data_42 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain ; _BMRB_accession_number 42 _BMRB_flat_file_name bmr42.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Robertson Andrew D. . 2 Westler William M. . 3 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" 305 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Robertson, Andrew D., Westler, William M., Markley, John L., "Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain," Biochemistry 27, 2519-2529 (1988). ; _Citation_title ; Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain ; _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 Robertson Andrew D. . 2 Westler William M. . 3 Markley John L. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 27 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2519 _Page_last 2529 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_ovomucoid_third_domain _Saveframe_category molecular_system _Mol_system_name 'ovomucoid third domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ovomucoid third domain' $ovomucoid_third_domain stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ovomucoid_third_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ovomucoid third domain' _Molecular_mass . _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 4068 "turkey 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 _Strain _Tissue $ovomucoid_third_domain turkey 9103 Eukaryota Metazoa Meleagris gallopavo generic egg 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 $ovomucoid_third_domain 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation 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_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'ovomucoid third domain' _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 LEU HA H 4.05 . 1 2 . 1 LEU HG H 1.7 . 1 3 . 1 LEU HD1 H 1 . 2 4 . 1 LEU HD2 H .96 . 2 5 . 2 ALA H H 8.65 . 1 6 . 2 ALA HA H 4.42 . 1 7 . 2 ALA HB H 1.42 . 1 8 . 3 ALA H H 8.42 . 1 9 . 3 ALA HA H 4.37 . 1 10 . 3 ALA HB H 1.41 . 1 11 . 4 VAL H H 8.15 . 1 12 . 4 VAL HA H 4.27 . 1 13 . 4 VAL HB H 2.05 . 1 14 . 4 VAL HG1 H .93 . 2 15 . 4 VAL HG2 H .88 . 2 16 . 5 SER H H 8.25 . 1 17 . 5 SER HA H 4.56 . 1 18 . 5 SER HB2 H 3.84 . 1 19 . 5 SER HB3 H 3.84 . 1 20 . 6 VAL H H 8.32 . 1 21 . 6 VAL HA H 4.29 . 1 22 . 6 VAL HB H 1.97 . 1 23 . 6 VAL HG1 H .82 . 2 24 . 6 VAL HG2 H .92 . 2 25 . 7 ASP H H 8.61 . 1 26 . 7 ASP HA H 4.76 . 1 27 . 7 ASP HB2 H 2.98 . 2 28 . 7 ASP HB3 H 2.72 . 2 29 . 8 CYS H H 8.9 . 1 30 . 8 CYS HA H 5.33 . 1 31 . 8 CYS HB2 H 2.55 . 2 32 . 8 CYS HB3 H 3.36 . 2 33 . 9 SER H H 8.69 . 1 34 . 9 SER HA H 4.27 . 1 35 . 9 SER HB2 H 3.98 . 2 36 . 9 SER HB3 H 4.08 . 2 37 . 10 GLU H H 8.73 . 1 38 . 10 GLU HA H 4.33 . 1 39 . 10 GLU HB2 H 1.78 . 2 40 . 10 GLU HB3 H 2.08 . 2 41 . 10 GLU HG2 H 2.31 . 1 42 . 10 GLU HG3 H 2.31 . 1 43 . 11 TYR H H 7.43 . 1 44 . 11 TYR HA H 4.07 . 1 45 . 11 TYR HB2 H 2.78 . 2 46 . 11 TYR HB3 H 2.9 . 2 47 . 11 TYR HD1 H 7.15 . 1 48 . 11 TYR HD2 H 7.15 . 1 49 . 12 PRO HA H 5.22 . 1 50 . 12 PRO HB2 H 2.08 . 2 51 . 12 PRO HB3 H 2.47 . 2 52 . 12 PRO HG2 H 1.87 . 2 53 . 12 PRO HG3 H 1.98 . 2 54 . 12 PRO HD2 H 3.56 . 2 55 . 12 PRO HD3 H 3.68 . 2 56 . 13 LYS H H 9.37 . 1 57 . 13 LYS HA H 4.89 . 1 58 . 13 LYS HB2 H 1.59 . 2 59 . 13 LYS HB3 H 1.9 . 2 60 . 13 LYS HG2 H .91 . 2 61 . 13 LYS HG3 H 1.14 . 2 62 . 13 LYS HD2 H 1.6 . 2 63 . 13 LYS HD3 H 1.43 . 2 64 . 13 LYS HE2 H 2.4 . 2 65 . 13 LYS HE3 H 2.57 . 2 66 . 14 PRO HA H 4.36 . 1 67 . 14 PRO HB2 H 2.31 . 1 68 . 14 PRO HB3 H 2.31 . 1 69 . 14 PRO HG2 H 2.05 . 1 70 . 14 PRO HG3 H 2.05 . 1 71 . 14 PRO HD2 H 3.76 . 2 72 . 14 PRO HD3 H 3.82 . 2 73 . 15 ALA H H 7.48 . 1 74 . 15 ALA HA H 4.58 . 1 75 . 15 ALA HB H 1.33 . 1 76 . 16 CYS H H 8.58 . 1 77 . 16 CYS HA H 5.32 . 1 78 . 16 CYS HB2 H 2.79 . 2 79 . 16 CYS HB3 H 3.37 . 2 80 . 17 THR H H 8.27 . 1 81 . 17 THR HA H 4.53 . 1 82 . 17 THR HB H 4.63 . 1 83 . 17 THR HG2 H 1.36 . 1 84 . 18 LEU H H 8.42 . 1 85 . 18 LEU HA H 4.42 . 1 86 . 18 LEU HB2 H 1.66 . 1 87 . 18 LEU HB3 H 1.66 . 1 88 . 18 LEU HG H 1.73 . 1 89 . 18 LEU HD1 H .9 . 2 90 . 18 LEU HD2 H .96 . 2 91 . 19 GLU H H 8.06 . 1 92 . 19 GLU HA H 4.14 . 1 93 . 19 GLU HB2 H 2 . 1 94 . 19 GLU HB3 H 2 . 1 95 . 19 GLU HG2 H 2.28 . 2 96 . 19 GLU HG3 H 2.37 . 2 97 . 20 TYR H H 8.93 . 1 98 . 20 TYR HA H 5.06 . 1 99 . 20 TYR HB2 H 2.92 . 2 100 . 20 TYR HB3 H 3.11 . 2 101 . 20 TYR HD1 H 7.28 . 1 102 . 20 TYR HD2 H 7.28 . 1 103 . 20 TYR HE1 H 6.82 . 1 104 . 20 TYR HE2 H 6.82 . 1 105 . 21 ARG H H 8.89 . 1 106 . 21 ARG HA H 4.46 . 1 107 . 21 ARG HB2 H 1.74 . 1 108 . 21 ARG HB3 H 1.74 . 1 109 . 21 ARG HG2 H 1.59 . 1 110 . 21 ARG HG3 H 1.59 . 1 111 . 21 ARG HD2 H 3.2 . 2 112 . 21 ARG HD3 H 3.29 . 2 113 . 21 ARG HE H 7.25 . 1 114 . 22 PRO HA H 4.52 . 1 115 . 22 PRO HB2 H 1.67 . 1 116 . 22 PRO HB3 H 1.67 . 1 117 . 22 PRO HG2 H 1.73 . 1 118 . 22 PRO HG3 H 1.73 . 1 119 . 22 PRO HD2 H 3.36 . 1 120 . 22 PRO HD3 H 3.36 . 1 121 . 23 LEU H H 8.48 . 1 122 . 23 LEU HA H 4.28 . 1 123 . 23 LEU HB2 H .98 . 1 124 . 23 LEU HB3 H .98 . 1 125 . 23 LEU HG H 1.39 . 1 126 . 23 LEU HD1 H .41 . 2 127 . 23 LEU HD2 H .48 . 2 128 . 24 CYS H H 8.17 . 1 129 . 24 CYS HA H 5.23 . 1 130 . 24 CYS HB2 H 1.35 . 2 131 . 24 CYS HB3 H 2.4 . 2 132 . 25 GLY H H 9.4 . 1 133 . 25 GLY HA2 H 4.5 . 2 134 . 25 GLY HA3 H 4.68 . 2 135 . 26 SER H H 9.37 . 1 136 . 26 SER HA H 4.15 . 1 137 . 26 SER HB2 H 3.82 . 2 138 . 26 SER HB3 H 4.1 . 2 139 . 27 ASP H H 8.43 . 1 140 . 27 ASP HA H 4.43 . 1 141 . 27 ASP HB2 H 2.59 . 2 142 . 27 ASP HB3 H 3.01 . 2 143 . 28 ASN H H 8.65 . 1 144 . 28 ASN HA H 4.4 . 1 145 . 28 ASN HB2 H 2.82 . 2 146 . 28 ASN HB3 H 3.17 . 2 147 . 28 ASN HD21 H 6.85 . 2 148 . 28 ASN HD22 H 7.53 . 2 149 . 29 LYS H H 7.8 . 1 150 . 29 LYS HA H 4.4 . 1 151 . 29 LYS HB2 H 1.44 . 2 152 . 29 LYS HB3 H 1.66 . 2 153 . 29 LYS HG2 H .81 . 2 154 . 29 LYS HG3 H 1.14 . 2 155 . 29 LYS HD2 H 1.43 . 2 156 . 29 LYS HD3 H 1.54 . 2 157 . 29 LYS HE2 H 2.82 . 1 158 . 29 LYS HE3 H 2.82 . 1 159 . 29 LYS HZ H 7.45 . 1 160 . 30 THR H H 8.29 . 1 161 . 30 THR HA H 4.78 . 1 162 . 30 THR HB H 4.02 . 1 163 . 30 THR HG2 H 1.18 . 1 164 . 31 TYR H H 9.7 . 1 165 . 31 TYR HA H 4.5 . 1 166 . 31 TYR HB2 H 2.79 . 2 167 . 31 TYR HB3 H 2.9 . 2 168 . 32 GLY H H 9.21 . 1 169 . 32 GLY HA2 H 3.68 . 2 170 . 32 GLY HA3 H 4.12 . 2 171 . 33 ASN H H 7.43 . 1 172 . 33 ASN HA H 4.81 . 1 173 . 33 ASN HB2 H 3.19 . 2 174 . 33 ASN HB3 H 3.67 . 2 175 . 33 ASN HD21 H 6.32 . 2 176 . 33 ASN HD22 H 8.11 . 2 177 . 34 LYS H H 8.92 . 1 178 . 34 LYS HA H 3.86 . 1 179 . 34 LYS HB2 H 1.86 . 2 180 . 34 LYS HB3 H 1.98 . 2 181 . 34 LYS HG2 H 1.34 . 2 182 . 34 LYS HG3 H 1.46 . 2 183 . 34 LYS HD2 H 1.78 . 1 184 . 34 LYS HD3 H 1.78 . 1 185 . 34 LYS HE2 H 3.04 . 2 186 . 34 LYS HE3 H 3.1 . 2 187 . 35 CYS H H 8.3 . 1 188 . 35 CYS HA H 4.53 . 1 189 . 35 CYS HB2 H 3.25 . 2 190 . 35 CYS HB3 H 3.47 . 2 191 . 36 ASN H H 8.39 . 1 192 . 36 ASN HA H 4.58 . 1 193 . 36 ASN HB2 H 2.84 . 2 194 . 36 ASN HB3 H 3.22 . 2 195 . 36 ASN HD21 H 7.11 . 2 196 . 36 ASN HD22 H 7.61 . 2 197 . 37 PHE H H 8.39 . 1 198 . 37 PHE HA H 3.51 . 1 199 . 37 PHE HB2 H 2.78 . 2 200 . 37 PHE HB3 H 2.848 . 2 201 . 37 PHE HD1 H 6.55 . 1 202 . 37 PHE HD2 H 6.55 . 1 203 . 37 PHE HE1 H 6.82 . 1 204 . 37 PHE HE2 H 6.82 . 1 205 . 37 PHE HZ H 6.55 . 1 206 . 38 CYS H H 9.19 . 1 207 . 38 CYS HA H 3.97 . 1 208 . 38 CYS HB2 H 1.38 . 2 209 . 38 CYS HB3 H 1.77 . 2 210 . 39 ASN H H 8.17 . 1 211 . 39 ASN HA H 4.69 . 1 212 . 39 ASN HB2 H 2.78 . 2 213 . 39 ASN HB3 H 2.98 . 2 214 . 39 ASN HD21 H 6.81 . 2 215 . 39 ASN HD22 H 7.52 . 2 216 . 40 ALA H H 7.22 . 1 217 . 40 ALA HA H 4.17 . 1 218 . 40 ALA HB H 1.3 . 1 219 . 41 VAL H H 8.6 . 1 220 . 41 VAL HA H 3.18 . 1 221 . 41 VAL HB H 2.06 . 1 222 . 41 VAL HG1 H .02 . 2 223 . 41 VAL HG2 H .72 . 2 224 . 42 VAL H H 8.06 . 1 225 . 42 VAL HA H 3.93 . 1 226 . 42 VAL HB H 2.31 . 1 227 . 42 VAL HG1 H 1 . 2 228 . 42 VAL HG2 H 1.05 . 2 229 . 43 GLU H H 7.63 . 1 230 . 43 GLU HA H 4.32 . 1 231 . 43 GLU HB2 H 2.1 . 2 232 . 43 GLU HB3 H 2.25 . 2 233 . 43 GLU HG2 H 2.58 . 1 234 . 43 GLU HG3 H 2.58 . 1 235 . 44 SER H H 7.8 . 1 236 . 44 SER HA H 4.52 . 1 237 . 44 SER HB2 H 3.98 . 2 238 . 44 SER HB3 H 4.22 . 2 239 . 45 ASN H H 8.5 . 1 240 . 45 ASN HA H 4.48 . 1 241 . 45 ASN HB2 H 2.85 . 2 242 . 45 ASN HB3 H 3.15 . 2 243 . 45 ASN HD21 H 6.85 . 2 244 . 45 ASN HD22 H 7.58 . 2 245 . 46 GLY H H 8.12 . 1 246 . 46 GLY HA2 H 3.58 . 2 247 . 46 GLY HA3 H 4.1 . 2 248 . 47 THR H H 7.58 . 1 249 . 47 THR HA H 4.22 . 1 250 . 47 THR HB H 4.26 . 1 251 . 47 THR HG2 H 1.26 . 1 252 . 48 LEU H H 7.65 . 1 253 . 48 LEU HA H 4.28 . 1 254 . 48 LEU HB2 H 1.51 . 1 255 . 48 LEU HB3 H 1.51 . 1 256 . 48 LEU HG H 1.12 . 1 257 . 48 LEU HD1 H .3 . 2 258 . 48 LEU HD2 H 1.17 . 2 259 . 49 THR H H 8.56 . 1 260 . 49 THR HA H 4.68 . 1 261 . 49 THR HB H 4.36 . 1 262 . 49 THR HG2 H 1.13 . 1 263 . 50 LEU H H 8.77 . 1 264 . 50 LEU HA H 4.1 . 1 265 . 50 LEU HB2 H 1 . 2 266 . 50 LEU HB3 H 1.78 . 2 267 . 50 LEU HG H .65 . 1 268 . 50 LEU HD1 H .12 . 2 269 . 50 LEU HD2 H .04 . 2 270 . 51 SER H H 8.85 . 1 271 . 51 SER HA H 4.53 . 1 272 . 51 SER HB2 H 3.38 . 2 273 . 51 SER HB3 H 3.53 . 2 274 . 52 HIS H H 7.27 . 1 275 . 52 HIS HA H 4.52 . 1 276 . 52 HIS HB2 H 3.32 . 2 277 . 52 HIS HB3 H 3.79 . 2 278 . 52 HIS HD2 H 7.26 . 1 279 . 52 HIS HE1 H 8.8 . 1 280 . 53 PHE H H 9.17 . 1 281 . 53 PHE HA H 4.32 . 1 282 . 53 PHE HB2 H 3.04 . 2 283 . 53 PHE HB3 H 3.24 . 2 284 . 53 PHE HD1 H 7.28 . 1 285 . 53 PHE HD2 H 7.28 . 1 286 . 53 PHE HE1 H 7.17 . 1 287 . 53 PHE HE2 H 7.17 . 1 288 . 54 GLY H H 8.26 . 1 289 . 54 GLY HA2 H 3.57 . 2 290 . 54 GLY HA3 H 4.61 . 2 291 . 55 LYS H H 7.99 . 1 292 . 55 LYS HA H 4.05 . 1 293 . 55 LYS HB2 H 1.74 . 2 294 . 55 LYS HB3 H 1.88 . 2 295 . 55 LYS HG2 H 1.49 . 2 296 . 55 LYS HG3 H 1.55 . 2 297 . 55 LYS HD2 H 1.75 . 1 298 . 55 LYS HD3 H 1.75 . 1 299 . 55 LYS HE2 H 3.09 . 1 300 . 55 LYS HE3 H 3.09 . 1 301 . 55 LYS HZ H 7.54 . 1 302 . 56 CYS H H 8.31 . 1 303 . 56 CYS HA H 4.39 . 1 304 . 56 CYS HB2 H 2.52 . 2 305 . 56 CYS HB3 H 3.15 . 2 stop_ save_