VAL C C 174.354 0.007 1 55 17 17 VAL CA C 62.907 0.050 1 56 17 17 VAL CB C 29.662 0.000 1 57 17 17 VAL N N 121.635 0.028 1 58 18 18 ARG H H 7.036 0.006 1 59 18 18 ARG C C 172.713 0.006 1 60 18 18 ARG CA C 53.892 0.054 1 61 18 18 ARG CB C 30.994 0.103 1 62 18 18 ARG N N 124.159 0.018 1 63 19 19 TRP H H 8.540 0.005 1 64 19 19 TRP C C 175.553 0.008 1 65 19 19 TRP CA C 56.678 0.051 1 66 19 19 TRP CB C 28.272 0.000 1 67 19 19 TRP N N 122.466 0.016 1 68 20 20 GLU H H 9.142 0.005 1 69 20 20 GLU C C 176.444 0.006 1 70 20 20 GLU CA C 54.378 0.060 1 71 20 20 GLU CB C 27.730 1.553 1 72 20 20 GLU N N 132.234 0.027 1 73 21 21 GLU H H 8.678 0.004 1 74 21 21 GLU C C 176.930 0.005 1 75 21 21 GLU CA C 58.133 0.050 1 76 21 21 GLU CB C 29.143 0.096 1 77 21 21 GLU N N 125.577 0.024 1 78 22 22 GLN H H 8.575 0.004 1 79 22 22 GLN C C 174.308 0.005 1 80 22 22 GLN CA C 54.423 0.116 1 81 22 22 GLN CB C 26.982 0.024 1 82 22 22 GLN N N 117.937 0.020 1 83 23 23 ALA H H 7.257 0.004 1 84 23 23 ALA C C 177.116 0.008 1 85 23 23 ALA CA C 51.255 0.055 1 86 23 23 ALA CB C 19.561 0.015 1 87 23 23 ALA N N 123.798 0.027 1 88 24 24 GLU H H 7.877 0.004 1 89 24 24 GLU C C 174.187 0.019 1 90 24 24 GLU CA C 55.829 0.050 1 91 24 24 GLU CB C 29.976 0.033 1 92 24 24 GLU N N 121.654 0.031 1 93 25 25 ILE H H 8.123 0.004 1 94 25 25 ILE C C 176.969 0.009 1 95 25 25 ILE CA C 59.371 0.137 1 96 25 25 ILE CB C 38.124 0.000 1 97 25 25 ILE N N 123.865 0.022 1 98 26 26 SER H H 8.699 0.006 1 99 26 26 SER C C 174.426 0.000 1 100 26 26 SER CA C 56.764 0.048 1 101 26 26 SER CB C 64.597 0.000 1 102 26 26 SER N N 120.878 0.013 1 103 30 30 PRO C C 174.532 0.000 1 104 30 30 PRO CA C 62.290 0.008 1 105 30 30 PRO CB C 31.553 0.000 1 106 31 31 ILE H H 7.918 0.007 1 107 31 31 ILE C C 175.984 0.005 1 108 31 31 ILE CA C 60.234 0.111 1 109 31 31 ILE CB C 37.843 0.000 1 110 31 31 ILE N N 118.241 0.016 1 111 32 32 LEU H H 8.586 0.008 1 112 32 32 LEU C C 175.442 0.022 1 113 32 32 LEU CA C 53.224 0.057 1 114 32 32 LEU CB C 45.239 0.011 1 115 32 32 LEU N N 127.108 0.022 1 116 33 33 SER H H 8.753 0.004 1 117 33 33 SER C C 174.206 0.029 1 118 33 33 SER CA C 57.637 0.021 1 119 33 33 SER CB C 62.846 0.162 1 120 33 33 SER N N 118.986 0.018 1 121 34 34 ILE H H 8.244 0.007 1 122 34 34 ILE C C 175.309 0.019 1 123 34 34 ILE CA C 57.883 0.045 1 124 34 34 ILE CB C 42.471 0.007 1 125 34 34 ILE N N 120.474 0.039 1 126 35 35 THR H H 8.679 0.004 1 127 35 35 THR C C 173.236 0.013 1 128 35 35 THR CA C 60.473 0.037 1 129 35 35 THR CB C 69.970 0.003 1 130 35 35 THR N N 117.029 0.024 1 131 36 36 ILE H H 8.614 0.005 1 132 36 36 ILE C C 176.741 0.016 1 133 36 36 ILE CA C 60.498 0.019 1 134 36 36 ILE CB C 37.664 0.001 1 135 36 36 ILE N N 127.174 0.012 1 136 37 37 SER H H 8.917 0.006 1 137 37 37 SER C C 175.259 0.000 1 138 37 37 SER CA C 58.070 0.034 1 139 37 37 SER CB C 63.502 0.000 1 140 37 37 SER N N 124.555 0.053 1 141 38 38 GLU C C 175.757 0.003 1 142 38 38 GLU CA C 58.615 0.000 1 143 38 38 GLU CB C 28.113 0.000 1 144 39 39 ASP H H 7.359 0.005 1 145 39 39 ASP C C 176.127 0.020 1 146 39 39 ASP CA C 52.225 0.138 1 147 39 39 ASP CB C 39.222 0.128 1 148 39 39 ASP N N 114.621 0.045 1 149 40 40 GLY H H 7.837 0.006 1 150 40 40 GLY C C 174.238 0.001 1 151 40 40 GLY CA C 45.213 0.030 1 152 40 40 GLY N N 107.946 0.049 1 153 41 41 SER H H 7.959 0.008 1 154 41 41 SER C C 173.138 0.010 1 155 41 41 SER CA C 58.369 0.024 1 156 41 41 SER CB C 63.444 0.190 1 157 41 41 SER N N 116.713 0.042 1 158 42 42 MET H H 9.442 0.009 1 159 42 42 MET C C 175.053 0.007 1 160 42 42 MET CA C 54.534 0.091 1 161 42 42 MET CB C 35.566 0.055 1 162 42 42 MET N N 120.473 0.022 1 163 43 43 SER H H 8.110 0.004 1 164 43 43 SER C C 173.117 0.020 1 165 43 43 SER CA C 56.297 0.012 1 166 43 43 SER CB C 65.068 0.050 1 167 43 43 SER N N 112.946 0.023 1 168 44 44 ILE H H 8.667 0.005 1 169 44 44 ILE C C 176.258 0.012 1 170 44 44 ILE CA C 61.828 0.049 1 171 44 44 ILE CB C 37.435 0.100 1 172 44 44 ILE N N 124.125 0.064 1 173 45 45 LYS H H 8.616 0.009 1 174 45 45 LYS C C 175.860 0.000 1 175 45 45 LYS CA C 56.198 0.051 1 176 45 45 LYS CB C 32.190 0.000 1 177 45 45 LYS N N 130.012 0.051 1 178 62 62 GLY CA C 44.633 0.053 1 179 63 63 ALA H H 7.693 0.005 1 180 63 63 ALA CA C 53.169 0.037 1 181 63 63 ALA CB C 19.224 0.000 1 182 63 63 ALA N N 129.649 0.014 1 183 70 70 PRO CA C 62.680 0.005 1 184 70 70 PRO CB C 31.090 0.000 1 185 71 71 SER H H 8.155 0.005 1 186 71 71 SER CA C 55.975 0.010 1 187 71 71 SER CB C 62.794 0.000 1 188 71 71 SER N N 117.783 0.013 1 189 76 76 GLY CA C 44.590 0.099 1 190 77 77 LYS H H 8.027 0.004 1 191 77 77 LYS CA C 55.613 0.023 1 192 77 77 LYS CB C 32.219 0.000 1 193 77 77 LYS N N 121.463 0.031 1 194 78 78 ALA H H 8.271 0.005 1 195 78 78 ALA C C 177.183 0.001 1 196 78 78 ALA CA C 51.956 0.004 1 197 78 78 ALA CB C 18.100 0.000 1 198 78 78 ALA N N 125.501 0.053 1 199 79 79 GLU H H 8.135 0.003 1 200 79 79 GLU C C 175.932 0.016 1 201 79 79 GLU CA C 55.899 0.052 1 202 79 79 GLU CB C 29.328 0.102 1 203 79 79 GLU N N 120.329 0.076 1 204 80 80 LEU H H 7.588 0.006 1 205 80 80 LEU C C 175.731 0.007 1 206 80 80 LEU CA C 54.297 0.009 1 207 80 80 LEU CB C 40.129 0.006 1 208 80 80 LEU N N 122.986 0.016 1 209 81 81 GLU H H 7.633 0.006 1 210 81 81 GLU C C 177.415 0.007 1 211 81 81 GLU CA C 55.384 0.020 1 212 81 81 GLU CB C 30.304 0.000 1 213 81 81 GLU N N 120.140 0.037 1 214 82 82 ASP H H 8.675 0.004 1 215 82 82 ASP C C 176.974 0.004 1 216 82 82 ASP CA C 55.292 0.100 1 217 82 82 ASP CB C 39.764 0.010 1 218 82 82 ASP N N 124.500 0.050 1 219 83 83 GLY H H 8.775 0.005 1 220 83 83 GLY C C 171.235 0.032 1 221 83 83 GLY CA C 44.816 0.063 1 222 83 83 GLY N N 108.227 0.034 1 223 84 84 ALA H H 9.310 0.004 1 224 84 84 ALA C C 176.548 0.006 1 225 84 84 ALA CA C 50.319 0.046 1 226 84 84 ALA CB C 18.904 0.006 1 227 84 84 ALA N N 123.120 0.008 1 228 85 85 TYR H H 9.469 0.008 1 229 85 85 TYR C C 174.680 0.013 1 230 85 85 TYR CA C 56.534 0.028 1 231 85 85 TYR CB C 41.816 0.011 1 232 85 85 TYR N N 123.339 0.057 1 233 86 86 ARG H H 9.093 0.005 1 234 86 86 ARG C C 174.810 0.006 1 235 86 86 ARG CA C 54.664 0.076 1 236 86 86 ARG CB C 31.715 0.023 1 237 86 86 ARG N N 117.323 0.032 1 238 87 87 ILE H H 8.789 0.006 1 239 87 87 ILE C C 175.363 0.007 1 240 87 87 ILE CA C 60.545 0.050 1 241 87 87 ILE CB C 37.656 0.027 1 242 87 87 ILE N N 121.962 0.027 1 243 88 88 LYS H H 9.549 0.006 1 244 88 88 LYS C C 173.876 0.005 1 245 88 88 LYS CA C 53.957 0.018 1 246 88 88 LYS CB C 34.834 0.021 1 247 88 88 LYS N N 127.169 0.022 1 248 89 89 GLN H H 8.879 0.007 1 249 89 89 GLN C C 175.500 0.012 1 250 89 89 GLN CA C 53.890 0.033 1 251 89 89 GLN CB C 32.110 0.000 1 252 89 89 GLN N N 121.160 0.049 1 253 90 90 LYS H H 9.091 0.006 1 254 90 90 LYS C C 175.293 0.006 1 255 90 90 LYS CA C 56.833 0.038 1 256 90 90 LYS CB C 31.399 0.039 1 257 90 90 LYS N N 131.366 0.024 1 258 91 91 GLY H H 7.690 0.005 1 259 91 91 GLY C C 174.693 0.000 1 260 91 91 GLY CA C 43.876 0.027 1 261 91 91 GLY N N 114.970 0.009 1 262 92 92 ILE CA C 63.259 0.125 1 263 92 92 ILE CB C 37.432 0.000 1 264 93 93 LEU H H 8.140 0.005 1 265 93 93 LEU C C 176.763 0.002 1 266 93 93 LEU CA C 53.745 0.070 1 267 93 93 LEU CB C 40.262 0.000 1 268 93 93 LEU N N 119.425 0.098 1 269 94 94 GLY H H 7.405 0.002 1 270 94 94 GLY N N 107.915 0.053 1 271 97 97 GLN C C 175.218 0.000 1 272 97 97 GLN CA C 55.826 0.147 1 273 97 97 GLN CB C 28.33 0.000 1 274 98 98 ILE H H 8.813 0.005 1 275 98 98 ILE C C 175.845 0.004 1 276 98 98 ILE CA C 60.931 0.001 1 277 98 98 ILE N N 122.158 0.038 1 278 99 99 GLY H H 7.406 0.004 1 279 99 99 GLY C C 170.808 0.003 1 280 99 99 GLY CA C 45.258 0.051 1 281 99 99 GLY N N 107.182 0.036 1 282 100 100 ALA H H 9.211 0.004 1 283 100 100 ALA C C 174.995 0.001 1 284 100 100 ALA CA C 50.779 0.066 1 285 100 100 ALA CB C 22.294 0.012 1 286 100 100 ALA N N 125.659 0.027 1 287 101 101 GLY H H 8.632 0.005 1 288 101 101 GLY C C 172.924 0.007 1 289 101 101 GLY CA C 46.374 0.019 1 290 101 101 GLY N N 104.488 0.039 1 291 102 102 VAL H H 8.313 0.006 1 292 102 102 VAL C C 174.925 0.005 1 293 102 102 VAL CA C 59.625 0.061 1 294 102 102 VAL CB C 35.648 0.154 1 295 102 102 VAL N N 116.578 0.016 1 296 103 103 TYR H H 10.031 0.004 1 297 103 103 TYR C C 175.087 0.027 1 298 103 103 TYR CA C 56.830 0.028 1 299 103 103 TYR CB C 40.708 0.000 1 300 103 103 TYR N N 134.869 0.024 1 301 104 104 LYS H H 8.894 0.006 1 302 104 104 LYS C C 174.693 0.008 1 303 104 104 LYS CA C 55.838 0.076 1 304 104 104 LYS CB C 35.627 0.020 1 305 104 104 LYS N N 128.239 0.029 1 306 105 105 GLU H H 9.196 0.006 1 307 105 105 GLU C C 176.466 0.002 1 308 105 105 GLU CA C 56.426 0.184 1 309 105 105 GLU CB C 27.455 0.057 1 310 105 105 GLU N N 126.412 0.014 1 311 106 106 GLY H H 8.383 0.007 1 312 106 106 GLY C C 173.619 0.002 1 313 106 106 GLY CA C 45.316 0.050 1 314 106 106 GLY N N 105.050 0.068 1 315 107 107 THR H H 7.358 0.007 1 316 107 107 THR C C 172.066 0.033 1 317 107 107 THR CA C 60.272 0.122 1 318 107 107 THR CB C 71.317 0.092 1 319 107 107 THR N N 117.535 0.038 1 320 108 108 PHE H H 8.895 0.005 1 321 108 108 PHE C C 172.738 0.015 1 322 108 108 PHE CA C 56.876 0.054 1 323 108 108 PHE CB C 39.421 0.000 1 324 108 108 PHE N N 126.949 0.053 1 325 109 109 HIS H H 7.904 0.002 1 326 109 109 HIS C C 173.417 0.008 1 327 109 109 HIS CA C 54.985 0.105 1 328 109 109 HIS CB C 29.999 0.000 1 329 109 109 HIS N N 127.293 0.073 1 330 110 110 THR H H 8.839 0.006 1 331 110 110 THR C C 172.303 0.045 1 332 110 110 THR CA C 60.236 0.038 1 333 110 110 THR CB C 67.344 0.078 1 334 110 110 THR N N 117.603 0.035 1 335 111 111 MET H H 8.320 0.005 1 336 111 111 MET C C 177.406 0.013 1 337 111 111 MET CA C 53.786 0.055 1 338 111 111 MET CB C 31.305 0.013 1 339 111 111 MET N N 117.477 0.041 1 340 112 112 TRP H H 7.612 0.006 1 341 112 112 TRP C C 179.152 0.000 1 342 112 112 TRP CA C 61.376 0.020 1 343 112 112 TRP CB C 26.748 0.000 1 344 112 112 TRP N N 127.358 0.063 1 345 113 113 HIS C C 175.427 0.000 1 346 113 113 HIS CA C 59.284 0.000 1 347 114 114 VAL H H 6.729 0.004 1 348 114 114 VAL C C 175.019 0.002 1 349 114 114 VAL CA C 64.783 0.044 1 350 114 114 VAL CB C 30.196 0.124 1 351 114 114 VAL N N 117.961 0.008 1 352 115 115 THR H H 6.224 0.007 1 353 115 115 THR C C 176.209 0.007 1 354 115 115 THR CA C 60.393 0.014 1 355 115 115 THR CB C 69.411 0.054 1 356 115 115 THR N N 100.185 0.071 1 357 116 116 ARG H H 9.117 0.006 1 358 116 116 ARG C C 175.681 0.038 1 359 116 116 ARG CA C 55.592 0.044 1 360 116 116 ARG CB C 25.979 0.000 1 361 116 116 ARG N N 122.400 0.051 1 362 117 117 GLY H H 6.713 0.009 1 363 117 117 GLY C C 173.140 0.016 1 364 117 117 GLY CA C 44.469 0.162 1 365 117 117 GLY N N 133.395 0.031 1 366 118 118 ALA H H 7.282 0.005 1 367 118 118 ALA C C 177.612 0.025 1 368 118 118 ALA CA C 51.581 0.018 1 369 118 118 ALA CB C 18.673 0.004 1 370 118 118 ALA N N 121.276 0.042 1 371 119 119 VAL H H 8.281 0.004 1 372 119 119 VAL C C 173.943 0.015 1 373 119 119 VAL CA C 63.520 0.023 1 374 119 119 VAL CB C 31.243 0.000 1 375 119 119 VAL N N 120.455 0.032 1 376 120 120 LEU H H 7.823 0.006 1 377 120 120 LEU C C 175.042 0.010 1 378 120 120 LEU CA C 52.195 0.095 1 379 120 120 LEU CB C 43.657 0.029 1 380 120 120 LEU N N 122.666 0.034 1 381 121 121 MET H H 8.191 0.007 1 382 121 121 MET C C 175.854 0.014 1 383 121 121 MET CA C 52.553 0.080 1 384 121 121 MET CB C 33.494 0.097 1 385 121 121 MET N N 117.803 0.031 1 386 122 122 HIS H H 8.697 0.004 1 387 122 122 HIS C C 174.498 0.000 1 388 122 122 HIS CA C 55.789 0.016 1 389 122 122 HIS CB C 31.316 0.161 1 390 122 122 HIS N N 120.402 0.034 1 391 123 123 LYS H H 9.372 0.004 1 392 123 123 LYS C C 176.528 0.012 1 393 123 123 LYS CA C 56.459 0.033 1 394 123 123 LYS CB C 28.684 0.140 1 395 123 123 LYS N N 128.596 0.064 1 396 124 124 GLY H H 8.591 0.007 1 397 124 124 GLY C C 173.608 0.004 1 398 124 124 GLY CA C 44.719 0.076 1 399 124 124 GLY N N 104.684 0.035 1 400 125 125 LYS H H 7.788 0.004 1 401 125 125 LYS C C 174.847 0.004 1 402 125 125 LYS CA C 54.442 0.030 1 403 125 125 LYS CB C 32.618 0.033 1 404 125 125 LYS N N 122.337 0.034 1 405 126 126 ARG H H 8.264 0.004 1 406 126 126 ARG C C 176.235 0.009 1 407 126 126 ARG CA C 55.586 0.116 1 408 126 126 ARG CB C 31.031 0.005 1 409 126 126 ARG N N 124.022 0.027 1 410 127 127 ILE H H 9.280 0.005 1 411 127 127 ILE C C 174.777 0.001 1 412 127 127 ILE CA C 60.481 0.043 1 413 127 127 ILE CB C 38.437 0.030 1 414 127 127 ILE N N 126.312 0.037 1 415 128 128 GLU H H 8.502 0.007 1 416 128 128 GLU C C 174.724 0.000 1 417 128 128 GLU CA C 53.888 0.017 1 418 128 128 GLU CB C 28.771 0.000 1 419 128 128 GLU N N 125.493 0.018 1 420 129 129 PRO CA C 62.952 0.009 1 421 129 129 PRO CB C 30.780 0.000 1 422 130 130 SER H H 9.271 0.007 1 423 130 130 SER C C 173.453 0.010 1 424 130 130 SER CA C 58.491 0.081 1 425 130 130 SER CB C 64.507 0.092 1 426 130 130 SER N N 117.289 0.066 1 427 131 131 TRP H H 7.805 0.005 1 428 131 131 TRP C C 172.398 0.015 1 429 131 131 TRP CA C 57.475 0.113 1 430 131 131 TRP CB C 29.474 0.106 1 431 131 131 TRP N N 124.285 0.059 1 432 132 132 ALA H H 6.926 0.009 1 433 132 132 ALA C C 174.917 0.004 1 434 132 132 ALA CA C 51.225 0.040 1 435 132 132 ALA CB C 21.752 0.032 1 436 132 132 ALA N N 125.811 0.044 1 437 133 133 ASP H H 7.433 0.003 1 438 133 133 ASP C C 176.290 0.025 1 439 133 133 ASP CA C 52.587 0.000 1 440 133 133 ASP CB C 42.734 0.046 1 441 133 133 ASP N N 118.164 0.027 1 442 134 134 VAL H H 8.056 0.006 1 443 134 134 VAL C C 176.907 0.008 1 444 134 134 VAL CA C 64.959 0.060 1 445 134 134 VAL CB C 29.862 0.000 1 446 134 134 VAL N N 124.663 0.034 1 447 135 135 LYS H H 7.495 0.006 1 448 135 135 LYS C C 178.533 0.009 1 449 135 135 LYS CA C 58.505 0.071 1 450 135 135 LYS CB C 30.700 0.000 1 451 135 135 LYS N N 118.942 0.051 1 452 136 136 LYS H H 7.222 0.007 1 453 136 136 LYS C C 175.049 0.004 1 454 136 136 LYS CA C 55.684 0.034 1 455 136 136 LYS CB C 32.639 0.000 1 456 136 136 LYS N N 117.287 0.053 1 457 137 137 ASP H H 7.771 0.005 1 458 137 137 ASP C C 175.066 0.009 1 459 137 137 ASP CA C 54.296 0.038 1 460 137 137 ASP CB C 39.362 0.023 1 461 137 137 ASP N N 119.485 0.059 1 462 138 138 LEU H H 7.309 0.007 1 463 138 138 LEU C C 174.860 0.036 1 464 138 138 LEU CA C 53.462 0.048 1 465 138 138 LEU CB C 45.975 0.001 1 466 138 138 LEU N N 116.071 0.039 1 467 139 139 ILE H H 8.480 0.005 1 468 139 139 ILE C C 171.502 0.009 1 469 139 139 ILE CA C 59.589 0.115 1 470 139 139 ILE CB C 40.719 0.070 1 471 139 139 ILE N N 118.065 0.048 1 472 140 140 SER H H 9.862 0.007 1 473 140 140 SER C C 173.936 0.019 1 474 140 140 SER CA C 56.357 0.025 1 475 140 140 SER CB C 67.385 0.006 1 476 140 140 SER N N 121.137 0.022 1 477 141 141 TYR H H 9.368 0.005 1 478 141 141 TYR C C 175.728 0.000 1 479 141 141 TYR CA C 56.794 0.020 1 480 141 141 TYR CB C 40.260 0.000 1 481 141 141 TYR N N 120.875 0.028 1 482 147 147 LEU CA C 54.645 0.010 1 483 148 148 GLU H H 9.001 0.005 1 484 148 148 GLU CA C 55.824 0.131 1 485 148 148 GLU CB C 31.454 0.036 1 486 148 148 GLU N N 121.704 0.022 1 487 149 149 GLY H H 7.670 0.005 1 488 149 149 GLY C C 172.587 0.012 1 489 149 149 GLY CA C 45.823 0.078 1 490 149 149 GLY N N 109.478 0.015 1 491 150 150 GLU H H 8.581 0.003 1 492 150 150 GLU C C 175.252 0.011 1 493 150 150 GLU CA C 54.048 0.017 1 494 150 150 GLU CB C 31.526 0.043 1 495 150 150 GLU N N 125.120 0.040 1 496 151 151 TRP H H 9.324 0.007 1 497 151 151 TRP C C 174.351 0.000 1 498 151 151 TRP CA C 58.607 0.069 1 499 151 151 TRP CB C 27.290 0.000 1 500 151 151 TRP N N 129.567 0.044 1 501 152 152 LYS C C 173.036 0.002 1 502 152 152 LYS CA C 53.260 0.090 1 503 152 152 LYS CB C 32.652 0.000 1 504 153 153 GLU H H 7.374 0.004 1 505 153 153 GLU C C 176.966 0.012 1 506 153 153 GLU CA C 57.130 0.059 1 507 153 153 GLU CB C 28.142 0.013 1 508 153 153 GLU N N 121.436 0.013 1 509 154 154 GLY H H 7.880 0.007 1 510 154 154 GLY C C 174.227 0.013 1 511 154 154 GLY CA C 44.489 0.121 1 512 154 154 GLY N N 113.447 0.037 1 513 155 155 GLU H H 7.766 0.005 1 514 155 155 GLU C C 177.233 0.005 1 515 155 155 GLU CA C 55.683 0.014 1 516 155 155 GLU CB C 29.329 0.000 1 517 155 155 GLU N N 120.230 0.041 1 518 156 156 GLU H H 8.637 0.004 1 519 156 156 GLU C C 175.524 0.013 1 520 156 156 GLU CA C 56.791 0.017 1 521 156 156 GLU CB C 31.044 0.140 1 522 156 156 GLU N N 121.382 0.020 1 523 157 157 VAL H H 8.691 0.005 1 524 157 157 VAL C C 174.816 0.008 1 525 157 157 VAL CA C 58.337 0.041 1 526 157 157 VAL CB C 35.005 0.034 1 527 157 157 VAL N N 110.116 0.031 1 528 158 158 GLN H H 9.050 0.005 1 529 158 158 GLN C C 176.185 0.007 1 530 158 158 GLN CA C 53.057 0.090 1 531 158 158 GLN CB C 29.293 0.000 1 532 158 158 GLN N N 117.123 0.025 1 533 159 159 VAL H H 8.711 0.004 1 534 159 159 VAL C C 174.213 0.007 1 535 159 159 VAL CA C 60.985 0.103 1 536 159 159 VAL CB C 30.743 0.026 1 537 159 159 VAL N N 121.202 0.021 1 538 160 160 LEU H H 8.239 0.004 1 539 160 160 LEU C C 173.083 0.002 1 540 160 160 LEU CA C 52.520 0.005 1 541 160 160 LEU CB C 38.257 0.029 1 542 160 160 LEU N N 132.250 0.023 1 543 161 161 ALA H H 7.624 0.004 1 544 161 161 ALA C C 178.366 0.003 1 545 161 161 ALA CA C 51.840 0.081 1 546 161 161 ALA CB C 16.221 0.048 1 547 161 161 ALA N N 123.193 0.023 1 548 162 162 LEU H H 7.363 0.005 1 549 162 162 LEU C C 174.998 0.005 1 550 162 162 LEU CA C 51.636 0.058 1 551 162 162 LEU CB C 38.427 0.000 1 552 162 162 LEU N N 127.998 0.040 1 553 163 163 GLU H H 7.954 0.005 1 554 163 163 GLU C C 175.895 0.000 1 555 163 163 GLU CA C 54.312 0.067 1 556 163 163 GLU CB C 28.385 0.000 1 557 163 163 GLU N N 120.908 0.036 1 558 165 165 GLY C C 173.068 0.000 1 559 165 165 GLY CA C 45.411 0.022 1 560 166 166 LYS H H 7.464 0.006 1 561 166 166 LYS C C 176.008 0.000 1 562 166 166 LYS CA C 53.102 0.015 1 563 166 166 LYS CB C 34.481 0.000 1 564 166 166 LYS N N 118.338 0.047 1 565 168 168 PRO C C 174.633 0.011 1 566 168 168 PRO CA C 63.199 0.045 1 567 168 168 PRO CB C 30.175 0.000 1 568 169 169 ARG H H 7.768 0.005 1 569 169 169 ARG C C 172.161 0.008 1 570 169 169 ARG CA C 54.527 0.058 1 571 169 169 ARG CB C 32.639 0.009 1 572 169 169 ARG N N 123.406 0.025 1 573 170 170 ALA H H 8.302 0.004 1 574 170 170 ALA C C 176.964 0.005 1 575 170 170 ALA CA C 49.905 0.071 1 576 170 170 ALA CB C 19.256 0.018 1 577 170 170 ALA N N 127.074 0.028 1 578 171 171 VAL H H 8.265 0.005 1 579 171 171 VAL C C 173.709 0.006 1 580 171 171 VAL CA C 61.164 0.093 1 581 171 171 VAL CB C 33.461 0.073 1 582 171 171 VAL N N 122.438 0.018 1 583 172 172 GLN H H 9.276 0.007 1 584 172 172 GLN C C 173.619 0.008 1 585 172 172 GLN CA C 53.946 0.016 1 586 172 172 GLN CB C 30.258 0.025 1 587 172 172 GLN N N 130.238 0.010 1 588 173 173 THR H H 9.059 0.004 1 589 173 173 THR C C 170.740 0.020 1 590 173 173 THR CA C 60.021 0.044 1 591 173 173 THR CB C 69.875 0.000 1 592 173 173 THR N N 118.117 0.022 1 593 174 174 LYS H H 7.830 0.004 1 594 174 174 LYS C C 173.497 0.000 1 595 174 174 LYS CA C 52.499 0.017 1 596 174 174 LYS CB C 31.832 0.000 1 597 174 174 LYS N N 127.700 0.031 1 598 175 175 PRO C C 178.230 0.025 1 599 175 175 PRO CA C 62.993 0.032 1 600 175 175 PRO CB C 31.220 0.000 1 601 176 176 GLY H H 8.530 0.007 1 602 176 176 GLY C C 172.304 0.017 1 603 176 176 GLY CA C 42.815 0.035 1 604 176 176 GLY N N 107.924 0.035 1 605 177 177 LEU H H 8.413 0.002 1 606 177 177 LEU C C 175.419 0.027 1 607 177 177 LEU CA C 53.703 0.013 1 608 177 177 LEU CB C 45.837 0.000 1 609 177 177 LEU N N 118.058 0.029 1 610 178 178 PHE H H 9.285 0.006 1 611 178 178 PHE C C 175.888 0.008 1 612 178 178 PHE CA C 53.119 0.119 1 613 178 178 PHE CB C 38.685 0.000 1 614 178 178 PHE N N 119.829 0.059 1 615 179 179 LYS H H 9.133 0.004 1 616 179 179 LYS C C 176.487 0.006 1 617 179 179 LYS CA C 55.388 0.036 1 618 179 179 LYS CB C 31.455 0.000 1 619 179 179 LYS N N 122.980 0.041 1 620 180 180 THR H H 8.201 0.009 1 621 180 180 THR C C 175.120 0.000 1 622 180 180 THR CA C 59.397 0.026 1 623 180 180 THR CB C 70.413 0.000 1 624 180 180 THR N N 116.232 0.054 1 625 183 183 GLY C C 173.044 0.000 1 626 183 183 GLY CA C 44.610 0.090 1 627 184 184 THR H H 8.433 0.004 1 628 184 184 THR C C 174.236 0.002 1 629 184 184 THR CA C 60.581 0.030 1 630 184 184 THR CB C 70.413 0.000 1 631 184 184 THR N N 116.341 0.050 1 632 185 185 ILE H H 8.976 0.006 1 633 185 185 ILE C C 174.964 0.002 1 634 185 185 ILE CA C 59.577 0.080 1 635 185 185 ILE CB C 41.906 0.032 1 636 185 185 ILE N N 123.619 0.031 1 637 186 186 GLY H H 8.881 0.007 1 638 186 186 GLY C C 171.612 0.009 1 639 186 186 GLY CA C 45.999 0.048 1 640 186 186 GLY N N 112.108 0.035 1 641 187 187 ALA H H 6.900 0.005 1 642 187 187 ALA C C 175.837 0.005 1 643 187 187 ALA CA C 49.486 0.145 1 644 187 187 ALA CB C 19.355 0.047 1 645 187 187 ALA N N 124.016 0.044 1 646 188 188 VAL H H 9.085 0.005 1 647 188 188 VAL C C 175.111 0.018 1 648 188 188 VAL CA C 58.584 0.117 1 649 188 188 VAL CB C 32.530 0.000 1 650 188 188 VAL N N 116.898 0.051 1 651 189 189 SER H H 9.652 0.009 1 652 189 189 SER C C 175.147 0.000 1 653 189 189 SER CA C 54.545 0.054 1 654 189 189 SER CB C 62.091 0.000 1 655 189 189 SER N N 127.725 0.100 1 656 191 191 ASP C C 173.946 0.000 1 657 191 191 ASP CA C 52.786 0.048 1 658 192 192 PHE H H 6.896 0.004 1 659 192 192 PHE C C 174.245 0.011 1 660 192 192 PHE CA C 55.838 0.118 1 661 192 192 PHE CB C 41.309 0.007 1 662 192 192 PHE N N 121.563 0.037 1 663 193 193 SER H H 9.367 0.006 1 664 193 193 SER C C 172.555 0.000 1 665 193 193 SER CA C 59.292 2.311 1 666 193 193 SER N N 115.534 0.072 1 667 196 196 THR C C 176.114 0.000 1 668 196 196 THR CA C 62.517 0.000 1 669 197 197 SER H H 8.360 0.007 1 670 197 197 SER C C 173.404 0.032 1 671 197 197 SER CA C 60.843 0.036 1 672 197 197 SER CB C 65.035 0.006 1 673 197 197 SER N N 125.162 0.040 1 674 198 198 GLY H H 9.719 0.006 1 675 198 198 GLY C C 172.575 0.055 1 676 198 198 GLY CA C 43.509 0.159 1 677 198 198 GLY N N 108.787 0.055 1 678 199 199 SER H H 8.203 0.004 1 679 199 199 SER N N 106.199 0.021 1 680 200 200 PRO C C 173.353 0.000 1 681 201 201 ILE H H 8.188 0.004 1 682 201 201 ILE C C 175.609 0.021 1 683 201 201 ILE CA C 59.722 0.015 1 684 201 201 ILE CB C 36.841 0.152 1 685 201 201 ILE N N 120.439 0.024 1 686 202 202 VAL H H 9.763 0.005 1 687 202 202 VAL C C 175.335 0.002 1 688 202 202 VAL CA C 59.857 0.083 1 689 202 202 VAL CB C 34.819 0.049 1 690 202 202 VAL N N 126.221 0.040 1 691 203 203 ASP H H 8.747 0.006 1 692 203 203 ASP C C 178.389 0.013 1 693 203 203 ASP CA C 51.653 0.024 1 694 203 203 ASP CB C 41.952 0.053 1 695 203 203 ASP N N 122.779 0.033 1 696 204 204 LYS H H 7.792 0.005 1 697 204 204 LYS C C 178.103 0.020 1 698 204 204 LYS CA C 57.574 0.036 1 699 204 204 LYS CB C 30.491 0.000 1 700 204 204 LYS N N 116.252 0.026 1 701 205 205 LYS H H 7.738 0.005 1 702 205 205 LYS C C 176.969 0.021 1 703 205 205 LYS CA C 54.925 0.057 1 704 205 205 LYS CB C 30.699 0.000 1 705 205 205 LYS N N 118.897 0.038 1 706 206 206 GLY H H 8.646 0.006 1 707 206 206 GLY C C 173.731 0.014 1 708 206 206 GLY CA C 45.138 0.042 1 709 206 206 GLY N N 110.099 0.056 1 710 207 207 LYS H H 8.398 0.004 1 711 207 207 LYS C C 175.454 0.004 1 712 207 207 LYS CA C 53.669 0.046 1 713 207 207 LYS CB C 30.711 0.000 1 714 207 207 LYS N N 120.326 0.038 1 715 208 208 VAL H H 8.884 0.006 1 716 208 208 VAL C C 176.695 0.017 1 717 208 208 VAL CA C 62.111 0.068 1 718 208 208 VAL CB C 29.781 0.000 1 719 208 208 VAL N N 123.083 0.038 1 720 209 209 VAL H H 8.908 0.005 1 721 209 209 VAL C C 174.423 0.021 1 722 209 209 VAL CA C 59.909 0.105 1 723 209 209 VAL CB C 29.727 0.000 1 724 209 209 VAL N N 121.010 0.039 1 725 210 210 GLY H H 7.383 0.004 1 726 210 210 GLY C C 169.680 0.028 1 727 210 210 GLY CA C 44.491 0.074 1 728 210 210 GLY N N 104.871 0.016 1 729 211 211 LEU H H 9.127 0.007 1 730 211 211 LEU C C 175.910 0.018 1 731 211 211 LEU CA C 52.947 0.045 1 732 211 211 LEU CB C 43.996 0.000 1 733 211 211 LEU N N 117.676 0.022 1 734 212 212 TYR H H 8.373 0.009 1 735 212 212 TYR C C 174.700 0.002 1 736 212 212 TYR CA C 57.521 0.099 1 737 212 212 TYR CB C 41.068 0.053 1 738 212 212 TYR N N 121.558 0.036 1 739 213 213 GLY H H 7.537 0.006 1 740 213 213 GLY C C 171.572 0.007 1 741 213 213 GLY CA C 45.825 0.089 1 742 213 213 GLY N N 114.001 0.030 1 743 214 214 ASN H H 9.014 0.007 1 744 214 214 ASN C C 175.206 0.015 1 745 214 214 ASN CA C 51.819 0.086 1 746 214 214 ASN CB C 38.519 0.051 1 747 214 214 ASN N N 122.001 0.065 1 748 215 215 GLY H H 6.667 0.006 1 749 215 215 GLY C C 171.761 0.026 1 750 215 215 GLY CA C 45.502 0.063 1 751 215 215 GLY N N 112.234 0.032 1 752 216 216 VAL H H 8.210 0.005 1 753 216 216 VAL C C 172.341 0.001 1 754 216 216 VAL CA C 58.434 0.015 1 755 216 216 VAL CB C 34.809 0.010 1 756 216 216 VAL N N 111.741 0.049 1 757 217 217 VAL H H 7.827 0.004 1 758 217 217 VAL C C 177.319 0.000 1 759 217 217 VAL CA C 60.012 0.162 1 760 217 217 VAL CB C 31.970 0.022 1 761 217 217 VAL N N 119.617 0.040 1 762 218 218 THR H H 8.797 0.009 1 763 218 218 THR C C 177.345 0.000 1 764 218 218 THR CA C 60.846 0.032 1 765 218 218 THR CB C 69.954 0.000 1 766 218 218 THR N N 117.525 0.050 1 767 220 220 SER C C 174.838 0.000 1 768 220 220 SER CA C 58.108 0.000 1 769 220 220 SER CB C 63.003 0.000 1 770 221 221 GLY H H 8.046 0.004 1 771 221 221 GLY C C 173.625 0.011 1 772 221 221 GLY CA C 44.363 0.117 1 773 221 221 GLY N N 111.219 0.028 1 774 222 222 ALA H H 7.232 0.006 1 775 222 222 ALA C C 175.576 0.014 1 776 222 222 ALA CA C 51.316 0.029 1 777 222 222 ALA CB C 17.760 0.009 1 778 222 222 ALA N N 124.381 0.044 1 779 223 223 TYR H H 7.992 0.004 1 780 223 223 TYR C C 174.635 0.011 1 781 223 223 TYR CA C 57.999 0.016 1 782 223 223 TYR CB C 39.364 0.148 1 783 223 223 TYR N N 123.474 0.015 1 784 224 224 VAL H H 7.800 0.006 1 785 224 224 VAL C C 174.112 0.017 1 786 224 224 VAL CA C 59.653 0.071 1 787 224 224 VAL CB C 32.920 0.044 1 788 224 224 VAL N N 126.525 0.034 1 789 225 225 SER H H 8.513 0.006 1 790 225 225 SER C C 175.682 0.004 1 791 225 225 SER CA C 55.451 0.066 1 792 225 225 SER CB C 66.182 0.160 1 793 225 225 SER N N 117.727 0.033 1 794 226 226 ALA H H 9.181 0.006 1 795 226 226 ALA C C 179.292 0.009 1 796 226 226 ALA CA C 52.937 0.013 1 797 226 226 ALA CB C 17.863 0.007 1 798 226 226 ALA N N 129.776 0.062 1 799 227 227 ILE H H 7.656 0.006 1 800 227 227 ILE C C 174.186 0.016 1 801 227 227 ILE CA C 61.529 0.091 1 802 227 227 ILE CB C 34.818 0.007 1 803 227 227 ILE N N 122.426 0.033 1 804 228 228 ALA H H 7.563 0.007 1 805 228 228 ALA C C 174.972 0.015 1 806 228 228 ALA CA C 53.012 0.003 1 807 228 228 ALA CB C 19.443 0.016 1 808 228 228 ALA N N 131.400 0.028 1 809 229 229 GLN H H 8.066 0.005 1 810 229 229 GLN C C 174.101 0.017 1 811 229 229 GLN CA C 52.967 0.023 1 812 229 229 GLN CB C 32.411 0.000 1 813 229 229 GLN N N 124.210 0.023 1 814 230 230 THR H H 7.942 0.007 1 815 230 230 THR C C 172.138 0.013 1 816 230 230 THR CA C 59.316 0.061 1 817 230 230 THR CB C 69.344 0.055 1 818 230 230 THR N N 118.670 0.046 1 819 231 231 GLU H H 7.674 0.007 1 820 231 231 GLU C C 176.028 0.010 1 821 231 231 GLU CA C 56.114 0.067 1 822 231 231 GLU CB C 29.252 0.137 1 823 231 231 GLU N N 121.675 0.023 1 824 232 232 LYS H H 8.204 0.007 1 825 232 232 LYS C C 176.595 0.009 1 826 232 232 LYS CA C 56.328 0.107 1 827 232 232 LYS CB C 31.712 0.043 1 828 232 232 LYS N N 123.301 0.048 1 829 233 233 SER H H 8.601 0.006 1 830 233 233 SER C C 174.456 0.012 1 831 233 233 SER CA C 57.566 0.098 1 832 233 233 SER CB C 63.303 0.023 1 833 233 233 SER N N 120.165 0.019 1 834 234 234 ILE H H 8.146 0.006 1 835 234 234 ILE C C 176.104 0.007 1 836 234 234 ILE CA C 60.571 0.049 1 837 234 234 ILE CB C 37.689 0.052 1 838 234 234 ILE N N 123.621 0.030 1 839 235 235 GLU H H 8.227 0.006 1 840 235 235 GLU C C 175.745 0.041 1 841 235 235 GLU CA C 55.736 0.122 1 842 235 235 GLU CB C 29.427 0.048 1 843 235 235 GLU N N 124.699 0.028 1 844 236 236 ASP H H 8.190 0.007 1 845 236 236 ASP C C 175.407 0.023 1 846 236 236 ASP CA C 53.898 0.093 1 847 236 236 ASP CB C 40.725 0.021 1 848 236 236 ASP N N 122.110 0.063 1 849 237 237 ASN H H 8.255 0.004 1 850 237 237 ASN C C 172.975 0.000 1 851 237 237 ASN CA C 50.981 0.075 1 852 237 237 ASN CB C 38.365 0.000 1 853 237 237 ASN N N 120.146 0.062 1 854 243 243 ASP C C 175.884 0.000 1 855 243 243 ASP CA C 53.861 0.006 1 856 244 244 ILE H H 7.936 0.002 1 857 244 244 ILE C C 175.885 0.022 1 858 244 244 ILE CA C 60.995 0.020 1 859 244 244 ILE CB C 37.516 0.000 1 860 244 244 ILE N N 120.736 0.014 1 861 245 245 PHE H H 8.119 0.007 1 862 245 245 PHE CA C 57.155 0.121 1 863 245 245 PHE CB C 38.248 0.121 1 864 245 245 PHE N N 123.722 0.021 1 865 246 246 ARG H H 7.881 0.004 1 866 246 246 ARG C C 174.732 0.000 1 867 246 246 ARG CA C 55.824 0.738 1 868 246 246 ARG CB C 29.526 0.153 1 869 246 246 ARG N N 124.130 0.041 1 870 247 247 LYS H H 7.712 0.004 1 871 247 247 LYS C C 181.200 0.000 1 872 247 247 LYS CA C 57.120 0.000 1 873 247 247 LYS CB C 32.465 0.000 1 874 247 247 LYS N N 128.488 0.017 1 stop_ save_