data_4068 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0 ; _BMRB_accession_number 4068 _BMRB_flat_file_name bmr4068.str _Entry_type original _Submission_date 1997-10-29 _Accession_date 1997-10-30 _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 Choe Soheui . . 2 Dzakula Zeljko . . 3 Kuloglu E. Sonay . 4 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 278 "13C chemical shifts" 191 "15N chemical shifts" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-05-01 original author . stop_ _Original_release_date 1998-05-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Choe, S., Dzakula, Z., Kuloglu, E. S., and Markley, J. L., "Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0," J. Biomol. NMR, in press (1998). ; _Citation_title 'Assignment of 1H, 13C, and IN Signals of Turkey Ovomucoid Third Domain at pH 2.0' _Citation_status 'in press' _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 Choe Soheui . . 2 Dzakula Zeljko . . 3 Kuloglu E. Sonay . 4 Markley John L. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 1998 _Details . loop_ _Keyword 'Donovan transition' 'NMR assignments' 'Proteinase inhibitor' 'Turkey Ovomucoid' stop_ save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name 'turkey ovomucoid third domain' _Abbreviation_common OMTKY3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OMTKY3 $OMTKY3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; Ovomucoid third domains have potent inhibitory activity toward serine proteinases ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OMTKY3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'turkey ovomucoid third domain' _Abbreviation_common OMTKY3 _Molecular_mass 6000 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 ALA 3 ALA 4 VAL 5 SER 6 VAL 7 ASP 8 CYS 9 SER 10 GLU 11 TYR 12 PRO 13 LYS 14 PRO 15 ALA 16 CYS 17 THR 18 LEU 19 GLU 20 TYR 21 ARG 22 PRO 23 LEU 24 CYS 25 GLY 26 SER 27 ASP 28 ASN 29 LYS 30 THR 31 TYR 32 GLY 33 ASN 34 LYS 35 CYS 36 ASN 37 PHE 38 CYS 39 ASN 40 ALA 41 VAL 42 VAL 43 GLU 44 SER 45 ASN 46 GLY 47 THR 48 LEU 49 THR 50 LEU 51 SER 52 HIS 53 PHE 54 GLY 55 LYS 56 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 1374 "ovomucoid third domain" 67.86 38 100.00 100.00 3.08e-18 BMRB 1375 "ovomucoid third domain" 67.86 38 100.00 100.00 3.08e-18 BMRB 42 "ovomucoid third domain" 100.00 56 100.00 100.00 7.23e-32 PDB 1CHO "Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 " 100.00 56 100.00 100.00 7.23e-32 PDB 1CSO "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ile18i In Complex With Sgpb" 91.07 51 98.04 100.00 3.07e-28 PDB 1CT0 "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ser18i In Complex With Sgpb" 91.07 51 98.04 98.04 1.33e-27 PDB 1CT2 "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Thr18i In Complex With Sgpb" 91.07 51 98.04 98.04 9.48e-28 PDB 1CT4 "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Val18i In Complex With Sgpb" 91.07 51 98.04 100.00 4.29e-28 PDB 1DS2 "Crystal Structure Of Sgpb:omtky3-Coo-Leu18i" 91.07 51 98.04 98.04 1.11e-27 PDB 1HJA "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" 91.07 51 98.04 98.04 1.36e-27 PDB 1IY5 "Solution Structure Of Wild Type Omsvp3" 96.43 54 98.15 100.00 2.30e-30 PDB 1M8B "Solution Structure Of The C State Of Turkey Ovomucoid At Ph 2.5" 100.00 56 98.21 98.21 8.59e-31 PDB 1M8C "Solution Structure Of The T State Of Turkey Ovomucoid At Ph 2.5" 100.00 56 98.21 98.21 8.59e-31 PDB 1OMT "Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Standard Noesy Analysi" 100.00 56 100.00 100.00 7.23e-32 PDB 1OMU "Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Refined Model Using Ne" 100.00 56 100.00 100.00 7.23e-32 PDB 1PPF "X-Ray Crystal Structure Of The Complex Of Human Leukocyte Elastase (Pmn Elastase) And The Third Domain Of The Turkey Ovomucoid " 100.00 56 100.00 100.00 7.23e-32 PDB 1R0R "1.1 Angstrom Resolution Structure Of The Complex Between The Protein Inhibitor, Omtky3, And The Serine Protease, Subtilisin Car" 91.07 51 100.00 100.00 1.71e-28 PDB 1SGD "Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" 91.07 51 98.04 98.04 2.16e-27 PDB 1SGE "Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" 91.07 51 98.04 98.04 1.59e-27 PDB 1SGN "Asn 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" 91.07 51 98.04 98.04 2.38e-27 PDB 1SGP "Ala 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" 91.07 51 98.04 98.04 9.07e-28 PDB 1SGQ "Gly 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" 91.07 51 98.04 98.04 2.46e-27 PDB 1SGR "Leu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" 91.07 51 100.00 100.00 1.71e-28 PDB 1SGY "Tyr 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" 91.07 51 98.04 98.04 1.10e-27 PDB 1TUR "Solution Structure Of Turkey Ovomucoid Third Domain As Determined From Nuclear Magnetic Resonance Data" 100.00 56 100.00 100.00 7.23e-32 PDB 1TUS "Solution Structure Of Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain By Nuclear Magnetic Resonance And Distance Geometr" 100.00 56 100.00 100.00 7.23e-32 PDB 2GKR "Crystal Structure Of The N-Terminally Truncated Omtky3- Del(1-5)" 91.07 51 100.00 100.00 1.71e-28 PDB 2GKT "Crystal Structure Of The P14'-Ala32 Variant Of The N- Terminally Truncated Omtky3-Del(1-5)" 91.07 51 98.04 98.04 6.84e-28 PDB 2GKV "Crystal Structure Of The Sgpb:p14'-Ala32 Omtky3-Del(1-5) Complex" 91.07 51 98.04 98.04 6.84e-28 PDB 2NU0 "Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i, And Tyr18i" 91.07 51 98.04 98.04 6.77e-28 PDB 2NU1 "Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i And Tyr18i" 91.07 51 98.04 98.04 1.54e-27 PDB 2NU2 "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" 91.07 51 98.04 98.04 1.04e-27 PDB 2NU3 "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" 91.07 51 98.04 98.04 1.36e-27 PDB 2NU4 "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" 91.07 51 98.04 98.04 1.36e-27 PDB 2OVO "The Crystal And Molecular Structure Of The Third Domain Of Silver Pheasant Ovomucoid (Omsvp3)" 100.00 56 98.21 100.00 1.00e-31 PDB 2SGD "Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" 91.07 51 98.04 98.04 2.16e-27 PDB 2SGE "Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" 91.07 51 98.04 98.04 1.59e-27 PDB 2SGF "Phe 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" 91.07 51 98.04 98.04 5.75e-28 PDB 2SGP "Pro 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" 91.07 51 98.04 98.04 2.05e-27 PDB 2SGQ "Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" 91.07 51 98.04 98.04 8.88e-28 PDB 3SGB "Structure Of The Complex Of Streptomyces Griseus Protease B And The Third Domain Of The Turkey Ovomucoid Inhibitor At 1.8 Angst" 100.00 56 100.00 100.00 7.23e-32 PDB 3SGQ "Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" 91.07 51 98.04 98.04 8.88e-28 PDB 4OVO "Refined X-Ray Crystal Structures Of The Reactive Site Modified Ovomucoid Inhibitor Third Domains From Silver Pheasant (Omsvp3(A" 98.21 56 98.18 100.00 4.94e-31 PIR A31445 "ovomucoid, third domain - ruffed grouse (fragment) [Bonasa umbellus]" 100.00 56 98.21 100.00 1.00e-31 PIR B61588 "ovomucoid (PSTI-type proteinase inhibitor), third domain - white-tailed ptarmigan [Lagopus leucura]" 100.00 56 98.21 100.00 1.00e-31 PIR C31438 "ovomucoid, third domain - cheer pheasant (fragment) [Catreus wallichii]" 100.00 56 98.21 100.00 1.00e-31 PIR E31437 "ovomucoid, third domain - silver pheasant (fragment) [Lophura nycthemera]" 100.00 56 98.21 100.00 1.00e-31 PIR E31442 "ovomucoid, third domain - koklass pheasant (fragment) [Pucrasia macrolopha]" 100.00 56 98.21 100.00 1.00e-31 SP P05609 "RecName: Full=Ovomucoid" 100.00 56 98.21 100.00 2.84e-31 SP P52245 "RecName: Full=Ovomucoid" 100.00 56 100.00 100.00 7.23e-32 SP P52263 "RecName: Full=Ovomucoid" 96.43 54 98.15 100.00 5.92e-30 SP P67944 "RecName: Full=Ovomucoid" 100.00 56 98.21 100.00 1.00e-31 SP P67945 "RecName: Full=Ovomucoid" 100.00 56 98.21 100.00 1.00e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $OMTKY3 turkey 9103 Eukaryota Metazoa Meleagris gallapavo stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $OMTKY3 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)/pLysS plasmid PTNOM3 ; native (OMTK3 was oveproduced as a fusion protein with Staphylococcal nuclease (SNase) in E. coli strain BL21(DE3)/pLysS transformed with PTNOM3 plasmid by using the T7 promoter/T7 polymerase expression system (Hinck et al., Protein Engineering 6, 221-227 (1993). IPTG was used to induce expression of the fusion protein.) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $OMTKY3 . mM 2 3 . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $OMTKY3 . mM 2 3 [U-15N] H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $OMTKY3 . mM 2 3 [U-15N;13C] H2O 90 % . . . D2O 10 % . . . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label . loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $OMTKY3 10 mg/L SDS-PAGE $OMTKY3 8.5 mg/L SDS-PAGE stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Molecular Simulations, Inc' 'San Diego, CA' . stop_ loop_ _Task 'NMR data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX-500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX-600 _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 methyl ppm 0.00 . indirect . . . 0.251449530 DSS H 1 methyl ppm 0.00 internal direct . . . 1.000000000 DSS N 15 methyl ppm 0.00 . 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_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_one stop_ loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name OMTKY3 _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 ALA H H 8.66 . 1 2 . 2 ALA HA H 4.38 . 1 3 . 2 ALA HB H 1.39 . 1 4 . 2 ALA C C 176.93 . 1 5 . 2 ALA CA C 52.33 . 1 6 . 2 ALA CB C 19.34 . 1 7 . 3 ALA H H 8.42 . 1 8 . 3 ALA HA H 4.34 . 1 9 . 3 ALA HB H 1.39 . 1 10 . 3 ALA C C 177.64 . 1 11 . 3 ALA CA C 52.45 . 1 12 . 3 ALA CB C 19.41 . 1 13 . 3 ALA N N 124.54 . 1 14 . 4 VAL H H 8.16 . 1 15 . 4 VAL HA H 4.23 . 1 16 . 4 VAL HB H 2.03 . 1 17 . 4 VAL HG1 H 0.89 . 2 18 . 4 VAL HG2 H 0.9 . 2 19 . 4 VAL C C 176.31 . 1 20 . 4 VAL CA C 61.76 . 1 21 . 4 VAL CB C 33.15 . 1 22 . 4 VAL CG1 C 21.05 . 2 23 . 4 VAL N N 118.91 . 1 24 . 5 SER H H 8.3 . 1 25 . 5 SER HA H 4.56 . 1 26 . 5 SER HB2 H 3.87 . 2 27 . 5 SER C C 173.4 . 1 28 . 5 SER CA C 64.73 . 1 29 . 5 SER CB C 57.82 . 1 30 . 5 SER N N 118.01 . 1 31 . 6 VAL H H 8.37 . 1 32 . 6 VAL HA H 4.34 . 1 33 . 6 VAL HB H 1.97 . 1 34 . 6 VAL HG1 H 0.92 . 2 35 . 6 VAL HG2 H 0.81 . 2 36 . 6 VAL C C 174.2 . 1 37 . 6 VAL CA C 61.26 . 1 38 . 6 VAL CB C 34.23 . 1 39 . 6 VAL CG1 C 20.5 . 2 40 . 6 VAL CG2 C 21.59 . 2 41 . 6 VAL N N 120.24 . 1 42 . 7 ASP H H 8.71 . 1 43 . 7 ASP HA H 4.83 . 1 44 . 7 ASP HB2 H 2.88 . 2 45 . 7 ASP HB3 H 3.19 . 2 46 . 7 ASP C C 176.18 . 1 47 . 7 ASP CA C 52.35 . 1 48 . 7 ASP CB C 38.27 . 1 49 . 7 ASP N N 123.31 . 1 50 . 8 CYS H H 9.02 . 1 51 . 8 CYS HA H 5.25 . 1 52 . 8 CYS HB2 H 3.29 . 1 53 . 8 CYS HB3 H 2.58 . 1 54 . 8 CYS C C 175.24 . 1 55 . 8 CYS CA C 51.85 . 1 56 . 8 CYS CB C 33.94 . 1 57 . 8 CYS N N 125.5 . 1 58 . 9 SER H H 8.32 . 1 59 . 9 SER HA H 4.35 . 1 60 . 9 SER HB2 H 4.03 . 2 61 . 9 SER C C 175.28 . 1 62 . 9 SER CA C 61.67 . 1 63 . 9 SER CB C 34.4 . 1 64 . 9 SER N N 118.04 . 1 65 . 10 GLU H H 8.69 . 1 66 . 10 GLU HA H 4.29 . 1 67 . 10 GLU HB2 H 1.87 . 1 68 . 10 GLU HB3 H 2.07 . 1 69 . 10 GLU HG2 H 2.4 . 2 70 . 10 GLU C C 173.79 . 1 71 . 10 GLU CA C 56.19 . 1 72 . 10 GLU CB C 28.95 . 1 73 . 10 GLU CG C 33.31 . 1 74 . 10 GLU N N 118.4 . 1 75 . 11 TYR H H 7.52 . 1 76 . 11 TYR HA H 4.16 . 1 77 . 11 TYR HB2 H 2.85 . 2 78 . 11 TYR HB3 H 2.8 . 2 79 . 11 TYR HD1 H 7.15 . 2 80 . 11 TYR HD2 H 7.1 . 2 81 . 11 TYR CA C 57.83 . 1 82 . 11 TYR CB C 38.48 . 1 83 . 11 TYR N N 118.61 . 1 84 . 12 PRO HA H 5.19 . 1 85 . 12 PRO HB2 H 2.44 . 2 86 . 12 PRO HB3 H 2.07 . 2 87 . 12 PRO HD2 H 3.53 . 2 88 . 12 PRO HD3 H 3.674 . 2 89 . 12 PRO C C 175.75 . 1 90 . 12 PRO CA C 62.22 . 1 91 . 12 PRO CB C 36.3 . 1 92 . 13 LYS H H 9.36 . 1 93 . 13 LYS HA H 4.86 . 1 94 . 13 LYS HB2 H 1.9 . 2 95 . 13 LYS HB3 H 1.59 . 2 96 . 13 LYS HG2 H 1.19 . 2 97 . 13 LYS HG3 H 0.98 . 2 98 . 13 LYS HD2 H 1.6 . 2 99 . 13 LYS HD3 H 1.44 . 2 100 . 13 LYS HE2 H 2.59 . 2 101 . 13 LYS HE3 H 2.44 . 2 102 . 13 LYS CA C 53.71 . 1 103 . 13 LYS CB C 35.21 . 1 104 . 13 LYS CG C 25.41 . 1 105 . 13 LYS CD C 29.22 . 1 106 . 13 LYS CE C 42.3 . 1 107 . 13 LYS N N 121.45 . 1 108 . 14 PRO HA H 4.35 . 1 109 . 14 PRO HB2 H 2.04 . 2 110 . 14 PRO HB3 H 2.26 . 2 111 . 14 PRO HG2 H 2.1 . 2 112 . 14 PRO HG3 H 2.04 . 2 113 . 14 PRO HD2 H 3.76 . 2 114 . 14 PRO HD3 H 3.8 . 2 115 . 14 PRO C C 175.69 . 1 116 . 14 PRO CA C 64.09 . 1 117 . 14 PRO CB C 32.3 . 1 118 . 14 PRO CG C 27.04 . 1 119 . 14 PRO CD C 51.02 . 1 120 . 15 ALA H H 7.51 . 1 121 . 15 ALA HA H 4.57 . 1 122 . 15 ALA HB H 1.33 . 1 123 . 15 ALA C C 175.96 . 1 124 . 15 ALA CA C 51.31 . 1 125 . 15 ALA CB C 21.09 . 1 126 . 15 ALA N N 118.88 . 1 127 . 16 CYS H H 8.59 . 1 128 . 16 CYS HA H 5.25 . 1 129 . 16 CYS HB2 H 2.76 . 2 130 . 16 CYS HB3 H 3.35 . 2 131 . 16 CYS C C 175.46 . 1 132 . 16 CYS CA C 52.1 . 1 133 . 16 CYS CB C 40.12 . 1 134 . 16 CYS N N 118.53 . 1 135 . 17 THR H H 8.39 . 1 136 . 17 THR HA H 4.39 . 1 137 . 17 THR HB H 4.55 . 1 138 . 17 THR HG2 H 1.37 . 1 139 . 17 THR C C 176.94 . 1 140 . 17 THR CA C 61.59 . 1 141 . 17 THR CB C 70.06 . 1 142 . 17 THR CG2 C 21.59 . 1 143 . 17 THR N N 113.72 . 1 144 . 18 LEU H H 8.4 . 1 145 . 18 LEU HA H 4.42 . 1 146 . 18 LEU HB2 H 1.79 . 2 147 . 18 LEU HB3 H 1.84 . 2 148 . 18 LEU HG H 1.66 . 1 149 . 18 LEU HD1 H 0.94 . 2 150 . 18 LEU HD2 H 0.9 . 2 151 . 18 LEU C C 177.38 . 1 152 . 18 LEU CA C 54.65 . 1 153 . 18 LEU CB C 41.23 . 1 154 . 18 LEU CG C 27.04 . 1 155 . 18 LEU CD1 C 27.04 . 2 156 . 18 LEU CD2 C 23.5 . 2 157 . 18 LEU N N 120.45 . 1 158 . 19 GLU H H 7.67 . 1 159 . 19 GLU HA H 4.14 . 1 160 . 19 GLU HB2 H 2.05 . 2 161 . 19 GLU HB3 H 1.98 . 2 162 . 19 GLU HG2 H 2.5 . 2 163 . 19 GLU C C 175.41 . 1 164 . 19 GLU CA C 57.00 . 1 165 . 19 GLU CB C 28.65 . 1 166 . 19 GLU CG C 31.94 . 1 167 . 19 GLU N N 120.78 . 1 168 . 20 TYR H H 8.95 . 1 169 . 20 TYR HA H 5.03 . 1 170 . 20 TYR HB2 H 3.12 . 1 171 . 20 TYR HB3 H 2.95 . 1 172 . 20 TYR HD1 H 7.28 . 2 173 . 20 TYR HE1 H 7.18 . 2 174 . 20 TYR C C 174.92 . 1 175 . 20 TYR CA C 57.57 . 1 176 . 20 TYR CB C 38.78 . 1 177 . 20 TYR N N 128.17 . 1 178 . 21 ARG H H 8.91 . 1 179 . 21 ARG HA H 4.46 . 1 180 . 21 ARG HB2 H 1.79 . 2 181 . 21 ARG HG2 H 1.59 . 2 182 . 21 ARG HD2 H 3.28 . 2 183 . 21 ARG HD3 H 3.27 . 2 184 . 21 ARG HE H 7.18 . 1 185 . 21 ARG CA C 58.11 . 1 186 . 21 ARG CB C 31.13 . 1 187 . 21 ARG CG C 27.31 . 1 188 . 21 ARG CD C 43.66 . 1 189 . 21 ARG N N 118.6 . 1 190 . 22 PRO HA H 4.5 . 1 191 . 22 PRO HB2 H 1.84 . 2 192 . 22 PRO HB3 H 1.68 . 2 193 . 22 PRO HG3 H 1.78 . 2 194 . 22 PRO HD2 H 3.56 . 2 195 . 22 PRO HD3 H 3.38 . 2 196 . 22 PRO C C 176.7 . 1 197 . 22 PRO CA C 63.12 . 1 198 . 22 PRO CB C 27.59 . 1 199 . 22 PRO CD C 49.65 . 1 200 . 23 LEU H H 8.5 . 1 201 . 23 LEU HA H 4.31 . 1 202 . 23 LEU HB2 H 1.4 . 2 203 . 23 LEU HG H 0.98 . 1 204 . 23 LEU HD1 H 0.49 . 2 205 . 23 LEU HD2 H 0.42 . 2 206 . 23 LEU C C 173.9 . 1 207 . 23 LEU CA C 55.13 . 1 208 . 23 LEU CB C 27.31 . 1 209 . 23 LEU CG C 45.3 . 1 210 . 23 LEU CD1 C 25.68 . 2 211 . 23 LEU CD2 C 26.22 . 2 212 . 23 LEU N N 119.1 . 1 213 . 24 CYS H H 8.21 . 1 214 . 24 CYS HA H 5.23 . 1 215 . 24 CYS HB2 H 1.37 . 1 216 . 24 CYS HB3 H 2.41 . 1 217 . 24 CYS C C 175.6 . 1 218 . 24 CYS CA C 54.39 . 1 219 . 24 CYS CB C 38.75 . 1 220 . 24 CYS N N 120.2 . 1 221 . 25 GLY H H 9.3 . 1 222 . 25 GLY HA2 H 4.3 . 2 223 . 25 GLY HA3 H 4.85 . 2 224 . 25 GLY C C 174.4 . 1 225 . 25 GLY CA C 45.27 . 1 226 . 25 GLY N N 115.13 . 1 227 . 26 SER H H 9.41 . 1 228 . 26 SER HA H 4.2 . 1 229 . 26 SER HB2 H 3.87 . 1 230 . 26 SER HB3 H 4.12 . 1 231 . 26 SER C C 173.88 . 1 232 . 26 SER CA C 45.43 . 1 233 . 26 SER N N 118.00 . 1 234 . 27 ASP H H 7.84 . 1 235 . 27 ASP HA H 4.65 . 1 236 . 27 ASP HB2 H 3.32 . 2 237 . 27 ASP HB3 H 2.87 . 2 238 . 27 ASP C C 174.94 . 1 239 . 27 ASP CA C 52.31 . 1 240 . 27 ASP CB C 37.89 . 1 241 . 27 ASP N N 118.00 . 1 242 . 28 ASN H H 8.69 . 1 243 . 28 ASN HA H 4.42 . 1 244 . 28 ASN HB2 H 2.79 . 1 245 . 28 ASN HB3 H 3.15 . 1 246 . 28 ASN HD21 H 7.56 . 2 247 . 28 ASN HD22 H 6.83 . 2 248 . 28 ASN C C 173.64 . 1 249 . 28 ASN CA C 54.9 . 1 250 . 28 ASN CB C 37.51 . 1 251 . 28 ASN N N 116.03 . 1 252 . 28 ASN ND2 N 109.313 . 1 253 . 29 LYS H H 7.21 . 1 254 . 29 LYS HA H 4.46 . 1 255 . 29 LYS HB2 H 1.39 . 2 256 . 29 LYS HB3 H 1.546 . 2 257 . 29 LYS HG2 H 1.16 . 2 258 . 29 LYS HG3 H 0.89 . 2 259 . 29 LYS HD2 H 1.51 . 2 260 . 29 LYS HE2 H 2.87 . 2 261 . 29 LYS C C 175.94 . 1 262 . 29 LYS CA C 56.05 . 1 263 . 29 LYS CB C 34.12 . 1 264 . 29 LYS CG C 25.13 . 1 265 . 29 LYS CD C 28.95 . 1 266 . 29 LYS CE C 42.57 . 1 267 . 29 LYS N N 116.95 . 1 268 . 30 THR H H 8.42 . 1 269 . 30 THR HA H 4.81 . 1 270 . 30 THR HB H 4.02 . 1 271 . 30 THR HG2 H 1.19 . 1 272 . 30 THR C C 174.67 . 1 273 . 30 THR CA C 62.83 . 1 274 . 30 THR N N 122.17 . 1 275 . 31 TYR H H 9.67 . 1 276 . 31 TYR HA H 4.57 . 1 277 . 31 TYR HB2 H 2.77 . 2 278 . 31 TYR HB3 H 2.96 . 2 279 . 31 TYR HD1 H 7.1 . 2 280 . 31 TYR C C 176.82 . 1 281 . 31 TYR CA C 58.19 . 1 282 . 31 TYR CB C 41.45 . 1 283 . 31 TYR N N 128.69 . 1 284 . 32 GLY H H 9.23 . 1 285 . 32 GLY HA2 H 4.12 . 2 286 . 32 GLY HA3 H 3.71 . 2 287 . 32 GLY C C 171.83 . 1 288 . 32 GLY CA C 47.93 . 1 289 . 32 GLY N N 109.63 . 1 290 . 33 ASN H H 7.42 . 1 291 . 33 ASN HA H 4.82 . 1 292 . 33 ASN HB2 H 3.24 . 1 293 . 33 ASN HB3 H 3.66 . 1 294 . 33 ASN HD21 H 8.09 . 2 295 . 33 ASN HD22 H 6.34 . 2 296 . 33 ASN C C 175.98 . 1 297 . 33 ASN CA C 52.01 . 1 298 . 33 ASN CB C 39.21 . 1 299 . 33 ASN N N 106.82 . 1 300 . 33 ASN ND2 N 115.479 . 1 301 . 34 LYS H H 8.92 . 1 302 . 34 LYS HA H 3.88 . 1 303 . 34 LYS HB2 H 1.91 . 1 304 . 34 LYS HB3 H 2.00 . 1 305 . 34 LYS HG2 H 1.5 . 2 306 . 34 LYS HG3 H 1.36 . 2 307 . 34 LYS HD2 H 1.81 . 2 308 . 34 LYS HE2 H 3.04 . 2 309 . 34 LYS HE3 H 3.1 . 2 310 . 34 LYS C C 176.03 . 1 311 . 34 LYS CA C 60.3 . 1 312 . 34 LYS CB C 32.76 . 1 313 . 34 LYS CG C 25.41 . 1 314 . 34 LYS CD C 29.77 . 1 315 . 34 LYS CE C 42.3 . 1 316 . 34 LYS N N 119.2 . 1 317 . 35 CYS H H 8.34 . 1 318 . 35 CYS HA H 4.46 . 1 319 . 35 CYS HB2 H 3.48 . 2 320 . 35 CYS HB3 H 3.31 . 2 321 . 35 CYS C C 175.86 . 1 322 . 35 CYS CA C 58.86 . 1 323 . 35 CYS CB C 36.66 . 1 324 . 35 CYS N N 121.7 . 1 325 . 36 ASN H H 8.44 . 1 326 . 36 ASN HA H 4.59 . 1 327 . 36 ASN HB2 H 3.22 . 1 328 . 36 ASN HB3 H 2.83 . 1 329 . 36 ASN HD21 H 7.62 . 2 330 . 36 ASN HD22 H 7.13 . 2 331 . 36 ASN C C 178.7 . 1 332 . 36 ASN CA C 56.68 . 1 333 . 36 ASN CB C 40.63 . 1 334 . 36 ASN N N 118.77 . 1 335 . 36 ASN ND2 N 111.41 . 1 336 . 37 PHE H H 8.41 . 1 337 . 37 PHE HA H 3.47 . 1 338 . 37 PHE HB2 H 2.85 . 1 339 . 37 PHE HB3 H 2.79 . 1 340 . 37 PHE HD1 H 6.57 . 2 341 . 37 PHE HE1 H 6.82 . 2 342 . 37 PHE C C 175.64 . 1 343 . 37 PHE CA C 61.2 . 1 344 . 37 PHE CB C 40.66 . 1 345 . 37 PHE N N 119.63 . 1 346 . 38 CYS H H 9.21 . 1 347 . 38 CYS HA H 3.99 . 1 348 . 38 CYS HB2 H 1.81 . 1 349 . 38 CYS HB3 H 1.53 . 1 350 . 38 CYS CA C 55.96 . 1 351 . 38 CYS CB C 32.76 . 1 352 . 38 CYS N N 117.17 . 1 353 . 39 ASN H H 8.17 . 1 354 . 39 ASN HA H 4.68 . 1 355 . 39 ASN HB2 H 2.99 . 2 356 . 39 ASN HB3 H 2.78 . 2 357 . 39 ASN HD21 H 7.59 . 2 358 . 39 ASN HD22 H 6.93 . 2 359 . 39 ASN C C 177.58 . 1 360 . 39 ASN CA C 55.75 . 1 361 . 39 ASN CB C 36.99 . 1 362 . 39 ASN N N 120.52 . 1 363 . 39 ASN ND2 N 112.64 . 1 364 . 40 ALA H H 7.22 . 1 365 . 40 ALA HA H 4.15 . 1 366 . 40 ALA HB H 1.26 . 1 367 . 40 ALA C C 181.03 . 1 368 . 40 ALA CA C 54.81 . 1 369 . 40 ALA CB C 18.52 . 1 370 . 40 ALA N N 123.23 . 1 371 . 41 VAL H H 8.59 . 1 372 . 41 VAL HA H 3.18 . 1 373 . 41 VAL HB H 2.04 . 1 374 . 41 VAL HG1 H 0.74 . 2 375 . 41 VAL HG2 H -0.02 . 2 376 . 41 VAL C C 181.47 . 1 377 . 41 VAL CA C 67.36 . 1 378 . 41 VAL CB C 31.94 . 1 379 . 41 VAL CG1 C 21.32 . 2 380 . 41 VAL CG2 C 22.68 . 2 381 . 41 VAL N N 123.3 . 1 382 . 42 VAL H H 8.08 . 1 383 . 42 VAL HA H 3.94 . 1 384 . 42 VAL HB H 2.31 . 1 385 . 42 VAL HG1 H 1.02 . 2 386 . 42 VAL HG2 H 1.06 . 2 387 . 42 VAL C C 178.91 . 1 388 . 42 VAL CA C 65.84 . 1 389 . 42 VAL CB C 31.13 . 1 390 . 42 VAL CG1 C 20.5 . 2 391 . 42 VAL N N 118.73 . 1 392 . 43 GLU H H 7.6 . 1 393 . 43 GLU HA H 4.36 . 1 394 . 43 GLU HB2 H 2.29 . 2 395 . 43 GLU HB3 H 2.09 . 2 396 . 43 GLU HG2 H 2.63 . 2 397 . 43 GLU C C 176.54 . 1 398 . 43 GLU CA C 57.15 . 1 399 . 43 GLU CB C 28.03 . 1 400 . 43 GLU CG C 33.03 . 1 401 . 43 GLU N N 119.63 . 1 402 . 44 SER H H 7.79 . 1 403 . 44 SER HA H 4.55 . 1 404 . 44 SER HB2 H 4.14 . 2 405 . 44 SER HB3 H 3.96 . 2 406 . 44 SER C C 175.47 . 1 407 . 44 SER CA C 59.17 . 1 408 . 44 SER CB C 64.44 . 1 409 . 44 SER N N 113.86 . 1 410 . 45 ASN H H 8.54 . 1 411 . 45 ASN HA H 4.49 . 1 412 . 45 ASN HB2 H 2.88 . 1 413 . 45 ASN HB3 H 3.16 . 1 414 . 45 ASN HD21 H 7.67 . 2 415 . 45 ASN HD22 H 6.93 . 2 416 . 45 ASN CA C 54.01 . 1 417 . 45 ASN CB C 37.56 . 1 418 . 45 ASN N N 120.96 . 1 419 . 45 ASN ND2 N 112.64 . 1 420 . 46 GLY H H 8.13 . 1 421 . 46 GLY HA2 H 3.59 . 2 422 . 46 GLY HA3 H 4.1 . 2 423 . 46 GLY C C 175.09 . 1 424 . 46 GLY CA C 45.86 . 1 425 . 46 GLY N N 103.6 . 1 426 . 47 THR H H 7.58 . 1 427 . 47 THR HA H 4.25 . 1 428 . 47 THR HB H 4.38 . 1 429 . 47 THR HG2 H 1.26 . 1 430 . 47 THR C C 174.53 . 1 431 . 47 THR CA C 70.08 . 1 432 . 47 THR CB C 63.08 . 1 433 . 47 THR CG2 C 22.00 . 1 434 . 47 THR N N 110.3 . 1 435 . 48 LEU H H 7.65 . 1 436 . 48 LEU HA H 4.29 . 1 437 . 48 LEU HB2 H 1.55 . 2 438 . 48 LEU HB3 H 1.12 . 2 439 . 48 LEU HG H 0.3 . 1 440 . 48 LEU HD1 H 1.25 . 2 441 . 48 LEU HD2 H 1.12 . 2 442 . 48 LEU C C 174.49 . 1 443 . 48 LEU CA C 55.38 . 1 444 . 48 LEU CB C 43.39 . 1 445 . 48 LEU CG C 21.59 . 1 446 . 48 LEU CD2 C 23.4 . 2 447 . 48 LEU N N 124.82 . 1 448 . 49 THR H H 8.58 . 1 449 . 49 THR HA H 4.64 . 1 450 . 49 THR HB H 4.42 . 1 451 . 49 THR HG2 H 1.14 . 1 452 . 49 THR C C 173.5 . 1 453 . 49 THR CA C 59.43 . 1 454 . 49 THR CB C 54.83 . 1 455 . 49 THR N N 116.04 . 1 456 . 50 LEU H H 8.83 . 1 457 . 50 LEU HA H 4.11 . 1 458 . 50 LEU HB2 H 1.01 . 2 459 . 50 LEU HB3 H 1.828 . 2 460 . 50 LEU HG H 0.68 . 1 461 . 50 LEU HD1 H 0.05 . 2 462 . 50 LEU HD2 H -0.11 . 2 463 . 50 LEU C C 176.43 . 1 464 . 50 LEU CA C 54.82 . 1 465 . 50 LEU CB C 42.81 . 1 466 . 50 LEU CG C 26.77 . 1 467 . 50 LEU CD1 C 25.95 . 2 468 . 50 LEU CD2 C 24.32 . 2 469 . 50 LEU N N 122.55 . 1 470 . 51 SER H H 8.83 . 1 471 . 51 SER HA H 4.52 . 1 472 . 51 SER HB2 H 3.39 . 1 473 . 51 SER HB3 H 3.57 . 1 474 . 51 SER C C 174.95 . 1 475 . 51 SER CA C 60.29 . 1 476 . 51 SER CB C 63.45 . 1 477 . 51 SER N N 123.12 . 1 478 . 52 HIS H H 7.28 . 1 479 . 52 HIS HA H 4.51 . 1 480 . 52 HIS HB2 H 3.78 . 2 481 . 52 HIS HB3 H 3.35 . 2 482 . 52 HIS HD2 H 8.76 . 1 483 . 52 HIS HE1 H 7.26 . 1 484 . 52 HIS C C 173.23 . 1 485 . 52 HIS CA C 54.69 . 1 486 . 52 HIS CB C 29.23 . 1 487 . 52 HIS N N 107.82 . 1 488 . 53 PHE H H 9.2 . 1 489 . 53 PHE HA H 4.33 . 1 490 . 53 PHE HB2 H 3.04 . 1 491 . 53 PHE HB3 H 3.24 . 1 492 . 53 PHE HD1 H 6.9 . 2 493 . 53 PHE HE1 H 6.67 . 2 494 . 53 PHE HZ H 6.62 . 1 495 . 53 PHE C C 178.01 . 1 496 . 53 PHE CA C 60.5 . 1 497 . 53 PHE CB C 39.65 . 1 498 . 53 PHE N N 120.46 . 1 499 . 54 GLY H H 8.27 . 1 500 . 54 GLY HA2 H 4.57 . 2 501 . 54 GLY HA3 H 3.58 . 2 502 . 54 GLY C C 177.99 . 1 503 . 54 GLY CA C 44.39 . 1 504 . 54 GLY N N 114.32 . 1 505 . 55 LYS H H 8.09 . 1 506 . 55 LYS HA H 4.06 . 1 507 . 55 LYS HB2 H 1.88 . 2 508 . 55 LYS HB3 H 1.77 . 2 509 . 55 LYS HG2 H 1.76 . 2 510 . 55 LYS HD2 H 1.53 . 2 511 . 55 LYS HE2 H 3.01 . 2 512 . 55 LYS HZ H 7.64 . 1 513 . 55 LYS CA C 56.19 . 1 514 . 55 LYS CB C 33.31 . 1 515 . 55 LYS CG C 29.77 . 1 516 . 55 LYS CD C 24.86 . 1 517 . 55 LYS CE C 42.3 . 1 518 . 55 LYS N N 113.43 . 1 519 . 56 CYS H H 8.5 . 1 520 . 56 CYS HA H 4.53 . 1 521 . 56 CYS HB2 H 2.59 . 2 522 . 56 CYS HB3 H 3.3 . 2 523 . 56 CYS CA C 54.83 . 1 524 . 56 CYS CB C 37.67 . 1 525 . 56 CYS N N 121.63 . 1 stop_ save_