data_5469 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Inhibitory Specificity Change of Ovomucoid Third Domain of Silver Pheasant upon Introduction of an Engineered Cys14-Cys39 Bond ; _BMRB_accession_number 5469 _BMRB_flat_file_name bmr5469.str _Entry_type original _Submission_date 2002-07-22 _Accession_date 2002-07-23 _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 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yamazaki Toshimasa . . 4 Kojima Shuichi . . 5 Yoshida Takuya . . 6 Kyogoku Yoshimasa . . 7 Katsu Masataka . . 8 Shinohara Fumikazu . . 9 Yokosawa Hideyoshi . . 10 Miura Kin-ichiro . . 11 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 297 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-03-06 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5470 'Double mutant p14c/n39c of omsvp3.' stop_ _Original_release_date 2002-07-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Inhibitory Specificity Change of Ovomucoid Third Domain of Silver Pheasant upon Introduction of an Engineered Cys14-Cys39 Bond ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yamazaki Toshimasa . . 4 Kojima Shuichi . . 5 Yoshida Takuya . . 6 Kyogoku Yoshimasa . . 7 Katsu Masataka . . 8 Shinohara Fumikazu . . 9 Yokosawa Hideyoshi . . 10 Miura Kin-ichiro . . 11 Kobayashi Yuji . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2524 _Page_last 2534 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_omsvp3 _Saveframe_category molecular_system _Mol_system_name 'omsvp3 monomer' _Abbreviation_common omsvp3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'omsvp3 monomer' $omsvp3 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_omsvp3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ovomucoid third domain from silver pheasant' _Abbreviation_common omsvp3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 54 _Mol_residue_sequence ; AVSVDCSEYPKPACTMEYRP LCGSDNKTYGNKCNFCNAVV ESNGTLTLSHFGKC ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 3 ALA 2 4 VAL 3 5 SER 4 6 VAL 5 7 ASP 6 8 CYS 7 9 SER 8 10 GLU 9 11 TYR 10 12 PRO 11 13 LYS 12 14 PRO 13 15 ALA 14 16 CYS 15 17 THR 16 18 MET 17 19 GLU 18 20 TYR 19 21 ARG 20 22 PRO 21 23 LEU 22 24 CYS 23 25 GLY 24 26 SER 25 27 ASP 26 28 ASN 27 29 LYS 28 30 THR 29 31 TYR 30 32 GLY 31 33 ASN 32 34 LYS 33 35 CYS 34 36 ASN 35 37 PHE 36 38 CYS 37 39 ASN 38 40 ALA 39 41 VAL 40 42 VAL 41 43 GLU 42 44 SER 43 45 ASN 44 46 GLY 45 47 THR 46 48 LEU 47 49 THR 48 50 LEU 49 51 SER 50 52 HIS 51 53 PHE 52 54 GLY 53 55 LYS 54 56 CYS 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 1374 'ovomucoid third domain' 70.37 38 100.00 100.00 3.73e-14 BMRB 1375 'ovomucoid third domain' 70.37 38 100.00 100.00 3.73e-14 BMRB 4068 'turkey ovomucoid third domain' 100.00 56 98.15 100.00 1.26e-23 BMRB 42 'ovomucoid third domain' 100.00 56 98.15 100.00 1.26e-23 BMRB 4864 'Ovomucoid Third Domain from Turkey' 100.00 56 98.15 100.00 1.26e-23 BMRB 4865 'Ovomucoid Third Domain from Turkey' 100.00 56 98.15 100.00 1.26e-23 BMRB 507 'ovomucoid third domain' 100.00 56 98.15 100.00 1.26e-23 BMRB 5411 'Turkey Ovomucoid Third Domain' 94.44 51 98.04 100.00 5.98e-22 BMRB 5424 'P1-Asp Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 2.51e-21 BMRB 5425 'P1-Glu Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 1.89e-21 BMRB 5426 'P1-Gly Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 2.55e-21 BMRB 5427 'P1-Ala Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 1.29e-21 BMRB 5428 'P1-His Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 1.71e-21 BMRB 5429 'P1-Lys Turkey Ovomucoid Third Domain' 94.44 51 98.04 98.04 1.44e-21 BMRB 5448 'Turkey Ovomucoid Third Domain' 94.44 51 98.04 100.00 5.98e-22 BMRB 5518 'Ovomucoid Third Domain from Turkey' 100.00 56 98.15 100.00 1.26e-23 BMRB 5520 'Ovomucoid Third Domain from Turkey' 70.37 38 100.00 100.00 3.73e-14 PDB 1CHO ; Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 Angstroms Resolution ; 100.00 56 98.15 100.00 1.26e-23 PDB 1CSO 'Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ile18i In Complex With Sgpb' 94.44 51 98.04 100.00 6.84e-22 PDB 1CT0 'Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ser18i In Complex With Sgpb' 94.44 51 98.04 98.04 1.68e-21 PDB 1CT2 'Crystal Structure Of The Omtky3 P1 Variant Omtky3-Thr18i In Complex With Sgpb' 94.44 51 98.04 98.04 1.31e-21 PDB 1CT4 'Crystal Structure Of The Omtky3 P1 Variant Omtky3-Val18i In Complex With Sgpb' 94.44 51 98.04 100.00 8.35e-22 PDB 1DS2 'Crystal Structure Of Sgpb:omtky3-Coo-Leu18i' 94.44 51 98.04 98.04 1.66e-21 PDB 1HJA 'Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin' 94.44 51 98.04 98.04 1.44e-21 PDB 1IY5 'Solution Structure Of Wild Type Omsvp3' 100.00 54 100.00 100.00 6.72e-24 PDB 1OMT ; Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Standard Noesy Analysis) ; 100.00 56 98.15 100.00 1.26e-23 PDB 1OMU ; Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Refined Model Using Network Editing Analysis) ; 100.00 56 98.15 100.00 1.26e-23 PDB 1PPF ; X-Ray Crystal Structure Of The Complex Of Human Leukocyte Elastase (Pmn Elastase) And The Third Domain Of The Turkey Ovomucoid Inhibitor ; 100.00 56 98.15 100.00 1.26e-23 PDB 1R0R ; 1.1 Angstrom Resolution Structure Of The Complex Between The Protein Inhibitor, Omtky3, And The Serine Protease, Subtilisin Carlsberg ; 94.44 51 98.04 100.00 5.98e-22 PDB 1SGD 'Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5' 94.44 51 98.04 98.04 2.51e-21 PDB 1SGE 'Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5' 94.44 51 98.04 98.04 1.89e-21 PDB 1SGN 'Asn 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 94.44 51 98.04 98.04 2.33e-21 PDB 1SGP 'Ala 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 94.44 51 98.04 98.04 1.29e-21 PDB 1SGQ 'Gly 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 94.44 51 98.04 98.04 2.55e-21 PDB 1SGR 'Leu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 94.44 51 98.04 100.00 5.98e-22 PDB 1SGY 'Tyr 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5' 94.44 51 98.04 98.04 1.77e-21 PDB 1TUR 'Solution Structure Of Turkey Ovomucoid Third Domain As Determined From Nuclear Magnetic Resonance Data' 100.00 56 98.15 100.00 1.26e-23 PDB 1TUS ; Solution Structure Of Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain By Nuclear Magnetic Resonance And Distance Geometry Methods ; 100.00 56 98.15 100.00 1.26e-23 PDB 2GKR 'Crystal Structure Of The N-Terminally Truncated Omtky3- Del(1-5)' 94.44 51 98.04 100.00 5.98e-22 PDB 2NU0 'Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i, And Tyr18i' 94.44 51 98.04 98.04 1.12e-21 PDB 2NU1 'Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i And Tyr18i' 94.44 51 98.04 98.04 1.71e-21 PDB 2NU2 ; Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Omtky3 Variants Lys18i And Arg18i ; 94.44 51 98.04 98.04 1.38e-21 PDB 2NU3 ; Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Omtky3 Variants Lys18i And Arg18i ; 94.44 51 98.04 98.04 1.44e-21 PDB 2NU4 ; Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Omtky3 Variants Lys18i And Arg18i ; 94.44 51 98.04 98.04 1.44e-21 PDB 2OVO 'The Crystal And Molecular Structure Of The Third Domain Of Silver Pheasant Ovomucoid (Omsvp3)' 100.00 56 100.00 100.00 5.14e-24 PDB 2SGD 'Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7' 94.44 51 98.04 98.04 2.51e-21 PDB 2SGE 'Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7' 94.44 51 98.04 98.04 1.89e-21 PDB 2SGF 'Phe 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 94.44 51 98.04 98.04 1.21e-21 PDB 2SGP 'Pro 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5' 94.44 51 98.04 98.04 2.60e-21 PDB 2SGQ 'Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5' 94.44 51 98.04 98.04 9.54e-22 PDB 3SGB ; Structure Of The Complex Of Streptomyces Griseus Protease B And The Third Domain Of The Turkey Ovomucoid Inhibitor At 1.8 Angstroms Resolution ; 100.00 56 98.15 100.00 1.26e-23 PDB 3SGQ 'Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7' 94.44 51 98.04 98.04 9.54e-22 PDB 4OVO ; Refined X-Ray Crystal Structures Of The Reactive Site Modified Ovomucoid Inhibitor Third Domains From Silver Pheasant (Omsvp3(Asterisk)) And From Japanese Quail (Omjpq3(Asterisk)) ; 100.00 56 100.00 100.00 5.41e-24 PIR A31445 'ovomucoid, third domain - ruffed grouse (fragment)' 100.00 56 100.00 100.00 5.14e-24 PIR B61588 'ovomucoid (PSTI-type proteinase inhibitor), third domain - white-tailed ptarmigan' 100.00 56 100.00 100.00 5.14e-24 PIR C31438 'ovomucoid, third domain - cheer pheasant (fragment)' 100.00 56 100.00 100.00 5.14e-24 PIR E31437 'ovomucoid, third domain - silver pheasant (fragment)' 100.00 56 100.00 100.00 5.14e-24 PIR E31442 'ovomucoid, third domain - koklass pheasant (fragment)' 100.00 56 100.00 100.00 5.14e-24 SWISS-PROT P52245 Ovomucoid 100.00 56 98.15 100.00 1.26e-23 SWISS-PROT P52258 Ovomucoid 100.00 56 98.15 98.15 2.68e-23 SWISS-PROT P52261 Ovomucoid 100.00 56 98.15 98.15 1.64e-23 SWISS-PROT P52269 Ovomucoid 100.00 54 98.15 98.15 4.28e-23 SWISS-PROT P67944 Ovomucoid 100.00 56 100.00 100.00 5.14e-24 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $omsvp3 'silver pheasant' 9046 Eukaryota Metazoa Lophura nycthemera stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $omsvp3 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET22b 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 $omsvp3 4.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_NMRPIPP _Saveframe_category software _Name NMRPIPP _Version . loop_ _Task assignment 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.1 n/a temperature 298 1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H NOESY' '1H-1H TOCSY' '1H-1H DQF-COSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'omsvp3 monomer' _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 ALA HA H 4.14 . 1 2 . 1 ALA HB H 1.29 . 1 3 . 2 VAL H H 8.23 . 1 4 . 2 VAL HA H 4.20 . 1 5 . 2 VAL HB H 1.88 . 1 6 . 2 VAL HG1 H 0.74 . 2 7 . 2 VAL HG2 H 0.83 . 2 8 . 3 SER H H 8.32 . 1 9 . 3 SER HA H 4.47 . 1 10 . 3 SER HB2 H 3.77 . 1 11 . 3 SER HB3 H 3.77 . 1 12 . 4 VAL H H 8.42 . 1 13 . 4 VAL HA H 4.21 . 1 14 . 4 VAL HB H 1.89 . 1 15 . 4 VAL HG1 H 0.78 . 2 16 . 4 VAL HG2 H 0.90 . 2 17 . 5 ASP H H 8.52 . 1 18 . 5 ASP HA H 4.67 . 1 19 . 5 ASP HB2 H 2.90 . 1 20 . 5 ASP HB3 H 2.68 . 1 21 . 6 CYS H H 8.84 . 1 22 . 6 CYS HA H 5.24 . 1 23 . 6 CYS HB2 H 2.48 . 2 24 . 6 CYS HB3 H 3.27 . 2 25 . 7 SER H H 8.62 . 1 26 . 7 SER HA H 4.18 . 1 27 . 7 SER HB2 H 3.91 . 2 28 . 7 SER HB3 H 3.99 . 2 29 . 8 GLU H H 8.64 . 1 30 . 8 GLU HA H 4.22 . 1 31 . 8 GLU HB2 H 1.72 . 1 32 . 8 GLU HB3 H 1.72 . 1 33 . 8 GLU HG2 H 1.96 . 2 34 . 8 GLU HG3 H 2.22 . 2 35 . 9 TYR H H 7.37 . 1 36 . 9 TYR HA H 3.99 . 1 37 . 9 TYR HB2 H 2.79 . 1 38 . 9 TYR HB3 H 2.79 . 1 39 . 9 TYR HD1 H 7.08 . 1 40 . 9 TYR HD2 H 7.08 . 1 41 . 9 TYR HE1 H 7.04 . 1 42 . 9 TYR HE2 H 7.04 . 1 43 . 10 PRO HA H 5.15 . 1 44 . 10 PRO HB2 H 2.00 . 2 45 . 10 PRO HB3 H 2.37 . 2 46 . 10 PRO HG2 H 1.78 . 2 47 . 10 PRO HG3 H 1.90 . 2 48 . 10 PRO HD2 H 3.49 . 2 49 . 10 PRO HD3 H 3.63 . 2 50 . 11 LYS H H 9.29 . 1 51 . 11 LYS HA H 4.81 . 1 52 . 11 LYS HB2 H 1.52 . 2 53 . 11 LYS HB3 H 1.81 . 2 54 . 11 LYS HG2 H 0.86 . 2 55 . 11 LYS HG3 H 1.10 . 2 56 . 11 LYS HD2 H 1.37 . 1 57 . 11 LYS HD3 H 1.37 . 1 58 . 12 PRO HA H 4.27 . 1 59 . 12 PRO HB2 H 2.23 . 1 60 . 12 PRO HB3 H 2.23 . 1 61 . 12 PRO HG2 H 1.97 . 1 62 . 12 PRO HG3 H 1.97 . 1 63 . 12 PRO HD2 H 3.68 . 2 64 . 12 PRO HD3 H 3.74 . 2 65 . 13 ALA H H 7.41 . 1 66 . 13 ALA HA H 4.48 . 1 67 . 13 ALA HB H 1.26 . 1 68 . 14 CYS H H 8.52 . 1 69 . 14 CYS HA H 5.19 . 1 70 . 14 CYS HB2 H 2.68 . 2 71 . 14 CYS HB3 H 3.28 . 2 72 . 15 THR H H 8.18 . 1 73 . 15 THR HA H 4.47 . 1 74 . 15 THR HB H 4.54 . 1 75 . 15 THR HG2 H 1.27 . 1 76 . 16 MET H H 8.41 . 1 77 . 16 MET HA H 4.54 . 1 78 . 16 MET HB2 H 2.29 . 1 79 . 16 MET HB3 H 2.29 . 1 80 . 16 MET HG2 H 2.48 . 2 81 . 16 MET HG3 H 2.67 . 2 82 . 17 GLU H H 8.13 . 1 83 . 17 GLU HA H 4.08 . 1 84 . 17 GLU HB2 H 1.94 . 1 85 . 17 GLU HB3 H 1.94 . 1 86 . 17 GLU HG2 H 2.18 . 2 87 . 17 GLU HG3 H 2.29 . 2 88 . 18 TYR H H 8.87 . 1 89 . 18 TYR HA H 4.97 . 1 90 . 18 TYR HB2 H 2.86 . 1 91 . 18 TYR HB3 H 3.02 . 1 92 . 18 TYR HD1 H 7.19 . 1 93 . 18 TYR HD2 H 7.19 . 1 94 . 18 TYR HE1 H 6.74 . 1 95 . 18 TYR HE2 H 6.74 . 1 96 . 19 ARG H H 8.81 . 1 97 . 19 ARG HA H 4.37 . 1 98 . 19 ARG HB2 H 1.67 . 1 99 . 19 ARG HB3 H 1.67 . 1 100 . 19 ARG HG2 H 1.49 . 1 101 . 19 ARG HG3 H 1.49 . 1 102 . 19 ARG HD2 H 3.12 . 2 103 . 19 ARG HD3 H 3.21 . 2 104 . 19 ARG HE H 7.16 . 1 105 . 20 PRO HA H 4.44 . 1 106 . 20 PRO HB2 H 1.58 . 1 107 . 20 PRO HB3 H 1.58 . 1 108 . 20 PRO HG2 H 1.27 . 1 109 . 20 PRO HG3 H 1.27 . 1 110 . 20 PRO HD2 H 3.29 . 1 111 . 20 PRO HD3 H 3.29 . 1 112 . 21 LEU H H 8.42 . 1 113 . 21 LEU HA H 4.21 . 1 114 . 21 LEU HB2 H 0.91 . 1 115 . 21 LEU HB3 H 0.91 . 1 116 . 21 LEU HG H 1.33 . 1 117 . 21 LEU HD1 H 0.34 . 2 118 . 21 LEU HD2 H 0.42 . 2 119 . 22 CYS H H 8.08 . 1 120 . 22 CYS HA H 5.15 . 1 121 . 22 CYS HB2 H 1.26 . 2 122 . 22 CYS HB3 H 2.30 . 2 123 . 23 GLY H H 9.31 . 1 124 . 23 GLY HA2 H 4.44 . 2 125 . 23 GLY HA3 H 4.63 . 2 126 . 24 SER H H 9.29 . 1 127 . 24 SER HA H 4.08 . 1 128 . 24 SER HB2 H 3.76 . 1 129 . 24 SER HB3 H 3.76 . 1 130 . 25 ASP H H 8.35 . 1 131 . 25 ASP HA H 4.36 . 1 132 . 25 ASP HB2 H 2.93 . 1 133 . 25 ASP HB3 H 2.50 . 1 134 . 26 ASN H H 8.56 . 1 135 . 26 ASN HA H 4.32 . 1 136 . 26 ASN HB2 H 3.08 . 1 137 . 26 ASN HB3 H 2.74 . 1 138 . 26 ASN HD21 H 6.77 . 2 139 . 26 ASN HD22 H 7.45 . 2 140 . 27 LYS H H 7.74 . 1 141 . 27 LYS HA H 4.32 . 1 142 . 27 LYS HB2 H 1.36 . 2 143 . 27 LYS HB3 H 1.60 . 2 144 . 27 LYS HG2 H 0.76 . 2 145 . 27 LYS HG3 H 1.06 . 2 146 . 27 LYS HD2 H 1.45 . 1 147 . 27 LYS HD3 H 1.45 . 1 148 . 27 LYS HE2 H 2.76 . 1 149 . 27 LYS HE3 H 2.76 . 1 150 . 27 LYS HZ H 7.38 . 1 151 . 28 THR H H 8.19 . 1 152 . 28 THR HA H 4.73 . 1 153 . 28 THR HB H 3.94 . 1 154 . 28 THR HG2 H 1.08 . 1 155 . 29 TYR H H 9.64 . 1 156 . 29 TYR HA H 4.43 . 1 157 . 29 TYR HB2 H 2.71 . 1 158 . 29 TYR HB3 H 2.81 . 1 159 . 29 TYR HD1 H 6.97 . 1 160 . 29 TYR HD2 H 6.97 . 1 161 . 29 TYR HE1 H 6.73 . 1 162 . 29 TYR HE2 H 6.73 . 1 163 . 30 GLY H H 9.12 . 1 164 . 30 GLY HA2 H 3.60 . 2 165 . 30 GLY HA3 H 4.04 . 2 166 . 31 ASN H H 7.34 . 1 167 . 31 ASN HA H 4.76 . 1 168 . 31 ASN HB2 H 3.06 . 2 169 . 31 ASN HB3 H 3.58 . 2 170 . 31 ASN HD21 H 6.29 . 2 171 . 31 ASN HD22 H 7.98 . 2 172 . 32 LYS H H 8.85 . 1 173 . 32 LYS HA H 3.78 . 1 174 . 32 LYS HB2 H 1.78 . 2 175 . 32 LYS HB3 H 1.88 . 2 176 . 32 LYS HG2 H 1.29 . 2 177 . 32 LYS HG3 H 1.36 . 2 178 . 32 LYS HD2 H 1.72 . 1 179 . 32 LYS HD3 H 1.72 . 1 180 . 32 LYS HE2 H 2.96 . 2 181 . 32 LYS HE3 H 3.03 . 2 182 . 33 CYS H H 8.20 . 1 183 . 33 CYS HA H 4.45 . 1 184 . 33 CYS HB2 H 3.18 . 1 185 . 33 CYS HB3 H 3.37 . 1 186 . 34 ASN H H 8.31 . 1 187 . 34 ASN HA H 4.47 . 1 188 . 34 ASN HB2 H 2.76 . 2 189 . 34 ASN HB3 H 3.12 . 2 190 . 34 ASN HD21 H 7.04 . 2 191 . 34 ASN HD22 H 7.52 . 2 192 . 35 PHE H H 8.32 . 1 193 . 35 PHE HA H 3.43 . 1 194 . 35 PHE HB2 H 2.68 . 1 195 . 35 PHE HB3 H 2.74 . 1 196 . 35 PHE HD1 H 6.48 . 1 197 . 35 PHE HD2 H 6.48 . 1 198 . 35 PHE HE1 H 6.74 . 1 199 . 35 PHE HE2 H 6.74 . 1 200 . 36 CYS H H 9.13 . 1 201 . 36 CYS HA H 3.90 . 1 202 . 36 CYS HB2 H 1.34 . 1 203 . 36 CYS HB3 H 1.73 . 1 204 . 37 ASN H H 8.07 . 1 205 . 37 ASN HA H 4.61 . 1 206 . 37 ASN HB2 H 2.90 . 1 207 . 37 ASN HB3 H 2.70 . 1 208 . 37 ASN HD21 H 6.74 . 2 209 . 37 ASN HD22 H 7.44 . 2 210 . 38 ALA H H 7.15 . 1 211 . 38 ALA HA H 4.08 . 1 212 . 38 ALA HB H 1.21 . 1 213 . 39 VAL H H 8.50 . 1 214 . 39 VAL HA H 3.09 . 1 215 . 39 VAL HB H 1.98 . 1 216 . 39 VAL HG1 H -0.09 . 2 217 . 39 VAL HG2 H 0.65 . 2 218 . 40 VAL H H 7.98 . 1 219 . 40 VAL HA H 3.84 . 1 220 . 40 VAL HB H 2.22 . 1 221 . 40 VAL HG1 H 0.92 . 2 222 . 40 VAL HG2 H 0.96 . 2 223 . 41 GLU H H 7.56 . 1 224 . 41 GLU HA H 4.26 . 1 225 . 41 GLU HB2 H 2.01 . 2 226 . 41 GLU HB3 H 2.16 . 2 227 . 41 GLU HG2 H 2.50 . 1 228 . 41 GLU HG3 H 2.50 . 1 229 . 42 SER H H 7.73 . 1 230 . 42 SER HA H 4.44 . 1 231 . 42 SER HB2 H 3.90 . 2 232 . 42 SER HB3 H 4.14 . 2 233 . 43 ASN H H 8.43 . 1 234 . 43 ASN HA H 4.40 . 1 235 . 43 ASN HB2 H 2.78 . 2 236 . 43 ASN HB3 H 3.08 . 2 237 . 43 ASN HD21 H 6.76 . 2 238 . 43 ASN HD22 H 7.50 . 2 239 . 44 GLY H H 8.04 . 1 240 . 44 GLY HA2 H 3.51 . 2 241 . 44 GLY HA3 H 4.02 . 2 242 . 45 THR H H 7.51 . 1 243 . 45 THR HA H 4.14 . 1 244 . 45 THR HB H 4.18 . 1 245 . 45 THR HG2 H 1.19 . 1 246 . 46 LEU H H 7.57 . 1 247 . 46 LEU HA H 4.20 . 1 248 . 46 LEU HB2 H 1.44 . 1 249 . 46 LEU HB3 H 1.44 . 1 250 . 46 LEU HG H 1.07 . 1 251 . 46 LEU HD1 H 0.21 . 2 252 . 46 LEU HD2 H 1.16 . 2 253 . 47 THR H H 8.49 . 1 254 . 47 THR HA H 4.60 . 1 255 . 47 THR HB H 4.26 . 1 256 . 47 THR HG2 H 1.06 . 1 257 . 48 LEU H H 8.74 . 1 258 . 48 LEU HA H 4.03 . 1 259 . 48 LEU HB2 H 0.89 . 1 260 . 48 LEU HB3 H 1.76 . 1 261 . 48 LEU HG H 0.56 . 1 262 . 48 LEU HD1 H -0.09 . 2 263 . 48 LEU HD2 H -0.20 . 2 264 . 49 SER H H 8.76 . 1 265 . 49 SER HA H 4.43 . 1 266 . 49 SER HB2 H 3.34 . 2 267 . 49 SER HB3 H 3.49 . 2 268 . 50 HIS H H 7.17 . 1 269 . 50 HIS HA H 4.44 . 1 270 . 50 HIS HB2 H 3.22 . 2 271 . 50 HIS HB3 H 3.71 . 2 272 . 50 HIS HD2 H 7.16 . 1 273 . 50 HIS HE1 H 8.73 . 1 274 . 51 PHE H H 9.07 . 1 275 . 51 PHE HA H 4.25 . 1 276 . 51 PHE HB2 H 2.95 . 1 277 . 51 PHE HB3 H 3.16 . 1 278 . 51 PHE HD1 H 7.19 . 1 279 . 51 PHE HD2 H 7.19 . 1 280 . 51 PHE HE1 H 7.11 . 1 281 . 51 PHE HE2 H 7.11 . 1 282 . 52 GLY H H 8.19 . 1 283 . 52 GLY HA2 H 3.50 . 2 284 . 52 GLY HA3 H 4.56 . 2 285 . 53 LYS H H 7.91 . 1 286 . 53 LYS HA H 3.97 . 1 287 . 53 LYS HB2 H 1.67 . 2 288 . 53 LYS HB3 H 1.83 . 2 289 . 53 LYS HG2 H 1.40 . 2 290 . 53 LYS HG3 H 1.47 . 2 291 . 53 LYS HE2 H 3.00 . 1 292 . 53 LYS HE3 H 3.00 . 1 293 . 53 LYS HZ H 7.48 . 1 294 . 54 CYS H H 8.22 . 1 295 . 54 CYS HA H 4.31 . 1 296 . 54 CYS HB2 H 2.44 . 2 297 . 54 CYS HB3 H 3.08 . 2 stop_ save_