data_5358 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C Backbone Chemical Shift Assignments for Trypsin-Bound Bovine Pancreatic Trypsin Inhibitor (BPTI) at pH 5.8 and 36 Degrees ; _BMRB_accession_number 5358 _BMRB_flat_file_name bmr5358.str _Entry_type original _Submission_date 2001-04-30 _Accession_date 2001-04-30 _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 Biamonti Clelia . . 2 Baran Michael C . 3 Montelione Gaetano T . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 93 "13C chemical shifts" 109 "15N chemical shifts" 53 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-08 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5359 'Free form of BPTI.' stop_ _Original_release_date 2002-04-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and Dynamic Investigations of Macromolecular Recognition Processes by Nuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type thesis _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Biamonti Clelia . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Thesis_institution 'Rutgers University' _Thesis_institution_city 'Piscataway, NJ' _Thesis_institution_country 'U. S. A.' _Page_first . _Page_last . _Year 1996 _Details . save_ ################################## # Molecular system description # ################################## save_system_BPTI _Saveframe_category molecular_system _Mol_system_name 'Trypsin-Bound Bovine Pancreatic Trypsin Inhibitor' _Abbreviation_common BPTI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BPTI $BPTI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BPTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bovine pancreatic trypsin inhibitor' _Abbreviation_common BPTI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _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 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 3.54e-26 BMRB 1156 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 1179 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 236 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 237 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 262 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 263 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 264 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 338 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 411 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 412 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 413 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 414 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 415 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 416 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 419 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 45 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 46 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 48 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 485 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 4868 BPTI-R52 100.00 58 98.28 98.28 2.63e-25 BMRB 49 'basic pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 4968 BPTI 100.00 58 100.00 100.00 3.54e-26 BMRB 5171 BPTI 100.00 58 98.28 98.28 1.04e-25 BMRB 5307 'Basic Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 BMRB 5359 'bovine pancreatic trypsin inhibitor' 100.00 58 100.00 100.00 3.54e-26 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 3.54e-26 PDB 1BHC 'Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate' 100.00 58 100.00 100.00 3.54e-26 PDB 1BPI 'The Structure Of Bovine Pancreatic Trypsin Inhibitor At 125k: Definition Of Carboxyl-Terminal Residues Glycine-57 And Alanine-58' 100.00 58 100.00 100.00 3.54e-26 PDB 1BPT 'Crevice-Forming Mutants Of Bpti: Crystal Structures Of F22a, Y23a, N43g, And F45a' 100.00 58 98.28 98.28 2.13e-25 PDB 1BTH 'Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 PDB 1BTI ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; 100.00 58 98.28 98.28 2.15e-25 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 3.54e-26 PDB 1BZX 'The Crystal Structure Of Anionic Salmon Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 PDB 1CBW 'Bovine Chymotrypsin Complexed To Bpti' 100.00 58 100.00 100.00 3.54e-26 PDB 1CO7 'R117h Mutant Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' 100.00 99 100.00 100.00 3.82e-27 PDB 1D0D 'Crystal Structure Of Tick Anticoagulant Protein Complexed With Bovine Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 PDB 1EAW 'Crystal Structure Of The Mtsp1 (Matriptase)-Bpti (Aprotinin) Complex' 100.00 58 100.00 100.00 3.54e-26 PDB 1F5R 'Rat Trypsinogen Mutant Complexed With Bovine Pancreatic Trypsin Inhibitor' 100.00 65 100.00 100.00 3.02e-26 PDB 1F7Z 'Rat Trypsinogen K15a Complexed With Bovine Pancreatic Trypsin Inhibitor' 100.00 65 100.00 100.00 3.02e-26 PDB 1FAN ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; 100.00 58 98.28 98.28 2.15e-25 PDB 1FY8 'Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex' 100.00 58 100.00 100.00 3.54e-26 PDB 1JV8 'Nmr Structure Of Bpti Mutant G37a' 100.00 58 98.28 98.28 1.04e-25 PDB 1JV9 'Nmr Structure Of Bpti Mutant G37a' 100.00 58 98.28 98.28 1.04e-25 PDB 1MTN 'Bovine Alpha-Chymotrypsin:bpti Crystallization' 100.00 58 100.00 100.00 3.54e-26 PDB 1NAG ; Crevice-Forming Mutants In The Rigid Core Of Bovine Pancreatic Trypsin Inhibitor: Crystal Structures Of F22a, Y23a, N43g, And F45a ; 100.00 58 98.28 98.28 1.77e-25 PDB 1OA5 'The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure' 100.00 58 100.00 100.00 3.54e-26 PDB 1OA6 'The Solution Structure Of Bovine Pancreatic Trypsin Inhibitor At High Pressure' 100.00 58 100.00 100.00 3.54e-26 PDB 1PIT ; Determination Of A High-Quality Nuclear Magnetic Resonance Solution Structure Of The Bovine Pancreatic Trypsin Inhibitor And Comparison With Three Crystal Structures ; 98.28 58 100.00 100.00 1.20e-25 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 3.54e-26 PDB 1UUA 'Solution Structure Of A Truncated Bovine Pancreatic Trypsin Inhibitor, 3-58 Bpti' 96.55 56 100.00 100.00 6.00e-25 PDB 1YKT 'TrypsinBPTI COMPLEX MUTANT' 96.55 56 100.00 100.00 4.09e-25 PDB 2FI4 'Crystal Structure Of A Bpti Variant (Cys14->ser) In Complex With Trypsin' 100.00 58 98.28 98.28 1.65e-25 PDB 2FI5 'Crystal Structure Of A Bpti Variant (Cys38->ser) In Complex With Trypsin' 100.00 58 98.28 98.28 1.65e-25 PDB 2FTL 'Crystal Structure Of Trypsin Complexed With Bpti At 100k' 100.00 58 100.00 100.00 3.54e-26 PDB 2FTM 'Crystal Structure Of Trypsin Complexed With The Bpti Variant (Tyr35->gly)' 100.00 58 98.28 98.28 3.52e-25 PDB 2HEX 'Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 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 3.54e-26 PDB 2KAI ; Refined 2.5 Angstroms X-Ray Crystal Structure Of The Complex Formed By Porcine Kallikrein A And The Bovine Pancreatic Trypsin Inhibitor. Crystallization, Patterson Search, Structure Determination, Refinement, Structure And Comparison With Its Components And With The Bovine Trypsin- Pancreatic Trypsin Inhibitor Complex ; 100.00 58 100.00 100.00 3.54e-26 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 3.54e-26 PDB 2R9P 'Human Mesotrypsin Complexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)' 100.00 58 100.00 100.00 3.54e-26 PDB 2RA3 'Human Cationic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' 100.00 58 100.00 100.00 3.54e-26 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 3.54e-26 PDB 2TPI 'On The Disordered Activation Domain In Trypsinogen. Chemical Labelling And Low-Temperature Crystallography' 100.00 58 100.00 100.00 3.54e-26 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 3.54e-26 PDB 3TGI 'Wild-Type Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' 100.00 65 100.00 100.00 3.02e-26 PDB 3TGJ 'S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)' 100.00 65 100.00 100.00 3.02e-26 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 3.02e-26 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 3.54e-26 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 3.54e-26 PDB 4TPI ; The Refined 2.2-Angstroms (0.22-Nm) X-Ray Crystal Structure Of The Ternary Complex Formed By Bovine Trypsinogen, Valine-Valine And The Arg15 Analogue Of Bovine Pancreatic Trypsin Inhibitor ; 100.00 58 98.28 100.00 8.10e-26 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 1.20e-25 PDB 6PTI 'Structure Of Form Iii Crystals Of Bovine Pancreatic Trypsin Inhibitor' 100.00 58 100.00 100.00 3.54e-26 PDB 8PTI 'Crystal Structure Of A Y35g Mutant Of Bovine Pancreatic Trypsin Inhibitor' 100.00 58 98.28 98.28 3.52e-25 PDB 9PTI 'Basic Pancreatic Trypsin Inhibitor (Met 52 Oxidized)' 100.00 58 100.00 100.00 3.54e-26 EMBL CAA27062 'unnamed protein product [Bos taurus]' 100.00 89 100.00 100.00 2.03e-26 EMBL CAA27063 'unnamed protein product [Bos taurus]' 100.00 58 100.00 100.00 3.54e-26 EMBL CAA28371 'unnamed protein product [synthetic construct]' 100.00 59 100.00 100.00 2.97e-26 EMBL CAA28886 'trypsin ihibitor precursor [Bos taurus]' 100.00 92 100.00 100.00 4.78e-27 EMBL CAA37967 'aprotinin [synthetic construct]' 100.00 59 100.00 100.00 3.60e-26 GenBank AAA72535 'alkaline phosphatase/pancreatic trypsin inhibitor precursor' 100.00 79 98.28 100.00 1.24e-26 GenBank AAB25189 'major cationic kallikrein inhibitor [cattle, posterior pituitary gland, Peptide, 58 aa]' 100.00 58 100.00 100.00 3.54e-26 GenBank AAD13685 'trypsin inhibitor [Bos taurus]' 100.00 100 100.00 100.00 3.43e-27 PRF 1405218A 'aprotinin analog' 98.28 57 100.00 100.00 1.07e-25 PRF 1405218D 'aprotinin analog' 100.00 59 100.00 100.00 3.05e-26 PRF 1510193A BPTI 100.00 100 98.28 100.00 1.02e-26 PRF 681071A 'inhibitor,basic pancreatic trypsin' 100.00 58 100.00 100.00 3.54e-26 SWISS-PROT P00974 'Pancreatic trypsin inhibitor precursor (Basic protease inhibitor) (BPTI) (BPI) (Aprotinin)' 100.00 100 100.00 100.00 3.43e-27 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BPTI Cow 9913 Eukaryota Metazoa Bos taurus 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 $BPTI 'recombinant technology' E.coli Escherichia coli . . 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 $BPTI 0.75 mM . CaCl2 25 mM . NaAzide 3 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_(HA)CANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CANH _Sample_label . save_ save_(HA)CA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CA(CO)NH _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label . save_ ####################### # Sample conditions # ####################### save_BPTI_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 . n/a temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 . ppm . . indirect . . . 0.251449537 DSS H 1 . ppm 0.00 external direct cylindrical external . 1.0 DSS N 15 . ppm . . 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_BPTI_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC HNCA (HA)CANH (HA)CA(CO)NH HNCO HCACO stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $BPTI_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BPTI _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 PRO C C 177.7 . 1 2 . 2 PRO CA C 63.1 . 1 3 . 2 PRO HA H 4.42 . 1 4 . 3 ASP N N 124.0 . 1 5 . 3 ASP H H 8.74 . 1 6 . 3 ASP C C 180.1 . 1 7 . 3 ASP CA C 57.4 . 1 8 . 3 ASP HA H 4.38 . 1 9 . 4 PHE N N 117.0 . 1 10 . 4 PHE H H 7.89 . 1 11 . 4 PHE C C 177.6 . 1 12 . 4 PHE CA C 59.2 . 1 13 . 4 PHE HA H 4.70 . 1 14 . 5 CYS N N 121.7 . 1 15 . 5 CYS H H 7.51 . 1 16 . 5 CYS C C 173.4 . 1 17 . 5 CYS CA C 57.9 . 1 18 . 5 CYS HA H 4.46 . 1 19 . 6 LEU N N 114.4 . 1 20 . 6 LEU H H 7.66 . 1 21 . 6 LEU C C 178.6 . 1 22 . 6 LEU CA C 54.8 . 1 23 . 6 LEU HA H 4.61 . 1 24 . 7 GLU N N 121.0 . 1 25 . 7 GLU H H 7.59 . 1 26 . 7 GLU C C 175.0 . 1 27 . 7 GLU CA C 55.0 . 1 28 . 7 GLU HA H 4.68 . 1 29 . 8 PRO C C 174.7 . 1 30 . 8 PRO CA C 61.9 . 1 31 . 8 PRO HA H 4.74 . 1 32 . 9 PRO C C 176.1 . 1 33 . 9 PRO CA C 62.7 . 1 34 . 9 PRO HA H 3.84 . 1 35 . 10 TYR N N 123.9 . 1 36 . 10 TYR H H 7.88 . 1 37 . 10 TYR C C 175.3 . 1 38 . 10 TYR CA C 56.6 . 1 39 . 10 TYR HA H 5.03 . 1 40 . 11 THR N N 129.2 . 1 41 . 11 THR H H 9.05 . 1 42 . 11 THR C C 177.0 . 1 43 . 11 THR CA C 67.4 . 1 44 . 11 THR HA H 4.72 . 1 45 . 12 GLY N N 107.5 . 1 46 . 12 GLY H H 7.34 . 1 47 . 12 GLY CA C 46.1 . 1 48 . 13 PRO C C 179.6 . 1 49 . 13 PRO CA C 64.3 . 1 50 . 13 PRO HA H 5.10 . 1 51 . 14 CYS N N 119.1 . 1 52 . 14 CYS H H 8.56 . 1 53 . 14 CYS C C 175.4 . 1 54 . 14 CYS CA C 61.1 . 1 55 . 15 LYS N N 118.6 . 1 56 . 15 LYS H H 6.76 . 1 57 . 15 LYS C C 178.3 . 1 58 . 15 LYS CA C 58.4 . 1 59 . 15 LYS HA H 4.67 . 1 60 . 16 ALA N N 126.1 . 1 61 . 16 ALA H H 9.35 . 1 62 . 16 ALA C C 175.1 . 1 63 . 16 ALA CA C 52.8 . 1 64 . 17 ARG N N 118.9 . 1 65 . 17 ARG H H 8.55 . 1 66 . 17 ARG C C 173.3 . 1 67 . 17 ARG CA C 55.2 . 1 68 . 18 ILE N N 123.8 . 1 69 . 18 ILE H H 8.13 . 1 70 . 18 ILE C C 176.2 . 1 71 . 18 ILE CA C 60.4 . 1 72 . 18 ILE HA H 4.69 . 1 73 . 19 ILE N N 127.9 . 1 74 . 19 ILE H H 8.28 . 1 75 . 19 ILE C C 176.4 . 1 76 . 19 ILE CA C 61.7 . 1 77 . 19 ILE HA H 4.22 . 1 78 . 20 ARG N N 130.8 . 1 79 . 20 ARG H H 8.36 . 1 80 . 20 ARG C C 173.5 . 1 81 . 20 ARG CA C 52.0 . 1 82 . 20 ARG HA H 4.26 . 1 83 . 21 TYR N N 115.8 . 1 84 . 21 TYR H H 9.23 . 1 85 . 21 TYR C C 175.8 . 1 86 . 21 TYR CA C 57.5 . 1 87 . 21 TYR HA H 5.78 . 1 88 . 22 PHE N N 120.5 . 1 89 . 22 PHE H H 9.86 . 1 90 . 22 PHE C C 173.1 . 1 91 . 22 PHE CA C 55.2 . 1 92 . 22 PHE HA H 5.35 . 1 93 . 23 TYR N N 125.7 . 1 94 . 23 TYR H H 10.61 . 1 95 . 23 TYR C C 173.9 . 1 96 . 23 TYR CA C 59.9 . 1 97 . 23 TYR HA H 4.42 . 1 98 . 24 ASN N N 126.0 . 1 99 . 24 ASN H H 7.81 . 1 100 . 24 ASN C C 175.5 . 1 101 . 24 ASN CA C 50.8 . 1 102 . 24 ASN HA H 4.69 . 1 103 . 25 ALA N N 127.0 . 1 104 . 25 ALA H H 8.85 . 1 105 . 25 ALA C C 179.6 . 1 106 . 25 ALA CA C 55.0 . 1 107 . 25 ALA HA H 3.87 . 1 108 . 26 LYS N N 117.5 . 1 109 . 26 LYS H H 7.98 . 1 110 . 26 LYS C C 177.8 . 1 111 . 26 LYS CA C 58.8 . 1 112 . 26 LYS HA H 4.14 . 1 113 . 27 ALA N N 119.0 . 1 114 . 27 ALA H H 6.88 . 1 115 . 27 ALA C C 178.2 . 1 116 . 27 ALA CA C 52.0 . 1 117 . 27 ALA HA H 4.38 . 1 118 . 28 GLY N N 107.1 . 1 119 . 28 GLY H H 8.21 . 1 120 . 28 GLY C C 173.8 . 1 121 . 28 GLY CA C 46.0 . 1 122 . 29 LEU N N 115.0 . 1 123 . 29 LEU H H 6.88 . 1 124 . 29 LEU C C 175.8 . 1 125 . 29 LEU CA C 53.9 . 1 126 . 29 LEU HA H 4.85 . 1 127 . 30 CYS N N 118.2 . 1 128 . 30 CYS H H 8.44 . 1 129 . 30 CYS C C 174.0 . 1 130 . 30 CYS CA C 58.0 . 1 131 . 31 GLN N N 123.5 . 1 132 . 31 GLN H H 8.83 . 1 133 . 31 GLN C C 174.4 . 1 134 . 31 GLN CA C 54.1 . 1 135 . 32 THR N N 109.0 . 1 136 . 32 THR H H 8.13 . 1 137 . 32 THR C C 175.5 . 1 138 . 32 THR CA C 60.7 . 1 139 . 32 THR HA H 5.36 . 1 140 . 33 PHE N N 119.3 . 1 141 . 33 PHE H H 9.38 . 1 142 . 33 PHE C C 172.0 . 1 143 . 33 PHE CA C 55.7 . 1 144 . 33 PHE HA H 4.96 . 1 145 . 34 VAL N N 118.0 . 1 146 . 34 VAL H H 8.45 . 1 147 . 34 VAL C C 173.1 . 1 148 . 34 VAL CA C 63.1 . 1 149 . 34 VAL HA H 3.94 . 1 150 . 35 TYR N N 130.7 . 1 151 . 35 TYR H H 9.55 . 1 152 . 35 TYR C C 174.8 . 1 153 . 35 TYR CA C 54.7 . 1 154 . 36 GLY N N 115.7 . 1 155 . 36 GLY H H 9.02 . 1 156 . 37 GLY N N 98.3 . 1 157 . 37 GLY H H 4.40 . 1 158 . 37 GLY C C 173.3 . 1 159 . 38 CYS N N 116.0 . 1 160 . 38 CYS H H 8.05 . 1 161 . 38 CYS C C 173.8 . 1 162 . 38 CYS CA C 55.6 . 1 163 . 38 CYS HA H 4.90 . 1 164 . 39 ARG N N 113.7 . 1 165 . 39 ARG H H 9.35 . 1 166 . 39 ARG C C 174.7 . 1 167 . 39 ARG CA C 57.1 . 1 168 . 39 ARG HA H 4.03 . 1 169 . 40 ALA N N 117.9 . 1 170 . 40 ALA H H 7.40 . 1 171 . 40 ALA C C 180.4 . 1 172 . 40 ALA CA C 53.9 . 1 173 . 41 LYS N N 121.4 . 1 174 . 41 LYS H H 8.34 . 1 175 . 41 LYS C C 176.9 . 1 176 . 41 LYS CA C 55.5 . 1 177 . 41 LYS HA H 4.54 . 1 178 . 42 ARG N N 116.2 . 1 179 . 42 ARG H H 8.41 . 1 180 . 42 ARG C C 178.0 . 1 181 . 42 ARG CA C 59.0 . 1 182 . 42 ARG HA H 3.75 . 1 183 . 43 ASN N N 116.8 . 1 184 . 43 ASN H H 7.31 . 1 185 . 43 ASN C C 174.9 . 1 186 . 43 ASN CA C 51.1 . 1 187 . 44 ASN N N 121.3 . 1 188 . 44 ASN H H 6.87 . 1 189 . 44 ASN C C 174.4 . 1 190 . 44 ASN CA C 54.1 . 1 191 . 45 PHE N N 123.0 . 1 192 . 45 PHE H H 10.02 . 1 193 . 45 PHE C C 176.7 . 1 194 . 45 PHE CA C 56.3 . 1 195 . 45 PHE HA H 5.24 . 1 196 . 46 LYS N N 120.9 . 1 197 . 46 LYS H H 10.01 . 1 198 . 46 LYS C C 176.2 . 1 199 . 46 LYS CA C 58.5 . 1 200 . 46 LYS HA H 4.49 . 1 201 . 47 SER N N 109.2 . 1 202 . 47 SER H H 7.54 . 1 203 . 47 SER C C 173.6 . 1 204 . 47 SER CA C 56.4 . 1 205 . 47 SER HA H 4.61 . 1 206 . 48 ALA N N 126.0 . 1 207 . 48 ALA H H 8.23 . 1 208 . 48 ALA C C 179.7 . 1 209 . 48 ALA CA C 55.4 . 1 210 . 48 ALA HA H 3.22 . 1 211 . 49 GLU N N 118.2 . 1 212 . 49 GLU H H 8.68 . 1 213 . 49 GLU C C 179.6 . 1 214 . 49 GLU CA C 60.5 . 1 215 . 49 GLU HA H 3.94 . 1 216 . 50 ASP N N 120.7 . 1 217 . 50 ASP H H 7.92 . 1 218 . 50 ASP C C 178.0 . 1 219 . 50 ASP CA C 57.6 . 1 220 . 50 ASP HA H 4.37 . 1 221 . 51 CYS N N 120.1 . 1 222 . 51 CYS H H 7.04 . 1 223 . 51 CYS C C 175.6 . 1 224 . 51 CYS CA C 58.9 . 1 225 . 51 CYS HA H 1.79 . 1 226 . 52 MET N N 121.5 . 1 227 . 52 MET C C 180.4 . 1 228 . 52 MET CA C 56.7 . 1 229 . 52 MET HA H 4.26 . 1 230 . 53 ARG N N 121.7 . 1 231 . 53 ARG H H 8.35 . 1 232 . 53 ARG C C 178.5 . 1 233 . 53 ARG CA C 59.5 . 1 234 . 53 ARG HA H 4.06 . 1 235 . 54 THR N N 113.7 . 1 236 . 54 THR H H 7.48 . 1 237 . 54 THR C C 176.5 . 1 238 . 54 THR CA C 66.3 . 1 239 . 54 THR HA H 4.18 . 1 240 . 55 CYS N N 115.2 . 1 241 . 55 CYS H H 8.30 . 1 242 . 55 CYS C C 174.1 . 1 243 . 55 CYS CA C 54.5 . 1 244 . 55 CYS HA H 4.73 . 1 245 . 56 GLY N N 107.9 . 1 246 . 56 GLY H H 8.01 . 1 247 . 56 GLY C C 174.8 . 1 248 . 56 GLY CA C 46.7 . 1 249 . 57 GLY N N 109.5 . 1 250 . 57 GLY H H 8.26 . 1 251 . 57 GLY C C 172.6 . 1 252 . 57 GLY CA C 45.2 . 1 253 . 58 ALA N N 129.9 . 1 254 . 58 ALA H H 8.01 . 1 255 . 58 ALA CA C 54.4 . 1 stop_ save_