data_5473 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structures of the Two Stable Conformers of Turkey Ovomucoid that Coexist at Low pH ; _BMRB_accession_number 5473 _BMRB_flat_file_name bmr5473.str _Entry_type original _Submission_date 2002-07-24 _Accession_date 2002-07-24 _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 Song Jikui . . 2 Laskowski Michael . Jr. 3 Qasim Mohammod A. . 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" 276 "13C chemical shifts" 204 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-07-30 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5472 'chemical shifts of cis conformer' stop_ _Original_release_date 2002-07-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Two Conformational States of Turkey Ovomucoid Third Domain at Low pH: Three-dimensional Structures, Internal Dynamics, and Interconversion Kinetics and Thermodynamics ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22652003 _PubMed_ID 12767219 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Song Jikui . . 2 Laskowski Michael . Jr. 3 Qasim Mohammod A. . 4 Markley John L. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6380 _Page_last 6391 _Year 2003 _Details 'cis-trans isomerization of prolyl peptide bond.' loop_ _Keyword OMTKY3 stop_ save_ ################################## # Molecular system description # ################################## save_system_OMTKY3 _Saveframe_category molecular_system _Mol_system_name 'Ovomucoid Third Domain' _Abbreviation_common OMTKY3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'P5-OMTKY3 T state' $P5-OMTKY3 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_P5-OMTKY3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ovomucoid Third Domain' _Abbreviation_common OMTKY3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; LAAVSVDCSEYPKDACTLEY 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 ASP 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 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' 67.86 38 100.00 100.00 3.19e-14 BMRB 1375 'ovomucoid third domain' 67.86 38 100.00 100.00 3.19e-14 BMRB 4068 'turkey ovomucoid third domain' 100.00 56 98.21 98.21 5.65e-24 BMRB 42 'ovomucoid third domain' 100.00 56 98.21 98.21 5.65e-24 BMRB 4864 'Ovomucoid Third Domain from Turkey' 100.00 56 98.21 98.21 5.65e-24 BMRB 4865 'Ovomucoid Third Domain from Turkey' 100.00 56 98.21 98.21 5.65e-24 BMRB 507 'ovomucoid third domain' 100.00 56 98.21 98.21 5.65e-24 BMRB 5411 'Turkey Ovomucoid Third Domain' 91.07 51 98.04 98.04 2.35e-21 BMRB 5440 'Turkey Ovomucoid Third Domain' 91.07 51 98.04 100.00 9.80e-22 BMRB 5448 'Turkey Ovomucoid Third Domain' 91.07 51 98.04 98.04 2.35e-21 BMRB 5449 'P5-His Turkey Ovomucoid Third Domain' 91.07 51 98.04 98.04 1.86e-21 BMRB 5472 'Ovomucoid Third Domain' 100.00 56 100.00 100.00 8.29e-25 BMRB 5518 'Ovomucoid Third Domain from Turkey' 100.00 56 98.21 98.21 5.65e-24 BMRB 5520 'Ovomucoid Third Domain from Turkey' 67.86 38 100.00 100.00 3.19e-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 98.21 98.21 5.65e-24 PDB 1M8B 'Solution Structure Of The C State Of Turkey Ovomucoid At Ph 2.5' 100.00 56 100.00 100.00 8.29e-25 PDB 1M8C 'Solution Structure Of The T State Of Turkey Ovomucoid At Ph 2.5' 100.00 56 100.00 100.00 8.29e-25 PDB 1OMT ; Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Standard Noesy Analysis) ; 100.00 56 98.21 98.21 5.65e-24 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 98.21 98.21 5.65e-24 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 98.21 98.21 5.65e-24 PDB 1R0R ; 1.1 Angstrom Resolution Structure Of The Complex Between The Protein Inhibitor, Omtky3, And The Serine Protease, Subtilisin Carlsberg ; 91.07 51 98.04 98.04 2.35e-21 PDB 1SGR 'Leu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B' 91.07 51 98.04 98.04 2.35e-21 PDB 1TUR 'Solution Structure Of Turkey Ovomucoid Third Domain As Determined From Nuclear Magnetic Resonance Data' 100.00 56 98.21 98.21 5.65e-24 PDB 1TUS ; Solution Structure Of Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain By Nuclear Magnetic Resonance And Distance Geometry Methods ; 100.00 56 98.21 98.21 5.65e-24 PDB 2GKR 'Crystal Structure Of The N-Terminally Truncated Omtky3- Del(1-5)' 91.07 51 98.04 98.04 2.35e-21 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 98.21 98.21 5.65e-24 SWISS-PROT P52245 Ovomucoid 100.00 56 98.21 98.21 5.65e-24 SWISS-PROT P68436 Ovomucoid 100.00 56 98.21 98.21 5.65e-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 $P5-OMTKY3 Turkey 9103 Eukaryota Metazoa Meleagris gallopavo 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 $P5-OMTKY3 'recombinant technology' . . . . . 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 $P5-OMTKY3 2 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 95 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_15N-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSY _Sample_label . save_ save_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCOCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CCONH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _Sample_label . save_ save_HCCONH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _Sample_label . save_ save_HCCHCOSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCHCOSY _Sample_label . save_ save_13C-NOESY_HNCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-NOESY HNCO' _Sample_label . save_ save_3h-HNCO_11 _Saveframe_category NMR_applied_experiment _Experiment_name 3h-HNCO _Sample_label . save_ save_1H-15N_TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HN(CO)CA_13 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_14 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.2 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shifts_OMTKY3_pH7.3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'P5-OMTKY3 T state' _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 CA C 54.592 0.000 1 2 . 1 LEU HA H 4.034 0.009 1 3 . 1 LEU HG H 0.977 0.000 1 4 . 2 ALA CA C 52.330 0.009 1 5 . 2 ALA CB C 19.364 0.011 1 6 . 2 ALA HA H 4.407 0.011 1 7 . 2 ALA H H 8.638 0.006 1 8 . 2 ALA N N 128.226 0.037 1 9 . 2 ALA HB H 1.430 0.009 1 10 . 3 ALA CA C 52.476 0.008 1 11 . 3 ALA CB C 19.359 0.000 1 12 . 3 ALA HA H 4.382 0.012 1 13 . 3 ALA H H 8.412 0.006 1 14 . 3 ALA N N 125.700 0.007 1 15 . 3 ALA HB H 1.425 0.009 1 16 . 4 VAL C C 175.161 0.000 1 17 . 4 VAL CA C 61.713 0.052 1 18 . 4 VAL CB C 32.991 0.031 1 19 . 4 VAL CG1 C 20.365 0.034 2 20 . 4 VAL CG2 C 21.636 0.132 2 21 . 4 VAL HA H 4.247 0.004 1 22 . 4 VAL HB H 2.047 0.013 1 23 . 4 VAL H H 8.150 0.006 1 24 . 4 VAL N N 120.090 0.027 1 25 . 4 VAL HG1 H 0.894 0.022 2 26 . 4 VAL HG2 H 0.917 0.014 2 27 . 5 SER C C 173.653 0.000 1 28 . 5 SER CA C 57.831 0.084 1 29 . 5 SER CB C 64.590 0.050 1 30 . 5 SER HA H 4.554 0.013 1 31 . 5 SER HB2 H 3.846 0.020 1 32 . 5 SER H H 8.246 0.039 1 33 . 5 SER N N 119.323 0.282 1 34 . 6 VAL C C 174.574 0.000 1 35 . 6 VAL CA C 61.646 0.113 1 36 . 6 VAL CB C 34.135 0.069 1 37 . 6 VAL CG1 C 21.828 0.052 2 38 . 6 VAL CG2 C 22.020 0.097 2 39 . 6 VAL HA H 4.189 0.016 1 40 . 6 VAL HB H 2.034 0.013 1 41 . 6 VAL H H 8.449 0.015 1 42 . 6 VAL N N 122.176 0.103 1 43 . 6 VAL HG1 H 0.815 0.017 2 44 . 6 VAL HG2 H 0.888 0.013 2 45 . 7 ASP C C 176.170 0.000 1 46 . 7 ASP CA C 51.906 0.015 1 47 . 7 ASP CB C 37.001 0.017 1 48 . 7 ASP HA H 4.911 0.010 1 49 . 7 ASP HB2 H 2.847 0.009 2 50 . 7 ASP HB3 H 3.179 0.007 2 51 . 7 ASP H H 8.731 0.010 1 52 . 7 ASP N N 125.200 0.046 1 53 . 8 CYS C C 176.680 0.000 1 54 . 8 CYS CA C 56.128 0.120 1 55 . 8 CYS CB C 36.274 0.045 1 56 . 8 CYS HA H 4.911 0.006 1 57 . 8 CYS HB2 H 3.218 0.011 2 58 . 8 CYS HB3 H 2.879 0.011 2 59 . 8 CYS H H 8.758 0.012 1 60 . 8 CYS N N 123.842 0.037 1 61 . 9 SER C C 174.849 0.000 1 62 . 9 SER CA C 60.747 0.039 1 63 . 9 SER CB C 62.840 0.029 1 64 . 9 SER HA H 4.269 0.008 1 65 . 9 SER H H 8.378 0.012 1 66 . 9 SER N N 118.999 0.085 1 67 . 9 SER HB2 H 3.949 0.010 1 68 . 10 GLU C C 174.581 0.000 1 69 . 10 GLU CA C 55.552 0.039 1 70 . 10 GLU CB C 28.403 0.028 1 71 . 10 GLU CG C 32.887 0.023 1 72 . 10 GLU HA H 4.205 0.011 2 73 . 10 GLU HB2 H 1.802 0.015 2 74 . 10 GLU HB3 H 1.840 0.017 1 75 . 10 GLU H H 7.723 0.011 1 76 . 10 GLU N N 118.886 0.027 1 77 . 10 GLU HG2 H 2.254 0.011 1 78 . 11 TYR CB C 38.848 0.081 1 79 . 11 TYR HA H 4.796 0.013 1 80 . 11 TYR HB2 H 3.160 0.007 1 81 . 11 TYR HB3 H 2.836 0.010 1 82 . 11 TYR H H 7.461 0.022 1 83 . 11 TYR N N 119.506 0.028 1 84 . 11 TYR HD1 H 7.110 0.008 1 85 . 11 TYR HE1 H 6.829 0.010 1 86 . 12 PRO C C 176.767 0.000 1 87 . 12 PRO CA C 63.043 0.052 1 88 . 12 PRO CB C 32.110 0.078 1 89 . 12 PRO CD C 50.338 0.047 1 90 . 12 PRO CG C 27.298 0.149 1 91 . 12 PRO HA H 4.546 0.010 1 92 . 12 PRO HB2 H 2.284 0.009 2 93 . 12 PRO HB3 H 2.076 0.005 2 94 . 12 PRO HD2 H 3.415 0.013 2 95 . 12 PRO HD3 H 3.461 0.013 2 96 . 12 PRO HG2 H 1.934 0.009 2 97 . 12 PRO HG3 H 1.991 0.009 2 98 . 12 PRO N N 133.5 0.000 1 99 . 13 LYS C C 177.558 0.000 1 100 . 13 LYS CA C 58.711 0.075 1 101 . 13 LYS CB C 32.786 0.033 1 102 . 13 LYS CD C 29.231 0.122 1 103 . 13 LYS CE C 42.084 0.020 1 104 . 13 LYS CG C 24.607 0.024 1 105 . 13 LYS HA H 4.084 0.012 1 106 . 13 LYS HB2 H 1.815 0.010 1 107 . 13 LYS HD2 H 1.701 0.017 1 108 . 13 LYS HE3 H 3.017 0.002 1 109 . 13 LYS HG2 H 1.433 0.013 1 110 . 13 LYS H H 8.281 0.010 1 111 . 13 LYS N N 119.867 0.045 1 112 . 14 ASP C C 175.418 0.000 1 113 . 14 ASP CA C 53.154 0.015 1 114 . 14 ASP CB C 38.251 0.049 1 115 . 14 ASP HA H 4.804 0.007 1 116 . 14 ASP H H 8.369 0.005 1 117 . 14 ASP N N 117.410 0.044 1 118 . 14 ASP HB2 H 2.998 0.020 1 119 . 15 ALA C C 177.550 0.000 1 120 . 15 ALA CA C 52.792 0.031 1 121 . 15 ALA CB C 19.079 0.026 1 122 . 15 ALA HA H 4.516 0.007 1 123 . 15 ALA H H 7.779 0.012 1 124 . 15 ALA N N 122.686 0.058 1 125 . 15 ALA HB H 1.521 0.009 1 126 . 16 CYS C C 175.128 0.000 1 127 . 16 CYS CA C 56.397 0.087 1 128 . 16 CYS CB C 38.150 0.059 1 129 . 16 CYS HA H 4.969 0.008 1 130 . 16 CYS HB2 H 3.206 0.016 2 131 . 16 CYS HB3 H 3.299 0.008 2 132 . 16 CYS H H 8.400 0.007 1 133 . 16 CYS N N 118.765 0.074 1 134 . 17 THR C C 174.782 0.000 1 135 . 17 THR CA C 63.072 0.023 1 136 . 17 THR CB C 69.589 0.017 1 137 . 17 THR CG2 C 21.743 0.015 1 138 . 17 THR HA H 4.220 0.005 1 139 . 17 THR HB H 4.328 0.015 1 140 . 17 THR H H 8.012 0.009 1 141 . 17 THR N N 115.080 0.114 1 142 . 17 THR HG2 H 1.320 0.011 1 143 . 18 LEU C C 176.865 0.000 1 144 . 18 LEU CA C 55.422 0.015 1 145 . 18 LEU CB C 40.963 0.028 1 146 . 18 LEU CD1 C 25.224 0.029 1 147 . 18 LEU CD2 C 22.879 0.052 1 148 . 18 LEU CG C 27.212 0.013 1 149 . 18 LEU HA H 4.278 0.013 2 150 . 18 LEU HB3 H 1.782 0.012 2 151 . 18 LEU HG H 1.686 0.008 1 152 . 18 LEU H H 8.572 0.010 1 153 . 18 LEU N N 122.044 0.056 1 154 . 18 LEU HD1 H 0.961 0.005 2 155 . 18 LEU HD2 H 0.920 0.005 2 156 . 19 GLU C C 175.653 0.000 1 157 . 19 GLU CA C 56.325 0.021 1 158 . 19 GLU CB C 29.479 0.036 1 159 . 19 GLU CG C 33.135 0.080 1 160 . 19 GLU HA H 4.333 0.015 1 161 . 19 GLU HB2 H 1.961 0.013 2 162 . 19 GLU HB3 H 2.026 0.008 2 163 . 19 GLU HG2 H 2.407 0.021 2 164 . 19 GLU HG3 H 2.451 0.018 2 165 . 19 GLU H H 7.859 0.005 1 166 . 19 GLU N N 120.634 0.035 1 167 . 20 TYR C C 174.723 0.000 1 168 . 20 TYR CA C 57.633 0.028 1 169 . 20 TYR CB C 38.673 0.072 1 170 . 20 TYR HA H 5.031 0.007 1 171 . 20 TYR HB2 H 2.954 0.019 2 172 . 20 TYR HB3 H 3.107 0.007 2 173 . 20 TYR HD2 H 7.271 0.009 1 174 . 20 TYR HE2 H 6.824 0.012 1 175 . 20 TYR H H 8.928 0.016 1 176 . 20 TYR N N 128.868 0.031 1 177 . 21 ARG CA C 53.135 0.022 1 178 . 21 ARG CB C 31.246 0.041 1 179 . 21 ARG CD C 43.595 0.018 1 180 . 21 ARG HA H 4.509 0.006 1 181 . 21 ARG HB2 H 1.764 0.005 1 182 . 21 ARG HD2 H 3.170 0.012 2 183 . 21 ARG HD3 H 3.282 0.011 2 184 . 21 ARG HE H 7.167 0.010 1 185 . 21 ARG HG2 H 1.584 0.012 1 186 . 21 ARG H H 8.717 0.011 1 187 . 21 ARG N N 130.151 0.043 1 188 . 21 ARG NE N 121.065 0.000 1 189 . 22 PRO C C 176.597 0.000 1 190 . 22 PRO CA C 63.030 0.130 1 191 . 22 PRO CB C 33.394 0.034 1 192 . 22 PRO CD C 49.655 0.057 1 193 . 22 PRO CG C 27.375 0.026 1 194 . 22 PRO HA H 4.608 0.005 1 195 . 22 PRO HB2 H 1.772 0.022 2 196 . 22 PRO HB3 H 1.396 0.009 2 197 . 22 PRO HD2 H 3.423 0.011 2 198 . 22 PRO HD3 H 2.052 0.030 2 199 . 22 PRO HG2 H 1.713 0.009 1 200 . 22 PRO N N 133.4 0.000 1 201 . 23 LEU C C 173.633 0.000 1 202 . 23 LEU CA C 55.047 0.067 1 203 . 23 LEU CB C 44.869 0.047 1 204 . 23 LEU CD1 C 26.068 0.119 2 205 . 23 LEU CD2 C 25.828 0.096 2 206 . 23 LEU CG C 27.130 0.152 1 207 . 23 LEU HA H 4.431 0.008 1 208 . 23 LEU HB2 H 1.109 0.013 2 209 . 23 LEU HB3 H 1.218 0.006 2 210 . 23 LEU HG H 1.414 0.012 1 211 . 23 LEU H H 8.556 0.012 1 212 . 23 LEU N N 120.182 0.059 1 213 . 23 LEU HD1 H 0.408 0.012 2 214 . 23 LEU HD2 H 0.455 0.007 2 215 . 24 CYS C C 175.637 0.000 1 216 . 24 CYS CA C 54.455 0.092 1 217 . 24 CYS CB C 39.027 0.072 1 218 . 24 CYS HA H 5.252 0.008 1 219 . 24 CYS HB2 H 2.385 0.015 2 220 . 24 CYS HB3 H 1.366 0.019 2 221 . 24 CYS H H 8.313 0.009 1 222 . 24 CYS N N 121.503 0.082 1 223 . 25 GLY C C 174.672 0.000 1 224 . 25 GLY CA C 45.347 0.040 1 225 . 25 GLY HA2 H 4.430 0.028 2 226 . 25 GLY HA3 H 4.770 0.024 2 227 . 25 GLY H H 9.362 0.019 1 228 . 25 GLY N N 116.541 0.053 1 229 . 26 SER C C 173.889 0.000 1 230 . 26 SER CA C 61.186 0.075 1 231 . 26 SER CB C 62.215 0.022 1 232 . 26 SER HA H 4.198 0.019 1 233 . 26 SER HB2 H 3.862 0.014 2 234 . 26 SER HB3 H 4.129 0.020 2 235 . 26 SER H H 9.381 0.007 1 236 . 26 SER N N 119.184 0.026 1 237 . 27 ASP C C 175.650 0.000 1 238 . 27 ASP CA C 52.654 0.052 1 239 . 27 ASP CB C 38.839 0.053 1 240 . 27 ASP HA H 4.549 0.010 1 241 . 27 ASP HB2 H 2.729 0.011 2 242 . 27 ASP HB3 H 3.180 0.015 2 243 . 27 ASP H H 8.170 0.075 1 244 . 27 ASP N N 120.835 0.051 1 245 . 28 ASN C C 173.883 0.000 1 246 . 28 ASN CA C 55.058 0.019 1 247 . 28 ASN CB C 37.660 0.018 1 248 . 28 ASN CG C 178.497 0.000 1 249 . 28 ASN HA H 4.429 0.016 1 250 . 28 ASN HB2 H 2.812 0.009 2 251 . 28 ASN HB3 H 3.179 0.010 2 252 . 28 ASN HD21 H 6.830 0.003 2 253 . 28 ASN HD22 H 7.534 0.003 2 254 . 28 ASN H H 8.661 0.011 1 255 . 28 ASN N N 116.966 0.058 1 256 . 28 ASN ND2 N 113.598 0.053 1 257 . 29 LYS C C 174.713 0.000 1 258 . 29 LYS CA C 54.877 0.029 1 259 . 29 LYS CB C 33.701 0.028 1 260 . 29 LYS CD C 28.892 0.021 1 261 . 29 LYS CE C 42.345 0.023 1 262 . 29 LYS CG C 25.133 0.078 1 263 . 29 LYS HA H 4.437 0.009 1 264 . 29 LYS HB2 H 1.385 0.006 2 265 . 29 LYS HB3 H 1.646 0.015 2 266 . 29 LYS HD2 H 1.559 0.010 1 267 . 29 LYS HE2 H 2.895 0.006 1 268 . 29 LYS HG2 H 0.935 0.013 2 269 . 29 LYS HG3 H 1.178 0.009 2 270 . 29 LYS H H 7.562 0.081 1 271 . 29 LYS N N 119.088 0.028 1 272 . 30 THR C C 174.877 0.000 1 273 . 30 THR CA C 62.585 0.001 1 274 . 30 THR CB C 69.272 0.025 1 275 . 30 THR CG2 C 23.718 0.034 1 276 . 30 THR HA H 4.843 0.023 1 277 . 30 THR HB H 3.997 0.008 1 278 . 30 THR H H 8.280 0.015 1 279 . 30 THR N N 122.183 0.050 1 280 . 30 THR HG2 H 1.189 0.009 1 281 . 31 TYR C C 176.967 0.000 1 282 . 31 TYR CA C 57.882 0.030 1 283 . 31 TYR CB C 41.598 0.127 1 284 . 31 TYR HA H 4.594 0.013 1 285 . 31 TYR HB2 H 2.988 0.014 2 286 . 31 TYR HB3 H 2.769 0.015 2 287 . 31 TYR H H 9.639 0.011 1 288 . 31 TYR N N 129.829 0.015 1 289 . 31 TYR HD1 H 7.079 0.015 1 290 . 31 TYR HE1 H 6.661 0.012 1 291 . 32 GLY C C 172.003 0.000 1 292 . 32 GLY CA C 47.787 0.053 1 293 . 32 GLY HA2 H 3.724 0.012 2 294 . 32 GLY HA3 H 4.093 0.013 2 295 . 32 GLY H H 9.202 0.006 1 296 . 32 GLY N N 110.062 0.098 1 297 . 33 ASN C C 176.224 0.000 1 298 . 33 ASN CA C 52.397 0.011 1 299 . 33 ASN CB C 39.385 0.054 1 300 . 33 ASN CG C 175.7 0.000 1 301 . 33 ASN HA H 4.775 0.012 1 302 . 33 ASN HB2 H 3.122 0.025 2 303 . 33 ASN HB3 H 3.569 0.025 2 304 . 33 ASN HD21 H 7.029 0.007 2 305 . 33 ASN HD22 H 7.885 0.044 2 306 . 33 ASN H H 7.405 0.011 1 307 . 33 ASN N N 108.014 0.048 1 308 . 33 ASN ND2 N 117.963 0.046 1 309 . 34 LYS C C 177.294 0.000 1 310 . 34 LYS CA C 60.581 0.034 1 311 . 34 LYS CB C 32.948 0.042 1 312 . 34 LYS CD C 30.047 0.091 1 313 . 34 LYS CE C 42.229 0.018 1 314 . 34 LYS CG C 26.791 0.045 1 315 . 34 LYS HA H 3.840 0.014 1 316 . 34 LYS HB2 H 1.432 0.011 2 317 . 34 LYS HD2 H 1.364 0.015 2 318 . 34 LYS HE2 H 2.847 0.016 1 319 . 34 LYS HE3 H 2.866 0.007 1 320 . 34 LYS HG2 H 1.144 0.014 2 321 . 34 LYS HG3 H 1.563 0.012 2 322 . 34 LYS H H 9.192 0.008 1 323 . 34 LYS N N 119.504 0.056 1 324 . 35 CYS C C 177.014 0.000 1 325 . 35 CYS CA C 62.082 0.037 1 326 . 35 CYS CB C 36.285 0.032 1 327 . 35 CYS HA H 4.378 0.006 1 328 . 35 CYS HB2 H 3.222 0.014 1 329 . 35 CYS HB3 H 3.282 0.015 2 330 . 35 CYS H H 8.378 0.017 2 331 . 35 CYS N N 119.958 0.043 1 332 . 36 ASN C C 178.554 0.000 1 333 . 36 ASN CA C 56.870 0.027 1 334 . 36 ASN CB C 39.363 0.050 1 335 . 36 ASN CG C 174.61 0.000 1 336 . 36 ASN HA H 4.573 0.011 1 337 . 36 ASN HB2 H 2.909 0.022 2 338 . 36 ASN HB3 H 3.201 0.007 2 339 . 36 ASN HD21 H 7.324 0.007 2 340 . 36 ASN HD22 H 7.550 0.006 2 341 . 36 ASN H H 8.765 0.009 1 342 . 36 ASN N N 122.029 0.029 1 343 . 36 ASN ND2 N 111.600 0.058 1 344 . 37 PHE C C 175.702 0.000 1 345 . 37 PHE CA C 61.156 0.043 1 346 . 37 PHE CB C 40.407 0.000 1 347 . 37 PHE HA H 3.506 0.009 1 348 . 37 PHE HB2 H 2.846 0.013 2 349 . 37 PHE HB3 H 2.886 0.011 2 350 . 37 PHE H H 8.238 0.010 1 351 . 37 PHE HZ H 6.646 0.004 1 352 . 37 PHE N N 122.026 0.048 1 353 . 37 PHE HD1 H 6.662 0.017 1 354 . 37 PHE HE1 H 6.901 0.022 1 355 . 38 CYS C C 176.886 0.000 1 356 . 38 CYS CA C 58.627 0.038 1 357 . 38 CYS CB C 36.220 0.017 1 358 . 38 CYS HA H 4.083 0.012 1 359 . 38 CYS HB2 H 3.021 0.015 2 360 . 38 CYS HB3 H 3.129 0.012 2 361 . 38 CYS H H 8.969 0.006 1 362 . 38 CYS N N 118.924 0.037 1 363 . 39 ASN C C 176.677 0.000 1 364 . 39 ASN CA C 56.586 0.019 1 365 . 39 ASN CB C 38.746 0.035 1 366 . 39 ASN CG C 175.472 0.014 1 367 . 39 ASN HA H 4.486 0.009 1 368 . 39 ASN HB2 H 2.836 0.013 2 369 . 39 ASN HD21 H 7.024 0.310 2 370 . 39 ASN HD22 H 7.658 0.310 2 371 . 39 ASN H H 8.081 0.009 2 372 . 39 ASN N N 120.910 0.053 1 373 . 39 ASN ND2 N 114.014 0.294 1 374 . 40 ALA C C 181.047 0.000 1 375 . 40 ALA CA C 54.788 0.047 1 376 . 40 ALA CB C 18.599 0.019 1 377 . 40 ALA HA H 4.132 0.010 1 378 . 40 ALA H H 7.307 0.006 1 379 . 40 ALA N N 124.037 0.043 1 380 . 40 ALA HB H 1.297 0.006 1 381 . 41 VAL C C 180.965 0.000 1 382 . 41 VAL CA C 66.931 0.068 1 383 . 41 VAL CB C 31.494 0.026 1 384 . 41 VAL CG1 C 22.370 0.027 1 385 . 41 VAL CG2 C 21.329 0.084 2 386 . 41 VAL HA H 3.254 0.010 2 387 . 41 VAL HB H 2.112 0.006 1 388 . 41 VAL H H 8.339 0.008 1 389 . 41 VAL N N 123.719 0.029 1 390 . 41 VAL HG1 H 0.095 0.008 1 391 . 41 VAL HG2 H 0.818 0.011 2 392 . 42 VAL C C 179.898 0.000 2 393 . 42 VAL CA C 66.488 0.037 1 394 . 42 VAL CB C 31.578 0.006 1 395 . 42 VAL CG1 C 20.962 0.018 1 396 . 42 VAL CG2 C 22.269 0.014 2 397 . 42 VAL HA H 3.788 0.015 2 398 . 42 VAL HB H 2.282 0.006 1 399 . 42 VAL H H 7.903 0.012 1 400 . 42 VAL N N 123.350 0.033 1 401 . 42 VAL HG1 H 0.993 0.011 1 402 . 42 VAL HG2 H 1.087 0.014 2 403 . 43 GLU C C 176.658 0.000 2 404 . 43 GLU CA C 57.832 0.036 1 405 . 43 GLU CB C 27.986 0.012 1 406 . 43 GLU CG C 33.094 0.067 1 407 . 43 GLU HA H 4.236 0.013 1 408 . 43 GLU HB2 H 2.246 0.015 1 409 . 43 GLU HB3 H 2.109 0.008 2 410 . 43 GLU HG2 H 2.603 0.028 2 411 . 43 GLU HG3 H 2.647 0.005 1 412 . 43 GLU H H 7.925 0.011 1 413 . 43 GLU N N 120.798 0.035 1 414 . 44 SER C C 175.391 0.000 1 415 . 44 SER CA C 59.082 0.041 1 416 . 44 SER CB C 64.563 0.048 1 417 . 44 SER HA H 4.547 0.011 1 418 . 44 SER HB2 H 3.978 0.030 2 419 . 44 SER HB3 H 4.239 0.010 2 420 . 44 SER H H 7.815 0.006 1 421 . 44 SER N N 114.650 0.027 1 422 . 45 ASN C C 175.625 0.000 1 423 . 45 ASN CA C 54.362 0.030 1 424 . 45 ASN CB C 37.237 0.058 1 425 . 45 ASN CG C 178.205 0.000 1 426 . 45 ASN HA H 4.515 0.006 1 427 . 45 ASN HB2 H 2.893 0.011 2 428 . 45 ASN HB3 H 3.177 0.005 2 429 . 45 ASN HD21 H 6.844 0.001 2 430 . 45 ASN HD22 H 7.573 0.005 2 431 . 45 ASN H H 8.398 0.013 1 432 . 45 ASN N N 121.603 0.099 1 433 . 45 ASN ND2 N 113.689 0.105 1 434 . 46 GLY C C 175.047 0.000 1 435 . 46 GLY CA C 45.870 0.020 1 436 . 46 GLY HA2 H 3.581 0.014 2 437 . 46 GLY HA3 H 4.137 0.009 2 438 . 46 GLY H H 8.066 0.015 1 439 . 46 GLY N N 104.457 0.059 1 440 . 47 THR C C 174.710 0.000 1 441 . 47 THR CA C 63.152 0.011 1 442 . 47 THR CB C 70.060 0.075 1 443 . 47 THR CG2 C 21.469 0.008 1 444 . 47 THR HA H 4.251 0.013 1 445 . 47 THR HB H 4.287 0.005 1 446 . 47 THR H H 7.599 0.008 1 447 . 47 THR N N 111.980 0.058 1 448 . 47 THR HG2 H 1.275 0.010 1 449 . 48 LEU C C 174.666 0.000 1 450 . 48 LEU CA C 55.494 0.026 1 451 . 48 LEU CB C 43.157 0.044 1 452 . 48 LEU CD1 C 23.374 0.156 2 453 . 48 LEU CD2 C 26.446 0.053 2 454 . 48 LEU CG C 26.560 0.091 1 455 . 48 LEU HA H 4.247 0.011 1 456 . 48 LEU HB2 H 1.263 0.018 2 457 . 48 LEU HB3 H 1.523 0.012 2 458 . 48 LEU HG H 1.193 0.008 1 459 . 48 LEU H H 7.634 0.006 1 460 . 48 LEU N N 126.041 0.026 1 461 . 48 LEU HD1 H 1.181 0.009 2 462 . 48 LEU HD2 H 0.357 0.012 2 463 . 49 THR C C 173.424 0.000 1 464 . 49 THR CB C 71.920 0.041 1 465 . 49 THR CG2 C 21.447 0.019 1 466 . 49 THR HA H 4.750 0.017 1 467 . 49 THR HB H 4.376 0.006 1 468 . 49 THR H H 8.540 0.007 1 469 . 49 THR N N 116.939 0.097 1 470 . 49 THR HG2 H 1.173 0.006 1 471 . 50 LEU C C 176.339 0.000 1 472 . 50 LEU CA C 54.937 0.024 1 473 . 50 LEU CB C 42.850 0.017 1 474 . 50 LEU CD1 C 24.281 0.030 2 475 . 50 LEU CD2 C 25.928 0.035 2 476 . 50 LEU CG C 26.736 0.063 1 477 . 50 LEU HA H 4.101 0.013 1 478 . 50 LEU HB2 H 1.005 0.013 2 479 . 50 LEU HB3 H 1.755 0.023 2 480 . 50 LEU HG H 0.691 0.019 1 481 . 50 LEU H H 8.753 0.019 1 482 . 50 LEU N N 123.586 0.053 1 483 . 50 LEU HD1 H -0.077 0.017 2 484 . 50 LEU HD2 H 0.040 0.020 2 485 . 51 SER C C 175.086 0.000 1 486 . 51 SER CA C 60.392 0.088 1 487 . 51 SER CB C 63.519 0.019 1 488 . 51 SER HA H 4.538 0.012 1 489 . 51 SER HB2 H 3.394 0.011 2 490 . 51 SER HB3 H 3.558 0.015 2 491 . 51 SER H H 8.784 0.023 1 492 . 51 SER N N 123.903 0.079 1 493 . 52 HIS C C 173.236 0.000 1 494 . 52 HIS CA C 54.755 0.036 1 495 . 52 HIS CB C 29.209 0.006 1 496 . 52 HIS HA H 4.535 0.011 1 497 . 52 HIS HB2 H 3.311 0.008 2 498 . 52 HIS HB3 H 3.800 0.010 2 499 . 52 HIS HD2 H 7.273 0.009 1 500 . 52 HIS HE1 H 8.771 0.019 1 501 . 52 HIS H H 7.276 0.016 1 502 . 52 HIS N N 109.156 0.057 1 503 . 53 PHE C C 178.120 0.000 1 504 . 53 PHE CA C 60.426 0.016 1 505 . 53 PHE CB C 39.681 0.014 1 506 . 53 PHE HA H 4.378 0.015 1 507 . 53 PHE HB2 H 3.042 0.014 2 508 . 53 PHE HB3 H 3.264 0.021 2 509 . 53 PHE H H 9.200 0.010 1 510 . 53 PHE HZ H 6.820 0.004 1 511 . 53 PHE N N 121.379 0.054 1 512 . 53 PHE HD1 H 7.264 0.011 1 513 . 53 PHE HE1 H 7.131 0.009 1 514 . 54 GLY C C 170.763 0.000 1 515 . 54 GLY CA C 44.444 0.043 1 516 . 54 GLY HA2 H 3.579 0.010 2 517 . 54 GLY HA3 H 4.627 0.011 2 518 . 54 GLY H H 8.287 0.021 1 519 . 54 GLY N N 115.475 0.033 1 520 . 55 LYS C C 177.971 0.000 1 521 . 55 LYS CA C 56.253 0.011 1 522 . 55 LYS CB C 33.074 0.049 1 523 . 55 LYS CD C 29.737 0.020 1 524 . 55 LYS CE C 42.114 0.002 1 525 . 55 LYS CG C 24.131 0.015 1 526 . 55 LYS HA H 4.040 0.011 1 527 . 55 LYS HB2 H 1.781 0.007 2 528 . 55 LYS HB3 H 1.877 0.008 2 529 . 55 LYS HD2 H 1.763 0.009 1 530 . 55 LYS HE2 H 3.079 0.015 1 531 . 55 LYS HG2 H 1.495 0.014 2 532 . 55 LYS HG3 H 1.530 0.004 2 533 . 55 LYS H H 8.013 0.013 1 534 . 55 LYS N N 114.683 0.037 1 535 . 56 CYS CA C 55.115 0.010 1 536 . 56 CYS CB C 37.719 0.039 1 537 . 56 CYS HA H 4.447 0.020 1 538 . 56 CYS HB2 H 2.538 0.018 2 539 . 56 CYS HB3 H 3.248 0.014 2 540 . 56 CYS H H 8.274 0.025 1 541 . 56 CYS N N 123.917 0.030 1 stop_ save_